메뉴 건너뛰기




Volumn 14, Issue 6, 2009, Pages 2269-2284

Five models for myosin V

Author keywords

Actin; Chemical kinetics; Discrete stochastic models; Mechano chemical models; Motility; Motor proteins; Myosin V; Processivity; Review

Indexed keywords

MYOSIN V;

EID: 63849298564     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/3378     Document Type: Article
Times cited : (17)

References (98)
  • 1
    • 5644235391 scopus 로고    scopus 로고
    • The myosin superfamily: An overview
    • Ed: Schliwa M. Chaper 1, Wiley-VCH, Weinheim, Germany
    • Kieke M. C., M. A. Titus: The myosin superfamily: An overview. In: Molecular Motors. Ed: Schliwa M., Chaper 1, 3-44, Wiley-VCH, Weinheim, Germany (2003).
    • (2003) Molecular Motors , pp. 3-44
    • Kieke, M.C.1    Titus, M.A.2
  • 3
    • 0036898465 scopus 로고    scopus 로고
    • Myosin-V, a versatile motor for short-range vesicle transport
    • DOI 10.1034/j.1600-0854.2002.31202.x
    • Langford G. M.: Myosin-V, a versatile motor for shortrange vesicle transport. Traffic 3, 859-865 (2002). (Pubitemid 35460591)
    • (2002) Traffic , vol.3 , Issue.12 , pp. 859-865
    • Langford, G.M.1
  • 8
    • 79959759830 scopus 로고    scopus 로고
    • Navigating the cytoskeleton with myosin X
    • Suppl. S, abstract 62-Symp
    • Rock R. S.: Navigating the cytoskeleton with myosin X. Biophys J 94, Part 2, Suppl. S, abstract 62-Symp (2008).
    • (2008) Biophys J , vol.94 , Issue.PART 2
    • Rock, R.S.1
  • 10
    • 0034431113 scopus 로고    scopus 로고
    • In vitro assays of processive myosin motors
    • DOI 10.1006/meth.2000.1089
    • Rock R. S., M. Rief, A. D. Mehta, J. A. Spudich: In vitro assays of processive myosin motors. Methods 22, 373-381 (2000). (Pubitemid 32896702)
    • (2000) Methods , vol.22 , Issue.4 , pp. 373-381
    • Rock, R.S.1    Rief, M.2    Mehta, A.D.3    Spudich, J.A.4
  • 12
    • 0036144267 scopus 로고    scopus 로고
    • The gated gait of the processive molecular motor, myosin V
    • DOI 10.1038/ncb732
    • Veigel C., F. Wang, M. L. Bartoo, J. R. Sellers, J. E. Molloy: The gated gait of the processive molecular motor, myosin V. Nat Cell Biol 4, 59-65 (2002). (Pubitemid 34071981)
    • (2002) Nature Cell Biology , vol.4 , Issue.1 , pp. 59-65
    • Veigel, C.1    Wang, F.2    Bartoo, M.L.3    Sellers, J.R.4    Molloy, J.E.5
  • 18
    • 0034700284 scopus 로고    scopus 로고
    • Actin and light chain isoform dependence of myosin V kinetics
    • De La Cruz E. M., A. L. Wells, H. L. Sweeney, E. M. Ostap: Actin and light chain isoform dependence of myosin V kinetics. Biochemistry 39, 14196-14202 (2000).
    • (2000) Biochemistry , vol.39 , pp. 14196-14202
    • De La Cruz, E.M.1    Wells, A.L.2    Sweeney, H.L.3    Ostap, E.M.4
  • 19
    • 0033850082 scopus 로고    scopus 로고
    • ADP inhibition of myosin V ATPase activity
    • De La Cruz E. M., H. L. Sweeney, E. M. Ostap: ADP inhibition of myosin V ATPase activity. Biophys J 79, 1524-1529 (2000).
    • (2000) Biophys J , vol.79 , pp. 1524-1529
    • De La Cruz, E.M.1    Sweeney, H.L.2    Ostap, E.M.3
  • 20
    • 0037007966 scopus 로고    scopus 로고
    • Kinetic characterization of the weak binding states of myosin V
    • DOI 10.1021/bi015969u
    • Yengo C. M., E. M. De la Cruz, D. Safer, E. M. Ostap, H. L. Sweeney: Kinetic characterization of the weak binding states of myosin V. Biochemistry 41, 8508-8517 (2002). (Pubitemid 34705506)
    • (2002) Biochemistry , vol.41 , Issue.26 , pp. 8508-8517
    • Yengo, C.M.1    De La Cruz, E.M.2    Safer, D.3    Ostap, E.M.4    Sweeney, H.L.5
