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Volumn 7, Issue 3, 1996, Pages 311-320

Functional and molecular diversity of dynein heavy chains

Author keywords

Cilia and flagella; Dynein; Isoforms; Motor proteins

Indexed keywords

EUKARYOTA;

EID: 0000822371     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1006/scdb.1996.0040     Document Type: Article
Times cited : (10)

References (75)
  • 1
    • 37049239183 scopus 로고
    • Dynein: A protein with adenosine triphosphatase activity from cilia
    • Gibbons IR, Rowe AJ (1965) Dynein: a protein with adenosine triphosphatase activity from cilia. Science 149:424-426
    • (1965) Science , vol.149 , pp. 424-426
    • Gibbons, I.R.1    Rowe, A.J.2
  • 2
    • 84935756758 scopus 로고
    • Studies on cilia. II. Examination of the distal region of the ciliary shaft and the role of the filaments in motility
    • Satir P (1965) Studies on cilia. II. Examination of the distal region of the ciliary shaft and the role of the filaments in motility. J Cell Biol 26:805-834
    • (1965) J Cell Biol , vol.26 , pp. 805-834
    • Satir, P.1
  • 3
    • 0015188644 scopus 로고
    • Adenosine-triphosphate induced sliding of tubules in trypsin-treated flagella of sea-urchin sperm
    • Summers KE, Gibbons IR (1971) Adenosine-triphosphate induced sliding of tubules in trypsin-treated flagella of sea-urchin sperm. Proc Natl Acad Sci USA 68:3092-3096
    • (1971) Proc Natl Acad Sci USA , vol.68 , pp. 3092-3096
    • Summers, K.E.1    Gibbons, I.R.2
  • 4
    • 0015132091 scopus 로고
    • Bend propagation by a sliding filament model for flagella
    • Brokaw CJ (1971) Bend propagation by a sliding filament model for flagella. J Exp Biol 55:289-304
    • (1971) J Exp Biol , vol.55 , pp. 289-304
    • Brokaw, C.J.1
  • 5
    • 0006163872 scopus 로고
    • Dynein is the motor for retrograde axonal transport of organelles
    • Schnapp BJ, Reese TS (1989) Dynein is the motor for retrograde axonal transport of organelles. Proc Natl Acad Sci USA 86:1548-1552
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 1548-1552
    • Schnapp, B.J.1    Reese, T.S.2
  • 6
    • 0029004332 scopus 로고
    • Retrograde but not anterograde bead movement in intact axons requires dynein
    • Wang C, Asai DJ, Robinson KR (1995) Retrograde but not anterograde bead movement in intact axons requires dynein. J Neurobiol 27:216-226
    • (1995) J Neurobiol , vol.27 , pp. 216-226
    • Wang, C.1    Asai, D.J.2    Robinson, K.R.3
  • 7
    • 0027730175 scopus 로고
    • Cytoplasmic dynein-dependent vesicular transport from early to late endosomes
    • Aniento F, Emans N, Griffiths G, Gruenberg J (1993) Cytoplasmic dynein-dependent vesicular transport from early to late endosomes. J Cell Biol 123:1373-1387
    • (1993) J Cell Biol , vol.123 , pp. 1373-1387
    • Aniento, F.1    Emans, N.2    Griffiths, G.3    Gruenberg, J.4
  • 9
    • 0026760941 scopus 로고
    • Cytoplasmic dynein participates in the centrosomal localization of the Golgi complex
    • Corthesy-Theulaz I, Pauloin A, Pfeffer SR (1992) Cytoplasmic dynein participates in the centrosomal localization of the Golgi complex. J Cell Biol 118:1333-1345
