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Volumn 27, Issue 5, 1998, Pages 466-473

The role of the dynein stalk in cytoplasmic and flagellar motility

Author keywords

Microtube; Molecular motor

Indexed keywords

CELL PROTEIN; DYNEIN ADENOSINE TRIPHOSPHATASE; KINESIN; MYOSIN;

EID: 0031664002     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002490050157     Document Type: Article
Times cited : (36)

References (64)
  • 1
    • 0024374973 scopus 로고
    • Brain dynein crossbridges microtubles into bundles
    • Amos LA (1989) Brain dynein crossbridges microtubles into bundles. J Cell Sci 93:19-28
    • (1989) J Cell Sci , vol.93 , pp. 19-28
    • Amos, L.A.1
  • 2
    • 0030961727 scopus 로고    scopus 로고
    • Structure and dynamics of molecular motors
    • Amos LA, Cross RA (1997) Structure and dynamics of molecular motors. Curr Opin Struct Biol 7:239-246
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 239-246
    • Amos, L.A.1    Cross, R.A.2
  • 3
    • 0001269216 scopus 로고
    • The structure and function of dynein heavy chains
    • Asai DJ, Lee S (1995) The structure and function of dynein heavy chains. Mol Cell Biol 5:299-305
    • (1995) Mol Cell Biol , vol.5 , pp. 299-305
    • Asai, D.J.1    Lee, S.2
  • 5
    • 0030592549 scopus 로고    scopus 로고
    • Fifty ways to love your lever: Myosin motors
    • Block SM (1996) Fifty ways to love your lever: myosin motors. Cell 87:151-157
    • (1996) Cell , vol.87 , pp. 151-157
    • Block, S.M.1
  • 6
    • 0029068861 scopus 로고
    • Rigor and relaxed outer dynein arms in replicas of cryofixed motile flagella
    • Burgess SA (1995) Rigor and relaxed outer dynein arms in replicas of cryofixed motile flagella. J Mol Biol 250:52-63
    • (1995) J Mol Biol , vol.250 , pp. 52-63
    • Burgess, S.A.1
  • 7
    • 0030727535 scopus 로고    scopus 로고
    • Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution
    • Burkhardt JK, Echeverri CJ, Nilsson T, Vallee RB (1997) Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution. J Cell Biol 139:469-484
    • (1997) J Cell Biol , vol.139 , pp. 469-484
    • Burkhardt, J.K.1    Echeverri, C.J.2    Nilsson, T.3    Vallee, R.B.4
  • 8
    • 15144351296 scopus 로고    scopus 로고
    • Conservation within the myosin motor domain: Implications for structure and function
    • Cope MJT, Whisstock J, Rayment I, Kendrick-Jones J (1996) Conservation within the myosin motor domain: implications for structure and function. Curr Biol 4:969-987
    • (1996) Curr Biol , vol.4 , pp. 969-987
    • Cope, M.J.T.1    Whisstock, J.2    Rayment, I.3    Kendrick-Jones, J.4
  • 9
    • 0026760941 scopus 로고
    • Cytoplasmic dynein participates in the centrosomal localization of the golgi complex
    • Corthésy-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
    • Corthésy-Theulaz, I.1    Pauloin, A.2    Pfeffer, S.R.3
  • 10
    • 0025043116 scopus 로고
    • A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A
    • Cusack S, Berthet-Colominas C, Hartlein M, Nassar N, Leberman R (1990) A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A. Nature 347:249-255
    • (1990) Nature , vol.347 , pp. 249-255
    • Cusack, S.1    Berthet-Colominas, C.2    Hartlein, M.3    Nassar, N.4    Leberman, R.5
  • 11
    • 0029913484 scopus 로고    scopus 로고
    • Molecular characterization of the 50 kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization during mitosis
    • Echeverri CJ, Paschal BM, Vaughan KT, Vallee RB (1996) Molecular characterization of the 50 kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization during mitosis. J Cell Biol 132:617-633
    • (1996) J Cell Biol , vol.132 , pp. 617-633
