메뉴 건너뛰기




Volumn 285, Issue C, 2010, Pages 1-74

Cell and molecular biology of microtubule plus end tracking proteins. End binding proteins and their partners

Author keywords

APC; CLIP 170; Dynein; EB1; Kinesin; Microtubule; Spectraplakin; STIM1

Indexed keywords

ADAPTOR PROTEIN; APC PROTEIN; BINDING PROTEIN; CYCLIN DEPENDENT KINASE 5 REGULATORY SUBUNIT ASSOCIATED PROTEIN 2; DYNACTIN; DYNEIN ADENOSINE TRIPHOSPHATASE; FUNGAL PROTEIN; GLYCINE; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE TRIPHOSPHATE; KINESIN; MELANOPHILIN; MICROTUBULE PROTEIN; MOLECULAR MOTOR; NERVE PROTEIN; PROTEIN CLASP; PROTEIN CLIP 170; PROTEIN KAR9; PROTEIN MCAK; PROTEIN P140CAP; PROTEIN TIP150; PROTEIN XMAP215; REGULATOR PROTEIN; RHO TYPE GUANINE NUCLEOTIDE EXCHANGE FACTOR; SERINE; SPECTRAPLAKIN; STROMAL INTERACTION MOLECULE 1; TUBULIN; TUMOR OVEREXPRESSED GENE PROTEIN; TUMOR PROTEIN; UNCLASSIFIED DRUG;

EID: 77958493799     PISSN: 19376448     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-381047-2.00001-3     Document Type: Chapter
Times cited : (56)

References (446)
  • 1
    • 77953898430 scopus 로고    scopus 로고
    • Disease-associated mutations in the p150(Glued) subunit destabilize the CAP-gly domain
    • Ahmed S., Sun S., Siglin A.E., Polenova T., Williams J.C. Disease-associated mutations in the p150(Glued) subunit destabilize the CAP-gly domain. Biochemistry 2010, 49:5083-5085.
    • (2010) Biochemistry , vol.49 , pp. 5083-5085
    • Ahmed, S.1    Sun, S.2    Siglin, A.E.3    Polenova, T.4    Williams, J.C.5
  • 2
    • 41149156427 scopus 로고    scopus 로고
    • Tracking the ends: a dynamic protein network controls the fate of microtubule tips
    • Akhmanova A., Steinmetz M.O. Tracking the ends: a dynamic protein network controls the fate of microtubule tips. Nat. Rev. Mol. Cell Biol. 2008, 9:309-322.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 309-322
    • Akhmanova, A.1    Steinmetz, M.O.2
  • 3
    • 17744372880 scopus 로고    scopus 로고
    • Clasps are CLIP-115 and -170 associating proteins involved in the regional regulation of microtubule dynamics in motile fibroblasts
    • Akhmanova A., Hoogenraad C.C., Drabek K., Stepanova T., Dortland B., Verkerk T., et al. Clasps are CLIP-115 and -170 associating proteins involved in the regional regulation of microtubule dynamics in motile fibroblasts. Cell 2001, 104:923-935.
    • (2001) Cell , vol.104 , pp. 923-935
    • Akhmanova, A.1    Hoogenraad, C.C.2    Drabek, K.3    Stepanova, T.4    Dortland, B.5    Verkerk, T.6
  • 4
    • 26944443679 scopus 로고    scopus 로고
    • The microtubule plus-end-tracking protein CLIP-170 associates with the spermatid manchette and is essential for spermatogenesis
    • Akhmanova A., Mausset-Bonnefont A.L., van Cappellen W., Keijzer N., Hoogenraad C.C., Stepanova T., et al. The microtubule plus-end-tracking protein CLIP-170 associates with the spermatid manchette and is essential for spermatogenesis. Genes Dev. 2005, 19:2501-2515.
    • (2005) Genes Dev. , vol.19 , pp. 2501-2515
    • Akhmanova, A.1    Mausset-Bonnefont, A.L.2    van Cappellen, W.3    Keijzer, N.4    Hoogenraad, C.C.5    Stepanova, T.6
  • 5
    • 33645306849 scopus 로고    scopus 로고
    • Stu2p binds tubulin and undergoes an open-to-closed conformational change
    • Al-Bassam J., van Breugel M., Harrison S.C., Hyman A. Stu2p binds tubulin and undergoes an open-to-closed conformational change. J. Cell Biol. 2006, 172:1009-1022.
    • (2006) J. Cell Biol. , vol.172 , pp. 1009-1022
    • Al-Bassam, J.1    van Breugel, M.2    Harrison, S.C.3    Hyman, A.4
  • 6
    • 34249800934 scopus 로고    scopus 로고
    • The kinesin ATK5 functions in early spindle assembly in Arabidopsis
    • Ambrose J.C., Cyr R. The kinesin ATK5 functions in early spindle assembly in Arabidopsis. Plant Cell 2007, 19:226-236.
    • (2007) Plant Cell , vol.19 , pp. 226-236
    • Ambrose, J.C.1    Cyr, R.2
  • 7
    • 56349088050 scopus 로고    scopus 로고
    • CLASP modulates microtubule-cortex interaction during self-organization of acentrosomal microtubules
    • Ambrose J.C., Wasteneys G.O. CLASP modulates microtubule-cortex interaction during self-organization of acentrosomal microtubules. Mol. Biol. Cell 2008, 19:4730-4737.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4730-4737
    • Ambrose, J.C.1    Wasteneys, G.O.2
  • 8
    • 16344378770 scopus 로고    scopus 로고
    • A minus-end-directed kinesin with plus-end tracking protein activity is involved in spindle morphogenesis
    • Ambrose J.C., Li W., Marcus A., Ma H., Cyr R. A minus-end-directed kinesin with plus-end tracking protein activity is involved in spindle morphogenesis. Mol. Biol. Cell 2005, 16:1584-1592.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1584-1592
    • Ambrose, J.C.1    Li, W.2    Marcus, A.3    Ma, H.4    Cyr, R.5
  • 9
    • 50649090270 scopus 로고    scopus 로고
    • Cortactin branches out: roles in regulating protrusive actin dynamics
    • Ammer A.G., Weed S.A. Cortactin branches out: roles in regulating protrusive actin dynamics. Cell Motil. Cytoskeleton 2008, 65:687-707.
    • (2008) Cell Motil. Cytoskeleton , vol.65 , pp. 687-707
    • Ammer, A.G.1    Weed, S.A.2
  • 10
    • 0036010599 scopus 로고    scopus 로고
    • Toward reconstitution of in vivo microtubule dynamics in vitro
    • Andersen S.S., Wittmann T. Toward reconstitution of in vivo microtubule dynamics in vitro. Bioessays 2002, 24:305-307.
    • (2002) Bioessays , vol.24 , pp. 305-307
    • Andersen, S.S.1    Wittmann, T.2
  • 12
    • 35648988947 scopus 로고    scopus 로고
    • Adenomatous polyposis coli (APC): a multi-functional tumor suppressor gene
    • Aoki K., Taketo M.M. Adenomatous polyposis coli (APC): a multi-functional tumor suppressor gene. J. Cell Sci. 2007, 120:3327-3335.
    • (2007) J. Cell Sci. , vol.120 , pp. 3327-3335
    • Aoki, K.1    Taketo, M.M.2
  • 13
    • 33747444678 scopus 로고    scopus 로고
    • CDC2 phosphorylation of the fission yeast dis1 ensures accurate chromosome segregation
    • Aoki K., Nakaseko Y., Kinoshita K., Goshima G., Yanagida M. CDC2 phosphorylation of the fission yeast dis1 ensures accurate chromosome segregation. Curr. Biol. 2006, 16:1627-1635.
    • (2006) Curr. Biol. , vol.16 , pp. 1627-1635
    • Aoki, K.1    Nakaseko, Y.2    Kinoshita, K.3    Goshima, G.4    Yanagida, M.5
  • 14
    • 77952328557 scopus 로고    scopus 로고
    • The spectraplakin short stop is an actin-microtubule crosslinker that contributes to organization of the microtubule network
    • Applewhite D.A., Grode K.D., Keller D., Zadeh A., Slep K.C., Rogers S.L. The spectraplakin short stop is an actin-microtubule crosslinker that contributes to organization of the microtubule network. Mol. Biol. Cell 2010, 21:1714-1724.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1714-1724
    • Applewhite, D.A.1    Grode, K.D.2    Keller, D.3    Zadeh, A.4    Slep, K.C.5    Rogers, S.L.6
  • 15
    • 0034658077 scopus 로고    scopus 로고
    • Structural transitions at microtubule ends correlate with their dynamic properties in Xenopus egg extracts
    • Arnal I., Karsenti E., Hyman A.A. Structural transitions at microtubule ends correlate with their dynamic properties in Xenopus egg extracts. J. Cell Biol. 2000, 149:767-774.
    • (2000) J. Cell Biol. , vol.149 , pp. 767-774
    • Arnal, I.1    Karsenti, E.2    Hyman, A.A.3
  • 16
    • 10344264479 scopus 로고    scopus 로고
    • CLIP-170/tubulin-curved oligomers coassemble at microtubule ends and promote rescues
    • Arnal I., Heichette C., Diamantopoulos G.S., Chretien D. CLIP-170/tubulin-curved oligomers coassemble at microtubule ends and promote rescues. Curr. Biol. 2004, 14:2086-2095.
    • (2004) Curr. Biol. , vol.14 , pp. 2086-2095
    • Arnal, I.1    Heichette, C.2    Diamantopoulos, G.S.3    Chretien, D.4
  • 17
    • 0034611602 scopus 로고    scopus 로고
    • Regulation and function of the interaction between the APC tumour suppressor protein and EB1
    • Askham J.M., Moncur P., Markham A.F., Morrison E.E. Regulation and function of the interaction between the APC tumour suppressor protein and EB1. Oncogene 2000, 19:1950-1958.
    • (2000) Oncogene , vol.19 , pp. 1950-1958
    • Askham, J.M.1    Moncur, P.2    Markham, A.F.3    Morrison, E.E.4
  • 18
    • 0036796793 scopus 로고    scopus 로고
    • Evidence that an interaction between EB1 and p150(Glued) is required for the formation and maintenance of a radial microtubule array anchored at the centrosome
    • Askham J.M., Vaughan K.T., Goodson H.V., Morrison E.E. Evidence that an interaction between EB1 and p150(Glued) is required for the formation and maintenance of a radial microtubule array anchored at the centrosome. Mol. Biol. Cell 2002, 13:3627-3645.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3627-3645
    • Askham, J.M.1    Vaughan, K.T.2    Goodson, H.V.3    Morrison, E.E.4
  • 20
    • 75349104314 scopus 로고    scopus 로고
    • Role of APC and its binding partners in regulating microtubules in mitosis
    • Bahmanyar S., Nelson W.J., Barth A.I. Role of APC and its binding partners in regulating microtubules in mitosis. Adv. Exp. Med. Biol. 2009, 656:65-74.
    • (2009) Adv. Exp. Med. Biol. , vol.656 , pp. 65-74
    • Bahmanyar, S.1    Nelson, W.J.2    Barth, A.I.3
  • 21
    • 70350490026 scopus 로고    scopus 로고
    • Mitotic regulation of the stability of microtubule plus-end tracking protein EB3 by ubiquitin ligase SIAH-1 and Aurora mitotic kinases
    • Ban R., Matsuzaki H., Akashi T., Sakashita G., Taniguchi H., Park S.Y., et al. Mitotic regulation of the stability of microtubule plus-end tracking protein EB3 by ubiquitin ligase SIAH-1 and Aurora mitotic kinases. J. Biol. Chem. 2009, 284:28367-28381.
    • (2009) J. Biol. Chem. , vol.284 , pp. 28367-28381
    • Ban, R.1    Matsuzaki, H.2    Akashi, T.3    Sakashita, G.4    Taniguchi, H.5    Park, S.Y.6
  • 22
    • 57349190213 scopus 로고    scopus 로고
    • MCAK-independent functions of ch-Tog/XMAP215 in microtubule plus-end dynamics
    • Barr A.R., Gergely F. MCAK-independent functions of ch-Tog/XMAP215 in microtubule plus-end dynamics. Mol. Cell. Biol. 2008, 28:7199-7211.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 7199-7211
    • Barr, A.R.1    Gergely, F.2
  • 23
    • 77950566340 scopus 로고    scopus 로고
    • CDK5RAP2 functions in centrosome to spindle pole attachment and DNA damage response
    • Barr A.R., Kilmartin J.V., Gergely F. CDK5RAP2 functions in centrosome to spindle pole attachment and DNA damage response. J. Cell Biol. 2010, 189:23-39.
    • (2010) J. Cell Biol. , vol.189 , pp. 23-39
    • Barr, A.R.1    Kilmartin, J.V.2    Gergely, F.3
  • 24
    • 0034735942 scopus 로고    scopus 로고
    • The role of the proteins Kar9 and Myo2 in orienting the mitotic spindle of budding yeast
    • Beach D.L., Thibodeaux J., Maddox P., Yeh E., Bloom K. The role of the proteins Kar9 and Myo2 in orienting the mitotic spindle of budding yeast. Curr. Biol. 2000, 10:1497-1506.
    • (2000) Curr. Biol. , vol.10 , pp. 1497-1506
    • Beach, D.L.1    Thibodeaux, J.2    Maddox, P.3    Yeh, E.4    Bloom, K.5
  • 25
    • 0030611667 scopus 로고    scopus 로고
    • Mal3, the fission yeast homologue of the human APC-interacting protein EB-1 is required for microtubule integrity and the maintenance of cell form
    • Beinhauer J.D., Hagan I.M., Hegemann J.H., Fleig U. Mal3, the fission yeast homologue of the human APC-interacting protein EB-1 is required for microtubule integrity and the maintenance of cell form. J. Cell Biol. 1997, 139:717-728.
    • (1997) J. Cell Biol. , vol.139 , pp. 717-728
    • Beinhauer, J.D.1    Hagan, I.M.2    Hegemann, J.H.3    Fleig, U.4
  • 26
    • 0025597940 scopus 로고
    • BIK1, a protein required for microtubule function during mating and mitosis in Saccharomyces cerevisiae, colocalizes with tubulin
    • Berlin V., Styles C.A., Fink G.R. BIK1, a protein required for microtubule function during mating and mitosis in Saccharomyces cerevisiae, colocalizes with tubulin. J. Cell Biol. 1990, 111:2573-2586.
    • (1990) J. Cell Biol. , vol.111 , pp. 2573-2586
    • Berlin, V.1    Styles, C.A.2    Fink, G.R.3
  • 27
    • 0032168986 scopus 로고    scopus 로고
    • The adenomatous polyposis coli-binding protein EB1 is associated with cytoplasmic and spindle microtubules
    • Berrueta L., Kraeft S.K., Tirnauer J.S., Schuyler S.C., Chen L.B., Hill D.E., et al. The adenomatous polyposis coli-binding protein EB1 is associated with cytoplasmic and spindle microtubules. Proc. Natl Acad. Sci. USA 1998, 95:10596-10601.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 10596-10601
    • Berrueta, L.1    Kraeft, S.K.2    Tirnauer, J.S.3    Schuyler, S.C.4    Chen, L.B.5    Hill, D.E.6
  • 28
    • 37249075604 scopus 로고    scopus 로고
    • Reconstitution of a microtubule plus-end tracking system in vitro
    • Bieling P., Laan L., Schek H., Munteanu E.L., Sandblad L., Dogterom M., et al. Reconstitution of a microtubule plus-end tracking system in vitro. Nature 2007, 450:1100-1105.
    • (2007) Nature , vol.450 , pp. 1100-1105
    • Bieling, P.1    Laan, L.2    Schek, H.3    Munteanu, E.L.4    Sandblad, L.5    Dogterom, M.6
  • 29
    • 59449100831 scopus 로고    scopus 로고
    • CLIP-170 tracks growing microtubule ends by dynamically recognizing composite EB1/tubulin-binding sites
    • Bieling P., Kandels-Lewis S., Telley I.A., van Dijk J., Janke C., Surrey T. CLIP-170 tracks growing microtubule ends by dynamically recognizing composite EB1/tubulin-binding sites. J. Cell Biol. 2008, 183:1223-1233.
    • (2008) J. Cell Biol. , vol.183 , pp. 1223-1233
    • Bieling, P.1    Kandels-Lewis, S.2    Telley, I.A.3    van Dijk, J.4    Janke, C.5    Surrey, T.6
  • 30
    • 0036270763 scopus 로고    scopus 로고
    • The subcellular destinations of APC proteins
    • Bienz M. The subcellular destinations of APC proteins. Nat. Rev. Mol. Cell Biol. 2002, 3:328-338.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 328-338
    • Bienz, M.1
  • 31
    • 0026523613 scopus 로고
    • Restin: a novel intermediate filament-associated protein highly expressed in the Reed-Sternberg cells of Hodgkin's disease
    • Bilbe G., Delabie J., Bruggen J., Richener H., Asselbergs F.A., Cerletti N., et al. Restin: a novel intermediate filament-associated protein highly expressed in the Reed-Sternberg cells of Hodgkin's disease. EMBO J. 1992, 11:2103-2113.
    • (1992) EMBO J. , vol.11 , pp. 2103-2113
    • Bilbe, G.1    Delabie, J.2    Bruggen, J.3    Richener, H.4    Asselbergs, F.A.5    Cerletti, N.6
  • 32
    • 44649162674 scopus 로고    scopus 로고
    • The microtubule plus-end binding protein EB1 functions in root responses to touch and gravity signals in Arabidopsis
    • Bisgrove S.R., Lee Y.R., Liu B., Peters N.T., Kropf D.L. The microtubule plus-end binding protein EB1 functions in root responses to touch and gravity signals in Arabidopsis. Plant Cell 2008, 20:396-410.
    • (2008) Plant Cell , vol.20 , pp. 396-410
    • Bisgrove, S.R.1    Lee, Y.R.2    Liu, B.3    Peters, N.T.4    Kropf, D.L.5
  • 33
    • 77953515706 scopus 로고    scopus 로고
    • Regulation of microtubule dynamics by Bim1 and Bik1, the budding yeast members of the EB1 and CLIP-170 families of plus-end tracking proteins
    • Blake-Hodek K.A., Cassimeris L., Huffaker T.C. Regulation of microtubule dynamics by Bim1 and Bik1, the budding yeast members of the EB1 and CLIP-170 families of plus-end tracking proteins. Mol. Biol. Cell 2010, 21:2013-2023.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2013-2023
    • Blake-Hodek, K.A.1    Cassimeris, L.2    Huffaker, T.C.3
  • 35
    • 34247119737 scopus 로고    scopus 로고
    • Kinetic analysis of tubulin assembly in the presence of the microtubule-associated protein TOGp
    • Bonfils C., Bec N., Lacroix B., Harricane M.C., Larroque C. Kinetic analysis of tubulin assembly in the presence of the microtubule-associated protein TOGp. J. Biol. Chem. 2007, 282:5570-5581.
    • (2007) J. Biol. Chem. , vol.282 , pp. 5570-5581
    • Bonfils, C.1    Bec, N.2    Lacroix, B.3    Harricane, M.C.4    Larroque, C.5
  • 36
    • 67349288068 scopus 로고    scopus 로고
    • Context-specific requirements of functional domains of the Spectraplakin Short stop in vivo
    • Bottenberg W., Sanchez-Soriano N., Alves-Silva J., Hahn I., Mende M., Prokop A. Context-specific requirements of functional domains of the Spectraplakin Short stop in vivo. Mech. Dev. 2009, 126:489-502.
    • (2009) Mech. Dev. , vol.126 , pp. 489-502
    • Bottenberg, W.1    Sanchez-Soriano, N.2    Alves-Silva, J.3    Hahn, I.4    Mende, M.5    Prokop, A.6
  • 37
    • 68849097872 scopus 로고    scopus 로고
    • The multipurpose 15-protofilament microtubules in C. elegans have specific roles in mechanosensation
    • Bounoutas A., O'Hagan R., Chalfie M. The multipurpose 15-protofilament microtubules in C. elegans have specific roles in mechanosensation. Curr. Biol. 2009, 19:1362-1367.
    • (2009) Curr. Biol. , vol.19 , pp. 1362-1367
    • Bounoutas, A.1    O'Hagan, R.2    Chalfie, M.3
  • 38
    • 36448939015 scopus 로고    scopus 로고
    • Stabilization of overlapping microtubules by fission yeast CLASP
    • Bratman S.V., Chang F. Stabilization of overlapping microtubules by fission yeast CLASP. Dev. Cell 2007, 13:812-827.
    • (2007) Dev. Cell , vol.13 , pp. 812-827
    • Bratman, S.V.1    Chang, F.2
  • 40
    • 16844377634 scopus 로고    scopus 로고
    • The EB1 homolog Mal3 stimulates the ATPase of the kinesin Tea2 by recruiting it to the microtubule
    • Browning H., Hackney D.D. The EB1 homolog Mal3 stimulates the ATPase of the kinesin Tea2 by recruiting it to the microtubule. J. Biol. Chem. 2005, 280:12299-12304.
    • (2005) J. Biol. Chem. , vol.280 , pp. 12299-12304
    • Browning, H.1    Hackney, D.D.2
  • 41
    • 0034597056 scopus 로고    scopus 로고
    • Tea2p is a kinesin-like protein required to generate polarized growth in fission yeast
    • Browning H., Hayles J., Mata J., Aveline L., Nurse P., McIntosh J.R. Tea2p is a kinesin-like protein required to generate polarized growth in fission yeast. J. Cell Biol. 2000, 151:15-28.
    • (2000) J. Cell Biol. , vol.151 , pp. 15-28
    • Browning, H.1    Hayles, J.2    Mata, J.3    Aveline, L.4    Nurse, P.5    McIntosh, J.R.6
  • 42
    • 0041689492 scopus 로고    scopus 로고
    • Targeted movement of cell end factors in fission yeast
    • Browning H., Hackney D.D., Nurse P. Targeted movement of cell end factors in fission yeast. Nat. Cell Biol. 2003, 5:812-818.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 812-818
    • Browning, H.1    Hackney, D.D.2    Nurse, P.3
  • 43
    • 0034266786 scopus 로고    scopus 로고
    • CLIP170-like tip1p spatially organizes microtubular dynamics in fission yeast
    • Brunner D., Nurse P. CLIP170-like tip1p spatially organizes microtubular dynamics in fission yeast. Cell 2000, 102:695-704.
    • (2000) Cell , vol.102 , pp. 695-704
    • Brunner, D.1    Nurse, P.2
  • 44
    • 0346749538 scopus 로고    scopus 로고
    • Characterization of functional domains of human EB1 family proteins
    • Bu W., Su L.K. Characterization of functional domains of human EB1 family proteins. J. Biol. Chem. 2003, 278:49721-49731.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49721-49731
    • Bu, W.1    Su, L.K.2
  • 45
    • 1842665850 scopus 로고    scopus 로고
    • The microtubule plus end-tracking proteins mal3p and tip1p cooperate for cell-end targeting of interphase microtubules
    • Busch K.E., Brunner D. The microtubule plus end-tracking proteins mal3p and tip1p cooperate for cell-end targeting of interphase microtubules. Curr. Biol. 2004, 14:548-559.
    • (2004) Curr. Biol. , vol.14 , pp. 548-559
    • Busch, K.E.1    Brunner, D.2
  • 46
    • 2942557233 scopus 로고    scopus 로고
    • Tea2p kinesin is involved in spatial microtubule organization by transporting tip1p on microtubules
    • Busch K.E., Hayles J., Nurse P., Brunner D. Tea2p kinesin is involved in spatial microtubule organization by transporting tip1p on microtubules. Dev. Cell 2004, 6:831-843.