    • (1992) J Cell Biol , vol.118 , pp. 1333-1345
    • Corthesy-Theulaz, I.1    Pauloin, A.2    Pfeffer, S.R.3
  • 11
    • 0025320820 scopus 로고
    • Localization of cytoplasmic dynein to mitotic spindles and kinetochores
    • Steuer ER, Wordeman L, Schroer TA, Sheetz MP (1990) Localization of cytoplasmic dynein to mitotic spindles and kinetochores. Nature 345:255-268
    • (1990) Nature , vol.345 , pp. 255-268
    • Steuer, E.R.1    Wordeman, L.2    Schroer, T.A.3    Sheetz, M.P.4
  • 12
    • 0027420391 scopus 로고
    • Cytoplasmic dynein plays a role in mammalian mitotic spindle formation
    • Vaisberg EA, Koonce MP, McIntosh JR (1993) Cytoplasmic dynein plays a role in mammalian mitotic spindle formation. J Cell Biol 123:849-858
    • (1993) J Cell Biol , vol.123 , pp. 849-858
    • Vaisberg, E.A.1    Koonce, M.P.2    McIntosh, J.R.3
  • 14
    • 0027453547 scopus 로고
    • Disruption of mitotic spindle orientation in a yeast dynein mutant
    • Li Y-Y, Yeh E, Hays T, Bloom K (1993) Disruption of mitotic spindle orientation in a yeast dynein mutant. Proc Natl Acad Sci USA 90:10096-10100
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10096-10100
    • Li, Y.-Y.1    Yeh, E.2    Hays, T.3    Bloom, K.4
  • 15
    • 0028067033 scopus 로고
    • Cytoplasmic dynein and actin-related Arp1 are required for normal nuclear distribution in filamentous fungi
    • Plamann M, Minke PF, Tinsley JH, Bruno KS (1994) Cytoplasmic dynein and actin-related Arp1 are required for normal nuclear distribution in filamentous fungi. J Cell Biol 127:139-149
    • (1994) J Cell Biol , vol.127 , pp. 139-149
    • Plamann, M.1    Minke, P.F.2    Tinsley, J.H.3    Bruno, K.S.4
  • 16
    • 0028890381 scopus 로고
    • Saccharomyces cerevisiae kinesin- and dynein-related proteins required for anaphase chromosome segregation
    • Saunders WS, Koshland D, Eshel D, Gibbons IR, Hoyt MA (1995) Saccharomyces cerevisiae kinesin- and dynein-related proteins required for anaphase chromosome segregation. J Cell Biol 128:617-624
    • (1995) J Cell Biol , vol.128 , pp. 617-624
    • Saunders, W.S.1    Koshland, D.2    Eshel, D.3    Gibbons, I.R.4    Hoyt, M.A.5
  • 17
    • 0028343929 scopus 로고
    • Cytoplasmic dynein is involved in nuclear migration in Aspergillus nidulans
    • Xiang X, Beckwith SM, Morris NR (1994) Cytoplasmic dynein is involved in nuclear migration in Aspergillus nidulans. Proc Natl Acad Sci USA 91:2100-2104
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 2100-2104
    • Xiang, X.1    Beckwith, S.M.2    Morris, N.R.3
  • 18
    • 0344390094 scopus 로고
    • Direction of active sliding of microtubules in Tetrahymena cilia
    • Sale WS, Satir P (1977) Direction of active sliding of microtubules in Tetrahymena cilia. Proc Natl Acad Sci USA 74:2045-2049
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 2045-2049
    • Sale, W.S.1    Satir, P.2
  • 19
    • 0023433972 scopus 로고
    • Direction of force generated by the inner row of dynein arms on flagellar microtubules
    • Fox LA, Sale WS (1987) Direction of force generated by the inner row of dynein arms on flagellar microtubules. J Cell Biol 105:1781-1787