  • 22
    • 0037468838 scopus 로고    scopus 로고
    • Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization
    • DOI 10.1038/nature01529
    • Forkey J. N., M. E. Quinlan, M. A. Shaw, J. E. Corrie, Y. E. Goldman: Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization. Nature 422, 399-404 (2003). (Pubitemid 36411387)
    • (2003) Nature , vol.422 , Issue.6930 , pp. 399-404
    • Forkey, J.N.1    Quinlan, M.E.2    Shaw, M.A.3    Corrie, J.E.T.4    Goldman, Y.E.5
  • 23
    • 0037832404 scopus 로고    scopus 로고
    • Myosin V walks hand-over-hand: Single fluorophore imaging with 1.5-nm localization
    • DOI 10.1126/science.1084398
    • Yildiz A., J. N. Forkey, S. A. McKinney, T. Ha, Y. E. Goldman, P. R. Selvin: Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization. Science 300, 2061-2065 (2003). (Pubitemid 36760126)
    • (2003) Science , vol.300 , Issue.5628 , pp. 2061-2065
    • Yildiz, A.1    Forkey, J.N.2    McKinney, S.A.3    Ha, T.4    Goldman, Y.E.5    Selvin, P.R.6
  • 27
    • 0141732282 scopus 로고    scopus 로고
    • A structural state of the myosin V motor without bound nucleotide
    • DOI 10.1038/nature01927
    • Coureux P. D., A. L. Wells, J. Menetrey, C. M. Yengo, C. A. Morris, H. L. Sweeney, A. Houdusse: A structural state of the myosin V motor without bound nucleotide. Nature 425, 419-423 (2003). (Pubitemid 37187273)
    • (2003) Nature , vol.425 , Issue.6956 , pp. 419-423
    • Coureux, P.-D.1    Wells, A.L.2    Menetrey, J.3    Yengo, C.M.4    Morris, C.A.5    Sweeney, H.L.6    Houdusse, A.7
  • 28
    • 17844385071 scopus 로고    scopus 로고
    • Differential labeling of myosin V heads with quantum dots allows direct visualization of hand-over-hand processivity
    • DOI 10.1529/biophysj.105.061903
    • Warshaw D. M., G. G. Kennedy, S. S. Work, E. B. Krementsova, S. Beck, K. M. Trybus: Differential labeling of myosin V heads with quantum dots allows direct visualization of hand-over-hand processivity. Biophys J 88, L30-L32 (2005). (Pubitemid 40586558)
    • (2005) Biophysical Journal , vol.88 , Issue.5
    • Warshaw, D.M.1    Kennedy, G.G.2    Work, S.S.3    Krementsova, E.B.4    Beck, S.5    Trybus, K.M.6
  • 31
    • 0031149266 scopus 로고    scopus 로고
    • Motor proteins: Myosin V - the multi-purpose transport motor
    • Titus M. A.: Motor proteins: myosin V-the multipurpose transport motor. Curr Biol 7, R301-R304 (1997). (Pubitemid 27195596)
    • (1997) Current Biology , vol.7 , Issue.5
    • Titus, M.A.1
  • 33
    • 34547986066 scopus 로고    scopus 로고
    • 'Should I stay or should I go?': Myosin V function in organelle trafficking
    • DOI 10.1042/BC20070021
    • Desnos C., S. Huet, F. Darchen: 'Should I stay or should I go?': myosin V function in organelle trafficking. Biol Cell 99, 411-423 (2007). (Pubitemid 47272224)
    • (2007) Biology of the Cell , vol.99 , Issue.8 , pp. 411-423
    • Desnos, C.1    Huet, S.2    Darchen, F.3
  • 34
    • 43049183000 scopus 로고    scopus 로고
    • Myosin V from head to tail
    • Trybus K. M.: Myosin V from head to tail. Cell and Mol Life Sci 65, 1378-1389 (2008).
    • (2008) Cell and Mol Life Sci , vol.65 , pp. 1378-1389
    • Trybus, K.M.1
  • 35
    • 43749088570 scopus 로고    scopus 로고
    • Myosin V
    • Ed: Coluccio L. M. Proteins and Cell Regulation, Springer Netherlands
    • Sellers J. R., L. S. Weisman: Myosin V. In: Myosins: A Superfamily of Molecular Motors, Ed: Coluccio L. M., Proteins and Cell Regulation 7, 289-323, Springer Netherlands (2008).
