메뉴 건너뛰기




Volumn 17, Issue 1, 2005, Pages 98-103

Recent progress in dynein structure and mechanism

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; DYNEIN ADENOSINE TRIPHOSPHATASE;

EID: 12344266732     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2004.12.006     Document Type: Review
Times cited : (84)

References (62)
  • 1
    • 37049239183 scopus 로고
    • Dynein: A protein with adenosine triphosphatase activity from cilia
    • I.R. Gibbons, and A.J. Rowe Dynein: a protein with adenosine triphosphatase activity from cilia Science 149 1965 424 426
    • (1965) Science , vol.149 , pp. 424-426
    • Gibbons, I.R.1    Rowe, A.J.2
  • 2
    • 0019781934 scopus 로고
    • Cilia and flagella of eukaryotes
    • I.R. Gibbons Cilia and flagella of eukaryotes J Cell Biol 91 1981 107s 124s
    • (1981) J Cell Biol , vol.91
    • Gibbons, I.R.1
  • 3
    • 0034833751 scopus 로고    scopus 로고
    • Dynein motors of the Chlamydomonas flagellum
    • L.M. Di Bella, and S.M. King Dynein motors of the Chlamydomonas flagellum Int Rev Cytol 210 2001 227 268
    • (2001) Int Rev Cytol , vol.210 , pp. 227-268
    • Di Bella, L.M.1    King, S.M.2
  • 4
    • 0035995284 scopus 로고    scopus 로고
    • Functional diversity of axonemal dyneins as studied in Chlamydomonas mutants
    • R. Kamiya Functional diversity of axonemal dyneins as studied in Chlamydomonas mutants Int Rev Cytol 219 2002 115 155
    • (2002) Int Rev Cytol , vol.219 , pp. 115-155
    • Kamiya, R.1
  • 5
    • 0027097082 scopus 로고
    • Translocation and rotation of microtubules caused by multiple species of Chlamydomonas inner-arm dynein
    • O. Kagami, and R. Kamiya Translocation and rotation of microtubules caused by multiple species of Chlamydomonas inner-arm dynein J Cell Sci 103 1992 653 664
    • (1992) J Cell Sci , vol.103 , pp. 653-664
    • Kagami, O.1    Kamiya, R.2
  • 6
    • 0024284804 scopus 로고
    • Rotation and translocation of microtubules in vitro induced by dynein from Tetrahymena cilia
    • R.D. Vale, and Y.Y. Toyoshima Rotation and translocation of microtubules in vitro induced by dynein from Tetrahymena cilia Cell 52 1988 459 469
    • (1988) Cell , vol.52 , pp. 459-469
    • Vale, R.D.1    Toyoshima, Y.Y.2
  • 8
    • 0842333851 scopus 로고    scopus 로고
    • Dynein: An ancient motor protein involved in multiple modes of transport
    • R.B. Vallee, J.C. Williams, D. Varma, and L.E. Barnhart Dynein: An ancient motor protein involved in multiple modes of transport J Neurobiol 58 2004 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
  • 9
    • 0032559260 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins and the mechanism of organelle transport
    • N. Hirokawa 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
  • 10
    • 0037459061 scopus 로고    scopus 로고
    • The molecular motor toolbox for intracellular transport
    • R.D. Vale The molecular motor toolbox for intracellular transport Cell 112 2003 467 480
    • (2003) Cell , vol.112 , pp. 467-480
    • Vale, R.D.1
  • 11
    • 0031444202 scopus 로고    scopus 로고
    • An extended microtubule-binding structure within the dynein motor domain
    • M.A. Gee, J.E. Heuser, and R.B. Vallee An extended microtubule-binding structure within the dynein motor domain Nature 390 1997 636 639
    • (1997) Nature , vol.390 , pp. 636-639
    • Gee, M.A.1    Heuser, J.E.2    Vallee, R.B.3
  • 12
    • 0034001336 scopus 로고    scopus 로고
    • Functional elements within the dynein microtubule-binding domain
    • M.P. Koonce, and I. Tikhonenko Functional elements within the dynein microtubule-binding domain Mol Biol Cell 11 2000 523 529
    • (2000) Mol Biol Cell , vol.11 , pp. 523-529
    • Koonce, M.P.1    Tikhonenko, I.2
  • 13
    • 2542441524 scopus 로고    scopus 로고
    • A single-headed recombinant fragment of Dictyostelium cytoplasmic dynein can drive the robust sliding of microtubules
    • M. Nishiura, T. Kon, K. Shiroguchi, R. Ohkura, T. Shima, Y.Y. Toyoshima, and K. Sutoh A single-headed recombinant fragment of Dictyostelium cytoplasmic dynein can drive the robust sliding of microtubules J Biol Chem 279 2004 22799 22802 The authors establish a method to express and purify the recombinant dynein while maintaining full motor activity.
