메뉴 건너뛰기




Volumn 12, Issue 12, 2002, Pages 585-591

Kinesin motors and disease

Author keywords

[No Author keywords available]

Indexed keywords

KINESIN; MOLECULAR MOTOR;

EID: 0036899825     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0962-8924(02)02400-5     Document Type: Review
Times cited : (112)

References (63)
  • 2
    • 0036468983 scopus 로고    scopus 로고
    • Principles of cargo attachment to cytoplasmic motor proteins
    • Kamal A., Goldstein L.S. Principles of cargo attachment to cytoplasmic motor proteins. Curr. Opin. Cell Biol. 14:2002;63-68.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 63-68
    • Kamal, A.1    Goldstein, L.S.2
  • 3
    • 0032548489 scopus 로고    scopus 로고
    • Alternating site mechanism of the kinesin ATPase
    • Gilbert S.P., et al. Alternating site mechanism of the kinesin ATPase. Biochemistry. 37:1998;792-799.
    • (1998) Biochemistry , vol.37 , pp. 792-799
    • Gilbert, S.P.1
  • 4
    • 0032966626 scopus 로고    scopus 로고
    • Structures of kinesin and kinesin-microtubule interactions
    • Mandelkow E., Hoenger A. Structures of kinesin and kinesin-microtubule interactions. Curr. Opin. Cell Biol. 11:1999;34-44.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 34-44
    • Mandelkow, E.1    Hoenger, A.2
  • 5
    • 0343415156 scopus 로고    scopus 로고
    • The way things move: Looking under the hood of molecular motor proteins
    • Vale R.D., Milligan R.A. The way things move: looking under the hood of molecular motor proteins. Science. 288:2000;88-95.
    • (2000) Science , vol.288 , pp. 88-95
    • Vale, R.D.1    Milligan, R.A.2
  • 6
    • 0033591331 scopus 로고    scopus 로고
    • Formation of the compact conformer of kinesin requires a COOH-terminal heavy chain domain and inhibits microtubule-stimulated ATPase activity
    • Stock M.F., et al. Formation of the compact conformer of kinesin requires a COOH-terminal heavy chain domain and inhibits microtubule-stimulated ATPase activity. J. Biol. Chem. 274:1999;14617-14623.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14617-14623
    • Stock, M.F.1
  • 7
    • 0033730445 scopus 로고    scopus 로고
    • Moving on to the cargo problem of microtubule-dependent motors in neurons
    • Terada S., Hirokawa N. Moving on to the cargo problem of microtubule-dependent motors in neurons. Curr. Opin. Neurobiol. 10:2000;566-573.
    • (2000) Curr. Opin. Neurobiol. , vol.10 , pp. 566-573
    • Terada, S.1    Hirokawa, N.2
  • 8
    • 0032559260 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins and the mechanism of organelle transport
    • Hirokawa N. Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science. 279:1998;519-526.
    • (1998) Science , vol.279 , pp. 519-526
    • Hirokawa, N.1
  • 9
    • 0033693656 scopus 로고    scopus 로고
    • A kinesin family tree
    • Kim A.J., Endow S.A. A kinesin family tree. J. Cell Sci. 113:2000;3681-3682.
    • (2000) J. Cell Sci. , vol.113 , pp. 3681-3682
    • Kim, A.J.1    Endow, S.A.2
  • 10
    • 0035912738 scopus 로고    scopus 로고
    • All kinesin superfamily protein, KIF, genes in mouse and human
    • Miki H., et al. All kinesin superfamily protein, KIF, genes in mouse and human. Proc. Natl. Acad. Sci. U. S. A. 98:2001;7004-7011.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 7004-7011
    • Miki, H.1
  • 11
    • 0036469070 scopus 로고    scopus 로고
    • Directionality and processivity of molecular motors
    • Higuchi H., Endow S.A. Directionality and processivity of molecular motors. Curr. Opin. Cell Biol. 14:2002;50-57.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 50-57
    • Higuchi, H.1    Endow, S.A.2
  • 12
    • 0037013148 scopus 로고    scopus 로고
    • Role of phosphatidylinositol(4,5)bisphosphate organization in membrane transport by the Unc104 kinesin motor
    • Klopfenstein D.R., et al. Role of phosphatidylinositol(4,5)bisphosphate organization in membrane transport by the Unc104 kinesin motor. Cell. 109:2002;347-358.