    • Echeverri, C.J.1    Paschal, B.M.2    Vaughan, K.T.3    Vallee, R.B.4
  • 12
    • 0031444202 scopus 로고    scopus 로고
    • An extended microtubule-binding structure within the dynein motor domain
    • Gee MA, Heuser JE, Vallee RB (1997) An extended microtubule-binding structure within the dynein motor domain. Nature 390: 636-639
    • (1997) Nature , vol.390 , pp. 636-639
    • Gee, M.A.1    Heuser, J.E.2    Vallee, R.B.3
  • 13
    • 0026425402 scopus 로고
    • Multiple nucleotide-binding sites in the sequence of dynein β heavy chain
    • Gibbons IR, Gibbons BH, Mocz G, Asai DJ (1991) Multiple nucleotide-binding sites in the sequence of 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
  • 15
    • 0029363836 scopus 로고
    • Mechanics of motility: Distinct dynein binding domains on α- and β-tubulin
    • Goldsmith M, Yarbrough L, van der Kooy D (1995) Mechanics of motility: distinct dynein binding domains on α- and β-tubulin. Biochem Cell Biol 73:665-671
    • (1995) Biochem Cell Biol , vol.73 , pp. 665-671
    • Goldsmith, M.1    Yarbrough, L.2    Van Der Kooy, D.3
  • 16
    • 0020410980 scopus 로고
    • Substructure of the outer dynein arm
    • Goodenough UW, Heuser JE (1982) Substructure of the outer dynein arm. J Cell Biol 95:798-815
    • (1982) J Cell Biol , vol.95 , pp. 798-815
    • Goodenough, U.W.1    Heuser, J.E.2
  • 17
    • 0021630304 scopus 로고
    • Structural comparison of purified dynein proteins with in situ dynein arms
    • Goodenough UW, Heuser JE (1984) Structural comparison of purified dynein proteins with in situ dynein arms. J Mol Biol 180: 1083-1118
    • (1984) J Mol Biol , vol.180 , pp. 1083-1118
    • Goodenough, U.W.1    Heuser, J.E.2
  • 19
    • 0029836330 scopus 로고    scopus 로고
    • Self-organization of microtubules into bipolar spindles around artificial bipolar spindles around artificial chromosomes in Xenopus egg extracts
    • Heald R, Tournebize R, Blank T, Sandaltzopoulos R, Becker P, Hyman A, Karsenti E (1996) Self-organization of microtubules into bipolar spindles around artificial bipolar spindles around artificial chromosomes in Xenopus egg extracts. Nature 382:420-425
    • (1996) Nature , vol.382 , pp. 420-425
    • Heald, R.1    Tournebize, R.2    Blank, T.3    Sandaltzopoulos, R.4    Becker, P.5    Hyman, A.6    Karsenti, E.7
  • 20
    • 0028170819 scopus 로고
    • Dyneins: Molecular structure and cellular function
    • Holzbaur ELF, Vallee RB (1994) Dyneins: molecular structure and cellular function. Annu Rev Cell Biol. 10:339-372
    • (1994) Annu Rev Cell Biol. , vol.10 , pp. 339-372
    • Holzbaur, E.L.F.1    Vallee, R.B.2
  • 21
    • 0029960345 scopus 로고    scopus 로고
    • The movement of kinesin along microtubules
    • Howard J (1996) The movement of kinesin along microtubules. Annu Rev Physiol 58:703-729
    • (1996) Annu Rev Physiol , vol.58 , pp. 703-729
    • Howard, J.1
  • 22
    • 0030773824 scopus 로고    scopus 로고
    • Molecular motors: Structural adaptations to cellular functions
    • Howard J (1997) Molecular motors: structural adaptations to cellular functions. Nature 389:561-567
    • (1997) Nature , vol.389 , pp. 561-567
    • Howard, J.1
  • 23
    • 0021975705 scopus 로고
    • Pathway of the microtubule-dynein ATPase and the structure of dynein: A comparison with actomyosin
    • Johnson KA (1985) Pathway of the microtubule-dynein ATPase and the structure of dynein: a comparison with actomyosin. Annu Rev Biophys Chem 14: 161-188
    • (1985) Annu Rev Biophys Chem , vol.14 , pp. 161-188
    • Johnson, K.A.1
  • 24
    • 0020730789 scopus 로고
    • Structure and molecular weight of the dynein ATPase