    • (2004) J Biol Chem , vol.279 , pp. 22799-22802
    • Nishiura, M.1    Kon, T.2    Shiroguchi, K.3    Ohkura, R.4    Shima, T.5    Toyoshima, Y.Y.6    Sutoh, K.7
  • 14
    • 0032969563 scopus 로고    scopus 로고
    • +: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • +: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes Genome Res 9 1999 27 43
    • (1999) Genome Res , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 15
    • 0034885052 scopus 로고    scopus 로고
    • + superfamily ATPases: Common structure - Diverse function
    • + superfamily ATPases: common structure - diverse function Genes Cells 6 2001 575 597
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 16
    • 0032513004 scopus 로고    scopus 로고
    • Structural characterization of a dynein motor domain
    • M. Samso, M. Radermacher, J. Frank, and M.P. Koonce Structural characterization of a dynein motor domain J Mol Biol 276 1998 927 937
    • (1998) J Mol Biol , vol.276 , pp. 927-937
    • Samso, M.1    Radermacher, M.2    Frank, J.3    Koonce, M.P.4
  • 17
    • 3242809790 scopus 로고    scopus 로고
    • 25-Å resolution structure of a cytoplasmic dynein motor reveals a seven-member planar ring
    • M. Samso, and M.P. Koonce 25-Å resolution structure of a cytoplasmic dynein motor reveals a seven-member planar ring J Mol Biol 340 2004 1059 1072 Using negative-stain electron microscopy, the authors provide 3D reconstructions of a cytoplasmic dynein motor domain at 25 Å resolution. Specific Fab tags were used to localize the microtubule-binding domain.
    • (2004) J Mol Biol , vol.340 , pp. 1059-1072
    • Samso, M.1    Koonce, M.P.2
  • 18
    • 0037434697 scopus 로고    scopus 로고
    • Dynein structure and power stroke
    • S.A. Burgess, M.L. Walker, H. Sakakibara, P.J. Knight, and K. Oiwa Dynein structure and power stroke Nature 421 2003 715 718 The authors provide detailed images of an axonemal dynein obtained with negative-stain electron microscopy followed by single-particle image processing. This give the first demonstration of a conformational change accompanying product release from single dynein molecules, and propose a structural mechanism for the power stroke.
    • (2003) Nature , vol.421 , pp. 715-718
    • Burgess, S.A.1    Walker, M.L.2    Sakakibara, H.3    Knight, P.J.4    Oiwa, K.5
  • 20
    • 0026425402 scopus 로고
    • Multiple nucleotide-binding sites in the sequence of dynein β heavy chain
    • I.R. Gibbons, B.H. Gibbons, G. Mocz, and D.J. Asai Multiple nucleotide-binding sites in the sequence of dynein β heavy chain Nature 352 1991 640 643
    • (1991) Nature , vol.352 , pp. 640-643
    • Gibbons, I.R.1    Gibbons, B.H.2    Mocz, G.3    Asai, D.J.4
  • 21
    • 0026425498 scopus 로고
    • Four ATP-binding sites in the midregion of the β heavy chain of dynein
    • K. Ogawa Four ATP-binding sites in the midregion of the β heavy chain of dynein Nature 352 1991 643 645
    • (1991) Nature , vol.352 , pp. 643-645
    • Ogawa, K.1
  • 22
    • 0027050116 scopus 로고
    • Dynein from Dictyostelium: Primary structure comparisons between a cytoplasmic motor enzyme and flagellar dynein
    • M.P. Koonce, P.M. Grissom, and J.R. McIntosh Dynein from Dictyostelium: primary structure comparisons between a cytoplasmic motor enzyme and flagellar dynein J Cell Biol 119 1992 1597 1604
    • (1992) J Cell Biol , vol.119 , pp. 1597-1604