    • (2002) Cell , vol.109 , pp. 347-358
    • Klopfenstein, D.R.1
  • 13
    • 0033534575 scopus 로고    scopus 로고
    • Kin-I kinesins are microtubule-destabilizing enzymes
    • Desai A., et al. Kin-I kinesins are microtubule-destabilizing enzymes. Cell. 96:1999;69-78.
    • (1999) Cell , vol.96 , pp. 69-78
    • Desai, A.1
  • 14
    • 0036242697 scopus 로고    scopus 로고
    • A mechanism for microtubule depolymerization by KinI kinesins
    • Moores C.A., et al. A mechanism for microtubule depolymerization by KinI kinesins. Mol. Cell. 9:2002;903-909.
    • (2002) Mol. Cell , vol.9 , pp. 903-909
    • Moores, C.A.1
  • 15
    • 0033563024 scopus 로고    scopus 로고
    • Motor and cargo interactions
    • Sheetz M.P. Motor and cargo interactions. Eur. J. Biochem. 262:1999;19-25.
    • (1999) Eur. J. Biochem. , vol.262 , pp. 19-25
    • Sheetz, M.P.1
  • 16
    • 0036901166 scopus 로고    scopus 로고
    • Intraflagellar transport and cilia-dependent diseases
    • Pazour, G.J. and Rosenbaum, J. (2002) Intraflagellar transport and cilia-dependent diseases., Trends Cell Biol. 12, 551-555.
    • (2002) Trends Cell Biol. , vol.12 , pp. 551-555
    • Pazour, G.J.1    Rosenbaum, J.2
  • 17
    • 0033022170 scopus 로고    scopus 로고
    • Proteolysis by presenilins and the renaissance of tau protein
    • Haass C., Mandelkow E. Proteolysis by presenilins and the renaissance of tau protein. Trends Cell Biol. 9:1999;241-244.
    • (1999) Trends Cell Biol. , vol.9 , pp. 241-244
    • Haass, C.1    Mandelkow, E.2
  • 18
    • 0029911064 scopus 로고    scopus 로고
    • Kinesin mutations cause motor neuron disease phenotypes by disrupting fast axonal transport in Drosophila
    • Hurd D.D., Saxton W.M. Kinesin mutations cause motor neuron disease phenotypes by disrupting fast axonal transport in Drosophila. Genetics. 144:1996;1075-1085.
    • (1996) Genetics , vol.144 , pp. 1075-1085
    • Hurd, D.D.1    Saxton, W.M.2
  • 19
    • 0035818998 scopus 로고    scopus 로고
    • Kinesin-mediated axonal transport of a membrane compartment containing beta-secretase and presenilin-1 requires APP
    • Kamal A., et al. Kinesin-mediated axonal transport of a membrane compartment containing beta-secretase and presenilin-1 requires APP. Nature. 414:2001;643-648.
    • (2001) Nature , vol.414 , pp. 643-648
    • Kamal, A.1
  • 20
    • 0035809914 scopus 로고    scopus 로고
    • Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules
    • Verhey K.J., et al. Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules. J. Cell Biol. 152:2001;959-970.
    • (2001) J. Cell Biol. , vol.152 , pp. 959-970
    • Verhey, K.J.1
  • 21
    • 0037128935 scopus 로고    scopus 로고
    • Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress
    • Stamer K., et al. Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress. J. Cell Biol. 156:2002;1051-1063.
    • (2002) J. Cell Biol. , vol.156 , pp. 1051-1063
    • Stamer, K.1
  • 22
    • 0035369084 scopus 로고    scopus 로고
    • Charcot-Marie-Tooth disease type 2A caused by mutation in a microtubule motor KIF1Bbeta
    • Zhao C., et al. Charcot-Marie-Tooth disease type 2A caused by mutation in a microtubule motor KIF1Bbeta. Cell. 105:2001;587-597.
    • (2001) Cell , vol.105 , pp. 587-597
    • Zhao, C.1
  • 23
    • 0033754604 scopus 로고    scopus 로고
    • Stirring up development with the heterotrimeric kinesin KIF3
    • Hirokawa N. Stirring up development with the heterotrimeric kinesin KIF3. Traffic. 1:2000;29-34.