    • (1987) J Cell Biol , vol.105 , pp. 1781-1787
    • Fox, L.A.1    Sale, W.S.2
  • 20
    • 85005051437 scopus 로고
    • Generation of the bending cycle in cilia and flagella
    • Brokaw CJ (1982) Generation of the bending cycle in cilia and flagella. Cell Motil Suppl 1:137-141
    • (1982) Cell Motil Suppl , vol.1 , pp. 137-141
    • Brokaw, C.J.1
  • 21
    • 0027360366 scopus 로고
    • Dynein heavy chain isoforms and axonemal motility
    • Asai DJ, Brokaw CJ (1993) Dynein heavy chain isoforms and axonemal motility. Trends Cell Biol 3:398-402
    • (1993) Trends Cell Biol , vol.3 , pp. 398-402
    • Asai, D.J.1    Brokaw, C.J.2
  • 22
    • 0028242278 scopus 로고
    • Control of flagellar bending: A new agenda based on dynein diversity
    • Brokaw CJ (1994) Control of flagellar bending: A new agenda based on dynein diversity. Cell Motil Cytoskel 28:199-204
    • (1994) Cell Motil Cytoskel , vol.28 , pp. 199-204
    • Brokaw, C.J.1
  • 23
    • 0015840312 scopus 로고
    • The effect of partial extraction of dynein arms on the movement of reactivated sea-urchin sperm
    • Gibbons BH, Gibbons IR (1973) The effect of partial extraction of dynein arms on the movement of reactivated sea-urchin sperm. J Cell Sci 13:337-357
    • (1973) J Cell Sci , vol.13 , pp. 337-357
    • Gibbons, B.H.1    Gibbons, I.R.2
  • 24
    • 0017141964 scopus 로고
    • Functional recombination of dynein 1 with demembranated sea urchin sperm partially extracted with KC1
    • Gibbons BH, Gibbons IR (1976) Functional recombination of dynein 1 with demembranated sea urchin sperm partially extracted with KC1. Biochem Biophys Res Commun 73:1-6
    • (1976) Biochem Biophys Res Commun , vol.73 , pp. 1-6
    • Gibbons, B.H.1    Gibbons, I.R.2
  • 25
    • 0026681097 scopus 로고
    • Three-headed outer arm dynein from Chlamydomonas that can functionally combine with outer-arm-missing axonemes
    • Takada S, Sakakibara H, Kamiya R (1992) Three-headed outer arm dynein from Chlamydomonas that can functionally combine with outer-arm-missing axonemes. J Biochem 111:758-762
    • (1992) J Biochem , vol.111 , pp. 758-762
    • Takada, S.1    Sakakibara, H.2    Kamiya, R.3
  • 26
    • 0023083510 scopus 로고
    • Bending patterns of Chlamydomonas flagella: IV. Mutants with defects in inner and outer dynein arms indicate differences in dynein arm function
    • Brokaw CJ, Kamiya R (1987) Bending patterns of Chlamydomonas flagella: IV. Mutants with defects in inner and outer dynein arms indicate differences in dynein arm function. Cell Motil Cytoskel 8:68-75
    • (1987) Cell Motil Cytoskel , vol.8 , pp. 68-75
    • Brokaw, C.J.1    Kamiya, R.2
  • 27
    • 0017575980 scopus 로고
    • Local reactivation of Triton-extracted flagella by iontophoretic application of ATP
    • Shingyoji C, Murakami A, Takahashi K (1977) Local reactivation of Triton-extracted flagella by iontophoretic application of ATP. Nature 265:269-270
    • (1977) Nature , vol.265 , pp. 269-270
    • Shingyoji, C.1    Murakami, A.2    Takahashi, K.3
  • 28
    • 0025655046 scopus 로고
    • Functional diversity of dyneins
    • Piperno G (1990) Functional diversity of dyneins. Cell Motil Cytoskel 17:147-149