    • Koonce, M.P.1    Grissom, P.M.2    McIntosh, J.R.3
  • 23
    • 0027264943 scopus 로고
    • Molecular cloning of the retrograde transport motor cytoplasmic dynein (MAP 1C)
    • A. Mikami, B.M. Paschal, M. Mazumdar, and R.B. Vallee Molecular cloning of the retrograde transport motor cytoplasmic dynein (MAP 1C) Neuron 10 1993 787 796
    • (1993) Neuron , vol.10 , pp. 787-796
    • Mikami, A.1    Paschal, B.M.2    Mazumdar, M.3    Vallee, R.B.4
  • 24
    • 0029896120 scopus 로고    scopus 로고
    • Phase partition analysis of nucleotide binding to axonemal dynein
    • G. Mocz, and I.R. Gibbons Phase partition analysis of nucleotide binding to axonemal dynein Biochemistry 35 1996 9204 9211
    • (1996) Biochemistry , vol.35 , pp. 9204-9211
    • Mocz, G.1    Gibbons, I.R.2
  • 25
    • 0032493320 scopus 로고    scopus 로고
    • Probing the nucleotide binding sites of axonemal dynein with the fluorescent nucleotide analogue 2′(3′)-O-(-N-Methylanthraniloyl)- adenosine 5′-triphosphate
    • G. Mocz, M.K. Helms, D.M. Jameson, and I.R. Gibbons Probing the nucleotide binding sites of axonemal dynein with the fluorescent nucleotide analogue 2′(3′)-O-(-N-Methylanthraniloyl)- adenosine 5′-triphosphate Biochemistry 37 1998 9862 9869
    • (1998) Biochemistry , vol.37 , pp. 9862-9869
    • Mocz, G.1    Helms, M.K.2    Jameson, D.M.3    Gibbons, I.R.4
  • 26
    • 0023664034 scopus 로고
    • Photosensitized cleavage of dynein heavy chains. Cleavage at the 'V1 site' by irradiation at 365 nm in the presence of ATP and vanadate
    • I.R. Gibbons, A. Lee-Eiford, G. Mocz, C.A. Phillipson, W.J. Tang, and B.H. Gibbons Photosensitized cleavage of dynein heavy chains. Cleavage at the 'V1 site' by irradiation at 365 nm in the presence of ATP and vanadate J Biol Chem 262 1987 2780 2786
    • (1987) J Biol Chem , vol.262 , pp. 2780-2786
    • Gibbons, I.R.1    Lee-Eiford, A.2    Mocz, G.3    Phillipson, C.A.4    Tang, W.J.5    Gibbons, B.H.6
  • 27
    • 4444330119 scopus 로고    scopus 로고
    • Distinct functions of nucleotide-binding/hydrolysis sites in the four AAA modules of cytoplasmic dynein
    • T. Kon, M. Nishiura, R. Ohkura, Y. Toyoshima, and K. Sutoh Distinct functions of nucleotide-binding/hydrolysis sites in the four AAA modules of cytoplasmic dynein Biochemistry 43 2004 11266 11274 By detailed biochemical analyses of expressed and purified P-loop mutants of the Dictyostelium dynein heavy chain, the authors show that four nucleotide-binding/hydrolysis sites have distinct functional roles in dynein motor activity.
    • (2004) Biochemistry , vol.43 , pp. 11266-11274
    • Kon, T.1    Nishiura, M.2    Ohkura, R.3    Toyoshima, Y.4    Sutoh, K.5
  • 28
    • 0037694982 scopus 로고    scopus 로고
    • The third P-loop domain in cytoplasmic dynein heavy chain is essential for dynein motor function and ATP-sensitive microtubule binding
    • A. Silvanovich, M.G. Li, M. Serr, S. Mische, and T.S. Hays The third P-loop domain in cytoplasmic dynein heavy chain is essential for dynein motor function and ATP-sensitive microtubule binding Mol Biol Cell 14 2003 1355 1365 The first mutational analysis of P-loop functions within the first and third AAA domains of the Drosophila cytoplasmic dynein heavy chain, revealing that mutations in the third P-loop disrupt the communication pathway between the hydrolytic site in first AAA and the microtubule-binding domain.