    • (2000) Traffic , vol.1 , pp. 29-34
    • Hirokawa, N.1
  • 24
    • 0035912767 scopus 로고    scopus 로고
    • Kinesin molecular motors: Transport pathways, receptors, and human disease
    • Goldstein L.S. Kinesin molecular motors: transport pathways, receptors, and human disease. Proc. Natl. Acad. Sci. U. S. A. 98:2001;6999-7003.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 6999-7003
    • Goldstein, L.S.1
  • 25
    • 0035916823 scopus 로고    scopus 로고
    • An autosomal recessive polycystic kidney disease gene homolog is involved in intraflagellar transport in C. elegans ciliated sensory neurons
    • Qin H., et al. An autosomal recessive polycystic kidney disease gene homolog is involved in intraflagellar transport in C. elegans ciliated sensory neurons. Curr. Biol. 11:2001;457-461.
    • (2001) Curr. Biol. , vol.11 , pp. 457-461
    • Qin, H.1
  • 26
    • 0034697971 scopus 로고    scopus 로고
    • Genetic evidence for selective transport of opsin and arrestin by kinesin-II in mammalian photoreceptors
    • Marszalek J.R., et al. Genetic evidence for selective transport of opsin and arrestin by kinesin-II in mammalian photoreceptors. Cell. 102:2000;175-187.
    • (2000) Cell , vol.102 , pp. 175-187
    • Marszalek, J.R.1
  • 27
    • 0032428685 scopus 로고    scopus 로고
    • Randomization of left-right asymmetry due to loss of nodal cilia generating leftward flow of extraembryonic fluid in mice lacking KIF3B motor protein
    • Nonaka S., et al. Randomization of left-right asymmetry due to loss of nodal cilia generating leftward flow of extraembryonic fluid in mice lacking KIF3B motor protein. Cell. 95:1998;829-837.
    • (1998) Cell , vol.95 , pp. 829-837
    • Nonaka, S.1
  • 28
    • 0033609103 scopus 로고    scopus 로고
    • Situs inversus and embryonic ciliary morphogenesis defects in mouse mutants lacking the KIF3A subunit of kinesin-II
    • Marszalek J.R., et al. Situs inversus and embryonic ciliary morphogenesis defects in mouse mutants lacking the KIF3A subunit of kinesin-II. Proc. Natl. Acad. Sci. U. S. A. 96:1999;5043-5048.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 5043-5048
    • Marszalek, J.R.1
  • 29
    • 0032502817 scopus 로고    scopus 로고
    • A marine natural product inhibitor of kinesin motors
    • Sakowicz R., et al. A marine natural product inhibitor of kinesin motors. Science. 280:1998;292-295.
    • (1998) Science , vol.280 , pp. 292-295
    • Sakowicz, R.1
  • 30
    • 0034646180 scopus 로고    scopus 로고
    • Inhibitors of kinesin activity from structure-based computer screening
    • Hopkins S.C., et al. Inhibitors of kinesin activity from structure-based computer screening. Biochemistry. 39:2000;2805-2814.
    • (2000) Biochemistry , vol.39 , pp. 2805-2814
    • Hopkins, S.C.1
  • 31
    • 0034605123 scopus 로고    scopus 로고
    • Probing spindle assembly mechanisms with monastrol, a small molecule inhibitor of the mitotic kinesin, Eg5
    • Kapoor T.M., et al. Probing spindle assembly mechanisms with monastrol, a small molecule inhibitor of the mitotic kinesin, Eg5. J. Cell Biol. 150:2000;975-988.
    • (2000) J. Cell Biol. , vol.150 , pp. 975-988
    • Kapoor, T.M.1
  • 32
    • 0033874150 scopus 로고    scopus 로고
    • Unnatural ligands for engineered proteins: New tools for chemical genetics
    • Bishop A., et al. Unnatural ligands for engineered proteins: new tools for chemical genetics. Annu. Rev. Biophys. Biomol. Struct. 29:2000;577-606.
    • (2000) Annu. Rev. Biophys. Biomol. Struct. , vol.29 , pp. 577-606
    • Bishop, A.1
  • 33
    • 0034045059 scopus 로고    scopus 로고
    • Direct inhibition of microtubule-based kinesin motility by local anesthetics
    • Miyamoto Y., et al. Direct inhibition of microtubule-based kinesin motility by local anesthetics. Biophys. J. 78:2000;940-949.