    • (2004) Dev. Cell , vol.6 , pp. 831-843
    • Busch, K.E.1    Hayles, J.2    Nurse, P.3    Brunner, D.4
  • 47
    • 34547748865 scopus 로고    scopus 로고
    • Poleward tubulin flux in spindles: regulation and function in mitotic cells
    • Buster D.W., Zhang D., Sharp D.J. Poleward tubulin flux in spindles: regulation and function in mitotic cells. Mol. Biol. Cell 2007, 18:3094-3104.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3094-3104
    • Buster, D.W.1    Zhang, D.2    Sharp, D.J.3
  • 48
    • 66949137457 scopus 로고    scopus 로고
    • STIMulating store-operated Ca(2+) entry
    • Cahalan M.D. STIMulating store-operated Ca(2+) entry. Nat. Cell Biol. 2009, 11:669-677.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 669-677
    • Cahalan, M.D.1
  • 49
    • 0029989442 scopus 로고    scopus 로고
    • Evidence that a single monolayer tubulin-GTP cap is both necessary and sufficient to stabilize microtubules
    • Caplow M., Shanks J. Evidence that a single monolayer tubulin-GTP cap is both necessary and sufficient to stabilize microtubules. Mol. Biol. Cell 1996, 7:663-675.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 663-675
    • Caplow, M.1    Shanks, J.2
  • 50
    • 0028149355 scopus 로고
    • The free energy for hydrolysis of a microtubule-bound nucleotide triphosphate is near zero: all of the free energy for hydrolysis is stored in the microtubule lattice
    • Caplow M., Ruhlen R.L., Shanks J. The free energy for hydrolysis of a microtubule-bound nucleotide triphosphate is near zero: all of the free energy for hydrolysis is stored in the microtubule lattice. J. Cell Biol. 1994, 127:779-788.
    • (1994) J. Cell Biol. , vol.127 , pp. 779-788
    • Caplow, M.1    Ruhlen, R.L.2    Shanks, J.3
  • 51
    • 2942617092 scopus 로고    scopus 로고
    • Cell cycle control of kinesin-mediated transport of Bik1 (CLIP-170) regulates microtubule stability and dynein activation
    • Carvalho P., Gupta M.L., Hoyt M.A., Pellman D. Cell cycle control of kinesin-mediated transport of Bik1 (CLIP-170) regulates microtubule stability and dynein activation. Dev. Cell 2004, 6:815-829.
    • (2004) Dev. Cell , vol.6 , pp. 815-829
    • Carvalho, P.1    Gupta, M.L.2    Hoyt, M.A.3    Pellman, D.4
  • 52
    • 0027372852 scopus 로고
    • Regulation of microtubule dynamic instability
    • Cassimeris L. Regulation of microtubule dynamic instability. Cell Motil. Cytoskeleton 1993, 26:275-281.
    • (1993) Cell Motil. Cytoskeleton , vol.26 , pp. 275-281
    • Cassimeris, L.1
  • 53
    • 60349099913 scopus 로고    scopus 로고
    • Microtubule assembly: lattice GTP to the rescue
    • Cassimeris L. Microtubule assembly: lattice GTP to the rescue. Curr. Biol. 2009, 19:R174-R176.
    • (2009) Curr. Biol. , vol.19
    • Cassimeris, L.1
  • 54
    • 1642464712 scopus 로고    scopus 로고
    • TOGp, the human homolog of XMAP215/Dis1, is required for centrosome integrity, spindle pole organization, and bipolar spindle assembly
    • Cassimeris L., Morabito J. TOGp, the human homolog of XMAP215/Dis1, is required for centrosome integrity, spindle pole organization, and bipolar spindle assembly. Mol. Biol. Cell 2004, 15:1580-1590.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1580-1590
    • Cassimeris, L.1    Morabito, J.2
  • 55
    • 0024202112 scopus 로고
    • Real-time observations of microtubule dynamic instability in living cells
    • Cassimeris L., Pryer N.K., Salmon E.D. Real-time observations of microtubule dynamic instability in living cells. J. Cell Biol. 1988, 107:2223-2231.
    • (1988) J. Cell Biol. , vol.107 , pp. 2223-2231
    • Cassimeris, L.1    Pryer, N.K.2    Salmon, E.D.3
  • 56
    • 0034839279 scopus 로고    scopus 로고
    • XMAP215 is a long thin molecule that does not increase microtubule stiffness
    • Cassimeris L., Gard D., Tran P.T., Erickson H.P. XMAP215 is a long thin molecule that does not increase microtubule stiffness. J. Cell Sci. 2001, 114:3025-3033.
    • (2001) J. Cell Sci. , vol.114 , pp. 3025-3033
    • Cassimeris, L.1    Gard, D.2    Tran, P.T.3    Erickson, H.P.4
  • 57
    • 67749113756 scopus 로고    scopus 로고
    • TOGp regulates microtubule assembly and density during mitosis and contributes to chromosome directional instability
    • Cassimeris L., Becker B., Carney B. TOGp regulates microtubule assembly and density during mitosis and contributes to chromosome directional instability. Cell Motil. Cytoskeleton 2009, 66:535-545.
    • (2009) Cell Motil. Cytoskeleton , vol.66 , pp. 535-545
    • Cassimeris, L.1    Becker, B.2    Carney, B.3
  • 58
    • 46649087150 scopus 로고    scopus 로고
    • A new role for kinesin-directed transport of Bik1p (CLIP-170) in Saccharomyces cerevisiae
    • Caudron F., Andrieux A., Job D., Boscheron C. A new role for kinesin-directed transport of Bik1p (CLIP-170) in Saccharomyces cerevisiae. J. Cell Sci. 2008, 121:1506-1513.
    • (2008) J. Cell Sci. , vol.121 , pp. 1506-1513
    • Caudron, F.1    Andrieux, A.2    Job, D.3    Boscheron, C.4
  • 59
    • 0242609977 scopus 로고    scopus 로고
    • EB1 reveals mobile microtubule nucleation sites in Arabidopsis
    • Chan J., Calder G.M., Doonan J.H., Lloyd C.W. EB1 reveals mobile microtubule nucleation sites in Arabidopsis. Nat. Cell Biol. 2003, 5:967-971.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 967-971
    • Chan, J.1    Calder, G.M.2    Doonan, J.H.3    Lloyd, C.W.4
  • 60
    • 32944461130 scopus 로고    scopus 로고
    • Localization of the microtubule end binding protein EB1 reveals alternative pathways of spindle development in Arabidopsis suspension cells
    • Chan J., Calder G., Fox S., Lloyd C. Localization of the microtubule end binding protein EB1 reveals alternative pathways of spindle development in Arabidopsis suspension cells. Plant Cell 2005, 17:1737-1748.
    • (2005) Plant Cell , vol.17 , pp. 1737-1748
    • Chan, J.1    Calder, G.2    Fox, S.3    Lloyd, C.4
  • 61
    • 33644792737 scopus 로고    scopus 로고
    • Regulation of actin assembly by microtubules in fission yeast cell polarity
    • Chang F., Feierbach B., Martin S. Regulation of actin assembly by microtubules in fission yeast cell polarity. Novartis Found. Symp. 2005, 269:59-66.
    • (2005) Novartis Found. Symp. , vol.269 , pp. 59-66
    • Chang, F.1    Feierbach, B.2    Martin, S.3
  • 62
    • 0028823831 scopus 로고
    • Characterization of the cDNA and pattern of expression of a new gene over-expressed in human hepatomas and colonic tumors
    • Charrasse S., Mazel M., Taviaux S., Berta P., Chow T., Larroque C. Characterization of the cDNA and pattern of expression of a new gene over-expressed in human hepatomas and colonic tumors. Eur. J. Biochem. 1995, 234:406-413.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 406-413
    • Charrasse, S.1    Mazel, M.2    Taviaux, S.3    Berta, P.4    Chow, T.5    Larroque, C.6
  • 63
    • 0031778750 scopus 로고    scopus 로고
    • The TOGp protein is a new human microtubule-associated protein homologous to the Xenopus XMAP215
    • Charrasse S., Schroeder M., Gauthier-Rouviere C., Ango F., Cassimeris L., Gard D.L., et al. The TOGp protein is a new human microtubule-associated protein homologous to the Xenopus XMAP215. J. Cell Sci. 1998, 111(Pt 10):1371-1383.
    • (1998) J. Cell Sci. , vol.111 , Issue.PART 10 , pp. 1371-1383
    • Charrasse, S.1    Schroeder, M.2    Gauthier-Rouviere, C.3    Ango, F.4    Cassimeris, L.5    Gard, D.L.6
  • 64
    • 18044376285 scopus 로고    scopus 로고
    • The CENP-F-like proteins HCP-1 and HCP-2 target CLASP to kinetochores to mediate chromosome segregation
    • Cheeseman I.M., MacLeod I., Yates J.R., Oegema K., Desai A. The CENP-F-like proteins HCP-1 and HCP-2 target CLASP to kinetochores to mediate chromosome segregation. Curr. Biol. 2005, 15:771-777.
    • (2005) Curr. Biol. , vol.15 , pp. 771-777
    • Cheeseman, I.M.1    MacLeod, I.2    Yates, J.R.3    Oegema, K.4    Desai, A.5
  • 65
    • 0032100813 scopus 로고    scopus 로고
    • The yeast spindle pole body component Spc72p interacts with Stu2p and is required for proper microtubule assembly
    • Chen X.P., Yin H., Huffaker T.C. The yeast spindle pole body component Spc72p interacts with Stu2p and is required for proper microtubule assembly. J. Cell Biol. 1998, 141:1169-1179.
    • (1998) J. Cell Biol. , vol.141 , pp. 1169-1179
    • Chen, X.P.1    Yin, H.2    Huffaker, T.C.3
  • 66
    • 45749094601 scopus 로고    scopus 로고
    • Lysosomal proliferation and distal degeneration in motor neurons expressing the G59S mutation in the p150Glued subunit of dynactin
    • Chevalier-Larsen E.S., Wallace K.E., Pennise C.R., Holzbaur E.L. Lysosomal proliferation and distal degeneration in motor neurons expressing the G59S mutation in the p150Glued subunit of dynactin. Hum. Mol. Genet. 2008, 17:1946-1955.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 1946-1955
    • Chevalier-Larsen, E.S.1    Wallace, K.E.2    Pennise, C.R.3    Holzbaur, E.L.4
  • 67
    • 75849140545 scopus 로고    scopus 로고
    • Evidence for the concerted evolution between short linear protein motifs and their flanking regions
    • Chica C., Diella F., Gibson T.J. Evidence for the concerted evolution between short linear protein motifs and their flanking regions. PLoS ONE 2009, 4:e6052.
    • (2009) PLoS ONE , vol.4
    • Chica, C.1    Diella, F.2    Gibson, T.J.3
  • 68
    • 0033977186 scopus 로고    scopus 로고
    • SNIP, a novel SNAP-25-interacting protein implicated in regulated exocytosis
    • Chin L.S., Nugent R.D., Raynor M.C., Vavalle J.P., Li L. SNIP, a novel SNAP-25-interacting protein implicated in regulated exocytosis. J. Biol. Chem. 2000, 275:1191-1200.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1191-1200
    • Chin, L.S.1    Nugent, R.D.2    Raynor, M.C.3    Vavalle, J.P.4    Li, L.5
  • 69
    • 0033964878 scopus 로고    scopus 로고
    • Cloning of three novel neuronal Cdk5 activator binding proteins
    • Ching Y.P., Qi Z., Wang J.H. Cloning of three novel neuronal Cdk5 activator binding proteins. Gene 2000, 242:285-294.
    • (2000) Gene , vol.242 , pp. 285-294
    • Ching, Y.P.1    Qi, Z.2    Wang, J.H.3
  • 72
    • 0025814877 scopus 로고
    • New data on the microtubule surface lattice
    • Chretien D., Wade R.H. New data on the microtubule surface lattice. Biol. Cell 1991, 71:161-174.
    • (1991) Biol. Cell , vol.71 , pp. 161-174
    • Chretien, D.1    Wade, R.H.2
  • 73
    • 0026667023 scopus 로고
    • Lattice defects in microtubules: protofilament numbers vary within individual microtubules
    • Chretien D., Metoz F., Verde F., Karsenti E., Wade R.H. Lattice defects in microtubules: protofilament numbers vary within individual microtubules. J. Cell Biol. 1992, 117:1031-1040.
    • (1992) J. Cell Biol. , vol.117 , pp. 1031-1040
    • Chretien, D.1    Metoz, F.2    Verde, F.3    Karsenti, E.4    Wade, R.H.5
  • 74
    • 0029041404 scopus 로고
    • Structure of growing microtubule ends: two-dimensional sheets close into tubes at variable rates
    • Chretien D., Fuller S.D., Karsenti E. Structure of growing microtubule ends: two-dimensional sheets close into tubes at variable rates. J. Cell Biol. 1995, 129:1311-1328.
    • (1995) J. Cell Biol. , vol.129 , pp. 1311-1328
    • Chretien, D.1    Fuller, S.D.2    Karsenti, E.3
  • 75
    • 58149098730 scopus 로고    scopus 로고
    • ATPase cycle of the nonmotile kinesin NOD allows microtubule end tracking and drives chromosome movement
    • Cochran J.C., Sindelar C.V., Mulko N.K., Collins K.A., Kong S.E., Hawley R.S., et al. ATPase cycle of the nonmotile kinesin NOD allows microtubule end tracking and drives chromosome movement. Cell 2009, 136:110-122.
    • (2009) Cell , vol.136 , pp. 110-122
    • Cochran, J.C.1    Sindelar, C.V.2    Mulko, N.K.3    Collins, K.A.4    Kong, S.E.5    Hawley, R.S.6
  • 76
    • 5444222543 scopus 로고    scopus 로고
    • Lis-1 is required for dynein-dependent cell division processes in C. elegans embryos
    • Cockell M.M., Baumer K., Gonczy P. lis-1 is required for dynein-dependent cell division processes in C. elegans embryos. J. Cell Sci. 2004, 117:4571-4582.
    • (2004) J. Cell Sci. , vol.117 , pp. 4571-4582
    • Cockell, M.M.1    Baumer, K.2    Gonczy, P.3
  • 78
    • 0037094416 scopus 로고    scopus 로고
    • Pore membrane and/or filament interacting like protein 1 (POMFIL1) is predominantly expressed in the nervous system and encodes different protein isoforms
    • Coy J.F., Wiemann S., Bechmann I., Bachner D., Nitsch R., Kretz O., et al. Pore membrane and/or filament interacting like protein 1 (POMFIL1) is predominantly expressed in the nervous system and encodes different protein isoforms. Gene 2002, 290:73-94.
    • (2002) Gene , vol.290 , pp. 73-94
    • Coy, J.F.1    Wiemann, S.2    Bechmann, I.3    Bachner, D.4    Nitsch, R.5    Kretz, O.6
  • 79
    • 27644509696 scopus 로고    scopus 로고
    • Drosophila Nod protein binds preferentially to the plus ends of microtubules and promotes microtubule polymerization in vitro
    • Cui W., Sproul L.R., Gustafson S.M., Matthies H.J., Gilbert S.P., Hawley R.S. Drosophila Nod protein binds preferentially to the plus ends of microtubules and promotes microtubule polymerization in vitro. Mol. Biol. Cell 2005, 16:5400-5409.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5400-5409
    • Cui, W.1    Sproul, L.R.2    Gustafson, S.M.3    Matthies, H.J.4    Gilbert, S.P.5    Hawley, R.S.6
  • 80
    • 0345363151 scopus 로고    scopus 로고
    • Mini spindles: a gene encoding a conserved microtubule-associated protein required for the integrity of the mitotic spindle in Drosophila
    • Cullen C.F., Deak P., Glover D.M., Ohkura H. Mini spindles: a gene encoding a conserved microtubule-associated protein required for the integrity of the mitotic spindle in Drosophila. J. Cell Biol. 1999, 146:1005-1018.
    • (1999) J. Cell Biol. , vol.146 , pp. 1005-1018
    • Cullen, C.F.1    Deak, P.2    Glover, D.M.3    Ohkura, H.4
  • 81
    • 33644747344 scopus 로고    scopus 로고
    • A microtubule-binding domain in dynactin increases dynein processivity by skating along microtubules
    • Culver-Hanlon T.L., Lex S.A., Stephens A.D., Quintyne N.J., King S.J. A microtubule-binding domain in dynactin increases dynein processivity by skating along microtubules. Nat. Cell Biol. 2006, 8:264-270.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 264-270
    • Culver-Hanlon, T.L.1    Lex, S.A.2    Stephens, A.D.3    Quintyne, N.J.4    King, S.J.5
  • 82
    • 33749159663 scopus 로고    scopus 로고
    • Self-organization of microtubule bundles in anucleate fission yeast cells
    • Daga R.R., Lee K.G., Bratman S., Salas-Pino S., Chang F. Self-organization of microtubule bundles in anucleate fission yeast cells. Nat. Cell Biol. 2006, 8:1108-1113.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1108-1113
    • Daga, R.R.1    Lee, K.G.2    Bratman, S.3    Salas-Pino, S.4    Chang, F.5
  • 83
    • 33746528109 scopus 로고    scopus 로고
    • Asymmetric microtubule pushing forces in nuclear centering
    • Daga R.R., Yonetani A., Chang F. Asymmetric microtubule pushing forces in nuclear centering. Curr. Biol. 2006, 16:1544-1550.
    • (2006) Curr. Biol. , vol.16 , pp. 1544-1550
    • Daga, R.R.1    Yonetani, A.2    Chang, F.3
  • 86
    • 0031459588 scopus 로고    scopus 로고
    • CLIP-115, a novel brain-specific cytoplasmic linker protein, mediates the localization of dendritic lamellar bodies
    • De Zeeuw C.I., Hoogenraad C.C., Goedknegt E., Hertzberg E., Neubauer A., Grosveld F., et al. CLIP-115, a novel brain-specific cytoplasmic linker protein, mediates the localization of dendritic lamellar bodies. Neuron 1997, 19:1187-1199.
    • (1997) Neuron , vol.19 , pp. 1187-1199
    • De Zeeuw, C.I.1    Hoogenraad, C.C.2    Goedknegt, E.3    Hertzberg, E.4    Neubauer, A.5    Grosveld, F.6
  • 87
    • 19744382953 scopus 로고    scopus 로고
    • The MAP2/Tau family of microtubule-associated proteins
    • Dehmelt L., Halpain S. The MAP2/Tau family of microtubule-associated proteins. Genome Biol. 2005, 6:204.
    • (2005) Genome Biol. , vol.6 , pp. 204
    • Dehmelt, L.1    Halpain, S.2
  • 90
    • 0033534575 scopus 로고    scopus 로고
    • Kin I kinesins are microtubule-destabilizing enzymes
    • Desai A., Verma S., Mitchison T.J., Walczak C.E. Kin I kinesins are microtubule-destabilizing enzymes. Cell 1999, 96:69-78.
    • (1999) Cell , vol.96 , pp. 69-78
    • Desai, A.1    Verma, S.2    Mitchison, T.J.3    Walczak, C.E.4
  • 91
    • 0742322966 scopus 로고    scopus 로고
    • P130Cas-associated protein (p140Cap) as a new tyrosine-phosphorylated protein involved in cell spreading
    • Di Stefano P., Cabodi S., Boeri Erba E., Margaria V., Bergatto E., Giuffrida M.G., et al. P130Cas-associated protein (p140Cap) as a new tyrosine-phosphorylated protein involved in cell spreading. Mol. Biol. Cell 2004, 15:787-800.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 787-800
    • Di Stefano, P.1    Cabodi, S.2    Boeri Erba, E.3    Margaria, V.4    Bergatto, E.5    Giuffrida, M.G.6
  • 92
    • 34250902995 scopus 로고    scopus 로고
    • P140Cap protein suppresses tumour cell properties, regulating Csk and Src kinase activity
    • Di Stefano P., Damiano L., Cabodi S., Aramu S., Tordella L., Praduroux A., et al. p140Cap protein suppresses tumour cell properties, regulating Csk and Src kinase activity. EMBO J. 2007, 26:2843-2855.
    • (2007) EMBO J. , vol.26 , pp. 2843-2855
    • Di Stefano, P.1    Damiano, L.2    Cabodi, S.3    Aramu, S.4    Tordella, L.5    Praduroux, A.6
  • 93
    • 57149102485 scopus 로고    scopus 로고
    • Detection of GTP-tubulin conformation in vivo reveals a role for GTP remnants in microtubule rescues
    • Dimitrov A., Quesnoit M., Moutel S., Cantaloube I., Pous C., Perez F. Detection of GTP-tubulin conformation in vivo reveals a role for GTP remnants in microtubule rescues. Science 2008, 322:1353-1356.
    • (2008) Science , vol.322 , pp. 1353-1356
    • Dimitrov, A.1    Quesnoit, M.2    Moutel, S.3    Cantaloube, I.4    Pous, C.5    Perez, F.6
  • 94
    • 0034697150 scopus 로고    scopus 로고
    • Ch-TOGp is required for microtubule aster formation in a mammalian mitotic extract
    • Dionne M.A., Sanchez A., Compton D.A. ch-TOGp is required for microtubule aster formation in a mammalian mitotic extract. J. Biol. Chem. 2000, 275:12346-12352.
    • (2000) J. Biol. Chem. , vol.275 , pp. 12346-12352
    • Dionne, M.A.1    Sanchez, A.2    Compton, D.A.3
  • 95
    • 57749110732 scopus 로고    scopus 로고
    • Regulation of dynactin through the differential expression of p150Glued isoforms
    • Dixit R., Levy J.R., Tokito M., Ligon L.A., Holzbaur E.L. Regulation of dynactin through the differential expression of p150Glued isoforms. J. Biol. Chem. 2008, 283:33611-33619.
    • (2008) J. Biol. Chem. , vol.283 , pp. 33611-33619
    • Dixit, R.1    Levy, J.R.2    Tokito, M.3    Ligon, L.A.4    Holzbaur, E.L.5
  • 97
    • 0027486966 scopus 로고
    • Lissencephaly. A human brain malformation associated with deletion of the LIS1 gene located at chromosome 17p13
    • Dobyns W.B., Reiner O., Carrozzo R., Ledbetter D.H. Lissencephaly. A human brain malformation associated with deletion of the LIS1 gene located at chromosome 17p13. JAMA 1993, 270:2838-2842.
    • (1993) JAMA , vol.270 , pp. 2838-2842
    • Dobyns, W.B.1    Reiner, O.2    Carrozzo, R.3    Ledbetter, D.H.4
  • 98
    • 0034518173 scopus 로고    scopus 로고
    • Structural basis for the interaction of tubulin with proteins and drugs that affect microtubule dynamics
    • Downing K.H. Structural basis for the interaction of tubulin with proteins and drugs that affect microtubule dynamics. Annu. Rev. Cell Dev. Biol. 2000, 16:89-111.
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 89-111
    • Downing, K.H.1
  • 99
  • 101
    • 0028675012 scopus 로고
    • The minimum GTP cap required to stabilize microtubules
    • Drechsel D.N., Kirschner M.W. The minimum GTP cap required to stabilize microtubules. Curr. Biol. 1994, 4:1053-1061.
    • (1994) Curr. Biol. , vol.4 , pp. 1053-1061
    • Drechsel, D.N.1    Kirschner, M.W.2
  • 105
    • 24944547584 scopus 로고    scopus 로고
    • Distinct mechanisms govern the localisation of Drosophila CLIP-190 to unattached kinetochores and microtubule plus-ends
    • Dzhindzhev N.S., Rogers S.L., Vale R.D., Ohkura H. Distinct mechanisms govern the localisation of Drosophila CLIP-190 to unattached kinetochores and microtubule plus-ends. J. Cell Sci. 2005, 118:3781-3790.
    • (2005) J. Cell Sci. , vol.118 , pp. 3781-3790
    • Dzhindzhev, N.S.1    Rogers, S.L.2    Vale, R.D.3    Ohkura, H.4
  • 106
    • 33745381601 scopus 로고    scopus 로고
    • CLIP-170 homologue and NUDE play overlapping roles in NUDF localization in Aspergillus nidulans
    • Efimov V.P., Zhang J., Xiang X. CLIP-170 homologue and NUDE play overlapping roles in NUDF localization in Aspergillus nidulans. Mol. Biol. Cell 2006, 17:2021-2034.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2021-2034
    • Efimov, V.P.1    Zhang, J.2    Xiang, X.3
  • 107
    • 34249305474 scopus 로고    scopus 로고
    • Asymmetric CLASP-dependent nucleation of noncentrosomal microtubules at the trans-Golgi network
    • Efimov A., Kharitonov A., Efimova N., Loncarek J., Miller P.M., Andreyeva N., et al. Asymmetric CLASP-dependent nucleation of noncentrosomal microtubules at the trans-Golgi network. Dev. Cell 2007, 12:917-930.