    • (1990) Cell Motil Cytoskel , vol.17 , pp. 147-149
    • Piperno, G.1
  • 29
    • 0022108755 scopus 로고
    • Rebinding of Tetrahymena 13S and 21S dynein ATPases to extracted doublet microtubules
    • Warner FD, Perreault JG, McIlvain JH (1985) Rebinding of Tetrahymena 13S and 21S dynein ATPases to extracted doublet microtubules. J Cell Sci 77:263-287
    • (1985) J Cell Sci , vol.77 , pp. 263-287
    • Warner, F.D.1    Perreault, J.G.2    McIlvain, J.H.3
  • 30
    • 0026606449 scopus 로고
    • Structural and functional reconstitution of inner dynein arms in Chlamydomonas flagellar axonemes
    • Smith EF, Sale WS (1992) Structural and functional reconstitution of inner dynein arms in Chlamydomonas flagellar axonemes. J Cell Biol 117:573-581
    • (1992) J Cell Biol , vol.117 , pp. 573-581
    • Smith, E.F.1    Sale, W.S.2
  • 31
    • 0025019981 scopus 로고
    • Three distinct inner dynein arms in Chlamydomonas flagella.: Molecular composition and location in the axoneme
    • Piperno G, Ramanis Z, Smith EF, Sale WS (1990) Three distinct inner dynein arms in Chlamydomonas flagella.: Molecular composition and location in the axoneme. J Cell Biol 110:379-389
    • (1990) J Cell Biol , vol.110 , pp. 379-389
    • Piperno, G.1    Ramanis, Z.2    Smith, E.F.3    Sale, W.S.4
  • 32
    • 0025968329 scopus 로고
    • The proximal portion of Chlamydomonas flagella contains a distinct set of inner dynein arms
    • Piperno G, Ramanis Z (1991) The proximal portion of Chlamydomonas flagella contains a distinct set of inner dynein arms. J Cell Biol 112:701-709
    • (1991) J Cell Biol , vol.112 , pp. 701-709
    • Piperno, G.1    Ramanis, Z.2
  • 33
    • 0026660469 scopus 로고
    • The α subunit of sea urchin sperm outer arm dynein mediates structural and rigor binding to microtubules
    • Moss AG, Sale WS, Fox LA, Witman GB (1992) The α subunit of sea urchin sperm outer arm dynein mediates structural and rigor binding to microtubules J Cell Biol 118:1189-1200
    • (1992) J Cell Biol , vol.118 , pp. 1189-1200
    • Moss, A.G.1    Sale, W.S.2    Fox, L.A.3    Witman, G.B.4
  • 34
    • 0024110708 scopus 로고
    • Isolated β-heavy chain subunit of dynein translocates microtubules in vitro
    • Sale WS, Fox LA (1988) Isolated β-heavy chain subunit of dynein translocates microtubules in vitro. J Cell Biol 107:1793-1797
    • (1988) J Cell Biol , vol.107 , pp. 1793-1797
    • Sale, W.S.1    Fox, L.A.2
  • 35
    • 0026726958 scopus 로고
    • The motile β/IC1 subunit of sea urchin sperm outer arm dynein does not form a rigor bond
    • Moss AG, Gatti J-L, Witman GB (1992) The motile β/IC1 subunit of sea urchin sperm outer arm dynein does not form a rigor bond. J Cell Biol 118:1177-1188
    • (1992) J Cell Biol , vol.118 , pp. 1177-1188
    • Moss, A.G.1    Gatti, J.-L.2    Witman, G.B.3
  • 36
    • 0025894163 scopus 로고
    • A Chlamydomonas outer arm dynein mutant missing the α heavy chain
    • Sakakibara H, Mitchell DR, Kamiya R (1991) A Chlamydomonas outer arm dynein mutant missing the α heavy chain. J Cell Biol 113:615-622
    • (1991) J Cell Biol , vol.113 , pp. 615-622
    • Sakakibara, H.1    Mitchell, D.R.2    Kamiya, R.3