    • (2000) Biophys. J. , vol.78 , pp. 940-949
    • Miyamoto, Y.1
  • 34
    • 0033401069 scopus 로고    scopus 로고
    • Neurotoxicants and the cytoskeleton
    • Graham D.G. Neurotoxicants and the cytoskeleton. Curr. Opin. Neurol. 12:1999;733-737.
    • (1999) Curr. Opin. Neurol. , vol.12 , pp. 733-737
    • Graham, D.G.1
  • 35
    • 0033712055 scopus 로고    scopus 로고
    • Kinesin-dependent axonal transport is mediated by the sunday driver (SYD) protein
    • Bowman A.B., et al. Kinesin-dependent axonal transport is mediated by the sunday driver (SYD) protein. Cell. 103:2000;583-594.
    • (2000) Cell , vol.103 , pp. 583-594
    • Bowman, A.B.1
  • 36
    • 0035312694 scopus 로고    scopus 로고
    • LIS1: Cellular function of a disease-causing gene
    • Vallee R.B., et al. LIS1: cellular function of a disease-causing gene. Trends Cell Biol. 11:2001;155-160.
    • (2001) Trends Cell Biol. , vol.11 , pp. 155-160
    • Vallee, R.B.1
  • 37
    • 0034307164 scopus 로고    scopus 로고
    • Mechanisms of viral transport in the cytoplasm
    • Sodeik B. Mechanisms of viral transport in the cytoplasm. Trends Microbiol. 8:2000;465-472.
    • (2000) Trends Microbiol. , vol.8 , pp. 465-472
    • Sodeik, B.1
  • 38
    • 0035736471 scopus 로고    scopus 로고
    • Kinesin-dependent movement on microtubules precedes actin-based motility of vaccinia virus
    • Rietdorf J., et al. Kinesin-dependent movement on microtubules precedes actin-based motility of vaccinia virus. Nat. Cell Biol. 3:2001;992-1000.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 992-1000
    • Rietdorf, J.1
  • 39
    • 17544392731 scopus 로고    scopus 로고
    • Binding of murine leukemia virus Gag polyproteins to KIF4, a microtubule-based motor protein
    • Kim W., et al. Binding of murine leukemia virus Gag polyproteins to KIF4, a microtubule-based motor protein. J. Virol. 72:1998;6898-6901.
    • (1998) J. Virol. , vol.72 , pp. 6898-6901
    • Kim, W.1
  • 40
    • 0033970820 scopus 로고    scopus 로고
    • Dynein- and microtubule-mediated translocation of adenovirus serotype 5 occurs after endosomal lysis
    • Leopold P.L., et al. Dynein- and microtubule-mediated translocation of adenovirus serotype 5 occurs after endosomal lysis. Hum. Gene Ther. 11:2000;151-165.
    • (2000) Hum. Gene Ther. , vol.11 , pp. 151-165
    • Leopold, P.L.1
  • 41
    • 0033821684 scopus 로고    scopus 로고
    • Optimal development of Chlamydophila psittaci in L929 fibroblast and BGM epithelial cells requires the participation of microfilaments and microtubule-motor proteins
    • Escalante-Ochoa C., et al. Optimal development of Chlamydophila psittaci in L929 fibroblast and BGM epithelial cells requires the participation of microfilaments and microtubule-motor proteins. Microb. Pathog. 28:2000;321-333.
    • (2000) Microb. Pathog. , vol.28 , pp. 321-333
    • Escalante-Ochoa, C.1
  • 42
    • 0036124245 scopus 로고    scopus 로고
    • Herpes simplex virus tegument protein US11 interacts with conventional kinesin heavy chain
    • Diefenbach R.J., et al. Herpes simplex virus tegument protein US11 interacts with conventional kinesin heavy chain. J. Virol. 76:2002;3282-3291.
    • (2002) J. Virol. , vol.76 , pp. 3282-3291
    • Diefenbach, R.J.1
  • 43
    • 0034710249 scopus 로고    scopus 로고
    • HIV-1 rev depolymerizes microtubules to form stable bilayered rings
    • Watts N.R., et al. HIV-1 rev depolymerizes microtubules to form stable bilayered rings. J. Cell Biol. 150:2000;349-360.