    • (2007) Dev. Cell , vol.12 , pp. 917-930
    • Efimov, A.1    Kharitonov, A.2    Efimova, N.3    Loncarek, J.4    Miller, P.M.5    Andreyeva, N.6
  • 108
    • 12844284470 scopus 로고    scopus 로고
    • EB1 is essential during Drosophila development and plays a crucial role in the integrity of chordotonal mechanosensory organs
    • Elliott S.L., Cullen C.F., Wrobel N., Kernan M.J., Ohkura H. EB1 is essential during Drosophila development and plays a crucial role in the integrity of chordotonal mechanosensory organs. Mol. Biol. Cell 2005, 16:891-901.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 891-901
    • Elliott, S.L.1    Cullen, C.F.2    Wrobel, N.3    Kernan, M.J.4    Ohkura, H.5
  • 109
    • 77949489741 scopus 로고    scopus 로고
    • Kinesin-13s in mitosis: key players in the spatial and temporal organization of spindle microtubules
    • Ems-McClung S.C., Walczak C.E. Kinesin-13s in mitosis: key players in the spatial and temporal organization of spindle microtubules. Semin. Cell Dev. Biol. 2010, 21:276-282.
    • (2010) Semin. Cell Dev. Biol. , vol.21 , pp. 276-282
    • Ems-McClung, S.C.1    Walczak, C.E.2
  • 110
    • 33846090626 scopus 로고    scopus 로고
    • The interplay of the N- and C-terminal domains of MCAK control microtubule depolymerization activity and spindle assembly
    • Ems-McClung S.C., Hertzer K.M., Zhang X., Miller M.W., Walczak C.E. The interplay of the N- and C-terminal domains of MCAK control microtubule depolymerization activity and spindle assembly. Mol. Biol. Cell 2007, 18:282-294.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 282-294
    • Ems-McClung, S.C.1    Hertzer, K.M.2    Zhang, X.3    Miller, M.W.4    Walczak, C.E.5
  • 112
    • 0016373254 scopus 로고
    • Assembly of microtubules from preformed, ring-shaped protofilaments and 6-S tubulin
    • Erickson H.P. Assembly of microtubules from preformed, ring-shaped protofilaments and 6-S tubulin. J. Supramol. Struct. 1974, 2:393-411.
    • (1974) J. Supramol. Struct. , vol.2 , pp. 393-411
    • Erickson, H.P.1
  • 114
    • 75749155892 scopus 로고    scopus 로고
    • From signaling pathways to microtubule dynamics: the key players
    • Etienne-Manneville S. From signaling pathways to microtubule dynamics: the key players. Curr. Opin. Cell Biol. 2009, 22:104-111.
    • (2009) Curr. Opin. Cell Biol. , vol.22 , pp. 104-111
    • Etienne-Manneville, S.1
  • 115
    • 24944577909 scopus 로고    scopus 로고
    • Cdc42 and Par6-PKCzeta regulate the spatially localized association of Dlg1 and APC to control cell polarization
    • Etienne-Manneville S., Manneville J.B., Nicholls S., Ferenczi M.A., Hall A. Cdc42 and Par6-PKCzeta regulate the spatially localized association of Dlg1 and APC to control cell polarization. J. Cell Biol. 2005, 170:895-901.
    • (2005) J. Cell Biol. , vol.170 , pp. 895-901
    • Etienne-Manneville, S.1    Manneville, J.B.2    Nicholls, S.3    Ferenczi, M.A.4    Hall, A.5
  • 118
    • 27644563566 scopus 로고    scopus 로고
    • Interactions between CLIP-170, tubulin, and microtubules: implications for the mechanism of Clip-170 plus-end tracking behavior
    • Folker E.S., Baker B.M., Goodson H.V. Interactions between CLIP-170, tubulin, and microtubules: implications for the mechanism of Clip-170 plus-end tracking behavior. Mol. Biol. Cell 2005, 16:5373-5384.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5373-5384
    • Folker, E.S.1    Baker, B.M.2    Goodson, H.V.3
  • 119
    • 69949104631 scopus 로고    scopus 로고
    • Interaction of CDK5RAP2 with EB1 to track growing microtubule tips and to regulate microtubule dynamics
    • Fong K.W., Hau S.Y., Kho Y.S., Jia Y., He L., Qi R.Z. Interaction of CDK5RAP2 with EB1 to track growing microtubule tips and to regulate microtubule dynamics. Mol. Biol. Cell 2009, 20:3660-3670.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 3660-3670
    • Fong, K.W.1    Hau, S.Y.2    Kho, Y.S.3    Jia, Y.4    He, L.5    Qi, R.Z.6
  • 120
    • 1642343784 scopus 로고    scopus 로고
    • Phylogenetic analysis of AAA proteins
    • Frickey T., Lupas A.N. Phylogenetic analysis of AAA proteins. J. Struct. Biol. 2004, 146:2-10.
    • (2004) J. Struct. Biol. , vol.146 , pp. 2-10
    • Frickey, T.1    Lupas, A.N.2
  • 121
    • 18444369936 scopus 로고    scopus 로고
    • Rac1 and Cdc42 capture microtubules through IQGAP1 and CLIP-170
    • Fukata M., Watanabe T., Noritake J., Nakagawa M., Yamaga M., Kuroda S., et al. Rac1 and Cdc42 capture microtubules through IQGAP1 and CLIP-170. Cell 2002, 109:873-885.
    • (2002) Cell , vol.109 , pp. 873-885
    • Fukata, M.1    Watanabe, T.2    Noritake, J.3    Nakagawa, M.4    Yamaga, M.5    Kuroda, S.6
  • 122
    • 17044383478 scopus 로고    scopus 로고
    • Versatile role of Rab27 in membrane trafficking: focus on the Rab27 effector families
    • Fukuda M. Versatile role of Rab27 in membrane trafficking: focus on the Rab27 effector families. J. Biochem. 2005, 137:9-16.
    • (2005) J. Biochem. , vol.137 , pp. 9-16
    • Fukuda, M.1
  • 123
    • 0023589342 scopus 로고
    • A microtubule-associated protein from Xenopus eggs that specifically promotes assembly at the plus-end
    • Gard D.L., Kirschner M.W. A microtubule-associated protein from Xenopus eggs that specifically promotes assembly at the plus-end. J. Cell Biol. 1987, 105:2203-2215.
    • (1987) J. Cell Biol. , vol.105 , pp. 2203-2215
    • Gard, D.L.1    Kirschner, M.W.2
  • 124
    • 5344234425 scopus 로고    scopus 로고
    • MAPping the eukaryotic tree of life: structure, function, and evolution of the MAP215/Dis1 family of microtubule-associated proteins
    • Gard D.L., Becker B.E., Josh Romney S. MAPping the eukaryotic tree of life: structure, function, and evolution of the MAP215/Dis1 family of microtubule-associated proteins. Int. Rev. Cytol. 2004, 239:179-272.
    • (2004) Int. Rev. Cytol. , vol.239 , pp. 179-272
    • Gard, D.L.1    Becker, B.E.2    Josh Romney, S.3
  • 125
    • 0141988361 scopus 로고    scopus 로고
    • Putative microtubule-associated proteins from the Arabidopsis genome
    • Gardiner J., Marc J. Putative microtubule-associated proteins from the Arabidopsis genome. Protoplasma 2003, 222:61-74.
    • (2003) Protoplasma , vol.222 , pp. 61-74
    • Gardiner, J.1    Marc, J.2
  • 126
    • 38349047839 scopus 로고    scopus 로고
    • The microtubule-based motor Kar3 and plus end-binding protein Bim1 provide structural support for the anaphase spindle
    • Gardner M.K., Haase J., Mythreye K., Molk J.N., Anderson M., Joglekar A.P., et al. The microtubule-based motor Kar3 and plus end-binding protein Bim1 provide structural support for the anaphase spindle. J. Cell Biol. 2008, 180:91-100.
    • (2008) J. Cell Biol. , vol.180 , pp. 91-100
    • Gardner, M.K.1    Haase, J.2    Mythreye, K.3    Molk, J.N.4    Anderson, M.5    Joglekar, A.P.6
  • 128
    • 46049112667 scopus 로고    scopus 로고
    • Kinesin-8 molecular motors: putting the brakes on chromosome oscillations
    • Gardner M.K., Odde D.J., Bloom K. Kinesin-8 molecular motors: putting the brakes on chromosome oscillations. Trends Cell Biol. 2008, 18:307-310.
    • (2008) Trends Cell Biol. , vol.18 , pp. 307-310
    • Gardner, M.K.1    Odde, D.J.2    Bloom, K.3
  • 129
    • 0037314330 scopus 로고    scopus 로고
    • The ch-TOG/XMAP215 protein is essential for spindle pole organization in human somatic cells
    • Gergely F., Draviam V.M., Raff J.W. The ch-TOG/XMAP215 protein is essential for spindle pole organization in human somatic cells. Genes Dev. 2003, 17:336-341.
    • (2003) Genes Dev. , vol.17 , pp. 336-341
    • Gergely, F.1    Draviam, V.M.2    Raff, J.W.3
  • 131
    • 77956292561 scopus 로고    scopus 로고
    • Tip1/CLIP-170 protein is required for correct chromosome poleward movement in fission yeast
    • Goldstone S., Reyes C., Gay G., Courtheoux T., Dubarry M., Tournier S., et al. Tip1/CLIP-170 protein is required for correct chromosome poleward movement in fission yeast. PLoS ONE 2010, 5:e10634.
    • (2010) PLoS ONE , vol.5
    • Goldstone, S.1    Reyes, C.2    Gay, G.3    Courtheoux, T.4    Dubarry, M.5    Tournier, S.6
  • 132
    • 0034676448 scopus 로고    scopus 로고
    • Functional genomic analysis of cell division in C. elegans using RNAi of genes on chromosome III
    • Gonczy P., Echeverri C., Oegema K., Coulson A., Jones S.J., Copley R.R., et al. Functional genomic analysis of cell division in C. elegans using RNAi of genes on chromosome III. Nature 2000, 408:331-336.
    • (2000) Nature , vol.408 , pp. 331-336
    • Gonczy, P.1    Echeverri, C.2    Oegema, K.3    Coulson, A.4    Jones, S.J.5    Copley, R.R.6
  • 133
    • 27544447708 scopus 로고    scopus 로고
    • Mechanisms for focusing mitotic spindle poles by minus end-directed motor proteins
    • Goshima G., Nedelec F., Vale R.D. Mechanisms for focusing mitotic spindle poles by minus end-directed motor proteins. J. Cell Biol. 2005, 171:229-240.
    • (2005) J. Cell Biol. , vol.171 , pp. 229-240
    • Goshima, G.1    Nedelec, F.2    Vale, R.D.3
  • 134
    • 0343092090 scopus 로고    scopus 로고
    • Dictyostelium DdCP224 is a microtubule-associated protein and a permanent centrosomal resident involved in centrosome duplication
    • Graf R., Daunderer C., Schliwa M. Dictyostelium DdCP224 is a microtubule-associated protein and a permanent centrosomal resident involved in centrosome duplication. J. Cell Sci. 2000, 113(Pt 10):1747-1758.
    • (2000) J. Cell Sci. , vol.113 , Issue.PART 10 , pp. 1747-1758
    • Graf, R.1    Daunderer, C.2    Schliwa, M.3
  • 135
    • 33748259773 scopus 로고    scopus 로고
    • S. pombe CLASP needs dynein, not EB1 or CLIP170, to induce microtubule instability and slows polymerization rates at cell tips in a dynein-dependent manner
    • Grallert A., Beuter C., Craven R.A., Bagley S., Wilks D., Fleig U., et al. S. pombe CLASP needs dynein, not EB1 or CLIP170, to induce microtubule instability and slows polymerization rates at cell tips in a dynein-dependent manner. Genes Dev. 2006, 20:2421-2436.
    • (2006) Genes Dev. , vol.20 , pp. 2421-2436
    • Grallert, A.1    Beuter, C.2    Craven, R.A.3    Bagley, S.4    Wilks, D.5    Fleig, U.6
  • 136
    • 26244463198 scopus 로고    scopus 로고
    • APC and EB1 function together in mitosis to regulate spindle dynamics and chromosome alignment
    • Green R.A., Wollman R., Kaplan K.B. APC and EB1 function together in mitosis to regulate spindle dynamics and chromosome alignment. Mol. Biol. Cell 2005, 16:4609-4622.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4609-4622
    • Green, R.A.1    Wollman, R.2    Kaplan, K.B.3
  • 138
    • 0032509775 scopus 로고    scopus 로고
    • Cloning and expression of chicken CLIP-170 and restin isoforms
    • Griparic L., Volosky J.M., Keller T.C. Cloning and expression of chicken CLIP-170 and restin isoforms. Gene 1998, 206:195-208.
    • (1998) Gene , vol.206 , pp. 195-208
    • Griparic, L.1    Volosky, J.M.2    Keller, T.C.3
  • 142
    • 0031965218 scopus 로고    scopus 로고
    • DRhoGEF2 encodes a member of the Dbl family of oncogenes and controls cell shape changes during gastrulation in Drosophila
    • Hacker U., Perrimon N. DRhoGEF2 encodes a member of the Dbl family of oncogenes and controls cell shape changes during gastrulation in Drosophila. Genes Dev. 1998, 12:274-284.
    • (1998) Genes Dev. , vol.12 , pp. 274-284
    • Hacker, U.1    Perrimon, N.2
  • 143
  • 144
    • 0035336825 scopus 로고    scopus 로고
    • The Aspergillus cytoplasmic dynein heavy chain and NUDF localize to microtubule ends and affect microtubule dynamics
    • Han G., Liu B., Zhang J., Zuo W., Morris N.R., Xiang X. The Aspergillus cytoplasmic dynein heavy chain and NUDF localize to microtubule ends and affect microtubule dynamics. Curr. Biol. 2001, 11:719-724.
    • (2001) Curr. Biol. , vol.11 , pp. 719-724
    • Han, G.1    Liu, B.2    Zhang, J.3    Zuo, W.4    Morris, N.R.5    Xiang, X.6
  • 145
    • 29944445541 scopus 로고    scopus 로고
    • Xorbit/CLASP links dynamic microtubules to chromosomes in the Xenopus meiotic spindle
    • Hannak E., Heald R. Xorbit/CLASP links dynamic microtubules to chromosomes in the Xenopus meiotic spindle. J. Cell Biol. 2006, 172:19-25.
    • (2006) J. Cell Biol. , vol.172 , pp. 19-25
    • Hannak, E.1    Heald, R.2
  • 146
    • 27144552677 scopus 로고    scopus 로고
    • Non-traditional roles for the Adenomatous Polyposis Coli (APC) tumor suppressor protein
    • Hanson C.A., Miller J.R. Non-traditional roles for the Adenomatous Polyposis Coli (APC) tumor suppressor protein. Gene 2005, 361:1-12.
    • (2005) Gene , vol.361 , pp. 1-12
    • Hanson, C.A.1    Miller, J.R.2
  • 147
    • 0141480958 scopus 로고    scopus 로고
    • Crystal structure of the amino-terminal microtubule-binding domain of end-binding protein 1 (EB1)
    • Hayashi I., Ikura M. Crystal structure of the amino-terminal microtubule-binding domain of end-binding protein 1 (EB1). J. Biol. Chem. 2003, 278:36430-36434.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36430-36434
    • Hayashi, I.1    Ikura, M.2
  • 148
    • 23744433896 scopus 로고    scopus 로고
    • Structural basis for the activation of microtubule assembly by the EB1 and p150Glued complex
    • Hayashi I., Wilde A., Mal T.K., Ikura M. Structural basis for the activation of microtubule assembly by the EB1 and p150Glued complex. Mol. Cell 2005, 19:449-460.
    • (2005) Mol. Cell , vol.19 , pp. 449-460
    • Hayashi, I.1    Wilde, A.2    Mal, T.K.3    Ikura, M.4
  • 149
    • 34948902333 scopus 로고    scopus 로고
    • CLIP170 autoinhibition mimics intermolecular interactions with p150Glued or EB1
    • Hayashi I., Plevin M.J., Ikura M. CLIP170 autoinhibition mimics intermolecular interactions with p150Glued or EB1. Nat. Struct. Mol. Biol. 2007, 14:980-981.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 980-981
    • Hayashi, I.1    Plevin, M.J.2    Ikura, M.3
  • 150
    • 33646950699 scopus 로고    scopus 로고
    • The depolymerizing kinesin MCAK uses lattice diffusion to rapidly target microtubule ends
    • Helenius J., Brouhard G., Kalaidzidis Y., Diez S., Howard J. The depolymerizing kinesin MCAK uses lattice diffusion to rapidly target microtubule ends. Nature 2006, 441:115-119.
    • (2006) Nature , vol.441 , pp. 115-119
    • Helenius, J.1    Brouhard, G.2    Kalaidzidis, Y.3    Diez, S.4    Howard, J.5
  • 152
    • 70349437416 scopus 로고    scopus 로고
    • Kinesin superfamily motor proteins and intracellular transport
    • Hirokawa N., Noda Y., Tanaka Y., Niwa S. Kinesin superfamily motor proteins and intracellular transport. Nat. Rev. Mol. Cell Biol. 2009, 10:682-696.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 682-696
    • Hirokawa, N.1    Noda, Y.2    Tanaka, Y.3    Niwa, S.4
  • 153
    • 1442338341 scopus 로고    scopus 로고
    • Differential functional interplay of TOGp/XMAP215 and the KinI kinesin MCAK during interphase and mitosis
    • Holmfeldt P., Stenmark S., Gullberg M. Differential functional interplay of TOGp/XMAP215 and the KinI kinesin MCAK during interphase and mitosis. EMBO J. 2004, 23:627-637.
    • (2004) EMBO J. , vol.23 , pp. 627-637
    • Holmfeldt, P.1    Stenmark, S.2    Gullberg, M.3
  • 154
    • 70350492009 scopus 로고    scopus 로고
    • Predominant regulators of tubulin monomer-polymer partitioning and their implication for cell polarization
    • Holmfeldt P., Sellin M.E., Gullberg M. Predominant regulators of tubulin monomer-polymer partitioning and their implication for cell polarization. Cell. Mol. Life Sci. 2009, 66:3263-3276.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 3263-3276
    • Holmfeldt, P.1    Sellin, M.E.2    Gullberg, M.3
  • 155
    • 0028241003 scopus 로고
    • Dynamic instability of microtubules as an efficient way to search in space
    • Holy T.E., Leibler S. Dynamic instability of microtubules as an efficient way to search in space. Proc. Natl Acad. Sci. USA 1994, 91:5682-5685.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5682-5685
    • Holy, T.E.1    Leibler, S.2
  • 156
  • 160
    • 33847185152 scopus 로고    scopus 로고
    • Organization of interphase microtubules in fission yeast analyzed by electron tomography
    • Hoog J.L., Schwartz C., Noon A.T., O'Toole E.T., Mastronarde D.N., McIntosh J.R., et al. Organization of interphase microtubules in fission yeast analyzed by electron tomography. Dev. Cell 2007, 12:349-361.
    • (2007) Dev. Cell , vol.12 , pp. 349-361
    • Hoog, J.L.1    Schwartz, C.2    Noon, A.T.3    O'Toole, E.T.4    Mastronarde, D.N.5    McIntosh, J.R.6
  • 162
    • 0036724985 scopus 로고    scopus 로고
    • Targeted mutation of Cyln2 in the Williams syndrome critical region links CLIP-115 haploinsufficiency to neurodevelopmental abnormalities in mice
    • Hoogenraad C.C., Koekkoek B., Akhmanova A., Krugers H., Dortland B., Miedema M., et al. Targeted mutation of Cyln2 in the Williams syndrome critical region links CLIP-115 haploinsufficiency to neurodevelopmental abnormalities in mice. Nat. Genet. 2002, 32:116-127.
    • (2002) Nat. Genet. , vol.32 , pp. 116-127
    • Hoogenraad, C.C.1    Koekkoek, B.2    Akhmanova, A.3    Krugers, H.4    Dortland, B.5    Miedema, M.6
  • 163
    • 33751534800 scopus 로고    scopus 로고
    • The dynein family at a glance
    • Hook P., Vallee R.B. The dynein family at a glance. J. Cell Sci. 2006, 119:4369-4371.
    • (2006) J. Cell Sci. , vol.119 , pp. 4369-4371
    • Hook, P.1    Vallee, R.B.2
  • 164
    • 0022492523 scopus 로고
    • Visualization of the dynamic instability of individual microtubules by dark-field microscopy
    • Horio T., Hotani H. Visualization of the dynamic instability of individual microtubules by dark-field microscopy. Nature 1986, 321:605-607.
    • (1986) Nature , vol.321 , pp. 605-607
    • Horio, T.1    Hotani, H.2
  • 165
    • 0023688553 scopus 로고
    • Dynamics of microtubules visualized by darkfield microscopy: treadmilling and dynamic instability
    • Hotani H., Horio T. Dynamics of microtubules visualized by darkfield microscopy: treadmilling and dynamic instability. Cell Motil. Cytoskeleton 1988, 10:229-236.
    • (1988) Cell Motil. Cytoskeleton , vol.10 , pp. 229-236
    • Hotani, H.1    Horio, T.2
  • 166
    • 77953146816 scopus 로고    scopus 로고
    • Laminin-based cell adhesion anchors microtubule plus ends to the epithelial cell basal cortex through LL5alpha/beta
    • Hotta A., Kawakatsu T., Nakatani T., Sato T., Matsui C., Sukezane T., et al. Laminin-based cell adhesion anchors microtubule plus ends to the epithelial cell basal cortex through LL5alpha/beta. J. Cell Biol. 2010, 189:901-917.
    • (2010) J. Cell Biol. , vol.189 , pp. 901-917
    • Hotta, A.1    Kawakatsu, T.2    Nakatani, T.3    Sato, T.4    Matsui, C.5    Sukezane, T.6
  • 167
    • 33846429185 scopus 로고    scopus 로고
    • Microtubule polymerases and depolymerases
    • Howard J., Hyman A.A. Microtubule polymerases and depolymerases. Curr. Opin. Cell Biol. 2007, 19:31-35.
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 31-35
    • Howard, J.1    Hyman, A.A.2
  • 168
    • 68049084655 scopus 로고    scopus 로고
    • Growth, fluctuation and switching at microtubule plus ends
    • Howard J., Hyman A.A. Growth, fluctuation and switching at microtubule plus ends. Nat. Rev. Mol. Cell Biol. 2009, 10:569-574.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 569-574
    • Howard, J.1    Hyman, A.A.2
  • 169
    • 14644399180 scopus 로고    scopus 로고
    • Cortical capture of microtubules and spindle polarity in budding yeast-where's the catch?
    • Huisman S.M., Segal M. Cortical capture of microtubules and spindle polarity in budding yeast-where's the catch?. J. Cell Sci. 2005, 118:463-471.
    • (2005) J. Cell Sci. , vol.118 , pp. 463-471
    • Huisman, S.M.1    Segal, M.2
  • 170
    • 34948826453 scopus 로고    scopus 로고
    • Rab27a and MyoVa are the primary Mlph interactors regulating melanosome transport in melanocytes
    • Hume A.N., Ushakov D.S., Tarafder A.K., Ferenczi M.A., Seabra M.C. Rab27a and MyoVa are the primary Mlph interactors regulating melanosome transport in melanocytes. J. Cell Sci. 2007, 120:3111-3122.
    • (2007) J. Cell Sci. , vol.120 , pp. 3111-3122
    • Hume, A.N.1    Ushakov, D.S.2    Tarafder, A.K.3    Ferenczi, M.A.4    Seabra, M.C.5
  • 171
    • 0034502831 scopus 로고    scopus 로고
    • How motor proteins influence microtubule polymerization dynamics
    • Hunter A.W., Wordeman L. How motor proteins influence microtubule polymerization dynamics. J. Cell Sci. 2000, 113(Pt 24):4379-4389.