    • (2003) Mol Biol Cell , vol.14 , pp. 1355-1365
    • Silvanovich, A.1    Li, M.G.2    Serr, M.3    Mische, S.4    Hays, T.S.5
  • 29
    • 0034533181 scopus 로고    scopus 로고
    • ADP-dependent microtubule translocation by flagellar inner-arm dyneins
    • T. Yagi ADP-dependent microtubule translocation by flagellar inner-arm dyneins Cell Struct Funct 25 2000 263 267
    • (2000) Cell Struct Funct , vol.25 , pp. 263-267
    • Yagi, T.1
  • 30
    • 0034871465 scopus 로고    scopus 로고
    • Regulation of monomeric dynein activity by ATP and ADP concentrations
    • K. Shiroguchi, and Y.Y. Toyoshima Regulation of monomeric dynein activity by ATP and ADP concentrations Cell Motil Cytoskeleton 49 2001 189 199
    • (2001) Cell Motil Cytoskeleton , vol.49 , pp. 189-199
    • Shiroguchi, K.1    Toyoshima, Y.Y.2
  • 31
    • 0035089503 scopus 로고    scopus 로고
    • Model for the motor component of dynein heavy chain based on homology to the AAA family of oligomeric ATPases
    • G. Mocz, and I.R. Gibbons Model for the motor component of dynein heavy chain based on homology to the AAA family of oligomeric ATPases Structure(Camb) 9 2001 93 103
    • (2001) Structure(Camb) , vol.9 , pp. 93-103
    • Mocz, G.1    Gibbons, I.R.2
  • 32
    • 4444368230 scopus 로고    scopus 로고
    • Multiple ATP-hydrolyzing sites that potentially function in cytoplasmic dynein
    • Y. Takahashi, M. Edamatsu, and Y.Y. Toyoshima Multiple ATP-hydrolyzing sites that potentially function in cytoplasmic dynein Proc Natl Acad Sci USA 101 2004 12865 12869 A molecular dissection of the function of multiple ATP binding sites in cytoplasmic dynein. The authors examine ATPase activities of truncated dynein fragments and their mutants expressed in E coli and show that multiple ATP-binding sites have the ability to hydrolyse ATP.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12865-12869
    • Takahashi, Y.1    Edamatsu, M.2    Toyoshima, Y.Y.3
  • 34
    • 0035341592 scopus 로고    scopus 로고
    • The dynein heavy chain: Structure, mechanics and evolution
    • D.J. Asai, and M.P. Koonce The dynein heavy chain: structure, mechanics and evolution Trends Cell Biol 11 2001 196 202
    • (2001) Trends Cell Biol , vol.11 , pp. 196-202
    • Asai, D.J.1    Koonce, M.P.2
  • 35
    • 3342957252 scopus 로고    scopus 로고
    • Dynein and kinesin share an overlapping microtubule-binding site
    • N. Mizuno, S. Toba, M. Edamatsu, J.W. Nishii, N. Hirokawa, Y.Y. Toyoshima, and M. Kikkawa Dynein and kinesin share an overlapping microtubule-binding site EMBO J 23 2004 2459 2467 The biochemical and structural properties of a recombinant dynein stalk head protein are studied using cryoelectron microscopy and helical three-dimensional image reconstruction.
    • (2004) EMBO J , vol.23 , pp. 2459-2467
    • Mizuno, N.1    Toba, S.2    Edamatsu, M.3    Nishii, J.W.4    Hirokawa, N.5    Toyoshima, Y.Y.6    Kikkawa, M.7
  • 36
    • 0035252931 scopus 로고    scopus 로고
    • Coiled coils: A highly versatile protein folding motif
    • P. Burkhard, J. Stetefeld, and S.V. Strelkov Coiled coils: a highly versatile protein folding motif Trends Cell Biol 11 2001 82 88
    • (2001) Trends Cell Biol , vol.11 , pp. 82-88
    • Burkhard, P.1    Stetefeld, J.2    Strelkov, S.V.3
  • 38
    • 0022345812 scopus 로고
    • Outer and inner dynein arms of cilia and flagella
    • U.W. Goodenough, and J.E. Heuser Outer and inner dynein arms of cilia and flagella Cell 41 1985 341 342
    • (1985) Cell , vol.41 , pp. 341-342
    • Goodenough, U.W.1    Heuser, J.E.2
  • 39
    • 0021630304 scopus 로고
    • Structural comparison of purified dynein proteins with in situ dynein arms
    • U. Goodenough, and J. Heuser Structural comparison of purified dynein proteins with in situ dynein arms J Mol Biol 180 1984 1083 1118
    • (1984) J Mol Biol , vol.180 , pp. 1083-1118
    • Goodenough, U.1    Heuser, J.2
  • 40
    • 0030606512 scopus 로고    scopus 로고
    • Is the lever arm of myosin a molecular elastic element?