    • (2000) J. Cell Biol. , vol.150 , pp. 349-360
    • Watts, N.R.1
  • 44
    • 0034865342 scopus 로고    scopus 로고
    • A Drosophila model of HIV-Tat-related pathogenicity
    • Battaglia P.A., et al. A Drosophila model of HIV-Tat-related pathogenicity. J. Cell Sci. 114:2001;2787-2794.
    • (2001) J. Cell Sci. , vol.114 , pp. 2787-2794
    • Battaglia, P.A.1
  • 45
    • 0034738963 scopus 로고    scopus 로고
    • Identification and characterization of a 500-kb homozygously deleted region at 1p36.2-p36.3 in a neuroblastoma cell line
    • Ohira M., et al. Identification and characterization of a 500-kb homozygously deleted region at 1p36.2-p36.3 in a neuroblastoma cell line. Oncogene. 19:2000;4302-4307.
    • (2000) Oncogene , vol.19 , pp. 4302-4307
    • Ohira, M.1
  • 46
    • 0037020237 scopus 로고    scopus 로고
    • The motor protein kinesin-1 links neurofibromin and merlin in a common cellular pathway of neurofibromatosis
    • Hakimi M.A., et al. The motor protein kinesin-1 links neurofibromin and merlin in a common cellular pathway of neurofibromatosis. J. Biol. Chem. 277:2002;36909-36912.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36909-36912
    • Hakimi, M.A.1
  • 47
    • 0034185683 scopus 로고    scopus 로고
    • Identification of the full-length KIAA0591 gene encoding a novel kinesin-related protein which is mapped to the neuroblastoma suppressor gene locus at 1p36.2
    • Nagai M., et al. Identification of the full-length KIAA0591 gene encoding a novel kinesin-related protein which is mapped to the neuroblastoma suppressor gene locus at 1p36.2. Int. J. Oncol. 16:2000;907-916.
    • (2000) Int. J. Oncol. , vol.16 , pp. 907-916
    • Nagai, M.1
  • 48
    • 0033588989 scopus 로고    scopus 로고
    • Defective kinesin heavy chain behavior in mouse kinesin light chain mutants
    • Rahman A., et al. Defective kinesin heavy chain behavior in mouse kinesin light chain mutants. J. Cell Biol. 146:1999;1277-1288.
    • (1999) J. Cell Biol. , vol.146 , pp. 1277-1288
    • Rahman, A.1
  • 49
    • 0033516659 scopus 로고    scopus 로고
    • All-trans**-retinoic acid-mediated growth inhibition involves inhibition of human kinesin-related protein HsEg5
    • Kaiser A., et al. All-trans**-retinoic acid-mediated growth inhibition involves inhibition of human kinesin-related protein HsEg5. J. Biol. Chem. 274:1999;18925-18931.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18925-18931
    • Kaiser, A.1
  • 50
    • 0033786096 scopus 로고    scopus 로고
    • Damage of the kinesin heavy chain gene contributes to the antagonism of cisplatin and paclitaxel
    • Efferth T., et al. Damage of the kinesin heavy chain gene contributes to the antagonism of cisplatin and paclitaxel. Anticancer Res. 20:2000;3211-3219.
    • (2000) Anticancer Res. , vol.20 , pp. 3211-3219
    • Efferth, T.1
  • 51
    • 17744397507 scopus 로고    scopus 로고
    • Kinesin-like protein CENP-E is upregulated in rheumatoid synovial fibroblasts
    • Kullmann F., et al. Kinesin-like protein CENP-E is upregulated in rheumatoid synovial fibroblasts. Arthritis Res. 1:1999;71-80.
    • (1999) Arthritis Res. , vol.1 , pp. 71-80
    • Kullmann, F.1
  • 52
    • 0034684977 scopus 로고    scopus 로고
    • Interaction between GADD34 and kinesin superfamily, KIF3A
    • Hasegawa T., et al. Interaction between GADD34 and kinesin superfamily, KIF3A. Biochem. Biophys. Res. Commun. 267:2000;593-596.
    • (2000) Biochem. Biophys. Res. Commun. , vol.267 , pp. 593-596
    • Hasegawa, T.1
  • 53
    • 0032472369 scopus 로고    scopus 로고
    • The MAP kinase kinase kinase MLK2 co-localizes with activated JNK along microtubules and associates with kinesin superfamily motor KIF3
    • Nagata K., et al. The MAP kinase kinase kinase MLK2 co-localizes with activated JNK along microtubules and associates with kinesin superfamily motor KIF3. EMBO J. 17:1998;149-158.