    • (2000) J. Cell Sci. , vol.113 , Issue.PART 24 , pp. 4379-4389
    • Hunter, A.W.1    Wordeman, L.2
  • 172
    • 0037292454 scopus 로고    scopus 로고
    • The kinesin-related protein MCAK is a microtubule depolymerase that forms an ATP-hydrolyzing complex at microtubule ends
    • Hunter A.W., Caplow M., Coy D.L., Hancock W.O., Diez S., Wordeman L., et al. The kinesin-related protein MCAK is a microtubule depolymerase that forms an ATP-hydrolyzing complex at microtubule ends. Mol. Cell 2003, 11:445-457.
    • (2003) Mol. Cell , vol.11 , pp. 445-457
    • Hunter, A.W.1    Caplow, M.2    Coy, D.L.3    Hancock, W.O.4    Diez, S.5    Wordeman, L.6
  • 173
    • 34247597863 scopus 로고    scopus 로고
    • Metastability of microtubules induced by competing internal forces
    • Hunyadi V., Janosi I.M. Metastability of microtubules induced by competing internal forces. Biophys. J. 2007, 92:3092-3097.
    • (2007) Biophys. J. , vol.92 , pp. 3092-3097
    • Hunyadi, V.1    Janosi, I.M.2
  • 174
    • 0027075124 scopus 로고
    • Role of GTP hydrolysis in microtubule dynamics: information from a slowly hydrolyzable analogue, GMPCPP
    • Hyman A.A., Salser S., Drechsel D.N., Unwin N., Mitchison T.J. Role of GTP hydrolysis in microtubule dynamics: information from a slowly hydrolyzable analogue, GMPCPP. Mol. Biol. Cell 1992, 3:1155-1167.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1155-1167
    • Hyman, A.A.1    Salser, S.2    Drechsel, D.N.3    Unwin, N.4    Mitchison, T.J.5
  • 175
    • 0342657750 scopus 로고    scopus 로고
    • Orbit, a novel microtubule-associated protein essential for mitosis in Drosophila melanogaster
    • Inoue Y.H., do Carmo Avides M., Shiraki M., Deak P., Yamaguchi M., Nishimoto Y., et al. Orbit, a novel microtubule-associated protein essential for mitosis in Drosophila melanogaster. J. Cell Biol. 2000, 149:153-166.
    • (2000) J. Cell Biol. , vol.149 , pp. 153-166
    • Inoue, Y.H.1    do Carmo Avides, M.2    Shiraki, M.3    Deak, P.4    Yamaguchi, M.5    Nishimoto, Y.6
  • 176
    • 3142773392 scopus 로고    scopus 로고
    • Mutations in orbit/mast reveal that the central spindle is comprised of two microtubule populations, those that initiate cleavage and those that propagate furrow ingression
    • Inoue Y.H., Savoian M.S., Suzuki T., Mathe E., Yamamoto M.T., Glover D.M. Mutations in orbit/mast reveal that the central spindle is comprised of two microtubule populations, those that initiate cleavage and those that propagate furrow ingression. J. Cell Biol. 2004, 166:49-60.
    • (2004) J. Cell Biol. , vol.166 , pp. 49-60
    • Inoue, Y.H.1    Savoian, M.S.2    Suzuki, T.3    Mathe, E.4    Yamamoto, M.T.5    Glover, D.M.6
  • 177
    • 51849113284 scopus 로고    scopus 로고
    • Characterization of a multidomain adaptor protein, p140Cap, as part of a pre-synaptic complex
    • Ito H., Atsuzawa K., Sudo K., Di Stefano P., Iwamoto I., Morishita R., et al. Characterization of a multidomain adaptor protein, p140Cap, as part of a pre-synaptic complex. J. Neurochem. 2008, 107:61-72.
    • (2008) J. Neurochem. , vol.107 , pp. 61-72
    • Ito, H.1    Atsuzawa, K.2    Sudo, K.3    Di Stefano, P.4    Iwamoto, I.5    Morishita, R.6
  • 178
    • 0036708442 scopus 로고    scopus 로고
    • Structural microtubule cap: stability, catastrophe, rescue, and third state
    • Janosi I.M., Chretien D., Flyvbjerg H. Structural microtubule cap: stability, catastrophe, rescue, and third state. Biophys. J. 2002, 83:1317-1330.
    • (2002) Biophys. J. , vol.83 , pp. 1317-1330
    • Janosi, I.M.1    Chretien, D.2    Flyvbjerg, H.3
  • 179
    • 33846280179 scopus 로고    scopus 로고
    • Crosslinkers and motors organize dynamic microtubules to form stable bipolar arrays in fission yeast
    • Janson M.E., Loughlin R., Loiodice I., Fu C., Brunner D., Nedelec F.J., et al. Crosslinkers and motors organize dynamic microtubules to form stable bipolar arrays in fission yeast. Cell 2007, 128:357-368.
    • (2007) Cell , vol.128 , pp. 357-368
    • Janson, M.E.1    Loughlin, R.2    Loiodice, I.3    Fu, C.4    Brunner, D.5    Nedelec, F.J.6
  • 181
    • 33744919546 scopus 로고    scopus 로고
    • Regulation of microtubule-dependent protein transport by the TSC2/mammalian target of rapamycin pathway
    • Jiang X., Yeung R.S. Regulation of microtubule-dependent protein transport by the TSC2/mammalian target of rapamycin pathway. Cancer Res. 2006, 66:5258-5269.
    • (2006) Cancer Res. , vol.66 , pp. 5258-5269
    • Jiang, X.1    Yeung, R.S.2
  • 182
    • 68249110721 scopus 로고    scopus 로고
    • TIP150 interacts with and targets MCAK at the microtubule plus ends
    • Jiang K., Wang J., Liu J., Ward T., Wordeman L., Davidson A., et al. TIP150 interacts with and targets MCAK at the microtubule plus ends. EMBO Rep. 2009, 10:857-865.
    • (2009) EMBO Rep. , vol.10 , pp. 857-865
    • Jiang, K.1    Wang, J.2    Liu, J.3    Ward, T.4    Wordeman, L.5    Davidson, A.6
  • 183
    • 0036226855 scopus 로고    scopus 로고
    • Identification of a link between the tumour suppressor APC and the kinesin superfamily
    • Jimbo T., Kawasaki Y., Koyama R., Sato R., Takada S., Haraguchi K., et al. Identification of a link between the tumour suppressor APC and the kinesin superfamily. Nat. Cell Biol. 2002, 4:323-327.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 323-327
    • Jimbo, T.1    Kawasaki, Y.2    Koyama, R.3    Sato, R.4    Takada, S.5    Haraguchi, K.6
  • 184
    • 75749117934 scopus 로고    scopus 로고
    • Mechanisms of force generation by end-on kinetochore-microtubule attachments
    • Joglekar A.P., Bloom K.S., Salmon E.D. Mechanisms of force generation by end-on kinetochore-microtubule attachments. Curr. Opin. Cell Biol. 2010, 22:57-67.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 57-67
    • Joglekar, A.P.1    Bloom, K.S.2    Salmon, E.D.3
  • 185
    • 0030783012 scopus 로고    scopus 로고
    • Stathmin: a tubulin-sequestering protein which forms a ternary T2S complex with two tubulin molecules
    • Jourdain L., Curmi P., Sobel A., Pantaloni D., Carlier M.F. Stathmin: a tubulin-sequestering protein which forms a ternary T2S complex with two tubulin molecules. Biochemistry 1997, 36:10817-10821.
    • (1997) Biochemistry , vol.36 , pp. 10817-10821
    • Jourdain, L.1    Curmi, P.2    Sobel, A.3    Pantaloni, D.4    Carlier, M.F.5
  • 186
    • 77955428666 scopus 로고    scopus 로고
    • Ubiquitylation regulates interactions of astral microtubules with the cleavage apparatus
    • Kammerer D., Stevermann L., Liakopoulos D. Ubiquitylation regulates interactions of astral microtubules with the cleavage apparatus. Curr. Biol. 2010, 20:1233-1243.
    • (2010) Curr. Biol. , vol.20 , pp. 1233-1243
    • Kammerer, D.1    Stevermann, L.2    Liakopoulos, D.3
  • 187
    • 70450228589 scopus 로고    scopus 로고
    • Regulators of the cytoplasmic dynein motor
    • Kardon J.R., Vale R.D. Regulators of the cytoplasmic dynein motor. Nat. Rev. Mol. Cell Biol. 2009, 10:854-865.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 854-865
    • Kardon, J.R.1    Vale, R.D.2
  • 188
    • 70350380999 scopus 로고    scopus 로고
    • Mal3 masks catastrophe events in Schizosaccharomyces pombe microtubules by inhibiting shrinkage and promoting rescue
    • Katsuki M., Drummond D.R., Osei M., Cross R.A. Mal3 masks catastrophe events in Schizosaccharomyces pombe microtubules by inhibiting shrinkage and promoting rescue. J. Biol. Chem. 2009, 284:29246-29250.
    • (2009) J. Biol. Chem. , vol.284 , pp. 29246-29250
    • Katsuki, M.1    Drummond, D.R.2    Osei, M.3    Cross, R.A.4
  • 189
    • 59249095575 scopus 로고    scopus 로고
    • MOR1, the Arabidopsis thaliana homologue of Xenopus MAP215, promotes rapid growth and shrinkage, and suppresses the pausing of microtubules in vivo
    • Kawamura E., Wasteneys G.O. MOR1, the Arabidopsis thaliana homologue of Xenopus MAP215, promotes rapid growth and shrinkage, and suppresses the pausing of microtubules in vivo. J. Cell Sci. 2008, 121:4114-4123.
    • (2008) J. Cell Sci. , vol.121 , pp. 4114-4123
    • Kawamura, E.1    Wasteneys, G.O.2
  • 191
    • 2942535001 scopus 로고    scopus 로고
    • The structure of the N-terminal domain of the product of the lissencephaly gene Lis1 and its functional implications
    • Kim M.H., Cooper D.R., Oleksy A., Devedjiev Y., Derewenda U., Reiner O., et al. The structure of the N-terminal domain of the product of the lissencephaly gene Lis1 and its functional implications. Structure 2004, 12:987-998.
    • (2004) Structure , vol.12 , pp. 987-998
    • Kim, M.H.1    Cooper, D.R.2    Oleksy, A.3    Devedjiev, Y.4    Derewenda, U.5    Reiner, O.6
  • 192
    • 33847343375 scopus 로고    scopus 로고
    • Microtubule binding by dynactin is required for microtubule organization but not cargo transport
    • Kim H., Ling S.C., Rogers G.C., Kural C., Selvin P.R., Rogers S.L., et al. Microtubule binding by dynactin is required for microtubule organization but not cargo transport. J. Cell Biol. 2007, 176:641-651.
    • (2007) J. Cell Biol. , vol.176 , pp. 641-651
    • Kim, H.1    Ling, S.C.2    Rogers, G.C.3    Kural, C.4    Selvin, P.R.5    Rogers, S.L.6
  • 193
    • 0033789351 scopus 로고    scopus 로고
    • Dynactin increases the processivity of the cytoplasmic dynein motor
    • King S.J., Schroer T.A. Dynactin increases the processivity of the cytoplasmic dynein motor. Nat. Cell Biol. 2000, 2:20-24.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 20-24
    • King, S.J.1    Schroer, T.A.2
  • 194
    • 0035834420 scopus 로고    scopus 로고
    • Reconstitution of physiological microtubule dynamics using purified components
    • Kinoshita K., Arnal I., Desai A., Drechsel D.N., Hyman A.A. Reconstitution of physiological microtubule dynamics using purified components. Science 2001, 294:1340-1343.
    • (2001) Science , vol.294 , pp. 1340-1343
    • Kinoshita, K.1    Arnal, I.2    Desai, A.3    Drechsel, D.N.4    Hyman, A.A.5
  • 195
    • 0036607995 scopus 로고    scopus 로고
    • XMAP215: a key component of the dynamic microtubule cytoskeleton
    • Kinoshita K., Habermann B., Hyman A.A. XMAP215: a key component of the dynamic microtubule cytoskeleton. Trends Cell Biol. 2002, 12:267-273.
    • (2002) Trends Cell Biol. , vol.12 , pp. 267-273
    • Kinoshita, K.1    Habermann, B.2    Hyman, A.A.3
  • 196
    • 0018195288 scopus 로고
    • Microtubule assembly and nucleation
    • Kirschner M.W. Microtubule assembly and nucleation. Int. Rev. Cytol. 1978, 54:1-71.
    • (1978) Int. Rev. Cytol. , vol.54 , pp. 1-71
    • Kirschner, M.W.1
  • 197
    • 0022919318 scopus 로고
    • Beyond self-assembly: from microtubules to morphogenesis
    • Kirschner M., Mitchison T. Beyond self-assembly: from microtubules to morphogenesis. Cell 1986, 45:329-342.
    • (1986) Cell , vol.45 , pp. 329-342
    • Kirschner, M.1    Mitchison, T.2
  • 198
    • 33745737636 scopus 로고    scopus 로고
    • Adenomatous polyposis coli on microtubule plus ends in cell extensions can promote microtubule net growth with or without EB1
    • Kita K., Wittmann T., Nathke I.S., Waterman-Storer C.M. Adenomatous polyposis coli on microtubule plus ends in cell extensions can promote microtubule net growth with or without EB1. Mol. Biol. Cell 2006, 17:2331-2345.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2331-2345
    • Kita, K.1    Wittmann, T.2    Nathke, I.S.3    Waterman-Storer, C.M.4
  • 199
    • 76249106878 scopus 로고    scopus 로고
    • Kinetochores generate microtubules with distal plus ends: their roles and limited lifetime in mitosis
    • Kitamura E., Tanaka K., Komoto S., Kitamura Y., Antony C., Tanaka T.U. Kinetochores generate microtubules with distal plus ends: their roles and limited lifetime in mitosis. Dev. Cell 2010, 18:248-259.
    • (2010) Dev. Cell , vol.18 , pp. 248-259
    • Kitamura, E.1    Tanaka, K.2    Komoto, S.3    Kitamura, Y.4    Antony, C.5    Tanaka, T.U.6
  • 200
    • 70649108819 scopus 로고    scopus 로고
    • Cell cycle-dependent microtubule-based dynamic transport of cytoplasmic dynein in mammalian cells
    • Kobayashi T., Murayama T. Cell cycle-dependent microtubule-based dynamic transport of cytoplasmic dynein in mammalian cells. PLoS ONE 2009, 4:e7827.
    • (2009) PLoS ONE , vol.4
    • Kobayashi, T.1    Murayama, T.2
  • 201
    • 0344845405 scopus 로고    scopus 로고
    • ACF7: an essential integrator of microtubule dynamics
    • Kodama A., Karakesisoglou I., Wong E., Vaezi A., Fuchs E. ACF7: an essential integrator of microtubule dynamics. Cell 2003, 115:343-354.
    • (2003) Cell , vol.115 , pp. 343-354
    • Kodama, A.1    Karakesisoglou, I.2    Wong, E.3    Vaezi, A.4    Fuchs, E.5
  • 202
    • 76649111718 scopus 로고    scopus 로고
    • Nuclear-localized subtype of end-binding 1 protein regulates spindle organization in Arabidopsis
    • Komaki S., Abe T., Coutuer S., Inze D., Russinova E., Hashimoto T. Nuclear-localized subtype of end-binding 1 protein regulates spindle organization in Arabidopsis. J. Cell Sci. 2010, 123:451-459.
    • (2010) J. Cell Sci. , vol.123 , pp. 451-459
    • Komaki, S.1    Abe, T.2    Coutuer, S.3    Inze, D.4    Russinova, E.5    Hashimoto, T.6
  • 206
    • 12844258049 scopus 로고    scopus 로고
    • The role of the kinesin motor KipA in microtubule organization and polarized growth of Aspergillus nidulans
    • Konzack S., Rischitor P.E., Enke C., Fischer R. The role of the kinesin motor KipA in microtubule organization and polarized growth of Aspergillus nidulans. Mol. Biol. Cell 2005, 16:497-506.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 497-506
    • Konzack, S.1    Rischitor, P.E.2    Enke, C.3    Fischer, R.4
  • 207
    • 77954068979 scopus 로고    scopus 로고
    • Finding the middle ground: how kinetochores power chromosome congression
    • Kops G.J., Saurin A.T., Meraldi P. Finding the middle ground: how kinetochores power chromosome congression. Cell. Mol. Life Sci. 2010, 67:2145-2161.
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 2145-2161
    • Kops, G.J.1    Saurin, A.T.2    Meraldi, P.3
  • 208
    • 0034708459 scopus 로고    scopus 로고
    • Molecular linkage underlying microtubule orientation toward cortical sites in yeast
    • Korinek W.S., Copeland M.J., Chaudhuri A., Chant J. Molecular linkage underlying microtubule orientation toward cortical sites in yeast. Science 2000, 287:2257-2259.
    • (2000) Science , vol.287 , pp. 2257-2259
    • Korinek, W.S.1    Copeland, M.J.2    Chaudhuri, A.3    Chant, J.4
  • 210
    • 66349130709 scopus 로고    scopus 로고
    • XMAP215-EB1 interaction is required for proper spindle assembly and chromosome segregation in Xenopus egg extract
    • Kronja I., Kruljac-Letunic A., Caudron-Herger M., Bieling P., Karsenti E. XMAP215-EB1 interaction is required for proper spindle assembly and chromosome segregation in Xenopus egg extract. Mol. Biol. Cell 2009, 20:2684-2696.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 2684-2696
    • Kronja, I.1    Kruljac-Letunic, A.2    Caudron-Herger, M.3    Bieling, P.4    Karsenti, E.5
  • 211
    • 64049115132 scopus 로고    scopus 로고
    • GSK3beta phosphorylation modulates CLASP-microtubule association and lamella microtubule attachment
    • Kumar P., Lyle K.S., Gierke S., Matov A., Danuser G., Wittmann T. GSK3beta phosphorylation modulates CLASP-microtubule association and lamella microtubule attachment. J. Cell Biol. 2009, 184:895-908.
    • (2009) J. Cell Biol. , vol.184 , pp. 895-908
    • Kumar, P.1    Lyle, K.S.2    Gierke, S.3    Matov, A.4    Danuser, G.5    Wittmann, T.6
  • 212
    • 38449097283 scopus 로고    scopus 로고
    • The G59S mutation in p150(glued) causes dysfunction of dynactin in mice
    • Lai C., Lin X., Chandran J., Shim H., Yang W.J., Cai H. The G59S mutation in p150(glued) causes dysfunction of dynactin in mice. J. Neurosci. 2007, 27:13982-13990.
    • (2007) J. Neurosci. , vol.27 , pp. 13982-13990
    • Lai, C.1    Lin, X.2    Chandran, J.3    Shim, H.4    Yang, W.J.5    Cai, H.6
  • 213
    • 39849107361 scopus 로고    scopus 로고
    • Motor neuron disease occurring in a mutant dynactin mouse model is characterized by defects in vesicular trafficking
    • Laird F.M., Farah M.H., Ackerley S., Hoke A., Maragakis N., Rothstein J.D., et al. Motor neuron disease occurring in a mutant dynactin mouse model is characterized by defects in vesicular trafficking. J. Neurosci. 2008, 28:1997-2005.
    • (2008) J. Neurosci. , vol.28 , pp. 1997-2005
    • Laird, F.M.1    Farah, M.H.2    Ackerley, S.3    Hoke, A.4    Maragakis, N.5    Rothstein, J.D.6
  • 214
    • 1542290607 scopus 로고    scopus 로고
    • Aurora B phosphorylates centromeric MCAK and regulates its localization and microtubule depolymerization activity
    • Lan W., Zhang X., Kline-Smith S.L., Rosasco S.E., Barrett-Wilt G.A., Shabanowitz J., et al. Aurora B phosphorylates centromeric MCAK and regulates its localization and microtubule depolymerization activity. Curr. Biol. 2004, 14:273-286.
    • (2004) Curr. Biol. , vol.14 , pp. 273-286
    • Lan, W.1    Zhang, X.2    Kline-Smith, S.L.3    Rosasco, S.E.4    Barrett-Wilt, G.A.5    Shabanowitz, J.6
  • 215
    • 33644504853 scopus 로고    scopus 로고
    • Examination of actin and microtubule dependent APC localisations in living mammalian cells
    • Langford K.J., Askham J.M., Lee T., Adams M., Morrison E.E. Examination of actin and microtubule dependent APC localisations in living mammalian cells. BMC Cell Biol. 2006, 7:3.
    • (2006) BMC Cell Biol. , vol.7 , pp. 3
    • Langford, K.J.1    Askham, J.M.2    Lee, T.3    Adams, M.4    Morrison, E.E.5
  • 216
    • 33745848829 scopus 로고    scopus 로고
    • Microtubule plus end: a hub of cellular activities
    • Lansbergen G., Akhmanova A. Microtubule plus end: a hub of cellular activities. Traffic 2006, 7:499-507.
    • (2006) Traffic , vol.7 , pp. 499-507
    • Lansbergen, G.1    Akhmanova, A.2
  • 217
    • 4644302721 scopus 로고    scopus 로고
    • Conformational changes in CLIP-170 regulate its binding to microtubules and dynactin localization
    • Lansbergen G., Komarova Y., Modesti M., Wyman C., Hoogenraad C.C., Goodson H.V., et al. Conformational changes in CLIP-170 regulate its binding to microtubules and dynactin localization. J. Cell Biol. 2004, 166:1003-1014.
    • (2004) J. Cell Biol. , vol.166 , pp. 1003-1014
    • Lansbergen, G.1    Komarova, Y.2    Modesti, M.3    Wyman, C.4    Hoogenraad, C.C.5    Goodson, H.V.6
  • 219
    • 0032559641 scopus 로고    scopus 로고
    • A class VI unconventional myosin is associated with a homologue of a microtubule-binding protein, cytoplasmic linker protein-170, in neurons and at the posterior pole of Drosophila embryos
    • Lantz V.A., Miller K.G. A class VI unconventional myosin is associated with a homologue of a microtubule-binding protein, cytoplasmic linker protein-170, in neurons and at the posterior pole of Drosophila embryos. J. Cell Biol. 1998, 140:897-910.
    • (1998) J. Cell Biol. , vol.140 , pp. 897-910
    • Lantz, V.A.1    Miller, K.G.2
  • 221
    • 0342666643 scopus 로고
    • Morphology of microtubules of plant cell
    • Ledbetter M.C., Porter K.R. Morphology of microtubules of plant cell. Science 1964, 144:872-874.
    • (1964) Science , vol.144 , pp. 872-874
    • Ledbetter, M.C.1    Porter, K.R.2
  • 222
    • 0034708606 scopus 로고    scopus 로고
    • Positioning of the mitotic spindle by a cortical-microtubule capture mechanism
    • Lee L., Tirnauer J.S., Li J., Schuyler S.C., Liu J.Y., Pellman D. Positioning of the mitotic spindle by a cortical-microtubule capture mechanism. Science 2000, 287:2260-2262.
    • (2000) Science , vol.287 , pp. 2260-2262
    • Lee, L.1    Tirnauer, J.S.2    Li, J.3    Schuyler, S.C.4    Liu, J.Y.5    Pellman, D.6
  • 223
    • 0037415644 scopus 로고    scopus 로고
    • The role of the lissencephaly protein Pac1 during nuclear migration in budding yeast
    • Lee W.L., Oberle J.R., Cooper J.A. The role of the lissencephaly protein Pac1 during nuclear migration in budding yeast. J. Cell Biol. 2003, 160:355-364.
    • (2003) J. Cell Biol. , vol.160 , pp. 355-364
    • Lee, W.L.1    Oberle, J.R.2    Cooper, J.A.3
  • 224
    • 2942753920 scopus 로고    scopus 로고
    • The microtubule plus end tracking protein Orbit/MAST/CLASP acts downstream of the tyrosine kinase Abl in mediating axon guidance
    • Lee H., Engel U., Rusch J., Scherrer S., Sheard K., Van Vactor D. The microtubule plus end tracking protein Orbit/MAST/CLASP acts downstream of the tyrosine kinase Abl in mediating axon guidance. Neuron 2004, 42:913-926.