  • 37
    • 0027183187 scopus 로고
    • A Chlamydomonas outer arm dynein mutant with a truncated β heavy chain
    • Sakakibara H, Takada S, King SM, Witman GB, Kamiya R (1993) A Chlamydomonas outer arm dynein mutant with a truncated β heavy chain. J Cell Biol 122:653-671
    • (1993) J Cell Biol , vol.122 , pp. 653-671
    • Sakakibara, H.1    Takada, S.2    King, S.M.3    Witman, G.B.4    Kamiya, R.5
  • 38
    • 0021630304 scopus 로고
    • Structural comparison of purified proteins with in situ dynein arms
    • Goodenough U, Heuser J (1984) Structural comparison of purified proteins with in situ dynein arms. J Mol Biol 180:1083-1118
    • (1984) J Mol Biol , vol.180 , pp. 1083-1118
    • Goodenough, U.1    Heuser, J.2
  • 40
    • 0028919594 scopus 로고
    • High molecular weight polypeptides related to dynein heavy chains in Nicotiana tabacum pollen tubes
    • Moscatelli A, Del Casino C, Lozzi L, Cai G, Scali M, Tiezzi A, Cresti M (1995) High molecular weight polypeptides related to dynein heavy chains in Nicotiana tabacum pollen tubes. J Cell Sci 108:1117-1125
    • (1995) J Cell Sci , vol.108 , pp. 1117-1125
    • Moscatelli, A.1    Del Casino, C.2    Lozzi, L.3    Cai, G.4    Scali, M.5    Tiezzi, A.6    Cresti, M.7
  • 41
    • 0022981653 scopus 로고
    • Specific cleavage of dynein heavy chains by ultraviolet irradiation in the presence of ATP and vanadate
    • Lee-Eiford A, Ow RA, Gibbons IR (1986) Specific cleavage of dynein heavy chains by ultraviolet irradiation in the presence of ATP and vanadate. J Biol Chem 261:2337-2342
    • (1986) J Biol Chem , vol.261 , pp. 2337-2342
    • Lee-Eiford, A.1    Ow, R.A.2    Gibbons, I.R.3
  • 42
    • 0026425402 scopus 로고
    • Multiple nucleotide-binding sites in the sequence of the dynein β heavy chain
    • Gibbons IR, Gibbons BH, Mocz G, Asai DJ (1991) Multiple nucleotide-binding sites in the sequence of the dynein β heavy chain. Nature 352:640-643
    • (1991) Nature , vol.352 , pp. 640-643
    • Gibbons, I.R.1    Gibbons, B.H.2    Mocz, G.3    Asai, D.J.4
  • 44
    • 0028040415 scopus 로고
    • Mutations in the SUP-PF-1 locus of Chlamydomonas reinhardtii identify a regulatory domain in the β-dynein heavy chain
    • Porter ME, Knott JA, Gardner LC, Mitchell DR, Dutcher SK (1994) Mutations in the SUP-PF-1 locus of Chlamydomonas reinhardtii identify a regulatory domain in the β-dynein heavy chain. J Cell Biol 126:1495-1507
    • (1994) J Cell Biol , vol.126 , pp. 1495-1507
    • Porter, M.E.1    Knott, J.A.2    Gardner, L.C.3    Mitchell, D.R.4    Dutcher, S.K.5
  • 45
    • 0027269506 scopus 로고
    • ATP-insensitive interaction of the amino-terminal region of the β heavy chain of dynein and microtubules
    • Mocz G, Gibbons IR (1993) ATP-insensitive interaction of the amino-terminal region of the β heavy chain of dynein and microtubules. Biochemistry 32:3456-3460
    • (1993) Biochemistry , vol.32 , pp. 3456-3460
    • Mocz, G.1    Gibbons, I.R.2
  • 46
    • 0028883881 scopus 로고
    • The dynein genes of Paramecium tetraurelia: The structure and expression of the ciliary β and cytoplasmic heavy chains
