메뉴 건너뛰기




Volumn 17, Issue 2, 2006, Pages 907-916

Conventional kinesin mediates microtubule-microtubule interactions in vivo

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; KINESIN; KINESIN 1; MUTANT PROTEIN; UNCLASSIFIED DRUG; YELLOW FLUORESCENT PROTEIN;

EID: 31944436781     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E05-06-0542     Document Type: Article
Times cited : (63)

References (57)
  • 1
    • 1642546209 scopus 로고    scopus 로고
    • Calcium signaling is involved in dynein-dependent microtubule organization
    • Adamikova, L., Straube, A., Schulz, I., and Steinberg, G. (2004). Calcium signaling is involved in dynein-dependent microtubule organization. Mol. Biol. Cell 15, 1969-1980.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1969-1980
    • Adamikova, L.1    Straube, A.2    Schulz, I.3    Steinberg, G.4
  • 2
    • 0029127631 scopus 로고
    • Membrane traffic motors
    • Allan, V. (1995). Membrane traffic motors. FEBS Lett 369, 101-106.
    • (1995) FEBS Lett , vol.369 , pp. 101-106
    • Allan, V.1
  • 3
    • 0023116649 scopus 로고
    • Kinesin from pig brain studied by electron microscopy
    • Amos, L. A. (1987). Kinesin from pig brain studied by electron microscopy. J. Cell Sci. 87, 105-111.
    • (1987) J. Cell Sci. , vol.87 , pp. 105-111
    • Amos, L.A.1
  • 5
    • 0036140644 scopus 로고    scopus 로고
    • Microtubule transport in the axon
    • Baas, P. W. (2002). Microtubule transport in the axon. Int. Rev. Cytol. 222, 41-62.
    • (2002) Int. Rev. Cytol. , vol.222 , pp. 41-62
    • Baas, P.W.1
  • 6
    • 0000451727 scopus 로고
    • Different a alleles of Ustilago maydis are necessary for maintenance of filamentous growth but not for meiosis
    • Banuett, F., and Herskowitz, I. (1989). Different a alleles of Ustilago maydis are necessary for maintenance of filamentous growth but not for meiosis. Proc. Natl. Acad. Sci. USA 86, 5878-5882.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5878-5882
    • Banuett, F.1    Herskowitz, I.2
  • 7
    • 0029449733 scopus 로고
    • Motor proteins 1, kinesins
    • Bloom, G. S., and Endow, S. A. (1995). Motor proteins 1, kinesins. Protein Profile 2, 1105-1171.
    • (1995) Protein Profile , vol.2 , pp. 1105-1171
    • Bloom, G.S.1    Endow, S.A.2
  • 8
    • 0030451029 scopus 로고    scopus 로고
    • Isolation of a carbon source-regulated gene from Ustilago maydis
    • Bottin, A., Kamper, J., and Kahmann, R. (1996). Isolation of a carbon source-regulated gene from Ustilago maydis. Mol. Gen. Genet. 253, 342-352.
    • (1996) Mol. Gen. Genet. , vol.253 , pp. 342-352
    • Bottin, A.1    Kamper, J.2    Kahmann, R.3
  • 9
    • 0021808444 scopus 로고
    • A novel brain ATPase with properties expected for the fast axonal transport motor
    • Brady, S. T. (1985). A novel brain ATPase with properties expected for the fast axonal transport motor. Nature 327, 73-75.
    • (1985) Nature , vol.327 , pp. 73-75
    • Brady, S.T.1
  • 11
    • 0024202112 scopus 로고
    • Real-time observations of microtubule dynamic instability in living cells
    • Cassimeris, L., Pryer, N. K., and Salmon, E. D. (1988). Real-time observations of microtubule dynamic instability in living cells. J. Cell Biol. 207, 2223-2231.
    • (1988) J. Cell Biol. , vol.207 , pp. 2223-2231
    • Cassimeris, L.1    Pryer, N.K.2    Salmon, E.D.3
  • 12
    • 0033193864 scopus 로고    scopus 로고
    • Kinesin's tail domain is an inhibitory regulator of the motor domain
    • Coy, D. L., Hancock, W. O., Wagenbach, M., and Howard, J. (1999). Kinesin's tail domain is an inhibitory regulator of the motor domain. Nat. Cell Biol. 2, 288-292.