    • Johnson KA, Wall JS (1983) Structure and molecular weight of the dynein ATPase. J Cell Biol 96:669-678
    • (1983) J Cell Biol , vol.96 , pp. 669-678
    • Johnson, K.A.1    Wall, J.S.2
  • 25
    • 0029150966 scopus 로고
    • Exploring the function of inner and outer dynein arms with Chlamydomonas mutants
    • Kamiya R (1995) Exploring the function of inner and outer dynein arms with Chlamydomonas mutants. Cell Motil Cytoskeleton 32:98-102
    • (1995) Cell Motil Cytoskeleton , vol.32 , pp. 98-102
    • Kamiya, R.1
  • 26
    • 0025203679 scopus 로고
    • Localization of an intermediate chain of outer arm dynein by immunoelectron microscopy
    • King SM, Witman GB (1990) Localization of an intermediate chain of outer arm dynein by immunoelectron microscopy. J Biol Chem 265:19807-19811
    • (1990) J Biol Chem , vol.265 , pp. 19807-19811
    • King, S.M.1    Witman, G.B.2
  • 27
    • 0030877444 scopus 로고    scopus 로고
    • Identification of a microtubule-binding domain in a cytoplasmic dynein heavy chain
    • Koonce MP (1997) Identification of a microtubule-binding domain in a cytoplasmic dynein heavy chain. J Biol Chem 272:19714-19718
    • (1997) J Biol Chem , vol.272 , pp. 19714-19718
    • Koonce, M.P.1
  • 28
    • 0029954331 scopus 로고    scopus 로고
    • Overexpression of cytoplasmic dynein's globular head causes a collapse of the interphase microtubule network in Dictyostelium
    • Koonce MP, Samso M (1996) Overexpression of cytoplasmic dynein's globular head causes a collapse of the interphase microtubule network in Dictyostelium. Mol Biol Cell 7:935-948
    • (1996) Mol Biol Cell , vol.7 , pp. 935-948
    • Koonce, M.P.1    Samso, M.2
  • 29
    • 0029989974 scopus 로고    scopus 로고
    • Crystal structure of the kinesin motor domain reveals a structural similarity to myosin
    • Kull FJ, Sablin EP, Lau R, Fletterick RJ, Vale RD (1996) Crystal structure of the kinesin motor domain reveals a structural similarity to myosin. Nature 380:550-555
    • (1996) Nature , vol.380 , pp. 550-555
    • Kull, F.J.1    Sablin, E.P.2    Lau, R.3    Fletterick, R.J.4    Vale, R.D.5
  • 30
    • 0029814394 scopus 로고    scopus 로고
    • Interaction of kinesin motor domains with α- and β-tubuline subunits at a Tau-independent binding site
    • Larcher J-C, Boucher D, Lazereg S, Gros F, Denoulet P (1996) Interaction of kinesin motor domains with α- and β-tubuline subunits at a Tau-independent binding site. J Biol Chem 271:22117-22124
    • (1996) J Biol Chem , vol.271 , pp. 22117-22124
    • Larcher, J.-C.1    Boucher, D.2    Lazereg, S.3    Gros, F.4    Denoulet, P.5
  • 31
    • 23544448938 scopus 로고
    • Identification of microtubule-binding sites on dynein heavy chain by using bacterially expressed MAPI C fusion proteins
    • Lee S-W, Asai DJ (1995) Identification of microtubule-binding sites on dynein heavy chain by using bacterially expressed MAPI C fusion proteins. Mol Biol Cell 6:35a
    • (1995) Mol Biol Cell , vol.6
    • Lee, S.-W.1    Asai, D.J.2
  • 32
    • 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
  • 33
    • 0029896120 scopus 로고    scopus 로고
    • Phase partition analysis of nucleotide binding to axonemal dynein
    • Mocz G, Gibbons IR (1996) Phase partition analysis of nucleotide binding to axonemal dynein. Biochemistry 35:9204-9211
    • (1996) Biochemistry , vol.35 , pp. 9204-9211
    • Mocz, G.1    Gibbons, I.R.2
  • 34
    • 0022525167 scopus 로고
    • Activation of the dynein adenosinetriphosphatase by microtubules
    • Omoto CK, Johnson KA (1986) Activation of the dynein adenosinetriphosphatase by microtubules. Biochemistry 25:419-427
    • (1986) Biochemistry , vol.25 , pp. 419-427
    • Omoto, C.K.1    Johnson, K.A.2