    • Kandl KA, Forney JD, Asai DJ (1995) The dynein genes of Paramecium tetraurelia: The structure and expression of the ciliary β and cytoplasmic heavy chains. Mol Biol Cell 6:1549-1562
    • (1995) Mol Biol Cell , vol.6 , pp. 1549-1562
    • Kandl, K.A.1    Forney, J.D.2    Asai, D.J.3
  • 47
    • 0001892137 scopus 로고
    • Vanadate-mediated photolysis of the dynein heavy chains
    • (Warner FD, Satir P, Gibbons IR, eds) Alan R. Liss, New York
    • Gibbons IR, Tang W-JY, Gibbons BH (1989) Vanadate-mediated photolysis of the dynein heavy chains, in Cell Movement, Volume 1: The Dynein ATPases(Warner FD, Satir P, Gibbons IR, eds) pp 77-88. Alan R. Liss, New York
    • (1989) Cell Movement, Volume 1: The Dynein Atpases , vol.1 , pp. 77-88
    • Gibbons, I.R.1    Tang, W.-J.Y.2    Gibbons, B.H.3
  • 49
    • 0029175441 scopus 로고
    • Identification of new dynein heavy chain genes by RNA-directed PCR
    • Asai DJ, Criswell PS (1995) Identification of new dynein heavy chain genes by RNA-directed PCR. Meth Cell Biol 47:579-585
    • (1995) Meth Cell Biol , vol.47 , pp. 579-585
    • Asai, D.J.1    Criswell, P.S.2
  • 52
    • 0029050552 scopus 로고
    • Identification and molecular evolution of new dynein-like protein sequences in rat brain
    • Tanaka Y, Zhang Z, Hirokawa N (1995) Identification and molecular evolution of new dynein-like protein sequences in rat brain. J Cell Sci 108:1883-1893
    • (1995) J Cell Sci , vol.108 , pp. 1883-1893
    • Tanaka, Y.1    Zhang, Z.2    Hirokawa, N.3
  • 53
    • 0028285025 scopus 로고
    • The dynein genes of Paramecium tetraurelia: Sequences adjacent to the catalytic P-loop identify cytoplasmic and axonemal heavy chain isoforms
    • Asai DJ, Beckwith SM, Kandl KA, Keating HH, Tjandra H, Forney JD (1994) The dynein genes of Paramecium tetraurelia: Sequences adjacent to the catalytic P-loop identify cytoplasmic and axonemal heavy chain isoforms. J Cell Sci 107:839-847
    • (1994) J Cell Sci , vol.107 , pp. 839-847
    • Asai, D.J.1    Beckwith, S.M.2    Kandl, K.A.3    Keating, H.H.4    Tjandra, H.5    Forney, J.D.6
  • 54
    • 0028203579 scopus 로고
    • Sequence analysis of the Chlamydomonas alpha and beta dynein heavy chain genes
    • Mitchell DR, Brown KS (1994) Sequence analysis of the Chlamydomonas alpha and beta dynein heavy chain genes. J Cell Sci 107:635-644
    • (1994) J Cell Sci , vol.107 , pp. 635-644
    • Mitchell, D.R.1    Brown, K.S.2
  • 55
    • 0028205103 scopus 로고
    • Molecular analysis of the γ heavy chain of Chlamydomonas flagellar outer-arm dynein
    • Wilkerson CG, King SM, Witman GB (1994) Molecular analysis of the γ heavy chain of Chlamydomonas flagellar outer-arm dynein. J Cell Sci 107:497-506
    • (1994) J Cell Sci , vol.107 , pp. 497-506
    • Wilkerson, C.G.1    King, S.M.2    Witman, G.B.3
  • 56
    • 0024280499 scopus 로고
    • Microtubule-associated protein 1C from brain is a two-headed cytosolic dynein
    • Vallee RB, Wall JS, Paschal BM, Shpetner HS (1988) Microtubule-associated protein 1C from brain is a two-headed cytosolic dynein. Nature 332:561-563
    • (1988) Nature , vol.332 , pp. 561-563
    • Vallee, R.B.1    Wall, J.S.2    Paschal, B.M.3    Shpetner, H.S.4
  • 57
    • 0025282178 scopus 로고