    • (1999) Nat. Cell Biol. , vol.2 , pp. 288-292
    • Coy, D.L.1    Hancock, W.O.2    Wagenbach, M.3    Howard, J.4
  • 13
    • 0032564307 scopus 로고    scopus 로고
    • The C-terminal region of the stalk domain of ubiquitous human kinesin heavy chain contains the binding site for kinesin light chain
    • Diefenbach, R. J., Mackay, J. P., Armati, P. J., and Cunningham, A. L. (1998). The C-terminal region of the stalk domain of ubiquitous human kinesin heavy chain contains the binding site for kinesin light chain. Biochemistry 37, 16663-16670.
    • (1998) Biochemistry , vol.37 , pp. 16663-16670
    • Diefenbach, R.J.1    Mackay, J.P.2    Armati, P.J.3    Cunningham, A.L.4
  • 14
    • 0033195492 scopus 로고    scopus 로고
    • Single-molecule analysis of kinesin motility reveals regulation by the cargo-binding tail domain
    • Friedman, D. S., and Vale, R. D. (1999). Single-molecule analysis of kinesin motility reveals regulation by the cargo-binding tail domain. Nat. Cell Biol. 2, 293-297.
    • (1999) Nat. Cell Biol. , vol.2 , pp. 293-297
    • Friedman, D.S.1    Vale, R.D.2
  • 16
    • 0032080019 scopus 로고    scopus 로고
    • Cloning and functional expression of a 'fast' fungal kinesin
    • Grummt, M., Pistor, S., Lottspeich, F., and Schliwa, M. (1998). Cloning and functional expression of a 'fast' fungal kinesin. FEBS Lett. 427, 79-84.
    • (1998) FEBS Lett. , vol.427 , pp. 79-84
    • Grummt, M.1    Pistor, S.2    Lottspeich, F.3    Schliwa, M.4
  • 17
    • 0033771901 scopus 로고    scopus 로고
    • Kinesin's IAK tail domain inhibits initial microtubule-stimulated ADP release
    • Hackney, D. D., and Stock, M. F. (2000). Kinesin's IAK tail domain inhibits initial microtubule-stimulated ADP release. Nat. Cell Biol. 2, 257-260.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 257-260
    • Hackney, D.D.1    Stock, M.F.2
  • 18
    • 0032559260 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins and the mechanism of organelle transport
    • Hirokawa, N. (1998). Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science 279, 519-526.
    • (1998) Science , vol.279 , pp. 519-526
    • Hirokawa, N.1
  • 19
    • 0024591237 scopus 로고
    • Submolecular domains of bovine brain kinesin identified by electron microscopy and monoclonal antibody decoration
    • Hirokawa, N., Pfister, K. K., Yorifuji, H., Wagner, M. C., Brady, S. T., and Bloom, G. S. (1989). Submolecular domains of bovine brain kinesin identified by electron microscopy and monoclonal antibody decoration. Cell 56, 867-878.
    • (1989) Cell , vol.56 , pp. 867-878
    • Hirokawa, N.1    Pfister, K.K.2    Yorifuji, H.3    Wagner, M.C.4    Brady, S.T.5    Bloom, G.S.6
  • 21
    • 0032972965 scopus 로고    scopus 로고
    • Identification of microtubule binding sites in the Ned tail domain
    • Karabay, A., and Walker, R. A. (1999). Identification of microtubule binding sites in the Ned tail domain. Biochemistry 38, 1838-1849.
    • (1999) Biochemistry , vol.38 , pp. 1838-1849
    • Karabay, A.1    Walker, R.A.2
  • 22
    • 0030831244 scopus 로고    scopus 로고
    • The bimC family of kinesins: Essential bipolar mitotic motors driving centrosome separation
    • Kashina, A. S., Rogers, G. C., and Scholey, J. M. (1997). The bimC family of kinesins: essential bipolar mitotic motors driving centrosome separation. Biochim. Biophys. Acta 1357, 257-271.