  • 35
    • 0023205148 scopus 로고
    • Retrograde transport by the microtubule associated protein MAP 1 C
    • Paschal BM, Vallee RB (1987) Retrograde transport by the microtubule associated protein MAP 1 C. Nature 330:181-183
    • (1987) Nature , vol.330 , pp. 181-183
    • Paschal, B.M.1    Vallee, R.B.2
  • 37
    • 0023608935 scopus 로고
    • MAP 1 C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties
    • Paschal BM, Shpetner HS, Vallee RB (1987) MAP 1 C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties. J Cell Biol 105:1273-1282
    • (1987) J Cell Biol , vol.105 , pp. 1273-1282
    • Paschal, B.M.1    Shpetner, H.S.2    Vallee, R.B.3
  • 38
    • 0024306241 scopus 로고
    • Interaction of brain cytoplasmic dynein and MAP 2 with a common sequence at the C terminus of tubulin
    • Paschal BM, Obar RA, Vallee RB (1989) Interaction of brain cytoplasmic dynein and MAP 2 with a common sequence at the C terminus of tubulin. Nature 342:569-572
    • (1989) Nature , vol.342 , pp. 569-572
    • Paschal, B.M.1    Obar, R.A.2    Vallee, R.B.3
  • 41
    • 0029878485 scopus 로고    scopus 로고
    • Crystal structure of the motor domain of the kinesin-related motor ncd
    • Sablin EP, Kull FJ, Cooke R, Vale RD, Fletterick RJ (1996) Crystal structure of the motor domain of the kinesin-related motor ncd. Nature 380:555-559
    • (1996) Nature , vol.380 , pp. 555-559
    • Sablin, E.P.1    Kull, F.J.2    Cooke, R.3    Vale, R.D.4    Fletterick, R.J.5
  • 42
    • 0024110708 scopus 로고
    • Isolated β-heavy chain subunit of dynein translocates microtubules in vitro
    • Sale WS, Fox L (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.2
  • 43
    • 0344911815 scopus 로고
    • Structural analysis of the dynein cross-bridge cycle
    • Satir P (1989) Structural analysis of the dynein cross-bridge cycle. Cell Movement 1:219-234
    • (1989) Cell Movement , vol.1 , pp. 219-234
    • Satir, P.1
  • 44
    • 0025789647 scopus 로고
    • Two activators of microtubule-based vesicle transport
    • Schroer TA, Sheetz MP (1991) Two activators of microtubule-based vesicle transport. J Cell Biol 115:1309-1318
    • (1991) J Cell Biol , vol.115 , pp. 1309-1318
    • Schroer, T.A.1    Sheetz, M.P.2
  • 45
    • 0021020392 scopus 로고
    • Kinetic Evidence for Multiple Dynein ATPase Sites
    • Shimizu T, Johnson KA (1983) Kinetic Evidence for Multiple Dynein ATPase Sites. J Biol Chem 258:13841-13846
    • (1983) J Biol Chem , vol.258 , pp. 13841-13846
    • Shimizu, T.1    Johnson, K.A.2
  • 46
    • 0024078184 scopus 로고
    • Characterization of the microtubule-activated ATPase of brain cytoplasmic dynein (MAP 1 C)
    • Shpetner HS, Paschal BM, Vallee RB (1988) Characterization of the microtubule-activated ATPase of brain cytoplasmic dynein (MAP 1 C). J Cell Biol 107:1001-1009
    • (1988) J Cell Biol , vol.107 , pp. 1001-1009
    • Shpetner, H.S.1    Paschal, B.M.2    Vallee, R.B.3
  • 47
    • 0030803260 scopus 로고    scopus 로고
    • The involvement of the intermediate chain of cytoplasmic dynein in binding the motor complex to membranous organelles of Xenopus Oocytes
    • Steffen W, Karki S, Vaughan KT, Vallee RB, Holzbaur ELF, Weiss DG, Kuznetsov SA (1997) The involvement of the intermediate chain of cytoplasmic dynein in binding the motor complex to membranous organelles of Xenopus Oocytes. Mol Biol Cell 8:2077-2088
    • (1997) Mol Biol Cell , vol.8 , pp. 2077-2088
    • Steffen, W.1    Karki, S.2    Vaughan, K.T.3    Vallee, R.B.4    Holzbaur, E.L.F.5    Weiss, D.G.6    Kuznetsov, S.A.7
  • 48
    • 0029919076 scopus 로고    scopus 로고
    • Mutational analysis of motor proteins
    • Annual Reviews, Inc.