    • HMW-2, the Sertoli cell cytoplasmic dynein from rat testis, is a dimer composed of nearly identical subunits
    • Neely MD, Erickson HP, Boekelheide K (1990) HMW-2, the Sertoli cell cytoplasmic dynein from rat testis, is a dimer composed of nearly identical subunits. J Biol Chem 265:8691-8698
    • (1990) J Biol Chem , vol.265 , pp. 8691-8698
    • Neely, M.D.1    Erickson, H.P.2    Boekelheide, K.3
  • 58
    • 0028200793 scopus 로고
    • Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis
    • Hackney D (1994) Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis. Proc Natl Acad Sci USA 91:6865-6869
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 6865-6869
    • Hackney, D.1
  • 59
    • 0028985886 scopus 로고
    • Pathway of processive ATP hydrolysis by kinesin
    • Gilbert SP, Webb MR, Brune M, Johnson KA (1995) Pathway of processive ATP hydrolysis by kinesin. Nature 373:671-679
    • (1995) Nature , vol.373 , pp. 671-679
    • Gilbert, S.P.1    Webb, M.R.2    Brune, M.3    Johnson, K.A.4
  • 60
    • 0027070849 scopus 로고
    • Directional instability of microtubule transport in the presence of kinesin and dynein, two opposite polarity motor proteins
    • Vale RD, Malik F, Brown D (1992) Directional instability of microtubule transport in the presence of kinesin and dynein, two opposite polarity motor proteins. J Cell Biol 119:1589-1596
    • (1992) J Cell Biol , vol.119 , pp. 1589-1596
    • Vale, R.D.1    Malik, F.2    Brown, D.3
  • 62
    • 0001269216 scopus 로고
    • The structure and function of dynein heavy chains
    • Asai DJ, Lee S-w (1995) The structure and function of dynein heavy chains. Mol Cells 5:299-305
    • (1995) Mol Cells , vol.5 , pp. 299-305
    • Asai, D.J.1    Lee, S.-W.2
  • 63
    • 0028176103 scopus 로고
    • Mutations in the 'dynein regulatory complex' alter the ATP-insensitive binding sites for inner arm dyneins in Chlamydomonas axonemes
    • Piperno G, Mead K, LeDizet M, Moscatelli A (1994) Mutations in the 'dynein regulatory complex' alter the ATP-insensitive binding sites for inner arm dyneins in Chlamydomonas axonemes. J Cell Biol 125:1109-1117
    • (1994) J Cell Biol , vol.125 , pp. 1109-1117
    • Piperno, G.1    Mead, K.2    LeDizet, M.3    Moscatelli, A.4
  • 64
    • 0028170976 scopus 로고
    • Components of a 'dynein regulatory complex' are located at the junction between the radial spokes and the dynein arms in Chlamydomonas flagella
    • Gardner LC, O'Toole E, Perrone CA, Giddings T, Porter ME (1994) Components of a 'dynein regulatory complex' are located at the junction between the radial spokes and the dynein arms in Chlamydomonas flagella. J Cell Biol 127:1311-1325
    • (1994) J Cell Biol , vol.127 , pp. 1311-1325
    • Gardner, L.C.1    O'Toole, E.2    Perrone, C.A.3    Giddings, T.4    Porter, M.E.5
  • 65
    • 0028199609 scopus 로고
    • The JNM1 gene in the yeast Saccharomyces cerevisiae is required for nuclear migration and spindle orientation during the mitotic cell cycle
    • McMillan JN, Tatchell K (1994) The JNM1 gene in the yeast Saccharomyces cerevisiae is required for nuclear migration and spindle orientation during the mitotic cell cycle. J Cell Biol 125:143-158