    • (1997) Biochim. Biophys. Acta , vol.1357 , pp. 257-271
    • Kashina, A.S.1    Rogers, G.C.2    Scholey, J.M.3
  • 23
    • 0032854874 scopus 로고    scopus 로고
    • Universal and unique features of kinesin motors: Insights from a comparison of fungal and animal conventional kinesins
    • Kirchner, J., Woehlke, G., and Schliwa, M. (1999). Universal and unique features of kinesin motors: insights from a comparison of fungal and animal conventional kinesins. Biol. Chem. 380, 915-921.
    • (1999) Biol. Chem. , vol.380 , pp. 915-921
    • Kirchner, J.1    Woehlke, G.2    Schliwa, M.3
  • 24
    • 0042020010 scopus 로고    scopus 로고
    • Kinesin motors and microtubule-based organelle transport in Dictyostelium discoideum
    • Klopfenstein, D. R., Holleran, E. A., and Vale, R. D. (2002). Kinesin motors and microtubule-based organelle transport in Dictyostelium discoideum. J. Muscle Res. Cell Motil. 23, 631-638.
    • (2002) J. Muscle Res. Cell Motil. , vol.23 , pp. 631-638
    • Klopfenstein, D.R.1    Holleran, E.A.2    Vale, R.D.3
  • 26
    • 0023660880 scopus 로고
    • Active sliding between cytoplasmic microtubules
    • Koonce, M. P., Tong, J., Euteneuer, U., and Schliwa, M. (1987). Active sliding between cytoplasmic microtubules. Nature 328, 737-739.
    • (1987) Nature , vol.328 , pp. 737-739
    • Koonce, M.P.1    Tong, J.2    Euteneuer, U.3    Schliwa, M.4
  • 27
    • 4644349081 scopus 로고    scopus 로고
    • A standardized kinesin nomenclature
    • Lawrence, C. J., et al. (2004). A standardized kinesin nomenclature. J. Cell Biol. 167, 19-22.
    • (2004) J. Cell Biol. , vol.167 , pp. 19-22
    • Lawrence, C.J.1
  • 28
    • 0030998212 scopus 로고    scopus 로고
    • Identification of a motor protein required for filamentous growth in Ustilago maydis
    • Lehmler, C., Steinberg, G., Snetselaar, K. M., Schliwa, M., Kahmann, R., and Bolker, M. (1997). Identification of a motor protein required for filamentous growth in Ustilago maydis. EMBO J. 26, 3464-3473.
    • (1997) EMBO J. , vol.26 , pp. 3464-3473
    • Lehmler, C.1    Steinberg, G.2    Snetselaar, K.M.3    Schliwa, M.4    Kahmann, R.5    Bolker, M.6
  • 29
    • 0025309665 scopus 로고
    • KAR3, a kinesin-related gene required for yeast nuclear fusion
    • Meluh, P. B., and Rose, M. D. (1990). KAR3, a kinesin-related gene required for yeast nuclear fusion. Cell 60, 1029-1041.
    • (1990) Cell , vol.60 , pp. 1029-1041
    • Meluh, P.B.1    Rose, M.D.2
  • 30
    • 0027128667 scopus 로고
    • Self-organization of polymer-motor systems in the cytoskeleton
    • Mitchison, T. J. (1992). Self-organization of polymer-motor systems in the cytoskeleton. Phil. Trans. R. Soc. Lond. B Biol. Sci. 336, 99-106.
    • (1992) Phil. Trans. R. Soc. Lond. B Biol. Sci. , vol.336 , pp. 99-106
    • Mitchison, T.J.1
  • 31
    • 0026632855 scopus 로고
    • Cloning and expression of a human kinesin heavy chain gene: Interaction of the COOH-terminal domain with cytoplasmic microtubules in transfected CV-1 cells
    • Navone, F., Niclas, J., Hom-Booher, N., Sparks, L., Bernstein, H. D., McCaffrey, G., and Vale, R. D. (1992). Cloning and expression of a human kinesin heavy chain gene: interaction of the COOH-terminal domain with cytoplasmic microtubules in transfected CV-1 cells. J. Cell Biol. 227, 1263-1275.