    • Sweeney HL, Holzbaur ELF (1996) Mutational analysis of motor proteins. Annual Review of Physiology, vol 58. Annual Reviews, Inc., pp 751-792
    • (1996) Annual Review of Physiology , vol.58 , pp. 751-792
    • Sweeney, H.L.1    Holzbaur, E.L.F.2
  • 49
    • 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
  • 50
    • 0023612104 scopus 로고
    • Photosensitized cleavage of dynein heavy chains
    • Tang W-JY, Gibbons IR (1987) Photosensitized cleavage of dynein heavy chains. J Biol Chem 263:17728-17734
    • (1987) J Biol Chem , vol.263 , pp. 17728-17734
    • Tang, W.-J.Y.1    Gibbons, I.R.2
  • 51
    • 0001876272 scopus 로고
    • Mechanism and energetics of actomyosin ATPase
    • Fozzard HA (ed) Raven Press, New York
    • Taylor EW (1992) Mechanism and energetics of actomyosin ATPase. In: Fozzard HA (ed) The heart and cardiovascular system, vol 2. Raven Press, New York, pp 1281-1293
    • (1992) The Heart and Cardiovascular System , vol.2 , pp. 1281-1293
    • Taylor, E.W.1
  • 52
    • 0020518435 scopus 로고
    • ATP-dependent structural changes of the outer dynein arm in Tetrahymena cilia: A freeze-etch replica study
    • Tsukita S, Tsukita S, Usukura J, Ishikawa H (1983) ATP-dependent structural changes of the outer dynein arm in Tetrahymena cilia: a freeze-etch replica study. J Cell Biol 96:1480-1485
    • (1983) J Cell Biol , vol.96 , pp. 1480-1485
    • Tsukita, S.1    Tsukita, S.2    Usukura, J.3    Ishikawa, H.4
  • 53
    • 0031004776 scopus 로고    scopus 로고
    • Probing the kinesin-microtubule interaction
    • Tucker C, Goldstein LSB (1997) Probing the kinesin-microtubule interaction. J Biol Chem 272:9481-9488
    • (1997) J Biol Chem , vol.272 , pp. 9481-9488
    • Tucker, C.1    Goldstein, L.S.B.2
  • 54
    • 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
  • 55
    • 0030267349 scopus 로고    scopus 로고
    • Switches, latches, and amplifiers: Common themes of G proteins and molecular motors
    • Vale RD (1996) Switches, latches, and amplifiers: common themes of G proteins and molecular motors. J Cell Biol 135:291-302
    • (1996) J Cell Biol , vol.135 , pp. 291-302
    • Vale, R.D.1
  • 56
    • 0024284804 scopus 로고
    • Rotation and translocation of microtubules in vitro induced by dyneins from Tetrahymena cilia
    • Vale RD, Toyoshima YY (1988) Rotation and translocation of microtubules in vitro induced by dyneins from Tetrahymena cilia. Cell 52:459-469
    • (1988) Cell , vol.52 , pp. 459-469
    • Vale, R.D.1    Toyoshima, Y.Y.2
  • 57
    • 0024687692 scopus 로고
    • Microtubule translocation properties of intact and proteolytically digested dyneins from Tetrahymena cilia
    • Vale RD, Toyoshima YY (1989) Microtubule translocation properties of intact and proteolytically digested dyneins from Tetrahymena cilia. J Cell Biol 108:2327-2334
    • (1989) J Cell Biol , vol.108 , pp. 2327-2334
    • Vale, R.D.1    Toyoshima, Y.Y.2
  • 58
    • 0024805563 scopus 로고
    • One-dimensional diffusion of microtubles in vitro bound to flagellar dynein
    • Vale RD, Soil DR, Gibbons IR (1989) One-dimensional diffusion of microtubles in vitro bound to flagellar dynein. Cell 59:915-925
    • (1989) Cell , vol.59 , pp. 915-925
    • Vale, R.D.1    Soil, D.R.2    Gibbons, I.R.3
  • 59
    • 0029932027 scopus 로고    scopus 로고
    • Targeting of motor proteins
    • Vallee RB, Sheetz MP (1996) Targeting of motor proteins. Science 271:1539-1544
    • (1996) Science , vol.271 , pp. 1539-1544
    • Vallee, R.B.1    Sheetz, M.P.2
  • 60
    • 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
  • 62
    • 0028859428 scopus 로고
    • Single cytoplasmic dynein molecule movements: Characterization and comparison with kinesin
    • Wang Z, Khan S, Sheetz MP (1995) Single cytoplasmic dynein molecule movements: Characterization and comparison with kinesin. Biophys J 69:2011-2023
    • (1995) Biophys J , vol.69 , pp. 2011-2023
    • Wang, Z.1    Khan, S.2    Sheetz, M.P.3
  • 63
    • 0001132343 scopus 로고
    • Fine structure and molecular weight of the outer arms of dyneins of Chlamydomonas
    • Witman GB, Johnson KA, Pfister KK, Wall JS (1983) Fine structure and molecular weight of the outer arms of dyneins of Chlamydomonas. J Submicrosc Cytol 15:193-197
    • (1983) J Submicrosc Cytol , vol.15 , pp. 193-197
    • Witman, G.B.1    Johnson, K.A.2    Pfister, K.K.3    Wall, J.S.4


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