    • J. Howard, and J.A. Spudich Is the lever arm of myosin a molecular elastic element? Proc Natl Acad Sci USA 93 1996 4462 4464
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4462-4464
    • Howard, J.1    Spudich, J.A.2
  • 41
    • 0345714919 scopus 로고    scopus 로고
    • Does axonemal dynein push, pull, or oscillate?
    • C.B. Lindemann, and A.J. Hunt Does axonemal dynein push, pull, or oscillate? Cell Motil Cytoskeleton 56 2003 237 244
    • (2003) Cell Motil Cytoskeleton , vol.56 , pp. 237-244
    • Lindemann, C.B.1    Hunt, A.J.2
  • 42
    • 0034646431 scopus 로고    scopus 로고
    • Processive movement of single 22S dynein molecules occurs only at low ATP concentrations
    • E. Hirakawa, H. Higuchi, and Y.Y. Toyoshima Processive movement of single 22S dynein molecules occurs only at low ATP concentrations Proc Natl Acad Sci USA 97 2000 2533 2537
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2533-2537
    • Hirakawa, E.1    Higuchi, H.2    Toyoshima, Y.Y.3
  • 43
    • 0033527027 scopus 로고    scopus 로고
    • Inner-arm dynein c of Chlamydomonas flagella is a single-headed processive motor
    • H. Sakakibara, H. Kojima, Y. Sakai, E. Katayama, and K. Oiwa Inner-arm dynein c of Chlamydomonas flagella is a single-headed processive motor Nature 400 1999 586 590
    • (1999) Nature , vol.400 , pp. 586-590
    • Sakakibara, H.1    Kojima, H.2    Sakai, Y.3    Katayama, E.4    Oiwa, K.5
  • 44
    • 0034632063 scopus 로고    scopus 로고
    • AAA proteins: Lords of the ring
    • R.D. Vale AAA proteins: lords of the ring J Cell Biol 150 2000 F13 F19
    • (2000) J Cell Biol , vol.150
    • Vale, R.D.1
  • 45
    • 1342325553 scopus 로고    scopus 로고
    • Cytoplasmic dynein functions as a gear in response to load
    • R. Mallik, B.C. Carter, S.A. Lex, S.J. King, and S.P. Gross Cytoplasmic dynein functions as a gear in response to load Nature 427 2004 649 652 Single-molecule nanometry of cytoplasmic dynein using an optical trap technique shows that its step size decreases with increasing load. The authors propose a model in which the stepping distance per ATP is changed by the load-induced binding of ATP at secondary sites in the dynein head.
    • (2004) Nature , vol.427 , pp. 649-652
    • Mallik, R.1    Carter, B.C.2    Lex, S.A.3    King, S.J.4    Gross, S.P.5
  • 46
    • 0028859428 scopus 로고
    • Single cytoplasmic dynein molecule movements: Characterization and comparison with kinesin
    • Z. Wang, S. Khan, and M.P. Sheetz Single cytoplasmic dynein molecule movements: characterization and comparison with kinesin Biophys J 69 1995 1011 1023
    • (1995) Biophys J , vol.69 , pp. 1011-1023
    • Wang, Z.1    Khan, S.2    Sheetz, M.P.3
  • 47
    • 0033582814 scopus 로고    scopus 로고
    • A processive single-headed motor: Kinesin superfamily protein KIF1A
    • Y. Okada, and N. Hirokawa A processive single-headed motor: kinesin superfamily protein KIF1A Science 283 1999 1152 1157
    • (1999) Science , vol.283 , pp. 1152-1157
    • Okada, Y.1    Hirokawa, N.2
  • 48
    • 0041522803 scopus 로고    scopus 로고
    • Processivity of the single-headed kinesin KIF1A through biased binding to tubulin
    • Y. Okada, H. Higuchi, and N. Hirokawa Processivity of the single-headed kinesin KIF1A through biased binding to tubulin Nature 424 2003 574 577
    • (2003) Nature , vol.424 , pp. 574-577
    • Okada, Y.1    Higuchi, H.2    Hirokawa, N.3
  • 49
    • 0034695259 scopus 로고    scopus 로고
    • 15 Å resolution model of the monomeric kinesin motor, KIF1A
    • M. Kikkawa, Y. Okada, and N. Hirokawa 15 Å resolution model of the monomeric kinesin motor, KIF1A Cell 100 2000 241 252
    • (2000) Cell , vol.100 , pp. 241-252
    • Kikkawa, M.1    Okada, Y.2    Hirokawa, N.3
  • 50
    • 0024805563 scopus 로고