    • (1992) J. Cell Biol. , vol.227 , pp. 1263-1275
    • Navone, F.1    Niclas, J.2    Hom-Booher, N.3    Sparks, L.4    Bernstein, H.D.5    McCaffrey, G.6    Vale, R.D.7
  • 32
    • 0033588989 scopus 로고    scopus 로고
    • Defective kinesin heavy chain behaviour in mouse kinesin light chain mutants
    • Rahmann, A., Kamal, A., Roberts, E. A., and Goldstein, L. S. (1999). Defective kinesin heavy chain behaviour in mouse kinesin light chain mutants. J. Cell Biol. 146, 1277-1288.
    • (1999) J. Cell Biol. , vol.146 , pp. 1277-1288
    • Rahmann, A.1    Kamal, A.2    Roberts, E.A.3    Goldstein, L.S.4
  • 33
    • 0037992582 scopus 로고    scopus 로고
    • A complete inventory of fungal kinesins in representative filamentous ascomycetes
    • Schoch, C. L., Aist, J. R., Yoder, O. C., and Gillian Turgeon, B. (2003). A complete inventory of fungal kinesins in representative filamentous ascomycetes. Fungal Genet. Biol. 39, 1-15.
    • (2003) Fungal Genet. Biol. , vol.39 , pp. 1-15
    • Schoch, C.L.1    Aist, J.R.2    Yoder, O.C.3    Gillian Turgeon, B.4
  • 34
    • 0024597974 scopus 로고
    • Identification of globular mechanochemical heads of kinesin
    • Scholey, J. M., Heuser, J., Yang, J. T., and Goldstein, L.S.B. (1989). Identification of globular mechanochemical heads of kinesin. Nature 338, 355-357.
    • (1989) Nature , vol.338 , pp. 355-357
    • Scholey, J.M.1    Heuser, J.2    Yang, J.T.3    Goldstein, L.S.B.4
  • 35
    • 0022371050 scopus 로고
    • Identification of kinesin in sea urchin eggs, and evidence for its localization in the mitotic spindle
    • Scholey, J. M., Porter, M. E., Grissom, P. M., and McIntosh, J. R. (1985). Identification of kinesin in sea urchin eggs, and evidence for its localization in the mitotic spindle. Nature 328, 483-486.
    • (1985) Nature , vol.328 , pp. 483-486
    • Scholey, J.M.1    Porter, M.E.2    Grissom, P.M.3    McIntosh, J.R.4
  • 36
    • 27644561872 scopus 로고    scopus 로고
    • Myosin-V, kinesin-1 and kinesin-3 cooperate in long-distance transport in hyphal growth of the fungus Ustilago maydis
    • Schuchardt, I., Aßmann, D., Thines, E., Schuberth, C., and Steinberg, G. (2005). Myosin-V, kinesin-1 and kinesin-3 cooperate in long-distance transport in hyphal growth of the fungus Ustilago maydis. Mol. Biol. Cell 26, 5191-5201.
    • (2005) Mol. Biol. Cell , vol.26 , pp. 5191-5201
    • Schuchardt, I.1    Aßmann, D.2    Thines, E.3    Schuberth, C.4    Steinberg, G.5
  • 38
    • 0038605070 scopus 로고    scopus 로고
    • The second microtubule-binding site of monomeric kid enhances the microtubule affinity
    • Shiroguchi, K., Ohsugi, M., Edamatsu, M., Yamamoto, T., and Toyoshima, Y. Y. (2003). The second microtubule-binding site of monomeric kid enhances the microtubule affinity. J. Biol. Chem. 278, 22460-22465.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22460-22465
    • Shiroguchi, K.1    Ohsugi, M.2    Edamatsu, M.3    Yamamoto, T.4    Toyoshima, Y.Y.5
  • 39
    • 0028157982 scopus 로고
    • The carboxyl-terminal domain of kinesin heavy chain is important for membrane binding
    • Skoufias, D. A., Cole, D. G., Wedaman, K. P., and Scholey, J. M. (1994). The carboxyl-terminal domain of kinesin heavy chain is important for membrane binding. J. Biol. Chem. 269, 1477-1485.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1477-1485
    • Skoufias, D.A.1    Cole, D.G.2    Wedaman, K.P.3    Scholey, J.M.4
  • 40
    • 0030972867 scopus 로고    scopus 로고
    • A kinesin-like mechanoenzyme from the zygomycete Sycephalastrum racemosum shows biochemical similarities with conventional kinesin from Neurospora crassa
    • Steinberg, G. (1997). A kinesin-like mechanoenzyme from the zygomycete Sycephalastrum racemosum shows biochemical similarities with conventional kinesin from Neurospora crassa. Eur. J. Cell Biol. 73, 124-131.