    • (1998) EMBO J. , vol.17 , pp. 149-158
    • Nagata, K.1
  • 54
    • 0034641135 scopus 로고    scopus 로고
    • Tumor necrosis factor induces hyperphosphorylation of kinesin light chain and inhibits kinesin-mediated transport of mitochondria
    • De Vos K., et al. Tumor necrosis factor induces hyperphosphorylation of kinesin light chain and inhibits kinesin-mediated transport of mitochondria. J. Cell Biol. 149:2000;1207-1214.
    • (2000) J. Cell Biol. , vol.149 , pp. 1207-1214
    • De Vos, K.1
  • 55
    • 0032476645 scopus 로고    scopus 로고
    • Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: Implications for Alzheimer's disease
    • Ebneth A., et al. Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: implications for Alzheimer's disease. J. Cell Biol. 143:1998;777-794.
    • (1998) J. Cell Biol. , vol.143 , pp. 777-794
    • Ebneth, A.1
  • 56
    • 0036469290 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 phosphorylates kinesin light chains and negatively regulates kinesin-based motility
    • Morfini G., et al. Glycogen synthase kinase 3 phosphorylates kinesin light chains and negatively regulates kinesin-based motility. EMBO J. 21:2002;281-293.
    • (2002) EMBO J. , vol.21 , pp. 281-293
    • Morfini, G.1
  • 57
    • 0035834521 scopus 로고    scopus 로고
    • Refined structure of alpha-beta-tubulin at 3.5 A resolution
    • Löwe J., et al. Refined structure of alpha-beta-tubulin at 3.5 A resolution. J. Mol. Biol. 313:2001;1045-1057.
    • (2001) J. Mol. Biol. , vol.313 , pp. 1045-1057
    • Löwe, J.1
  • 58
    • 0031471243 scopus 로고    scopus 로고
    • The crystal structure of dimeric kinesin and implications for microtubule-dependent motility
    • Kozielski F., et al. The crystal structure of dimeric kinesin and implications for microtubule-dependent motility. Cell. 91:1997;985-994.
    • (1997) Cell , vol.91 , pp. 985-994
    • Kozielski, F.1
  • 59
    • 0029965788 scopus 로고    scopus 로고
    • Tetratrico peptide repeats are present in the kinesin light chain
    • Gindhart J.G., Goldstein L.S. Tetratrico peptide repeats are present in the kinesin light chain. Trends Biochem. Sci. 21:1996a;52-53.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 52-53
    • Gindhart, J.G.1    Goldstein, L.S.2
  • 60
    • 0034086882 scopus 로고    scopus 로고
    • Release of kinesin from vesicles by hsc70 and regulation of fast axonal transport
    • Tsai M.Y., et al. Release of kinesin from vesicles by hsc70 and regulation of fast axonal transport. Mol. Biol. Cell. 11:2000;2161-2173.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2161-2173
    • Tsai, M.Y.1
  • 61
    • 0032473425 scopus 로고    scopus 로고
    • The structure of the tetratricopeptide repeats of protein phosphatase 5: Implications for TPR-mediated protein-protein interactions
    • Das A.K., et al. The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. EMBO J. 17:1998;1192-1199.
    • (1998) EMBO J. , vol.17 , pp. 1192-1199
    • Das, A.K.1
  • 62
    • 0000451314 scopus 로고    scopus 로고
    • Armadillo repeats in the SpKAP115 subunit of kinesin-II
    • Gindhart J.G., Goldstein L.S. Armadillo repeats in the SpKAP115 subunit of kinesin-II. Trends Cell Biol. 6:1996b;415-416.
    • (1996) Trends Cell Biol. , vol.6 , pp. 415-416
    • Gindhart, J.G.1    Goldstein, L.S.2
  • 63
    • 0030800831 scopus 로고    scopus 로고
    • Three-dimensional structure of the armadillo repeat region of beta-catenin
    • Huber A.H., et al. Three-dimensional structure of the armadillo repeat region of beta-catenin. Cell. 90:1997;871-882.
    • (1997) Cell , vol.90 , pp. 871-882
    • Huber, A.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.