    • (2004) Neuron , vol.42 , pp. 913-926
    • Lee, H.1    Engel, U.2    Rusch, J.3    Scherrer, S.4    Sheard, K.5    Van Vactor, D.6
  • 227
    • 49649109248 scopus 로고    scopus 로고
    • Regulation of mitotic spindle asymmetry by SUMO and the spindle-assembly checkpoint in yeast
    • Leisner C., Kammerer D., Denoth A., Britschi M., Barral Y., Liakopoulos D. Regulation of mitotic spindle asymmetry by SUMO and the spindle-assembly checkpoint in yeast. Curr. Biol. 2008, 18:1249-1255.
    • (2008) Curr. Biol. , vol.18 , pp. 1249-1255
    • Leisner, C.1    Kammerer, D.2    Denoth, A.3    Britschi, M.4    Barral, Y.5    Liakopoulos, D.6
  • 228
    • 0034679590 scopus 로고    scopus 로고
    • Mast, a conserved microtubule-associated protein required for bipolar mitotic spindle organization
    • Lemos C.L., Sampaio P., Maiato H., Costa M., Omel'yanchuk L.V., Liberal V., et al. Mast, a conserved microtubule-associated protein required for bipolar mitotic spindle organization. EMBO J. 2000, 19:3668-3682.
    • (2000) EMBO J. , vol.19 , pp. 3668-3682
    • Lemos, C.L.1    Sampaio, P.2    Maiato, H.3    Costa, M.4    Omel'yanchuk, L.V.5    Liberal, V.6
  • 229
    • 0033552634 scopus 로고    scopus 로고
    • Microtubule actin cross-linking factor (MACF): a hybrid of dystonin and dystrophin that can interact with the actin and microtubule cytoskeletons
    • Leung C.L., Sun D., Zheng M., Knowles D.R., Liem R.K. Microtubule actin cross-linking factor (MACF): a hybrid of dystonin and dystrophin that can interact with the actin and microtubule cytoskeletons. J. Cell Biol. 1999, 147:1275-1286.
    • (1999) J. Cell Biol. , vol.147 , pp. 1275-1286
    • Leung, C.L.1    Sun, D.2    Zheng, M.3    Knowles, D.R.4    Liem, R.K.5
  • 230
    • 33644551565 scopus 로고    scopus 로고
    • A motor neuron disease-associated mutation in p150Glued perturbs dynactin function and induces protein aggregation
    • Levy J.R., Sumner C.J., Caviston J.P., Tokito M.K., Ranganathan S., Ligon L.A., et al. A motor neuron disease-associated mutation in p150Glued perturbs dynactin function and induces protein aggregation. J. Cell Biol. 2006, 172:733-745.
    • (2006) J. Cell Biol. , vol.172 , pp. 733-745
    • Levy, J.R.1    Sumner, C.J.2    Caviston, J.P.3    Tokito, M.K.4    Ranganathan, S.5    Ligon, L.A.6
  • 231
    • 59449094652 scopus 로고    scopus 로고
    • The microtubule-binding protein CLIP-170 coordinates mDia1 and actin reorganization during CR3-mediated phagocytosis
    • Lewkowicz E., Herit F., Le Clainche C., Bourdoncle P., Perez F., Niedergang F. The microtubule-binding protein CLIP-170 coordinates mDia1 and actin reorganization during CR3-mediated phagocytosis. J. Cell Biol. 2008, 183:1287-1298.
    • (2008) J. Cell Biol. , vol.183 , pp. 1287-1298
    • Lewkowicz, E.1    Herit, F.2    Le Clainche, C.3    Bourdoncle, P.4    Perez, F.5    Niedergang, F.6
  • 232
    • 0037073702 scopus 로고    scopus 로고
    • Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain
    • Li S., Finley J., Liu Z.J., Qiu S.H., Chen H., Luan C.H., et al. Crystal structure of the cytoskeleton-associated protein glycine-rich (CAP-Gly) domain. J. Biol. Chem. 2002, 277:48596-48601.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48596-48601
    • Li, S.1    Finley, J.2    Liu, Z.J.3    Qiu, S.H.4    Chen, H.5    Luan, C.H.6
  • 233
    • 0037459058 scopus 로고    scopus 로고
    • Asymmetric loading of Kar9 onto spindle poles and microtubules ensures proper spindle alignment
    • Liakopoulos D., Kusch J., Grava S., Vogel J., Barral Y. Asymmetric loading of Kar9 onto spindle poles and microtubules ensures proper spindle alignment. Cell 2003, 112:561-574.
    • (2003) Cell , vol.112 , pp. 561-574
    • Liakopoulos, D.1    Kusch, J.2    Grava, S.3    Vogel, J.4    Barral, Y.5
  • 234
  • 235
    • 77952201222 scopus 로고    scopus 로고
    • Cdk5rap2 regulates centrosome function and chromosome segregation in neuronal progenitors
    • Lizarraga S.B., Margossian S.P., Harris M.H., Campagna D.R., Han A.P., Blevins S., et al. Cdk5rap2 regulates centrosome function and chromosome segregation in neuronal progenitors. Development 2010, 137:1907-1917.
    • (2010) Development , vol.137 , pp. 1907-1917
    • Lizarraga, S.B.1    Margossian, S.P.2    Harris, M.H.3    Campagna, D.R.4    Han, A.P.5    Blevins, S.6
  • 236
    • 69949115962 scopus 로고    scopus 로고
    • CLIP-170-dependent capture of membrane organelles by microtubules initiates minus-end directed transport
    • Lomakin A.J., Semenova I., Zaliapin I., Kraikivski P., Nadezhdina E., Slepchenko B.M., et al. CLIP-170-dependent capture of membrane organelles by microtubules initiates minus-end directed transport. Dev. Cell 2009, 17:323-333.
    • (2009) Dev. Cell , vol.17 , pp. 323-333
    • Lomakin, A.J.1    Semenova, I.2    Zaliapin, I.3    Kraikivski, P.4    Nadezhdina, E.5    Slepchenko, B.M.6
  • 237
    • 1842479447 scopus 로고    scopus 로고
    • Adenomatous polyposis coli and EB1 localize in close proximity of the mother centriole and EB1 is a functional component of centrosomes
    • Louie R.K., Bahmanyar S., Siemers K.A., Votin V., Chang P., Stearns T., et al. Adenomatous polyposis coli and EB1 localize in close proximity of the mother centriole and EB1 is a functional component of centrosomes. J. Cell Sci. 2004, 117:1117-1128.
    • (2004) J. Cell Sci. , vol.117 , pp. 1117-1128
    • Louie, R.K.1    Bahmanyar, S.2    Siemers, K.A.3    Votin, V.4    Chang, P.5    Stearns, T.6
  • 238
    • 77958485121 scopus 로고    scopus 로고
    • Parallel genetic and proteomic screens identify Msps as a CLASP-Abl pathway interactor in Drosophila
    • Lowery L.A., Lee H., Lu C., Murphy R., Obar R.A., Zhai B., et al. Parallel genetic and proteomic screens identify Msps as a CLASP-Abl pathway interactor in Drosophila. Genetics 2010, 185:1311-1325.
    • (2010) Genetics , vol.185 , pp. 1311-1325
    • Lowery, L.A.1    Lee, H.2    Lu, C.3    Murphy, R.4    Obar, R.A.5    Zhai, B.6
  • 239
    • 0030709242 scopus 로고    scopus 로고
    • Multiple forms of tubulin: different gene products and covalent modifications
    • Luduena R.F. Multiple forms of tubulin: different gene products and covalent modifications. Int. Rev. Cytol. 1998, 178:207-275.
    • (1998) Int. Rev. Cytol. , vol.178 , pp. 207-275
    • Luduena, R.F.1
  • 240
    • 58249088192 scopus 로고    scopus 로고
    • SnapShot: microtubule regulators I
    • 380 e1
    • Lyle K., Kumar P., Wittmann T. SnapShot: microtubule regulators I. Cell 2009, 136:380. 380 e1.
    • (2009) Cell , vol.136 , pp. 380
    • Lyle, K.1    Kumar, P.2    Wittmann, T.3
  • 241
    • 59049103079 scopus 로고    scopus 로고
    • SnapShot: microtubule regulators II
    • 566 e1
    • Lyle K., Kumar P., Wittmann T. SnapShot: microtubule regulators II. Cell 2009, 136:566. 566 e1.
    • (2009) Cell , vol.136 , pp. 566
    • Lyle, K.1    Kumar, P.2    Wittmann, T.3
  • 242
    • 23944463214 scopus 로고    scopus 로고
    • Microtubules: Kar3 eats up the track
    • Maddox P.S. Microtubules: Kar3 eats up the track. Curr. Biol. 2005, 15:R622-R624.
    • (2005) Curr. Biol. , vol.15
    • Maddox, P.S.1
  • 243
    • 0042426023 scopus 로고    scopus 로고
    • The minus end-directed motor Kar3 is required for coupling dynamic microtubule plus ends to the cortical shmoo tip in budding yeast
    • Maddox P.S., Stemple J.K., Satterwhite L., Salmon E.D., Bloom K. The minus end-directed motor Kar3 is required for coupling dynamic microtubule plus ends to the cortical shmoo tip in budding yeast. Curr. Biol. 2003, 13:1423-1428.
    • (2003) Curr. Biol. , vol.13 , pp. 1423-1428
    • Maddox, P.S.1    Stemple, J.K.2    Satterwhite, L.3    Salmon, E.D.4    Bloom, K.5
  • 244
    • 0037415689 scopus 로고    scopus 로고
    • Yeast Cdk1 translocates to the plus end of cytoplasmic microtubules to regulate bud cortex interactions
    • Maekawa H., Usui T., Knop M., Schiebel E. Yeast Cdk1 translocates to the plus end of cytoplasmic microtubules to regulate bud cortex interactions. EMBO J. 2003, 22:438-449.
    • (2003) EMBO J. , vol.22 , pp. 438-449
    • Maekawa, H.1    Usui, T.2    Knop, M.3    Schiebel, E.4
  • 245
    • 0036296624 scopus 로고    scopus 로고
    • Neuron navigator: a human gene family with homology to unc-53, a cell guidance gene from Caenorhabditis elegans
    • Maes T., Barcelo A., Buesa C. Neuron navigator: a human gene family with homology to unc-53, a cell guidance gene from Caenorhabditis elegans. Genomics 2002, 80:21-30.
    • (2002) Genomics , vol.80 , pp. 21-30
    • Maes, T.1    Barcelo, A.2    Buesa, C.3
  • 246
    • 70349284429 scopus 로고    scopus 로고
    • Motor-independent targeting of CLASPs to kinetochores by CENP-E promotes microtubule turnover and poleward flux
    • Maffini S., Maia A.R., Manning A.L., Maliga Z., Pereira A.L., Junqueira M., et al. Motor-independent targeting of CLASPs to kinetochores by CENP-E promotes microtubule turnover and poleward flux. Curr. Biol. 2009, 19:1566-1572.
    • (2009) Curr. Biol. , vol.19 , pp. 1566-1572
    • Maffini, S.1    Maia, A.R.2    Manning, A.L.3    Maliga, Z.4    Pereira, A.L.5    Junqueira, M.6
  • 247
    • 0037182592 scopus 로고    scopus 로고
    • MAST/Orbit has a role in microtubule-kinetochore attachment and is essential for chromosome alignment and maintenance of spindle bipolarity
    • Maiato H., Sampaio P., Lemos C.L., Findlay J., Carmena M., Earnshaw W.C., et al. MAST/Orbit has a role in microtubule-kinetochore attachment and is essential for chromosome alignment and maintenance of spindle bipolarity. J. Cell Biol. 2002, 157:749-760.
    • (2002) J. Cell Biol. , vol.157 , pp. 749-760
    • Maiato, H.1    Sampaio, P.2    Lemos, C.L.3    Findlay, J.4    Carmena, M.5    Earnshaw, W.C.6
  • 248
    • 0038385019 scopus 로고    scopus 로고
    • Human CLASP1 is an outer kinetochore component that regulates spindle microtubule dynamics
    • Maiato H., Fairley E.A., Rieder C.L., Swedlow J.R., Sunkel C.E., Earnshaw W.C. Human CLASP1 is an outer kinetochore component that regulates spindle microtubule dynamics. Cell 2003, 113:891-904.
    • (2003) Cell , vol.113 , pp. 891-904
    • Maiato, H.1    Fairley, E.A.2    Rieder, C.L.3    Swedlow, J.R.4    Sunkel, C.E.5    Earnshaw, W.C.6
  • 249
    • 12344300350 scopus 로고    scopus 로고
    • Drosophila CLASP is required for the incorporation of microtubule subunits into fluxing kinetochore fibres
    • Maiato H., Khodjakov A., Rieder C.L. Drosophila CLASP is required for the incorporation of microtubule subunits into fluxing kinetochore fibres. Nat. Cell Biol. 2005, 7:42-47.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 42-47
    • Maiato, H.1    Khodjakov, A.2    Rieder, C.L.3
  • 250
    • 9244232349 scopus 로고    scopus 로고
    • Molecular motors: strategies to get along
    • Mallik R., Gross S.P. Molecular motors: strategies to get along. Curr. Biol. 2004, 14:R971-R982.
    • (2004) Curr. Biol. , vol.14
    • Mallik, R.1    Gross, S.P.2
  • 251
    • 0022384496 scopus 로고
    • Unstained microtubules studied by cryo-electron microscopy. Substructure, supertwist and disassembly
    • Mandelkow E.M., Mandelkow E. Unstained microtubules studied by cryo-electron microscopy. Substructure, supertwist and disassembly. J. Mol. Biol. 1985, 181:123-135.
    • (1985) J. Mol. Biol. , vol.181 , pp. 123-135
    • Mandelkow, E.M.1    Mandelkow, E.2
  • 252
    • 0022483059 scopus 로고
    • On the surface lattice of microtubules: helix starts, protofilament number, seam, and handedness
    • Mandelkow E.M., Schultheiss R., Rapp R., Muller M., Mandelkow E. On the surface lattice of microtubules: helix starts, protofilament number, seam, and handedness. J. Cell Biol. 1986, 102:1067-1073.
    • (1986) J. Cell Biol. , vol.102 , pp. 1067-1073
    • Mandelkow, E.M.1    Schultheiss, R.2    Rapp, R.3    Muller, M.4    Mandelkow, E.5
  • 253
    • 0025868445 scopus 로고
    • Microtubule dynamics and microtubule caps: a time-resolved cryo-electron microscopy study
    • Mandelkow E.M., Mandelkow E., Milligan R.A. Microtubule dynamics and microtubule caps: a time-resolved cryo-electron microscopy study. J. Cell Biol. 1991, 114:977-991.
    • (1991) J. Cell Biol. , vol.114 , pp. 977-991
    • Mandelkow, E.M.1    Mandelkow, E.2    Milligan, R.A.3
  • 254
    • 0035860717 scopus 로고    scopus 로고
    • Molecular dissection of the microtubule depolymerizing activity of mitotic centromere-associated kinesin
    • Maney T., Wagenbach M., Wordeman L. Molecular dissection of the microtubule depolymerizing activity of mitotic centromere-associated kinesin. J. Biol. Chem. 2001, 276:34753-34758.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34753-34758
    • Maney, T.1    Wagenbach, M.2    Wordeman, L.3
  • 255
    • 38849159958 scopus 로고    scopus 로고
    • Suppression of microtubule dynamic instability by the +TIP protein EB1 and its modulation by the CAP-Gly domain of p150glued
    • Manna T., Honnappa S., Steinmetz M.O., Wilson L. Suppression of microtubule dynamic instability by the +TIP protein EB1 and its modulation by the CAP-Gly domain of p150glued. Biochemistry 2008, 47:779-786.
    • (2008) Biochemistry , vol.47 , pp. 779-786
    • Manna, T.1    Honnappa, S.2    Steinmetz, M.O.3    Wilson, L.4
  • 256
    • 59349084461 scopus 로고    scopus 로고
    • Motor- and tail-dependent targeting of dynein to microtubule plus ends and the cell cortex
    • Markus S.M., Punch J.J., Lee W.L. Motor- and tail-dependent targeting of dynein to microtubule plus ends and the cell cortex. Curr. Biol. 2009, 19:196-205.
    • (2009) Curr. Biol. , vol.19 , pp. 196-205
    • Markus, S.M.1    Punch, J.J.2    Lee, W.L.3
  • 257
    • 16244409515 scopus 로고    scopus 로고
    • Tea4p links microtubule plus ends with the formin for3p in the establishment of cell polarity
    • Martin S.G., McDonald W.H., Yates J.R., Chang F. Tea4p links microtubule plus ends with the formin for3p in the establishment of cell polarity. Dev. Cell 2005, 8:479-491.
    • (2005) Dev. Cell , vol.8 , pp. 479-491
    • Martin, S.G.1    McDonald, W.H.2    Yates, J.R.3    Chang, F.4
  • 259
    • 70450246898 scopus 로고    scopus 로고
    • Myosin V spatially regulates microtubule dynamics and promotes the ubiquitin-dependent degradation of the fission yeast CLIP-170 homologue, Tip1
    • Martin-Garcia R., Mulvihill D.P. Myosin V spatially regulates microtubule dynamics and promotes the ubiquitin-dependent degradation of the fission yeast CLIP-170 homologue, Tip1. J. Cell Sci. 2009, 122:3862-3872.
    • (2009) J. Cell Sci. , vol.122 , pp. 3862-3872
    • Martin-Garcia, R.1    Mulvihill, D.P.2
  • 260
    • 0035964395 scopus 로고    scopus 로고
    • Mutations in Mlph, encoding a member of the Rab effector family, cause the melanosome transport defects observed in leaden mice
    • Matesic L.E., Yip R., Reuss A.E., Swing D.A., O'Sullivan T.N., Fletcher C.F., et al. Mutations in Mlph, encoding a member of the Rab effector family, cause the melanosome transport defects observed in leaden mice. Proc. Natl Acad. Sci. USA 2001, 98:10238-10243.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 10238-10243
    • Matesic, L.E.1    Yip, R.2    Reuss, A.E.3    Swing, D.A.4    O'Sullivan, T.N.5    Fletcher, C.F.6
  • 261
    • 0037344894 scopus 로고    scopus 로고
    • Orbit/Mast, the CLASP orthologue of Drosophila, is required for asymmetric stem cell and cystocyte divisions and development of the polarised microtubule network that interconnects oocyte and nurse cells during oogenesis
    • Mathe E., Inoue Y.H., Palframan W., Brown G., Glover D.M. Orbit/Mast, the CLASP orthologue of Drosophila, is required for asymmetric stem cell and cystocyte divisions and development of the polarised microtubule network that interconnects oocyte and nurse cells during oogenesis. Development 2003, 130:901-915.
    • (2003) Development , vol.130 , pp. 901-915
    • Mathe, E.1    Inoue, Y.H.2    Palframan, W.3    Brown, G.4    Glover, D.M.5
  • 262
    • 0242625182 scopus 로고    scopus 로고
    • A novel localization pattern for an EB1-like protein links microtubule dynamics to endomembrane organization
    • Mathur J., Mathur N., Kernebeck B., Srinivas B.P., Hulskamp M. A novel localization pattern for an EB1-like protein links microtubule dynamics to endomembrane organization. Curr. Biol. 2003, 13:1991-1997.
    • (2003) Curr. Biol. , vol.13 , pp. 1991-1997
    • Mathur, J.1    Mathur, N.2    Kernebeck, B.3    Srinivas, B.P.4    Hulskamp, M.5
  • 263
    • 0032101370 scopus 로고    scopus 로고
    • ZYG-9, a Caenorhabditis elegans protein required for microtubule organization and function, is a component of meiotic and mitotic spindle poles
    • Matthews L.R., Carter P., Thierry-Mieg D., Kemphues K. ZYG-9, a Caenorhabditis elegans protein required for microtubule organization and function, is a component of meiotic and mitotic spindle poles. J. Cell Biol. 1998, 141:1159-1168.
    • (1998) J. Cell Biol. , vol.141 , pp. 1159-1168
    • Matthews, L.R.1    Carter, P.2    Thierry-Mieg, D.3    Kemphues, K.4
  • 264
    • 77954056702 scopus 로고    scopus 로고
    • Contrasting models for kinetochore microtubule attachment in mammalian cells
    • McEwen B.F., Dong Y. Contrasting models for kinetochore microtubule attachment in mammalian cells. Cell. Mol. Life Sci. 2010, 67:2163-2172.
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 2163-2172
    • McEwen, B.F.1    Dong, Y.2
  • 265
    • 53549118867 scopus 로고    scopus 로고
    • Fibrils connect microtubule tips with kinetochores: a mechanism to couple tubulin dynamics to chromosome motion
    • McIntosh J.R., Grishchuk E.L., Morphew M.K., Efremov A.K., Zhudenkov K., Volkov V.A., et al. Fibrils connect microtubule tips with kinetochores: a mechanism to couple tubulin dynamics to chromosome motion. Cell 2008, 135:322-333.
    • (2008) Cell , vol.135 , pp. 322-333
    • McIntosh, J.R.1    Grishchuk, E.L.2    Morphew, M.K.3    Efremov, A.K.4    Zhudenkov, K.5    Volkov, V.A.6
  • 267
    • 77951701022 scopus 로고    scopus 로고
    • LIS1 and NudE induce a persistent dynein force-producing state
    • McKenney R.J., Vershinin M., Kunwar A., Vallee R.B., Gross S.P. LIS1 and NudE induce a persistent dynein force-producing state. Cell 2010, 141:304-314.
    • (2010) Cell , vol.141 , pp. 304-314
    • McKenney, R.J.1    Vershinin, M.2    Kunwar, A.3    Vallee, R.B.4    Gross, S.P.5
  • 268
    • 0030060174 scopus 로고    scopus 로고
    • Modulation of microtubule dynamics during the cell cycle
    • McNally F.J. Modulation of microtubule dynamics during the cell cycle. Curr. Opin. Cell Biol. 1996, 8:23-29.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 23-29
    • McNally, F.J.1
  • 269
    • 0027424297 scopus 로고
    • Identification of katanin, an ATPase that severs and disassembles stable microtubules
    • McNally F.J., Vale R.D. Identification of katanin, an ATPase that severs and disassembles stable microtubules. Cell 1993, 75:419-429.
    • (1993) Cell , vol.75 , pp. 419-429
    • McNally, F.J.1    Vale, R.D.2
  • 270
    • 61849109220 scopus 로고    scopus 로고
    • The spindle positioning protein Kar9p interacts with the sumoylation machinery in Saccharomyces cerevisiae
    • Meednu N., Hoops H., D'Silva S., Pogorzala L., Wood S., Farkas D., et al. The spindle positioning protein Kar9p interacts with the sumoylation machinery in Saccharomyces cerevisiae. Genetics 2008, 180:2033-2055.
    • (2008) Genetics , vol.180 , pp. 2033-2055
    • Meednu, N.1    Hoops, H.2    D'Silva, S.3    Pogorzala, L.4    Wood, S.5    Farkas, D.6
  • 272
    • 0025060807 scopus 로고
    • GTP analogues interact with the tubulin exchangeable site during assembly and upon binding
    • Mejillano M.R., Barton J.S., Nath J.P., Himes R.H. GTP analogues interact with the tubulin exchangeable site during assembly and upon binding. Biochemistry 1990, 29:1208-1216.
    • (1990) Biochemistry , vol.29 , pp. 1208-1216
    • Mejillano, M.R.1    Barton, J.S.2    Nath, J.P.3    Himes, R.H.4
  • 273
    • 0025309665 scopus 로고
    • KAR3, a kinesin-related gene required for yeast nuclear fusion
    • Meluh P.B., Rose M.D. KAR3, a kinesin-related gene required for yeast nuclear fusion. Cell 1990, 60:1029-1041.
    • (1990) Cell , vol.60 , pp. 1029-1041
    • Meluh, P.B.1    Rose, M.D.2
  • 274
    • 14744287039 scopus 로고    scopus 로고
    • Functionally distinct kinesin-13 family members cooperate to regulate microtubule dynamics during interphase
    • Mennella V., Rogers G.C., Rogers S.L., Buster D.W., Vale R.D., Sharp D.J. Functionally distinct kinesin-13 family members cooperate to regulate microtubule dynamics during interphase. Nat. Cell Biol. 2005, 7:235-245.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 235-245
    • Mennella, V.1    Rogers, G.C.2    Rogers, S.L.3    Buster, D.W.4    Vale, R.D.5    Sharp, D.J.6
  • 275
    • 24344465919 scopus 로고    scopus 로고
    • Analysis of the kinesin superfamily: insights into structure and function
    • Miki H., Okada Y., Hirokawa N. Analysis of the kinesin superfamily: insights into structure and function. Trends Cell Biol. 2005, 15:467-476.