    • (1994) J Cell Biol , vol.125 , pp. 143-158
    • McMillan, J.N.1    Tatchell, K.2
  • 67
    • 0021360693 scopus 로고
    • Genetic and biochemical dissection of the eucaryotic flagellum
    • Luck DJL (1984) Genetic and biochemical dissection of the eucaryotic flagellum. J Cell Biol 98:789-794
    • (1984) J Cell Biol , vol.98 , pp. 789-794
    • Luck, D.J.L.1
  • 68
    • 0028293627 scopus 로고
    • Electroporation-mediated replacement of a positively and negatively selectable β-tubulin gene in Tetrahymena thermophila
    • Gaertig J, Thatcher TH, Gu L, Gorovsky MA (1994) Electroporation-mediated replacement of a positively and negatively selectable β-tubulin gene in Tetrahymena thermophila. Proc Natl Acad Sci USA 91:4549-4553
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4549-4553
    • Gaertig, J.1    Thatcher, T.H.2    Gu, L.3    Gorovsky, M.A.4
  • 69
    • 0026425498 scopus 로고
    • Four ATP-binding sites in the midregion of the β heavy chain of dynein
    • Ogawa K (1991) Four ATP-binding sites in the midregion of the β heavy chain of dynein. Nature 352:643-645
    • (1991) Nature , vol.352 , pp. 643-645
    • Ogawa, K.1
  • 70
    • 0029163352 scopus 로고
    • Genomic structure of a cytoplasmic dynein heavy chain from the nematode Caenorhabditis elegans
    • Lye RJ, Wilson RK, Waterston RH (1995) Genomic structure of a cytoplasmic dynein heavy chain from the nematode Caenorhabditis elegans. Cell Motil Cytoskel 32:26-36
    • (1995) Cell Motil Cytoskel , vol.32 , pp. 26-36
    • Lye, R.J.1    Wilson, R.K.2    Waterston, R.H.3
  • 71
    • 0027050116 scopus 로고
    • Dynein from Dictyostelium: Primary structure comparisons between a cytoplasmic motor enzyme and flagellar dynein
    • Koonce MP, Grissom PM, McIntosh JR (1992) Dynein from Dictyostelium: Primary structure comparisons between a cytoplasmic motor enzyme and flagellar dynein. J Cell Biol 119:1597-1604
    • (1992) J Cell Biol , vol.119 , pp. 1597-1604
    • Koonce, M.P.1    Grissom, P.M.2    McIntosh, J.R.3
  • 72
    • 0028144963 scopus 로고
    • Drosophila cytoplasmic dynein, a microtubule motor that is asymmetrically localized in the oocyte
    • Li M-g, McGrail M, Serr M, Hays TS (1994) Drosophila cytoplasmic dynein, a microtubule motor that is asymmetrically localized in the oocyte. J Cell Biol 126:1475-1494
    • (1994) J Cell Biol , vol.126 , pp. 1475-1494
    • Li, M.-G.1    McGrail, M.2    Serr, M.3    Hays, T.S.4
  • 73
    • 0027264943 scopus 로고
    • Molecular cloning of the retrograde transport motor cytoplasmic dynein (MAP1C)
    • Mikami A, Paschal BM, Mazumdar M, Vallee RB (1993) Molecular cloning of the retrograde transport motor cytoplasmic dynein (MAP1C). Neuron 10:787-796
    • (1993) Neuron , vol.10 , pp. 787-796
    • Mikami, A.1    Paschal, B.M.2    Mazumdar, M.3    Vallee, R.B.4
  • 75
    • 0017288694 scopus 로고
    • The function of tubulin in motile systems
    • Mohri H (1976) The function of tubulin in motile systems. Biochem Biophys Acta 456:85-127
    • (1976) Biochem Biophys Acta , vol.456 , pp. 85-127
    • Mohri, H.1


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