    • (1997) Eur. J. Cell Biol. , vol.73 , pp. 124-131
    • Steinberg, G.1
  • 41
    • 0028826175 scopus 로고
    • The Neurospora organelle motor: A distant relative of conventional kinesin with unconventional properties
    • Steinberg, G., and Schliwa, M. (1995). The Neurospora organelle motor: a distant relative of conventional kinesin with unconventional properties. Mol. Biol. Cell 6, 1605-1618.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1605-1618
    • Steinberg, G.1    Schliwa, M.2
  • 42
    • 0029980479 scopus 로고    scopus 로고
    • Characterization of the biophysical and motility properties of kinesin from the fungus Neurospora crassa
    • Steinberg, G., and Schliwa, M. (1996). Characterization of the biophysical and motility properties of kinesin from the fungus Neurospora crassa. J. Biol. Chem. 271, 7516-7521.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7516-7521
    • Steinberg, G.1    Schliwa, M.2
  • 43
    • 0031688364 scopus 로고    scopus 로고
    • Kinesin from the plant pathogenic fungus Ustilago maydis is involved in vacuole formation and cytoplasmic migration
    • Steinberg, G., Schliwa, M., Lehmler, C., Bolker, M., Kahmann, R., and McIntosh, J. R. (1998). Kinesin from the plant pathogenic fungus Ustilago maydis is involved in vacuole formation and cytoplasmic migration. J. Cell Sci. 111, 2235-2246.
    • (1998) J. Cell Sci. , vol.111 , pp. 2235-2246
    • Steinberg, G.1    Schliwa, M.2    Lehmler, C.3    Bolker, M.4    Kahmann, R.5    McIntosh, J.R.6
  • 44
    • 0035117421 scopus 로고    scopus 로고
    • Microtubules in the fungal pathogen Ustilago maydis are highly dynamic and determine cell polarity
    • Steinberg, G., Wedlich-Soldner, R., Brill, M., and Schulz, I. (2001). Microtubules in the fungal pathogen Ustilago maydis are highly dynamic and determine cell polarity. J. Cell Sci. 114, 609-622.
    • (2001) J. Cell Sci. , vol.114 , pp. 609-622
    • Steinberg, G.1    Wedlich-Soldner, R.2    Brill, M.3    Schulz, I.4
  • 45
    • 0033591331 scopus 로고    scopus 로고
    • Formation of the compact confomer of kinesin requires a COOH-terminal heavy chain domain and inhibits microtubule-stimulated ATPase activity
    • Stock, M. F., Guerrero, J., Cobb, B., Eggers, C. T., Huang, T. G., Li, X., and Hackney, D. D. (1999). Formation of the compact confomer of kinesin requires a COOH-terminal heavy chain domain and inhibits microtubule-stimulated ATPase activity. J. Biol. Chem. 274, 14617-14623.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14617-14623
    • Stock, M.F.1    Guerrero, J.2    Cobb, B.3    Eggers, C.T.4    Huang, T.G.5    Li, X.6    Hackney, D.D.7
  • 46
    • 0037329235 scopus 로고    scopus 로고
    • Microtubule organization requires cell cycle-dependent nucleation at dispersed cytoplasmic sites: Polar and perinuclear microtubule organizing centers in the plant pathogen Ustilago maydis
    • Straube, A., Brill, M., Oakley, B. R., Horio, T., and Steinberg, G. (2003). Microtubule organization requires cell cycle-dependent nucleation at dispersed cytoplasmic sites: polar and perinuclear microtubule organizing centers in the plant pathogen Ustilago maydis. Mol. Biol. Cell 14, 642-657.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 642-657
    • Straube, A.1    Brill, M.2    Oakley, B.R.3    Horio, T.4    Steinberg, G.5
  • 48
    • 0025930998 scopus 로고
    • Microtubule behavior in the growth cones of living neurons during axon elongation
    • Tanaka, E. M., and Kirschner, M. W. (1991). Microtubule behavior in the growth cones of living neurons during axon elongation. J. Cell Biol. 115, 345-363.