    • (2005) Trends Cell Biol. , vol.15 , pp. 467-476
    • Miki, H.1    Okada, Y.2    Hirokawa, N.3
  • 276
    • 0032567757 scopus 로고    scopus 로고
    • Kar9p is a novel cortical protein required for cytoplasmic microtubule orientation in yeast
    • Miller R.K., Rose M.D. Kar9p is a novel cortical protein required for cytoplasmic microtubule orientation in yeast. J. Cell Biol. 1998, 140:377-390.
    • (1998) J. Cell Biol. , vol.140 , pp. 377-390
    • Miller, R.K.1    Rose, M.D.2
  • 277
    • 0034490532 scopus 로고    scopus 로고
    • Bim1p/Yeb1p mediates the Kar9p-dependent cortical attachment of cytoplasmic microtubules
    • Miller R.K., Cheng S.C., Rose M.D. Bim1p/Yeb1p mediates the Kar9p-dependent cortical attachment of cytoplasmic microtubules. Mol. Biol. Cell 2000, 11:2949-2959.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2949-2959
    • Miller, R.K.1    Cheng, S.C.2    Rose, M.D.3
  • 278
    • 33751026978 scopus 로고    scopus 로고
    • The CLIP-170 orthologue Bik1p and positioning the mitotic spindle in yeast
    • Miller R.K., D'Silva S., Moore J.K., Goodson H.V. The CLIP-170 orthologue Bik1p and positioning the mitotic spindle in yeast. Curr. Top. Dev. Biol. 2006, 76:49-87.
    • (2006) Curr. Top. Dev. Biol. , vol.76 , pp. 49-87
    • Miller, R.K.1    D'Silva, S.2    Moore, J.K.3    Goodson, H.V.4
  • 280
    • 0142026440 scopus 로고    scopus 로고
    • "Search-and-capture" of microtubules through plus-end-binding proteins (+TIPs)
    • Mimori-Kiyosue Y., Tsukita S. "Search-and-capture" of microtubules through plus-end-binding proteins (+TIPs). J. Biochem. 2003, 134:321-326.
    • (2003) J. Biochem. , vol.134 , pp. 321-326
    • Mimori-Kiyosue, Y.1    Tsukita, S.2
  • 281
    • 0034644119 scopus 로고    scopus 로고
    • The dynamic behavior of the APC-binding protein EB1 on the distal ends of microtubules
    • Mimori-Kiyosue Y., Shiina N., Tsukita S. The dynamic behavior of the APC-binding protein EB1 on the distal ends of microtubules. Curr. Biol. 2000, 10:865-868.
    • (2000) Curr. Biol. , vol.10 , pp. 865-868
    • Mimori-Kiyosue, Y.1    Shiina, N.2    Tsukita, S.3
  • 282
  • 283
    • 34547532472 scopus 로고    scopus 로고
    • Structural basis for tubulin recognition by cytoplasmic linker protein 170 and its autoinhibition
    • Mishima M., Maesaki R., Kasa M., Watanabe T., Fukata M., Kaibuchi K., et al. Structural basis for tubulin recognition by cytoplasmic linker protein 170 and its autoinhibition. Proc. Natl Acad. Sci. USA 2007, 104:10346-10351.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 10346-10351
    • Mishima, M.1    Maesaki, R.2    Kasa, M.3    Watanabe, T.4    Fukata, M.5    Kaibuchi, K.6
  • 284
    • 0021686169 scopus 로고
    • Dynamic instability of microtubule growth
    • Mitchison T., Kirschner M. Dynamic instability of microtubule growth. Nature 1984, 312:237-242.
    • (1984) Nature , vol.312 , pp. 237-242
    • Mitchison, T.1    Kirschner, M.2
  • 286
    • 34247257333 scopus 로고    scopus 로고
    • The cyclin-dependent kinase Cdc28p regulates multiple aspects of Kar9p function in yeast
    • Moore J.K., Miller R.K. The cyclin-dependent kinase Cdc28p regulates multiple aspects of Kar9p function in yeast. Mol. Biol. Cell 2007, 18:1187-1202.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1187-1202
    • Moore, J.K.1    Miller, R.K.2
  • 287
    • 4644219804 scopus 로고    scopus 로고
    • The mechanism, function and regulation of depolymerizing kinesins during mitosis
    • Moore A., Wordeman L. The mechanism, function and regulation of depolymerizing kinesins during mitosis. Trends Cell Biol. 2004, 14:537-546.
    • (2004) Trends Cell Biol. , vol.14 , pp. 537-546
    • Moore, A.1    Wordeman, L.2
  • 289
    • 30044444178 scopus 로고    scopus 로고
    • The CLIP-170 homologue Bik1p promotes the phosphorylation and asymmetric localization of Kar9p
    • Moore J.K., D'Silva S., Miller R.K. The CLIP-170 homologue Bik1p promotes the phosphorylation and asymmetric localization of Kar9p. Mol. Biol. Cell 2006, 17:178-191.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 178-191
    • Moore, J.K.1    D'Silva, S.2    Miller, R.K.3
  • 290
    • 67749142344 scopus 로고    scopus 로고
    • Function of dynein in budding yeast: mitotic spindle positioning in a polarized cell
    • Moore J.K., Stuchell-Brereton M.D., Cooper J.A. Function of dynein in budding yeast: mitotic spindle positioning in a polarized cell. Cell Motil. Cytoskeleton 2009, 66:546-555.
    • (2009) Cell Motil. Cytoskeleton , vol.66 , pp. 546-555
    • Moore, J.K.1    Stuchell-Brereton, M.D.2    Cooper, J.A.3
  • 292
    • 33846999330 scopus 로고    scopus 로고
    • Action and interactions at microtubule ends
    • Morrison E.E. Action and interactions at microtubule ends. Cell. Mol. Life Sci. 2007, 64:307-317.
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 307-317
    • Morrison, E.E.1
  • 293
    • 75349105002 scopus 로고    scopus 로고
    • The APC-EB1 interaction
    • Morrison E.E. The APC-EB1 interaction. Adv. Exp. Med. Biol. 2009, 656:41-50.
    • (2009) Adv. Exp. Med. Biol. , vol.656 , pp. 41-50
    • Morrison, E.E.1
  • 294
    • 0032585647 scopus 로고    scopus 로고
    • EB1, a protein which interacts with the APC tumour suppressor, is associated with the microtubule cytoskeleton throughout the cell cycle
    • Morrison E.E., Wardleworth B.N., Askham J.M., Markham A.F., Meredith D.M. EB1, a protein which interacts with the APC tumour suppressor, is associated with the microtubule cytoskeleton throughout the cell cycle. Oncogene 1998, 17:3471-3477.
    • (1998) Oncogene , vol.17 , pp. 3471-3477
    • Morrison, E.E.1    Wardleworth, B.N.2    Askham, J.M.3    Markham, A.F.4    Meredith, D.M.5
  • 296
    • 0032584067 scopus 로고    scopus 로고
    • Structural changes at microtubule ends accompanying GTP hydrolysis: information from a slowly hydrolyzable analogue of GTP, guanylyl (alpha, beta)methylenediphosphonate
    • Muller-Reichert T., Chretien D., Severin F., Hyman A.A. Structural changes at microtubule ends accompanying GTP hydrolysis: information from a slowly hydrolyzable analogue of GTP, guanylyl (alpha, beta)methylenediphosphonate. Proc. Natl Acad. Sci. USA 1998, 95:3661-3666.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 3661-3666
    • Muller-Reichert, T.1    Chretien, D.2    Severin, F.3    Hyman, A.A.4
  • 297
    • 0027930066 scopus 로고
    • The APC gene product associates with microtubules in vivo and promotes their assembly in vitro
    • Munemitsu S., Souza B., Muller O., Albert I., Rubinfeld B., Polakis P. The APC gene product associates with microtubules in vivo and promotes their assembly in vitro. Cancer Res. 1994, 54:3676-3681.
    • (1994) Cancer Res. , vol.54 , pp. 3676-3681
    • Munemitsu, S.1    Souza, B.2    Muller, O.3    Albert, I.4    Rubinfeld, B.5    Polakis, P.6
  • 298
    • 0037165662 scopus 로고    scopus 로고
    • Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions
    • Nagashima K., Torii S., Yi Z., Igarashi M., Okamoto K., Takeuchi T., et al. Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions. FEBS Lett. 2002, 517:233-238.
    • (2002) FEBS Lett. , vol.517 , pp. 233-238
    • Nagashima, K.1    Torii, S.2    Yi, Z.3    Igarashi, M.4    Okamoto, K.5    Takeuchi, T.6
  • 299
    • 0034642479 scopus 로고    scopus 로고
    • EB3, a novel member of the EB1 family preferentially expressed in the central nervous system, binds to a CNS-specific APC homologue
    • Nakagawa H., Koyama K., Murata Y., Morito M., Akiyama T., Nakamura Y. EB3, a novel member of the EB1 family preferentially expressed in the central nervous system, binds to a CNS-specific APC homologue. Oncogene 2000, 19:210-216.
    • (2000) Oncogene , vol.19 , pp. 210-216
    • Nakagawa, H.1    Koyama, K.2    Murata, Y.3    Morito, M.4    Akiyama, T.5    Nakamura, Y.6
  • 300
    • 0035838422 scopus 로고    scopus 로고
    • Critical role for the EB1 and APC interaction in the regulation of microtubule polymerization
    • Nakamura M., Zhou X.Z., Lu K.P. Critical role for the EB1 and APC interaction in the regulation of microtubule polymerization. Curr. Biol. 2001, 11:1062-1067.
    • (2001) Curr. Biol. , vol.11 , pp. 1062-1067
    • Nakamura, M.1    Zhou, X.Z.2    Lu, K.P.3
  • 301
    • 77953121697 scopus 로고    scopus 로고
    • AMPK controls the speed of microtubule polymerization and directional cell migration through CLIP-170 phosphorylation
    • Nakano A., Kato H., Watanabe T., Min K.D., Yamazaki S., Asano Y., et al. AMPK controls the speed of microtubule polymerization and directional cell migration through CLIP-170 phosphorylation. Nat. Cell Biol. 2010, 12:583-590.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 583-590
    • Nakano, A.1    Kato, H.2    Watanabe, T.3    Min, K.D.4    Yamazaki, S.5    Asano, Y.6
  • 302
    • 8444236025 scopus 로고    scopus 로고
    • The adenomatous polyposis coli protein: the Achilles heel of the gut epithelium
    • Nathke I.S. The adenomatous polyposis coli protein: the Achilles heel of the gut epithelium. Annu. Rev. Cell Dev. Biol. 2004, 20:337-366.
    • (2004) Annu. Rev. Cell Dev. Biol. , vol.20 , pp. 337-366
    • Nathke, I.S.1
  • 303
    • 0033782987 scopus 로고    scopus 로고
    • HEAT repeats associated with condensins, cohesins, and other complexes involved in chromosome-related functions
    • Neuwald A.F., Hirano T. HEAT repeats associated with condensins, cohesins, and other complexes involved in chromosome-related functions. Genome Res. 2000, 10:1445-1452.
    • (2000) Genome Res. , vol.10 , pp. 1445-1452
    • Neuwald, A.F.1    Hirano, T.2
  • 304
    • 4143095005 scopus 로고    scopus 로고
    • MCAK, a Kin I kinesin, increases the catastrophe frequency of steady-state HeLa cell microtubules in an ATP-dependent manner in vitro
    • Newton C.N., Wagenbach M., Ovechkina Y., Wordeman L., Wilson L. MCAK, a Kin I kinesin, increases the catastrophe frequency of steady-state HeLa cell microtubules in an ATP-dependent manner in vitro. FEBS Lett. 2004, 572:80-84.
    • (2004) FEBS Lett. , vol.572 , pp. 80-84
    • Newton, C.N.1    Wagenbach, M.2    Ovechkina, Y.3    Wordeman, L.4    Wilson, L.5
  • 305
    • 35548975477 scopus 로고    scopus 로고
    • Coupling of cortical dynein and G alpha proteins mediates spindle positioning in Caenorhabditis elegans
    • Nguyen-Ngoc T., Afshar K., Gonczy P. Coupling of cortical dynein and G alpha proteins mediates spindle positioning in Caenorhabditis elegans. Nat. Cell Biol. 2007, 9:1294-1302.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1294-1302
    • Nguyen-Ngoc, T.1    Afshar, K.2    Gonczy, P.3
  • 307
    • 0033791649 scopus 로고    scopus 로고
    • Structural insights into microtubule function
    • Nogales E. Structural insights into microtubule function. Annu. Rev. Biochem. 2000, 69:277-302.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 277-302
    • Nogales, E.1
  • 308
    • 33644853818 scopus 로고    scopus 로고
    • Structural intermediates in microtubule assembly and disassembly: how and why?
    • Nogales E., Wang H.W. Structural intermediates in microtubule assembly and disassembly: how and why?. Curr. Opin. Cell Biol. 2006, 18:179-184.
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 179-184
    • Nogales, E.1    Wang, H.W.2
  • 309
    • 33646494080 scopus 로고    scopus 로고
    • Structural mechanisms underlying nucleotide-dependent self-assembly of tubulin and its relatives
    • Nogales E., Wang H.W. Structural mechanisms underlying nucleotide-dependent self-assembly of tubulin and its relatives. Curr. Opin. Struct. Biol. 2006, 16:221-229.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 221-229
    • Nogales, E.1    Wang, H.W.2
  • 310
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the alpha beta tubulin dimer by electron crystallography
    • Nogales E., Wolf S.G., Downing K.H. Structure of the alpha beta tubulin dimer by electron crystallography. Nature 1998, 391:199-203.
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 311
    • 0025366035 scopus 로고
    • Effects of magnesium on the dynamic instability of individual microtubules
    • O'Brien E.T., Salmon E.D., Walker R.A., Erickson H.P. Effects of magnesium on the dynamic instability of individual microtubules. Biochemistry 1990, 29:6648-6656.
    • (1990) Biochemistry , vol.29 , pp. 6648-6656
    • O'Brien, E.T.1    Salmon, E.D.2    Walker, R.A.3    Erickson, H.P.4
  • 312
    • 0029091976 scopus 로고
    • Kinetics of microtubule catastrophe assessed by probabilistic analysis
    • Odde D.J., Cassimeris L., Buettner H.M. Kinetics of microtubule catastrophe assessed by probabilistic analysis. Biophys. J. 1995, 69:796-802.
    • (1995) Biophys. J. , vol.69 , pp. 796-802
    • Odde, D.J.1    Cassimeris, L.2    Buettner, H.M.3
  • 313
    • 1342296567 scopus 로고    scopus 로고
    • A common mechanism for microtubule destabilizers-M type kinesins stabilize curling of the protofilament using the class-specific neck and loops
    • Ogawa T., Nitta R., Okada Y., Hirokawa N. A common mechanism for microtubule destabilizers-M type kinesins stabilize curling of the protofilament using the class-specific neck and loops. Cell 2004, 116:591-602.
    • (2004) Cell , vol.116 , pp. 591-602
    • Ogawa, T.1    Nitta, R.2    Okada, Y.3    Hirokawa, N.4
  • 314
    • 0041941573 scopus 로고    scopus 로고
    • An inner centromere protein that stimulates the microtubule depolymerizing activity of a KinI kinesin
    • Ohi R., Coughlin M.L., Lane W.S., Mitchison T.J. An inner centromere protein that stimulates the microtubule depolymerizing activity of a KinI kinesin. Dev. Cell 2003, 5:309-321.
    • (2003) Dev. Cell , vol.5 , pp. 309-321
    • Ohi, R.1    Coughlin, M.L.2    Lane, W.S.3    Mitchison, T.J.4
  • 315
    • 0024007279 scopus 로고
    • Cold-sensitive and caffeine-supersensitive mutants of the Schizosaccharomyces pombe dis genes implicated in sister chromatid separation during mitosis
    • Ohkura H., Adachi Y., Kinoshita N., Niwa O., Toda T., Yanagida M. Cold-sensitive and caffeine-supersensitive mutants of the Schizosaccharomyces pombe dis genes implicated in sister chromatid separation during mitosis. EMBO J. 1988, 7:1465-1473.
    • (1988) EMBO J. , vol.7 , pp. 1465-1473
    • Ohkura, H.1    Adachi, Y.2    Kinoshita, N.3    Niwa, O.4    Toda, T.5    Yanagida, M.6
  • 316
    • 0035188405 scopus 로고    scopus 로고
    • Dis1/TOG universal microtubule adaptors-one MAP for all?
    • Ohkura H., Garcia M.A., Toda T. Dis1/TOG universal microtubule adaptors-one MAP for all?. J. Cell Sci. 2001, 114:3805-3812.
    • (2001) J. Cell Sci. , vol.114 , pp. 3805-3812
    • Ohkura, H.1    Garcia, M.A.2    Toda, T.3
  • 317
    • 0022850973 scopus 로고
    • Microtubule-associated proteins
    • Olmsted J.B. Microtubule-associated proteins. Annu. Rev. Cell Biol. 1986, 2:421-457.
    • (1986) Annu. Rev. Cell Biol. , vol.2 , pp. 421-457
    • Olmsted, J.B.1
  • 318
    • 72549084707 scopus 로고    scopus 로고
    • Stu1 inversely regulates kinetochore capture and spindle stability
    • Ortiz J., Funk C., Schafer A., Lechner J. Stu1 inversely regulates kinetochore capture and spindle stability. Genes Dev. 2009, 23:2778-2791.
    • (2009) Genes Dev. , vol.23 , pp. 2778-2791
    • Ortiz, J.1    Funk, C.2    Schafer, A.3    Lechner, J.4
  • 319
    • 0028597069 scopus 로고
    • STU1, a suppressor of a beta-tubulin mutation, encodes a novel and essential component of the yeast mitotic spindle
    • Pasqualone D., Huffaker T.C. STU1, a suppressor of a beta-tubulin mutation, encodes a novel and essential component of the yeast mitotic spindle. J. Cell Biol. 1994, 127:1973-1984.
    • (1994) J. Cell Biol. , vol.127 , pp. 1973-1984
    • Pasqualone, D.1    Huffaker, T.C.2
  • 320
    • 0242625186 scopus 로고    scopus 로고
    • The Microtubule plus end-tracking protein EB1 is localized to the flagellar tip and basal bodies in Chlamydomonas reinhardtii
    • Pedersen L.B., Geimer S., Sloboda R.D., Rosenbaum J.L. The Microtubule plus end-tracking protein EB1 is localized to the flagellar tip and basal bodies in Chlamydomonas reinhardtii. Curr. Biol. 2003, 13:1969-1974.
    • (2003) Curr. Biol. , vol.13 , pp. 1969-1974
    • Pedersen, L.B.1    Geimer, S.2    Sloboda, R.D.3    Rosenbaum, J.L.4
  • 322
    • 33749480148 scopus 로고    scopus 로고
    • Mammalian CLASP1 and CLASP2 cooperate to ensure mitotic fidelity by regulating spindle and kinetochore function
    • Pereira A.L., Pereira A.J., Maia A.R., Drabek K., Sayas C.L., Hergert P.J., et al. Mammalian CLASP1 and CLASP2 cooperate to ensure mitotic fidelity by regulating spindle and kinetochore function. Mol. Biol. Cell 2006, 17:4526-4542.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4526-4542
    • Pereira, A.L.1    Pereira, A.J.2    Maia, A.R.3    Drabek, K.4    Sayas, C.L.5    Hergert, P.J.6
  • 323
    • 0033582659 scopus 로고    scopus 로고
    • CLIP-170 highlights growing microtubule ends in vivo
    • Perez F., Diamantopoulos G.S., Stalder R., Kreis T.E. CLIP-170 highlights growing microtubule ends in vivo. Cell 1999, 96:517-527.
    • (1999) Cell , vol.96 , pp. 517-527
    • Perez, F.1    Diamantopoulos, G.S.2    Stalder, R.3    Kreis, T.E.4
  • 324
    • 33748557490 scopus 로고    scopus 로고
    • Tubulin tyrosination is a major factor affecting the recruitment of CAP-Gly proteins at microtubule plus ends
    • Peris L., Thery M., Faure J., Saoudi Y., Lafanechere L., Chilton J.K., et al. Tubulin tyrosination is a major factor affecting the recruitment of CAP-Gly proteins at microtubule plus ends. J. Cell Biol. 2006, 174:839-849.
    • (2006) J. Cell Biol. , vol.174 , pp. 839-849
    • Peris, L.1    Thery, M.2    Faure, J.3    Saoudi, Y.4    Lafanechere, L.5    Chilton, J.K.6
  • 326
    • 48449090926 scopus 로고    scopus 로고
    • The TACC proteins: TACC-ling microtubule dynamics and centrosome function
    • Peset I., Vernos I. The TACC proteins: TACC-ling microtubule dynamics and centrosome function. Trends Cell Biol. 2008, 18:379-388.
    • (2008) Trends Cell Biol. , vol.18 , pp. 379-388
    • Peset, I.1    Vernos, I.2
  • 327
    • 0026793891 scopus 로고
    • CLIP-170 links endocytic vesicles to microtubules
    • Pierre P., Scheel J., Rickard J.E., Kreis T.E. CLIP-170 links endocytic vesicles to microtubules. Cell 1992, 70:887-900.
    • (1992) Cell , vol.70 , pp. 887-900
    • Pierre, P.1    Scheel, J.2    Rickard, J.E.3    Kreis, T.E.4
  • 329
  • 330
    • 0142188568 scopus 로고    scopus 로고
    • Stu2p and XMAP215: turncoat microtubule-associated proteins?
    • Popov A.V., Karsenti E. Stu2p and XMAP215: turncoat microtubule-associated proteins?. Trends Cell Biol. 2003, 13:547-550.
    • (2003) Trends Cell Biol. , vol.13 , pp. 547-550
    • Popov, A.V.1    Karsenti, E.2
  • 333
    • 0036325592 scopus 로고    scopus 로고
    • Dictyostelium EB1 is a genuine centrosomal component required for proper spindle formation
    • Rehberg M., Graf R. Dictyostelium EB1 is a genuine centrosomal component required for proper spindle formation. Mol. Biol. Cell 2002, 13:2301-2310.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2301-2310
    • Rehberg, M.1    Graf, R.2
  • 334
    • 69649098888 scopus 로고    scopus 로고
    • Dynein and Mast/Orbit/CLASP have antagonistic roles in regulating kinetochore-microtubule plus-end dynamics
    • Reis R., Feijao T., Gouveia S., Pereira A.J., Matos I., Sampaio P., et al. Dynein and Mast/Orbit/CLASP have antagonistic roles in regulating kinetochore-microtubule plus-end dynamics. J. Cell Sci. 2009, 122:2543-2553.
    • (2009) J. Cell Sci. , vol.122 , pp. 2543-2553
    • Reis, R.1    Feijao, T.2    Gouveia, S.3    Pereira, A.J.4    Matos, I.5    Sampaio, P.6
  • 335
    • 0026075806 scopus 로고
    • Binding of pp 170 to microtubules is regulated by phosphorylation
    • Rickard J.E., Kreis T.E. Binding of pp 170 to microtubules is regulated by phosphorylation. J. Biol. Chem. 1991, 266:17597-17605.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17597-17605
    • Rickard, J.E.1    Kreis, T.E.2
  • 336
    • 0027535154 scopus 로고
    • Sequence homologies between four cytoskeleton-associated proteins
    • Riehemann K., Sorg C. Sequence homologies between four cytoskeleton-associated proteins. Trends Biochem. Sci. 1993, 18:82-83.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 82-83
    • Riehemann, K.1    Sorg, C.2
  • 337
    • 0037009077 scopus 로고    scopus 로고
    • Drosophila EB1 is important for proper assembly, dynamics, and positioning of the mitotic spindle
    • Rogers S.L., Rogers G.C., Sharp D.J., Vale R.D. Drosophila EB1 is important for proper assembly, dynamics, and positioning of the mitotic spindle. J. Cell Biol. 2002, 158:873-884.