    • One-dimensional diffusion of microtubules bound to flagellar dynein
    • R.D. Vale, D.R. Soll, and I.R. Gibbons One-dimensional diffusion of microtubules bound to flagellar dynein Cell 59 1989 915 925
    • (1989) Cell , vol.59 , pp. 915-925
    • Vale, R.D.1    Soll, D.R.2    Gibbons, I.R.3
  • 51
    • 0242677759 scopus 로고    scopus 로고
    • Myosin V motor proteins: Marching stepwise towards a mechanism
    • R.D. Vale Myosin V motor proteins: marching stepwise towards a mechanism J Cell Biol 163 2003 445 450
    • (2003) J Cell Biol , vol.163 , pp. 445-450
    • Vale, R.D.1
  • 52
    • 0035146785 scopus 로고    scopus 로고
    • Conformational changes during kinesin motility
    • W.R. Schief, and J. Howard Conformational changes during kinesin motility Curr Opin Cell Biol 13 2001 19 28
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 19-28
    • Schief, W.R.1    Howard, J.2
  • 56
    • 0024322107 scopus 로고
    • High-frequency nanometre-scale vibration in 'quiescent' flagellar axonemes
    • S. Kamimura, and R. Kamiya High-frequency nanometre-scale vibration in 'quiescent' flagellar axonemes Nature 340 1989 476 478
    • (1989) Nature , vol.340 , pp. 476-478
    • Kamimura, S.1    Kamiya, R.2
  • 57
    • 0346057939 scopus 로고    scopus 로고
    • Diameter oscillation of axonemes in sea-urchin sperm flagella
    • H.M. Sakakibara, Y. Kunioka, T. Yamada, and S. Kamimura Diameter oscillation of axonemes in sea-urchin sperm flagella Biophys J 86 2004 346 352
    • (2004) Biophys J , vol.86 , pp. 346-352
    • Sakakibara, H.M.1    Kunioka, Y.2    Yamada, T.3    Kamimura, S.4
  • 58
    • 0036785117 scopus 로고    scopus 로고
    • Computer simulation of flagellar movement VIII: Coordination of dynein by local curvature control can generate helical bending waves
    • C.J. Brokaw Computer simulation of flagellar movement VIII: coordination of dynein by local curvature control can generate helical bending waves Cell Motil Cytoskeleton 53 2002 103 124
    • (2002) Cell Motil Cytoskeleton , vol.53 , pp. 103-124
    • Brokaw, C.J.1
  • 59
    • 0034619681 scopus 로고    scopus 로고
    • An integrative model of internal axoneme mechanics and external fluid dynamics in ciliary beating
    • R.H. Dillon, and L.J. Fauci An integrative model of internal axoneme mechanics and external fluid dynamics in ciliary beating J Theor Biol 207 2000 415 430
    • (2000) J Theor Biol , vol.207 , pp. 415-430
    • Dillon, R.H.1    Fauci, L.J.2
  • 60
    • 0037763860 scopus 로고    scopus 로고
    • Structural-functional relationships of the dynein, spokes, and central-pair projections predicted from an analysis of the forces acting within a flagellum
    • C.B. Lindemann Structural-functional relationships of the dynein, spokes, and central-pair projections predicted from an analysis of the forces acting within a flagellum Biophys J 84 2003 4115 4126
    • (2003) Biophys J , vol.84 , pp. 4115-4126
    • Lindemann, C.B.1
  • 61
    • 0035932296 scopus 로고    scopus 로고
    • A three-dimensional model for ciliary motion based on the internal 9+2 structure
    • S. Gueron, and K. Levit-Gurevich A three-dimensional model for ciliary motion based on the internal 9+2 structure Proc R Soc Lond B Biol Sci 268 2001 599 607
    • (2001) Proc R Soc Lond B Biol Sci , vol.268 , pp. 599-607
    • Gueron, S.1    Levit-Gurevich, K.2
  • 62
    • 0021975705 scopus 로고
    • Pathway of the microtubule-dynein ATPase and the structure of dynein: A comparison with actomyosin
    • K.A. Johnson Pathway of the microtubule-dynein ATPase and the structure of dynein: a comparison with actomyosin Annu Rev Biophys Biophys Chem 14 1985 161 188
    • (1985) Annu Rev Biophys Biophys Chem , vol.14 , pp. 161-188
    • Johnson, K.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.