    • (1991) J. Cell Biol. , vol.115 , pp. 345-363
    • Tanaka, E.M.1    Kirschner, M.W.2
  • 49
    • 0026009462 scopus 로고
    • Purified kinesin promotes vesicle motility and induces active sliding between microtubules in vitro
    • Urrutia, R., McNiven, M. A., Albanesi, J. P., Murphy, D. B., and Kachar, B. (1991). Purified kinesin promotes vesicle motility and induces active sliding between microtubules in vitro. Proc. Natl. Acad. Sci. USA 88, 6701-6705.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6701-6705
    • Urrutia, R.1    McNiven, M.A.2    Albanesi, J.P.3    Murphy, D.B.4    Kachar, B.5
  • 50
    • 0022385727 scopus 로고
    • Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility
    • Vale, R. D., Reese, T. S., and Sheetz, M. P. (1985). Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility. Cell 42, 39-50.
    • (1985) Cell , vol.42 , pp. 39-50
    • Vale, R.D.1    Reese, T.S.2    Sheetz, M.P.3
  • 52
    • 13144251122 scopus 로고    scopus 로고
    • A model for the proposed roles of different microtubule-based motor proteins in establishing spindle bipolarity
    • Walczak, C. E., Vernos, I., Mitchison, T. J., Karsenti, E., and Heald, R. (1998). A model for the proposed roles of different microtubule-based motor proteins in establishing spindle bipolarity. Curr. Biol. 8, 903-913.
    • (1998) Curr. Biol. , vol.8 , pp. 903-913
    • Walczak, C.E.1    Vernos, I.2    Mitchison, T.J.3    Karsenti, E.4    Heald, R.5
  • 53
    • 0037124364 scopus 로고    scopus 로고
    • A balance of KIF1A-like kinesin and dynein organizes early endosomes in the fungus Ustilago maydis
    • Wedlich-Soldner, R., Straube, A., Friedrich, M. W., and Steinberg, G. (2002). A balance of KIF1A-like kinesin and dynein organizes early endosomes in the fungus Ustilago maydis. EMBO J. 21, 2946-2957.
    • (2002) EMBO J. , vol.21 , pp. 2946-2957
    • Wedlich-Soldner, R.1    Straube, A.2    Friedrich, M.W.3    Steinberg, G.4
  • 54
    • 0034351418 scopus 로고    scopus 로고
    • The molecular motors of cilia and eukaryotic flagella
    • Woolley, D. (2000). The molecular motors of cilia and eukaryotic flagella. Essays Biochem. 35, 103-115.
    • (2000) Essays Biochem. , vol.35 , pp. 103-115
    • Woolley, D.1
  • 55
    • 0031932986 scopus 로고    scopus 로고
    • A fungal kinesin required for Organelle motility, hyphal growth, and morphogenesis
    • Wu, Q., Sandrock, T. M., Turgeon, B. G., Yoder, O. C., Wirsel, S. G., and Aist, J. R. (1998). A fungal kinesin required for Organelle motility, hyphal growth, and morphogenesis. Mol. Biol. Cell 9, 89-101.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 89-101
    • Wu, Q.1    Sandrock, T.M.2    Turgeon, B.G.3    Yoder, O.C.4    Wirsel, S.G.5    Aist, J.R.6
  • 56
    • 0024550571 scopus 로고
    • A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses
    • Yang, J. T., Laymon, R. A., and Goldstein, L. S. (1989). A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses. Cell 56, 879-889.
    • (1989) Cell , vol.56 , pp. 879-889
    • Yang, J.T.1    Laymon, R.A.2    Goldstein, L.S.3
  • 57
    • 0025362646 scopus 로고
    • Evidence that the head of kinesin is sufficient for force generation and motility in vitro
    • Yang, J. T., Saxton, W. M., Stewart, R. J., Raff, E. C., and Goldstein, L.S.B. (1990). Evidence that the head of kinesin is sufficient for force generation and motility in vitro. Science 249, 42-47.
    • (1990) Science , vol.249 , pp. 42-47
    • Yang, J.T.1    Saxton, W.M.2    Stewart, R.J.3    Raff, E.C.4    Goldstein, L.S.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.