    • (2002) J. Cell Biol. , vol.158 , pp. 873-884
    • Rogers, S.L.1    Rogers, G.C.2    Sharp, D.J.3    Vale, R.D.4
  • 338
    • 6944252346 scopus 로고    scopus 로고
    • Drosophila RhoGEF2 associates with microtubule plus ends in an EB1-dependent manner
    • Rogers S.L., Wiedemann U., Hacker U., Turck C., Vale R.D. Drosophila RhoGEF2 associates with microtubule plus ends in an EB1-dependent manner. Curr. Biol. 2004, 14:1827-1833.
    • (2004) Curr. Biol. , vol.14 , pp. 1827-1833
    • Rogers, S.L.1    Wiedemann, U.2    Hacker, U.3    Turck, C.4    Vale, R.D.5
  • 339
    • 51349104215 scopus 로고    scopus 로고
    • A multicomponent assembly pathway contributes to the formation of acentrosomal microtubule arrays in interphase Drosophila cells
    • Rogers G.C., Rusan N.M., Peifer M., Rogers S.L. A multicomponent assembly pathway contributes to the formation of acentrosomal microtubule arrays in interphase Drosophila cells. Mol. Biol. Cell 2008, 19:3163-3178.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3163-3178
    • Rogers, G.C.1    Rusan, N.M.2    Peifer, M.3    Rogers, S.L.4
  • 340
    • 77952359189 scopus 로고    scopus 로고
    • Aurora A contributes to p150(glued) phosphorylation and function during mitosis
    • Rome P., Montembault E., Franck N., Pascal A., Glover D.M., Giet R. Aurora A contributes to p150(glued) phosphorylation and function during mitosis. J. Cell Biol. 2010, 189:651-659.
    • (2010) J. Cell Biol. , vol.189 , pp. 651-659
    • Rome, P.1    Montembault, E.2    Franck, N.3    Pascal, A.4    Glover, D.M.5    Giet, R.6
  • 341
    • 0141641125 scopus 로고    scopus 로고
    • Maintaining epithelial integrity: a function for gigantic spectraplakin isoforms in adherens junctions
    • Roper K., Brown N.H. Maintaining epithelial integrity: a function for gigantic spectraplakin isoforms in adherens junctions. J. Cell Biol. 2003, 162:1305-1315.
    • (2003) J. Cell Biol. , vol.162 , pp. 1305-1315
    • Roper, K.1    Brown, N.H.2
  • 342
    • 1142302220 scopus 로고    scopus 로고
    • A spectraplakin is enriched on the fusome and organizes microtubules during oocyte specification in Drosophila
    • Roper K., Brown N.H. A spectraplakin is enriched on the fusome and organizes microtubules during oocyte specification in Drosophila. Curr. Biol. 2004, 14:99-110.
    • (2004) Curr. Biol. , vol.14 , pp. 99-110
    • Roper, K.1    Brown, N.H.2
  • 343
    • 0037112997 scopus 로고    scopus 로고
    • The 'spectraplakins': cytoskeletal giants with characteristics of both spectrin and plakin families
    • Roper K., Gregory S.L., Brown N.H. The 'spectraplakins': cytoskeletal giants with characteristics of both spectrin and plakin families. J. Cell Sci. 2002, 115:4215-4225.
    • (2002) J. Cell Sci. , vol.115 , pp. 4215-4225
    • Roper, K.1    Gregory, S.L.2    Brown, N.H.3
  • 344
    • 55949096455 scopus 로고    scopus 로고
    • Putting the model to the test: are APC proteins essential for neuronal polarity, axon outgrowth, and axon targeting?
    • Rusan N.M., Akong K., Peifer M. Putting the model to the test: are APC proteins essential for neuronal polarity, axon outgrowth, and axon targeting?. J. Cell Biol. 2008, 183:203-212.
    • (2008) J. Cell Biol. , vol.183 , pp. 203-212
    • Rusan, N.M.1    Akong, K.2    Peifer, M.3
  • 345
    • 36148937920 scopus 로고    scopus 로고
    • The role of peptide motifs in the evolution of a protein network
    • Saito H., Kashida S., Inoue T., Shiba K. The role of peptide motifs in the evolution of a protein network. Nucleic Acids Res. 2007, 35:6357-6366.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 6357-6366
    • Saito, H.1    Kashida, S.2    Inoue, T.3    Shiba, K.4
  • 346
    • 18044371707 scopus 로고    scopus 로고
    • Microtubules: a ring for the depolymerization motor
    • Salmon E.D. Microtubules: a ring for the depolymerization motor. Curr. Biol. 2005, 15:R299-R302.
    • (2005) Curr. Biol. , vol.15
    • Salmon, E.D.1
  • 347
  • 348
    • 33845683023 scopus 로고    scopus 로고
    • The Schizosaccharomyces pombe EB1 homolog Mal3p binds and stabilizes the microtubule lattice seam
    • Sandblad L., Busch K.E., Tittmann P., Gross H., Brunner D., Hoenger A. The Schizosaccharomyces pombe EB1 homolog Mal3p binds and stabilizes the microtubule lattice seam. Cell 2006, 127:1415-1424.
    • (2006) Cell , vol.127 , pp. 1415-1424
    • Sandblad, L.1    Busch, K.E.2    Tittmann, P.3    Gross, H.4    Brunner, D.5    Hoenger, A.6
  • 349
    • 0030695246 scopus 로고    scopus 로고
    • Reduction of microtubule catastrophe events by LIS1, platelet-activating factor acetylhydrolase subunit
    • Sapir T., Elbaum M., Reiner O. Reduction of microtubule catastrophe events by LIS1, platelet-activating factor acetylhydrolase subunit. EMBO J. 1997, 16:6977-6984.
    • (1997) EMBO J. , vol.16 , pp. 6977-6984
    • Sapir, T.1    Elbaum, M.2    Reiner, O.3
  • 354
    • 0035906940 scopus 로고    scopus 로고
    • Microtubule "plus-end-tracking proteins": the end is just the beginning
    • Schuyler S.C., Pellman D. Microtubule "plus-end-tracking proteins": the end is just the beginning. Cell 2001, 105:421-424.
    • (2001) Cell , vol.105 , pp. 421-424
    • Schuyler, S.C.1    Pellman, D.2
  • 355
    • 73449097193 scopus 로고    scopus 로고
    • Clostridium difficile toxin CDT induces formation of microtubule-based protrusions and increases adherence of bacteria
    • Schwan C., Stecher B., Tzivelekidis T., van Ham M., Rohde M., Hardt W.D., et al. Clostridium difficile toxin CDT induces formation of microtubule-based protrusions and increases adherence of bacteria. PLoS Pathog. 2009, 5:e1000626.
    • (2009) PLoS Pathog. , vol.5
    • Schwan, C.1    Stecher, B.2    Tzivelekidis, T.3    van Ham, M.4    Rohde, M.5    Hardt, W.D.6
  • 356
    • 0030668145 scopus 로고    scopus 로고
    • BIM1 encodes a microtubule-binding protein in yeast
    • Schwartz K., Richards K., Botstein D. BIM1 encodes a microtubule-binding protein in yeast. Mol. Biol. Cell 1997, 8:2677-2691.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2677-2691
    • Schwartz, K.1    Richards, K.2    Botstein, D.3
  • 357
    • 33846695393 scopus 로고    scopus 로고
    • Microtubule plus-end-tracking proteins target gap junctions directly from the cell interior to adherens junctions
    • Shaw R.M., Fay A.J., Puthenveedu M.A., von Zastrow M., Jan Y.N., Jan L.Y. Microtubule plus-end-tracking proteins target gap junctions directly from the cell interior to adherens junctions. Cell 2007, 128:547-560.
    • (2007) Cell , vol.128 , pp. 547-560
    • Shaw, R.M.1    Fay, A.J.2    Puthenveedu, M.A.3    von Zastrow, M.4    Jan, Y.N.5    Jan, L.Y.6
  • 358
    • 0037418576 scopus 로고    scopus 로고
    • Determinants of S. cerevisiae dynein localization and activation: implications for the mechanism of spindle positioning
    • Sheeman B., Carvalho P., Sagot I., Geiser J., Kho D., Hoyt M.A., et al. Determinants of S. cerevisiae dynein localization and activation: implications for the mechanism of spindle positioning. Curr. Biol. 2003, 13:364-372.
    • (2003) Curr. Biol. , vol.13 , pp. 364-372
    • Sheeman, B.1    Carvalho, P.2    Sagot, I.3    Geiser, J.4    Kho, D.5    Hoyt, M.A.6
  • 359
    • 70349113514 scopus 로고    scopus 로고
    • APC2 plays an essential role in axonal projections through the regulation of microtubule stability
    • Shintani T., Ihara M., Tani S., Sakuraba J., Sakuta H., Noda M. APC2 plays an essential role in axonal projections through the regulation of microtubule stability. J. Neurosci. 2009, 29:11628-11640.
    • (2009) J. Neurosci. , vol.29 , pp. 11628-11640
    • Shintani, T.1    Ihara, M.2    Tani, S.3    Sakuraba, J.4    Sakuta, H.5    Noda, M.6
  • 360
    • 0038408571 scopus 로고    scopus 로고
    • Identification of XMAP215 as a microtubule-destabilizing factor in Xenopus egg extract by biochemical purification
    • Shirasu-Hiza M., Coughlin P., Mitchison T. Identification of XMAP215 as a microtubule-destabilizing factor in Xenopus egg extract by biochemical purification. J. Cell Biol. 2003, 161:349-358.
    • (2003) J. Cell Biol. , vol.161 , pp. 349-358
    • Shirasu-Hiza, M.1    Coughlin, P.2    Mitchison, T.3
  • 361
    • 77649086983 scopus 로고    scopus 로고
    • Effect of GFP tags on the localization of EB1 and EB1 fragments in vivo
    • Skube S.B., Chaverri J.M., Goodson H.V. Effect of GFP tags on the localization of EB1 and EB1 fragments in vivo. Cytoskeleton (Hoboken) 2010, 67:1-12.
    • (2010) Cytoskeleton (Hoboken) , vol.67 , pp. 1-12
    • Skube, S.B.1    Chaverri, J.M.2    Goodson, H.V.3
  • 362
    • 70350172940 scopus 로고    scopus 로고
    • The role of TOG domains in microtubule plus end dynamics
    • Slep K.C. The role of TOG domains in microtubule plus end dynamics. Biochem. Soc. Trans. 2009, 37:1002-1006.
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 1002-1006
    • Slep, K.C.1
  • 363
    • 34748862943 scopus 로고    scopus 로고
    • Structural basis of microtubule plus end tracking by XMAP215, CLIP-170, and EB1
    • Slep K.C., Vale R.D. Structural basis of microtubule plus end tracking by XMAP215, CLIP-170, and EB1. Mol. Cell 2007, 27:976-991.
    • (2007) Mol. Cell , vol.27 , pp. 976-991
    • Slep, K.C.1    Vale, R.D.2
  • 364
    • 13944255721 scopus 로고    scopus 로고
    • Structural determinants for EB1-mediated recruitment of APC and spectraplakins to the microtubule plus end
    • Slep K.C., Rogers S.L., Elliott S.L., Ohkura H., Kolodziej P.A., Vale R.D. Structural determinants for EB1-mediated recruitment of APC and spectraplakins to the microtubule plus end. J. Cell Biol. 2005, 168:587-598.
    • (2005) J. Cell Biol. , vol.168 , pp. 587-598
    • Slep, K.C.1    Rogers, S.L.2    Elliott, S.L.3    Ohkura, H.4    Kolodziej, P.A.5    Vale, R.D.6
  • 365
    • 74949132242 scopus 로고    scopus 로고
    • Limited forward trafficking of connexin 43 reduces cell-cell coupling in stressed human and mouse myocardium
    • Smyth J.W., Hong T.T., Gao D., Vogan J.M., Jensen B.C., Fong T.S., et al. Limited forward trafficking of connexin 43 reduces cell-cell coupling in stressed human and mouse myocardium. J. Clin. Invest. 2010, 120:266-279.
    • (2010) J. Clin. Invest. , vol.120 , pp. 266-279
    • Smyth, J.W.1    Hong, T.T.2    Gao, D.3    Vogan, J.M.4    Jensen, B.C.5    Fong, T.S.6
  • 366
    • 0027405349 scopus 로고
    • Recombinant kinesin motor domain binds to beta-tubulin and decorates microtubules with a B surface lattice
    • Song Y.H., Mandelkow E. Recombinant kinesin motor domain binds to beta-tubulin and decorates microtubules with a B surface lattice. Proc. Natl Acad. Sci. USA 1993, 90:1671-1675.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 1671-1675
    • Song, Y.H.1    Mandelkow, E.2
  • 367
    • 34249685610 scopus 로고    scopus 로고
    • Plakins in development and disease
    • Sonnenberg A., Liem R.K. Plakins in development and disease. Exp. Cell Res. 2007, 313:2189-2203.
    • (2007) Exp. Cell Res. , vol.313 , pp. 2189-2203
    • Sonnenberg, A.1    Liem, R.K.2
  • 368
    • 34547120685 scopus 로고    scopus 로고
    • The Drosophila CLASP homologue, Mast/Orbit regulates the dynamic behaviour of interphase microtubules by promoting the pause state
    • Sousa A., Reis R., Sampaio P., Sunkel C.E. The Drosophila CLASP homologue, Mast/Orbit regulates the dynamic behaviour of interphase microtubules by promoting the pause state. Cell Motil. Cytoskeleton 2007, 64:605-620.
    • (2007) Cell Motil. Cytoskeleton , vol.64 , pp. 605-620
    • Sousa, A.1    Reis, R.2    Sampaio, P.3    Sunkel, C.E.4
  • 369
    • 23244462047 scopus 로고    scopus 로고
    • Cik1 targets the minus-end kinesin depolymerase kar3 to microtubule plus ends
    • Sproul L.R., Anderson D.J., Mackey A.T., Saunders W.S., Gilbert S.P. Cik1 targets the minus-end kinesin depolymerase kar3 to microtubule plus ends. Curr. Biol. 2005, 15:1420-1427.
    • (2005) Curr. Biol. , vol.15 , pp. 1420-1427
    • Sproul, L.R.1    Anderson, D.J.2    Mackey, A.T.3    Saunders, W.S.4    Gilbert, S.P.5
  • 370
    • 22944457527 scopus 로고    scopus 로고
    • Identification and characterization of factors required for microtubule growth and nucleation in the early C. elegans embryo
    • Srayko M., Kaya A., Stamford J., Hyman A.A. Identification and characterization of factors required for microtubule growth and nucleation in the early C. elegans embryo. Dev. Cell 2005, 9:223-236.
    • (2005) Dev. Cell , vol.9 , pp. 223-236
    • Srayko, M.1    Kaya, A.2    Stamford, J.3    Hyman, A.A.4
  • 371
    • 54249131103 scopus 로고    scopus 로고
    • Capturing protein tails by CAP-Gly domains
    • Steinmetz M.O., Akhmanova A. Capturing protein tails by CAP-Gly domains. Trends Biochem. Sci. 2008, 33:535-545.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 535-545
    • Steinmetz, M.O.1    Akhmanova, A.2
  • 372
    • 77955657331 scopus 로고    scopus 로고
    • History-dependent catastrophes regulate axonal microtubule behavior
    • Stepanova T., Smal I., van Haren J., Akinci U., Liu Z., Miedema M., et al. History-dependent catastrophes regulate axonal microtubule behavior. Curr. Biol. 2010, 20:1023-1028.
    • (2010) Curr. Biol. , vol.20 , pp. 1023-1028
    • Stepanova, T.1    Smal, I.2    van Haren, J.3    Akinci, U.4    Liu, Z.5    Miedema, M.6
  • 373
    • 77952335884 scopus 로고    scopus 로고
    • Clasp-mediated microtubule bundling regulates persistent motility and contact repulsion in Drosophila macrophages in vivo
    • Stramer B., Moreira S., Millard T., Evans I., Huang C.Y., Sabet O., et al. Clasp-mediated microtubule bundling regulates persistent motility and contact repulsion in Drosophila macrophages in vivo. J. Cell Biol. 2010, 189:681-689.
    • (2010) J. Cell Biol. , vol.189 , pp. 681-689
    • Stramer, B.1    Moreira, S.2    Millard, T.3    Evans, I.4    Huang, C.Y.5    Sabet, O.6
  • 374
    • 34547469942 scopus 로고    scopus 로고
    • EB3 regulates microtubule dynamics at the cell cortex and is required for myoblast elongation and fusion
    • Straube A., Merdes A. EB3 regulates microtubule dynamics at the cell cortex and is required for myoblast elongation and fusion. Curr. Biol. 2007, 17:1318-1325.
    • (2007) Curr. Biol. , vol.17 , pp. 1318-1325
    • Straube, A.1    Merdes, A.2
  • 375
    • 29044443249 scopus 로고    scopus 로고
    • Interaction between EB1 and p150glued is required for anaphase astral microtubule elongation and stimulation of cytokinesis
    • Strickland L.I., Wen Y., Gundersen G.G., Burgess D.R. Interaction between EB1 and p150glued is required for anaphase astral microtubule elongation and stimulation of cytokinesis. Curr. Biol. 2005, 15:2249-2255.
    • (2005) Curr. Biol. , vol.15 , pp. 2249-2255
    • Strickland, L.I.1    Wen, Y.2    Gundersen, G.G.3    Burgess, D.R.4
  • 376
    • 0035862546 scopus 로고    scopus 로고
    • Characterization of human MAPRE genes and their proteins
    • Su L.K., Qi Y. Characterization of human MAPRE genes and their proteins. Genomics 2001, 71:142-149.
    • (2001) Genomics , vol.71 , pp. 142-149
    • Su, L.K.1    Qi, Y.2
  • 378
    • 0037482856 scopus 로고    scopus 로고
    • Shortstop recruits EB1/APC1 and promotes microtubule assembly at the muscle-tendon junction
    • Subramanian A., Prokop A., Yamamoto M., Sugimura K., Uemura T., Betschinger J., et al. Shortstop recruits EB1/APC1 and promotes microtubule assembly at the muscle-tendon junction. Curr. Biol. 2003, 13:1086-1095.
    • (2003) Curr. Biol. , vol.13 , pp. 1086-1095
    • Subramanian, A.1    Prokop, A.2    Yamamoto, M.3    Sugimura, K.4    Uemura, T.5    Betschinger, J.6
  • 379
    • 0018597768 scopus 로고
    • Characteristics of the polar assembly and disassembly of microtubules observed in vitro by darkfield light microscopy
    • Summers K., Kirschner M.W. Characteristics of the polar assembly and disassembly of microtubules observed in vitro by darkfield light microscopy. J. Cell Biol. 1979, 83:205-217.
    • (1979) J. Cell Biol. , vol.83 , pp. 205-217
    • Summers, K.1    Kirschner, M.W.2
  • 380
    • 0035147233 scopus 로고    scopus 로고
    • Characterization of the microtubule binding domain of microtubule actin crosslinking factor (MACF): identification of a novel group of microtubule associated proteins
    • Sun D., Leung C.L., Liem R.K. Characterization of the microtubule binding domain of microtubule actin crosslinking factor (MACF): identification of a novel group of microtubule associated proteins. J. Cell Sci. 2001, 114:161-172.
    • (2001) J. Cell Sci. , vol.114 , pp. 161-172
    • Sun, D.1    Leung, C.L.2    Liem, R.K.3
  • 381
    • 44449137659 scopus 로고    scopus 로고
    • EB1 promotes Aurora-B kinase activity through blocking its inactivation by protein phosphatase 2A
    • Sun L., Gao J., Dong X., Liu M., Li D., Shi X., et al. EB1 promotes Aurora-B kinase activity through blocking its inactivation by protein phosphatase 2A. Proc. Natl Acad. Sci. USA 2008, 105:7153-7158.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 7153-7158
    • Sun, L.1    Gao, J.2    Dong, X.3    Liu, M.4    Li, D.5    Shi, X.6
  • 382
    • 0037128930 scopus 로고    scopus 로고
    • Role of dynein, dynactin, and CLIP-170 interactions in LIS1 kinetochore function
    • Tai C.Y., Dujardin D.L., Faulkner N.E., Vallee R.B. Role of dynein, dynactin, and CLIP-170 interactions in LIS1 kinetochore function. J. Cell Biol. 2002, 156:959-968.
    • (2002) J. Cell Biol. , vol.156 , pp. 959-968
    • Tai, C.Y.1    Dujardin, D.L.2    Faulkner, N.E.3    Vallee, R.B.4
  • 383
    • 30444454338 scopus 로고    scopus 로고
    • CLIP-170 facilitates the formation of kinetochore-microtubule attachments
    • Tanenbaum M.E., Galjart N., van Vugt M.A., Medema R.H. CLIP-170 facilitates the formation of kinetochore-microtubule attachments. EMBO J. 2006, 25:45-57.
    • (2006) EMBO J. , vol.25 , pp. 45-57
    • Tanenbaum, M.E.1    Galjart, N.2    van Vugt, M.A.3    Medema, R.H.4
  • 384
    • 9644259058 scopus 로고    scopus 로고
    • Coupling PAF signaling to dynein regulation: structure of LIS1 in complex with PAF-acetylhydrolase
    • Tarricone C., Perrina F., Monzani S., Massimiliano L., Kim M.H., Derewenda Z.S., et al. Coupling PAF signaling to dynein regulation: structure of LIS1 in complex with PAF-acetylhydrolase. Neuron 2004, 44:809-821.
    • (2004) Neuron , vol.44 , pp. 809-821
    • Tarricone, C.1    Perrina, F.2    Monzani, S.3    Massimiliano, L.4    Kim, M.H.5    Derewenda, Z.S.6
  • 385
    • 0035881576 scopus 로고    scopus 로고
    • CLIP-50 immunolocalization during mouse spermiogenesis suggests a role in shaping the sperm nucleus
    • Tarsounas M., Pearlman R.E., Moens P.B. CLIP-50 immunolocalization during mouse spermiogenesis suggests a role in shaping the sperm nucleus. Dev. Biol. 2001, 236:400-410.
    • (2001) Dev. Biol. , vol.236 , pp. 400-410
    • Tarsounas, M.1    Pearlman, R.E.2    Moens, P.B.3
  • 388
    • 1842854468 scopus 로고    scopus 로고
    • EB1 targets to kinetochores with attached, polymerizing microtubules
    • Tirnauer J.S., Canman J.C., Salmon E.D., Mitchison T.J. EB1 targets to kinetochores with attached, polymerizing microtubules. Mol. Biol. Cell 2002, 13:4308-4316.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4308-4316
    • Tirnauer, J.S.1    Canman, J.C.2    Salmon, E.D.3    Mitchison, T.J.4
  • 389
    • 0036798432 scopus 로고    scopus 로고
    • EB1-microtubule interactions in Xenopus egg extracts: role of EB1 in microtubule stabilization and mechanisms of targeting to microtubules
    • Tirnauer J.S., Grego S., Salmon E.D., Mitchison T.J. EB1-microtubule interactions in Xenopus egg extracts: role of EB1 in microtubule stabilization and mechanisms of targeting to microtubules. Mol. Biol. Cell 2002, 13:3614-3626.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3614-3626
    • Tirnauer, J.S.1    Grego, S.2    Salmon, E.D.3    Mitchison, T.J.4
  • 390
    • 0029742626 scopus 로고    scopus 로고
    • Functionally distinct isoforms of dynactin are expressed in human neurons
    • Tokito M.K., Howland D.S., Lee V.M., Holzbaur E.L. Functionally distinct isoforms of dynactin are expressed in human neurons. Mol. Biol. Cell 1996, 7:1167-1180.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1167-1180
    • Tokito, M.K.1    Howland, D.S.2    Lee, V.M.3    Holzbaur, E.L.4
  • 391
    • 0033792092 scopus 로고    scopus 로고
    • Control of microtubule dynamics by the antagonistic activities of XMAP215 and XKCM1 in Xenopus egg extracts
    • Tournebize R., Popov A., Kinoshita K., Ashford A.J., Rybina S., Pozniakovsky A., et al. Control of microtubule dynamics by the antagonistic activities of XMAP215 and XKCM1 in Xenopus egg extracts. Nat. Cell Biol. 2000, 2:13-19.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 13-19
    • Tournebize, R.1    Popov, A.2    Kinoshita, K.3    Ashford, A.J.4    Rybina, S.5    Pozniakovsky, A.6
  • 392
    • 33947596005 scopus 로고    scopus 로고
    • Integrin-mediated adhesion orients the spindle parallel to the substratum in an EB1- and myosin X-dependent manner
    • Toyoshima F., Nishida E. Integrin-mediated adhesion orients the spindle parallel to the substratum in an EB1- and myosin X-dependent manner. EMBO J. 2007, 26:1487-1498.
    • (2007) EMBO J. , vol.26 , pp. 1487-1498
    • Toyoshima, F.1    Nishida, E.2
  • 394
    • 0025626368 scopus 로고
    • Structural diversity and dynamics of microtubules and polymorphic tubulin assemblies
    • Unger E., Bohm K.J., Vater W. Structural diversity and dynamics of microtubules and polymorphic tubulin assemblies. Electron Microsc. Rev. 1990, 3:355-395.
    • (1990) Electron Microsc. Rev. , vol.3 , pp. 355-395
    • Unger, E.1    Bohm, K.J.2    Vater, W.3
  • 395
    • 0035312694 scopus 로고    scopus 로고
    • LIS1: cellular function of a disease-causing gene
    • Vallee R.B., Tai C., Faulkner N.E. LIS1: cellular function of a disease-causing gene. Trends Cell Biol. 2001, 11:155-160.
    • (2001) Trends Cell Biol. , vol.11 , pp. 155-160
    • Vallee, R.B.1    Tai, C.2    Faulkner, N.E.3
  • 396
    • 0842333851 scopus 로고    scopus 로고
    • Dynein: an ancient motor protein involved in multiple modes of transport
    • Vallee R.B., Williams J.C., Varma D., Barnhart L.E. Dynein: an ancient motor protein involved in multiple modes of transport. J. Neurobiol. 2004, 58:189-200.
    • (2004) J. Neurobiol. , vol.58 , pp. 189-200
    • Vallee, R.B.1    Williams, J.C.2    Varma, D.3    Barnhart, L.E.4
  • 397
    • 0038305620 scopus 로고    scopus 로고
    • Stu2p, the budding yeast member of the conserved Dis1/XMAP215 family of microtubule-associated proteins is a plus end-binding microtubule destabilizer
    • van Breugel M., Drechsel D., Hyman A. Stu2p, the budding yeast member of the conserved Dis1/XMAP215 family of microtubule-associated proteins is a plus end-binding microtubule destabilizer. J. Cell Biol. 2003, 161:359-369.
    • (2003) J. Cell Biol. , vol.161 , pp. 359-369
    • van Breugel, M.1    Drechsel, D.2    Hyman, A.3
  • 398
    • 7044246167 scopus 로고    scopus 로고
    • Molecular dissection of plant cytokinesis and phragmoplast structure: a survey of GFP-tagged proteins
    • Van Damme D., Bouget F.Y., Van Poucke K., Inze D., Geelen D. Molecular dissection of plant cytokinesis and phragmoplast structure: a survey of GFP-tagged proteins. Plant J. 2004, 40:386-398.
    • (2004) Plant J. , vol.40 , pp. 386-398
    • Van Damme, D.1    Bouget, F.Y.2    Van Poucke, K.3    Inze, D.4    Geelen, D.5
  • 401
    • 70349432309 scopus 로고    scopus 로고
    • Mammalian Navigators are microtubule plus-end tracking proteins that can reorganize the cytoskeleton to induce neurite-like extensions
    • van Haren J., Draegestein K., Keijzer N., Abrahams J.P., Grosveld F., Peeters P.J., et al. Mammalian Navigators are microtubule plus-end tracking proteins that can reorganize the cytoskeleton to induce neurite-like extensions. Cell Motil. Cytoskeleton 2009, 66:824-838.
    • (2009) Cell Motil. Cytoskeleton , vol.66 , pp. 824-838
    • van Haren, J.1    Draegestein, K.2    Keijzer, N.3    Abrahams, J.P.4    Grosveld, F.5    Peeters, P.J.6
  • 402
    • 27744548870 scopus 로고    scopus 로고
    • Mechanochemical model of microtubule structure and self-assembly kinetics
    • VanBuren V., Cassimeris L., Odde D.J. Mechanochemical model of microtubule structure and self-assembly kinetics. Biophys. J. 2005, 89:2911-2926.
    • (2005) Biophys. J. , vol.89 , pp. 2911-2926
    • VanBuren, V.1    Cassimeris, L.2    Odde, D.J.3
  • 403
    • 70149111601 scopus 로고    scopus 로고
    • Kinesin-8 motors act cooperatively to mediate length-dependent microtubule depolymerization
    • Varga V., Leduc C., Bormuth V., Diez S., Howard J. Kinesin-8 motors act cooperatively to mediate length-dependent microtubule depolymerization. Cell 2009, 138:1174-1183.
    • (2009) Cell , vol.138 , pp. 1174-1183
    • Varga, V.1    Leduc, C.2    Bormuth, V.3    Diez, S.4    Howard, J.5
  • 404
    • 0028062756 scopus 로고
    • XMAP from Xenopus eggs promotes rapid plus end assembly of microtubules and rapid microtubule polymer turnover
    • Vasquez R.J., Gard D.L., Cassimeris L. XMAP from Xenopus eggs promotes rapid plus end assembly of microtubules and rapid microtubule polymer turnover. J. Cell Biol. 1994, 127:985-993.
    • (1994) J. Cell Biol. , vol.127 , pp. 985-993
    • Vasquez, R.J.1    Gard, D.L.2    Cassimeris, L.3
  • 405
    • 27544464474 scopus 로고    scopus 로고
    • TIP maker and TIP marker; EB1 as a master controller of microtubule plus ends
    • Vaughan K.T. TIP maker and TIP marker; EB1 as a master controller of microtubule plus ends. J. Cell Biol. 2005, 171:197-200.
    • (2005) J. Cell Biol. , vol.171 , pp. 197-200
    • Vaughan, K.T.1
  • 406
    • 0033051741 scopus 로고    scopus 로고
    • Colocalization of cytoplasmic dynein with dynactin and CLIP-170 at microtubule distal ends
    • Vaughan K.T., Tynan S.H., Faulkner N.E., Echeverri C.J., Vallee R.B. Colocalization of cytoplasmic dynein with dynactin and CLIP-170 at microtubule distal ends. J. Cell Sci. 1999, 112(Pt 10):1437-1447.
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 10 , pp. 1437-1447
    • Vaughan, K.T.1    Tynan, S.H.2    Faulkner, N.E.3    Echeverri, C.J.4    Vallee, R.B.5
  • 407
    • 0037157845 scopus 로고    scopus 로고
    • A role for regulated binding of p150(Glued) to microtubule plus ends in organelle transport
    • Vaughan P.S., Miura P., Henderson M., Byrne B., Vaughan K.T. A role for regulated binding of p150(Glued) to microtubule plus ends in organelle transport. J. Cell Biol. 2002, 158:305-319.
    • (2002) J. Cell Biol. , vol.158 , pp. 305-319
    • Vaughan, P.S.1    Miura, P.2    Henderson, M.3    Byrne, B.4    Vaughan, K.T.5
  • 408
  • 410
    • 0026008120 scopus 로고
    • Dilution-induced disassembly of microtubules: relation to dynamic instability and the GTP cap
    • Voter W.A., O'Brien E.T., Erickson H.P. Dilution-induced disassembly of microtubules: relation to dynamic instability and the GTP cap. Cell Motil. Cytoskeleton 1991, 18:55-62.
    • (1991) Cell Motil. Cytoskeleton , vol.18 , pp. 55-62
    • Voter, W.A.1    O'Brien, E.T.2    Erickson, H.P.3
  • 411
    • 38449090921 scopus 로고    scopus 로고
    • Microtubules: an overview
    • Wade R.H. Microtubules: an overview. Methods Mol. Med. 2007, 137:1-16.
    • (2007) Methods Mol. Med. , vol.137 , pp. 1-16
    • Wade, R.H.1
  • 412
    • 70350571135 scopus 로고    scopus 로고
    • On and around microtubules: an overview
    • Wade R.H. On and around microtubules: an overview. Mol. Biotechnol. 2009, 43:177-191.
    • (2009) Mol. Biotechnol. , vol.43 , pp. 177-191
    • Wade, R.H.1
  • 413
    • 0024094432 scopus 로고
    • Dynamic instability of individual microtubules analyzed by video light microscopy: rate constants and transition frequencies
    • Walker R.A., O'Brien E.T., Pryer N.K., Soboeiro M.F., Voter W.A., Erickson H.P., et al. Dynamic instability of individual microtubules analyzed by video light microscopy: rate constants and transition frequencies. J. Cell Biol. 1988, 107:1437-1448.
    • (1988) J. Cell Biol. , vol.107 , pp. 1437-1448
    • Walker, R.A.1    O'Brien, E.T.2    Pryer, N.K.3    Soboeiro, M.F.4    Voter, W.A.5    Erickson, H.P.6
  • 414
    • 0030728492 scopus 로고    scopus 로고
    • Stu2p: a microtubule-binding protein that is an essential component of the yeast spindle pole body
    • Wang P.J., Huffaker T.C. Stu2p: a microtubule-binding protein that is an essential component of the yeast spindle pole body. J. Cell Biol. 1997, 139:1271-1280.
    • (1997) J. Cell Biol. , vol.139 , pp. 1271-1280
    • Wang, P.J.1    Huffaker, T.C.2
  • 415
    • 20544463212 scopus 로고    scopus 로고
    • Nucleotide-dependent bending flexibility of tubulin regulates microtubule assembly
    • Wang H.W., Nogales E. Nucleotide-dependent bending flexibility of tubulin regulates microtubule assembly. Nature 2005, 435:911-915.
    • (2005) Nature , vol.435 , pp. 911-915
    • Wang, H.W.1    Nogales, E.2
  • 416
    • 25444519945 scopus 로고    scopus 로고
    • Assembly of GMPCPP-bound tubulin into helical ribbons and tubes and effect of colchicine
    • Wang H.W., Long S., Finley K.R., Nogales E. Assembly of GMPCPP-bound tubulin into helical ribbons and tubes and effect of colchicine. Cell Cycle 2005, 4:1157-1160.
    • (2005) Cell Cycle , vol.4 , pp. 1157-1160
    • Wang, H.W.1    Long, S.2    Finley, K.R.3    Nogales, E.4
  • 417
    • 10644281068 scopus 로고    scopus 로고
    • Interaction with IQGAP1 links APC to Rac1, Cdc42, and actin filaments during cell polarization and migration
    • Watanabe T., Wang S., Noritake J., Sato K., Fukata M., Takefuji M., et al. Interaction with IQGAP1 links APC to Rac1, Cdc42, and actin filaments during cell polarization and migration. Dev. Cell 2004, 7:871-883.
    • (2004) Dev. Cell , vol.7 , pp. 871-883
    • Watanabe, T.1    Wang, S.2    Noritake, J.3    Sato, K.4    Fukata, M.5    Takefuji, M.6
  • 418
    • 70350020891 scopus 로고    scopus 로고
    • Phosphorylation of CLASP2 by GSK-3beta regulates its interaction with IQGAP1, EB1 and microtubules
    • Watanabe T., Noritake J., Kakeno M., Matsui T., Harada T., Wang S., et al. Phosphorylation of CLASP2 by GSK-3beta regulates its interaction with IQGAP1, EB1 and microtubules. J. Cell Sci. 2009, 122:2969-2979.
    • (2009) J. Cell Sci. , vol.122 , pp. 2969-2979
    • Watanabe, T.1    Noritake, J.2    Kakeno, M.3    Matsui, T.4    Harada, T.5    Wang, S.6
  • 419
    • 33746903069 scopus 로고    scopus 로고
    • Microtubule plus-end loading of p150(Glued) is mediated by EB1 and CLIP-170 but is not required for intracellular membrane traffic in mammalian cells
    • Watson P., Stephens D.J. Microtubule plus-end loading of p150(Glued) is mediated by EB1 and CLIP-170 but is not required for intracellular membrane traffic in mammalian cells. J. Cell Sci. 2006, 119:2758-2767.
    • (2006) J. Cell Sci. , vol.119 , pp. 2758-2767
    • Watson, P.1    Stephens, D.J.2
  • 421
    • 4444360489 scopus 로고    scopus 로고
    • EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and promote cell migration
    • Wen Y., Eng C.H., Schmoranzer J., Cabrera-Poch N., Morris E.J., Chen M., et al. EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and promote cell migration. Nat. Cell Biol. 2004, 6:820-830.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 820-830
    • Wen, Y.1    Eng, C.H.2    Schmoranzer, J.3    Cabrera-Poch, N.4    Morris, E.J.5    Chen, M.6
  • 422
    • 0345169048 scopus 로고    scopus 로고
    • Post-translational modifications regulate microtubule function
    • Westermann S., Weber K. Post-translational modifications regulate microtubule function. Nat. Rev. Mol. Cell Biol. 2003, 4:938-947.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 938-947
    • Westermann, S.1    Weber, K.2
  • 423
    • 35948979262 scopus 로고    scopus 로고
    • Dyneins across eukaryotes: a comparative genomic analysis
    • Wickstead B., Gull K. Dyneins across eukaryotes: a comparative genomic analysis. Traffic 2007, 8:1708-1721.
    • (2007) Traffic , vol.8 , pp. 1708-1721
    • Wickstead, B.1    Gull, K.2
  • 424
    • 3242703137 scopus 로고    scopus 로고
    • Functional complementation of human centromere protein A (CENP-A) by Cse4p from Saccharomyces cerevisiae
    • Wieland G., Orthaus S., Ohndorf S., Diekmann S., Hemmerich P. Functional complementation of human centromere protein A (CENP-A) by Cse4p from Saccharomyces cerevisiae. Mol. Cell. Biol. 2004, 24:6620-6630.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6620-6630
    • Wieland, G.1    Orthaus, S.2    Ohndorf, S.3    Diekmann, S.4    Hemmerich, P.5
  • 425
    • 33751160346 scopus 로고    scopus 로고
    • Microtubule nucleation: gamma-tubulin and beyond
    • Wiese C., Zheng Y. Microtubule nucleation: gamma-tubulin and beyond. J. Cell Sci. 2006, 119:4143-4153.
    • (2006) J. Cell Sci. , vol.119 , pp. 4143-4153
    • Wiese, C.1    Zheng, Y.2
  • 426
    • 59449085251 scopus 로고    scopus 로고
    • EBs clip CLIPs to growing microtubule ends
    • Wittmann T. EBs clip CLIPs to growing microtubule ends. J. Cell Biol. 2008, 183:1183-1185.
    • (2008) J. Cell Biol. , vol.183 , pp. 1183-1185
    • Wittmann, T.1
  • 427
    • 22344435165 scopus 로고    scopus 로고
    • Spatial regulation of CLASP affinity for microtubules by Rac1 and GSK3beta in migrating epithelial cells
    • Wittmann T., Waterman-Storer C.M. Spatial regulation of CLASP affinity for microtubules by Rac1 and GSK3beta in migrating epithelial cells. J. Cell Biol. 2005, 169:929-939.
    • (2005) J. Cell Biol. , vol.169 , pp. 929-939
    • Wittmann, T.1    Waterman-Storer, C.M.2
  • 428
    • 33744733741 scopus 로고    scopus 로고
    • The regulation of microtubule dynamics in Saccharomyces cerevisiae by three interacting plus-end tracking proteins
    • Wolyniak M.J., Blake-Hodek K., Kosco K., Hwang E., You L., Huffaker T.C. The regulation of microtubule dynamics in Saccharomyces cerevisiae by three interacting plus-end tracking proteins. Mol. Biol. Cell 2006, 17:2789-2798.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2789-2798
    • Wolyniak, M.J.1    Blake-Hodek, K.2    Kosco, K.3    Hwang, E.4    You, L.5    Huffaker, T.C.6
  • 430
    • 27544458296 scopus 로고    scopus 로고
    • Melanophilin and myosin Va track the microtubule plus end on EB1
    • Wu X.S., Tsan G.L., Hammer J.A. Melanophilin and myosin Va track the microtubule plus end on EB1. J. Cell Biol. 2005, 171:201-207.
    • (2005) J. Cell Biol. , vol.171 , pp. 201-207
    • Wu, X.S.1    Tsan, G.L.2    Hammer, J.A.3
  • 431
    • 34447101903 scopus 로고    scopus 로고
    • Some assembly required: constructing the elementary units of store-operated Ca2+ entry
    • Wu M.M., Luik R.M., Lewis R.S. Some assembly required: constructing the elementary units of store-operated Ca2+ entry. Cell Calcium 2007, 42:163-172.
    • (2007) Cell Calcium , vol.42 , pp. 163-172
    • Wu, M.M.1    Luik, R.M.2    Lewis, R.S.3
  • 432
    • 52949098421 scopus 로고    scopus 로고
    • ACF7 regulates cytoskeletal-focal adhesion dynamics and migration and has ATPase activity
    • Wu X., Kodama A., Fuchs E. ACF7 regulates cytoskeletal-focal adhesion dynamics and migration and has ATPase activity. Cell 2008, 135:137-148.
    • (2008) Cell , vol.135 , pp. 137-148
    • Wu, X.1    Kodama, A.2    Fuchs, E.3
  • 433
    • 70350023621 scopus 로고    scopus 로고
    • Simulations of tubulin sheet polymers as possible structural intermediates in microtubule assembly
    • Wu Z., Wang H.W., Mu W., Ouyang Z., Nogales E., Xing J. Simulations of tubulin sheet polymers as possible structural intermediates in microtubule assembly. PLoS ONE 2009, 4:e7291.
    • (2009) PLoS ONE , vol.4
    • Wu, Z.1    Wang, H.W.2    Mu, W.3    Ouyang, Z.4    Nogales, E.5    Xing, J.6
  • 434
    • 0037415576 scopus 로고    scopus 로고
    • LIS1 at the microtubule plus end and its role in dynein-mediated nuclear migration
    • Xiang X. LIS1 at the microtubule plus end and its role in dynein-mediated nuclear migration. J. Cell Biol. 2003, 160:289-290.
    • (2003) J. Cell Biol. , vol.160 , pp. 289-290
    • Xiang, X.1
  • 435
    • 0032782945 scopus 로고    scopus 로고
    • Isolation of a new set of Aspergillus nidulans mutants defective in nuclear migration
    • Xiang X., Zuo W., Efimov V.P., Morris N.R. Isolation of a new set of Aspergillus nidulans mutants defective in nuclear migration. Curr. Genet. 1999, 35:626-630.
    • (1999) Curr. Genet. , vol.35 , pp. 626-630
    • Xiang, X.1    Zuo, W.2    Efimov, V.P.3    Morris, N.R.4
  • 436
    • 31944450657 scopus 로고    scopus 로고
    • A complex of two centrosomal proteins, CAP350 and FOP, cooperates with EB1 in microtubule anchoring
    • Yan X., Habedanck R., Nigg E.A. A complex of two centrosomal proteins, CAP350 and FOP, cooperates with EB1 in microtubule anchoring. Mol. Biol. Cell 2006, 17:634-644.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 634-644
    • Yan, X.1    Habedanck, R.2    Nigg, E.A.3
  • 437
    • 70350400765 scopus 로고    scopus 로고
    • Cdc2-mediated phosphorylation of CLIP-170 is essential for its inhibition of centrosome reduplication
    • Yang X., Li H., Liu X.S., Deng A., Liu X. Cdc2-mediated phosphorylation of CLIP-170 is essential for its inhibition of centrosome reduplication. J. Biol. Chem. 2009, 284:28775-28782.
    • (2009) J. Biol. Chem. , vol.284 , pp. 28775-28782
    • Yang, X.1    Li, H.2    Liu, X.S.3    Deng, A.4    Liu, X.5
  • 438
    • 0034739004 scopus 로고    scopus 로고
    • Myosin V orientates the mitotic spindle in yeast
    • Yin H., Pruyne D., Huffaker T.C., Bretscher A. Myosin V orientates the mitotic spindle in yeast. Nature 2000, 406:1013-1015.
    • (2000) Nature , vol.406 , pp. 1013-1015
    • Yin, H.1    Pruyne, D.2    Huffaker, T.C.3    Bretscher, A.4
  • 439
    • 0035985166 scopus 로고    scopus 로고
    • Stu1p is physically associated with beta-tubulin and is required for structural integrity of the mitotic spindle
    • Yin H., You L., Pasqualone D., Kopski K.M., Huffaker T.C. Stu1p is physically associated with beta-tubulin and is required for structural integrity of the mitotic spindle. Mol. Biol. Cell 2002, 13:1881-1892.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1881-1892
    • Yin, H.1    You, L.2    Pasqualone, D.3    Kopski, K.M.4    Huffaker, T.C.5
  • 440
    • 58149239950 scopus 로고    scopus 로고
    • The adenomatous polyposis coli protein is an essential regulator of radial glial polarity and construction of the cerebral cortex
    • Yokota Y., Kim W.Y., Chen Y., Wang X., Stanco A., Komuro Y., et al. The adenomatous polyposis coli protein is an essential regulator of radial glial polarity and construction of the cerebral cortex. Neuron 2009, 61:42-56.
    • (2009) Neuron , vol.61 , pp. 42-56
    • Yokota, Y.1    Kim, W.Y.2    Chen, Y.3    Wang, X.4    Stanco, A.5    Komuro, Y.6
  • 441
    • 70449574092 scopus 로고    scopus 로고
    • EB1 recognizes the nucleotide state of tubulin in the microtubule lattice
    • Zanic M., Stear J.H., Hyman A.A., Howard J. EB1 recognizes the nucleotide state of tubulin in the microtubule lattice. PLoS ONE 2009, 4:e7585.
    • (2009) PLoS ONE , vol.4
    • Zanic, M.1    Stear, J.H.2    Hyman, A.A.3    Howard, J.4
  • 442
    • 0038709367 scopus 로고    scopus 로고
    • Accumulation of cytoplasmic dynein and dynactin at microtubule plus ends in Aspergillus nidulans is kinesin dependent
    • Zhang J., Li S., Fischer R., Xiang X. Accumulation of cytoplasmic dynein and dynactin at microtubule plus ends in Aspergillus nidulans is kinesin dependent. Mol. Biol. Cell 2003, 14:1479-1488.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1479-1488
    • Zhang, J.1    Li, S.2    Fischer, R.3    Xiang, X.4
  • 444
    • 68549121078 scopus 로고    scopus 로고
    • Phosphoregulation of the budding yeast EB1 homologue Bim1p by Aurora/Ipl1p
    • Zimniak T., Stengl K., Mechtler K., Westermann S. Phosphoregulation of the budding yeast EB1 homologue Bim1p by Aurora/Ipl1p. J. Cell Biol. 2009, 186:379-391.
    • (2009) J. Cell Biol. , vol.186 , pp. 379-391
    • Zimniak, T.1    Stengl, K.2    Mechtler, K.3    Westermann, S.4
  • 445
    • 51349158036 scopus 로고    scopus 로고
    • Microtubule plus-end conformations and dynamics in the periphery of interphase mouse fibroblasts
    • Zovko S., Abrahams J.P., Koster A.J., Galjart N., Mommaas A.M. Microtubule plus-end conformations and dynamics in the periphery of interphase mouse fibroblasts. Mol. Biol. Cell 2008, 19:3138-3146.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3138-3146
    • Zovko, S.1    Abrahams, J.P.2    Koster, A.J.3    Galjart, N.4    Mommaas, A.M.5
  • 446
    • 0035176077 scopus 로고    scopus 로고
    • Binding of the adenomatous polyposis coli protein to microtubules increases microtubule stability and is regulated by GSK3 beta phosphorylation
    • Zumbrunn J., Kinoshita K., Hyman A.A., Nathke I.S. Binding of the adenomatous polyposis coli protein to microtubules increases microtubule stability and is regulated by GSK3 beta phosphorylation. Curr. Biol. 2001, 11:44-49.
    • (2001) Curr. Biol. , vol.11 , pp. 44-49
    • Zumbrunn, J.1    Kinoshita, K.2    Hyman, A.A.3    Nathke, I.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.