    • (2008) Myosins: A Superfamily of Molecular Motors , vol.7 , pp. 289-323
    • Sellers, J.R.1    Weisman, L.S.2
  • 36
    • 33846380243 scopus 로고    scopus 로고
    • Regulation and recycling of myosin V
    • DOI 10.1016/j.ceb.2006.12.014, PII S0955067406001955
    • Taylor K. A.: Regulation and recycling of myosin V. Curr Opin Cell Biol 19, 67-74 (2007). (Pubitemid 46127837)
    • (2007) Current Opinion in Cell Biology , vol.19 , Issue.1 , pp. 67-74
    • Taylor, K.A.1
  • 38
    • 0242677759 scopus 로고    scopus 로고
    • Myosin V motor proteins: Marching stepwise towards a mechanism
    • DOI 10.1083/jcb.200308093
    • Vale R. D.: Myosin V motor proteins: marching stepwise towards a mechanism. J Cell Biol 163, 445-450 (2003). (Pubitemid 37429857)
    • (2003) Journal of Cell Biology , vol.163 , Issue.3 , pp. 445-450
    • Vale, R.D.1
  • 39
    • 30844455998 scopus 로고    scopus 로고
    • Walking with myosin V
    • DOI 10.1016/j.ceb.2005.12.014, PII S0955067405001924, Cell Structure and Dynamics
    • Sellers J. R., C. Veigel: Walking with myosin V. Curr Opin Cell Biol 18, 68-73 (2006). (Pubitemid 43107610)
    • (2006) Current Opinion in Cell Biology , vol.18 , Issue.1 , pp. 68-73
    • Sellers, J.R.1    Veigel, C.2
  • 40
    • 0034949894 scopus 로고    scopus 로고
    • Myosin learns to walk
    • Mehta A.: Myosin learns to walk. J Cell Sci 114, 1981-1998 (2001). (Pubitemid 32586624)
    • (2001) Journal of Cell Science , vol.114 , Issue.11 , pp. 1981-1998
    • Mehta, A.1
  • 41
    • 0142075164 scopus 로고    scopus 로고
    • Myosin-V motility: These levers were made for walking
    • DOI 10.1016/S0962-8924(03)00172-7
    • Tyska M. J., M. S. Mooseker: Myosin-V motility: these levers were made for walking. Trends Cell Biol 13, 447-451 (2003). (Pubitemid 37289392)
    • (2003) Trends in Cell Biology , vol.13 , Issue.9 , pp. 447-451
    • Tyska, M.J.1    Mooseker, M.S.2
  • 44
    • 0037342115 scopus 로고    scopus 로고
    • A simple kinetic model describes the processivity of myosin-V
    • Kolomeisky A. B., M. E. Fisher: A simple kinetic model describes the processivity of myosin-V. Biophys J 84, 1642-1650 (2003). (Pubitemid 36322928)
    • (2003) Biophysical Journal , vol.84 , Issue.3 , pp. 1642-1650
    • Kolomeisky, A.B.1    Fisher, M.E.2
  • 45
    • 22244472947 scopus 로고    scopus 로고
    • Elastic lever-arm model for myosin V
    • DOI 10.1529/biophysj.104.046763
    • Vilfan A.: Elastic lever-arm model for myosin V. Biophys J 88, 3792-3805 (2005). (Pubitemid 40991095)
    • (2005) Biophysical Journal , vol.88 , Issue.6 , pp. 3792-3805
    • Vilfan, A.1
  • 46
    • 21244502885 scopus 로고    scopus 로고
    • Dynamics of myosin-V processivity
    • DOI 10.1529/biophysj.104.047662
    • Lan G., S. X. Sun: Dynamics of myosin-V processivity. Biophys J 88, 999-1008 (2005). (Pubitemid 40975933)
    • (2005) Biophysical Journal , vol.88 , Issue.2 , pp. 999-1008
    • Lan, G.1    Sun, S.X.2
  • 47
    • 33749435355 scopus 로고    scopus 로고
    • A kinetic model describing the processivity of myosin-V
    • DOI 10.1529/biophysj.105.070888
    • Skau K. I., R. B. Hoyle, M. S. Turner: A kinetic model describing the processivity of myosin-V. Biophys J 91, 2475-2489 (2006). (Pubitemid 44511703)
    • (2006) Biophysical Journal , vol.91 , Issue.7 , pp. 2475-2489
    • Skau, K.I.1    Hoyle, R.B.2    Turner, M.S.3
  • 48
    • 34249709457 scopus 로고    scopus 로고
    • A kinetic model of coordinated myosin V
    • DOI 10.1021/bi700526r
    • Wu Y., Y. Q. Gao, M. Karplus: A kinetic model of coordinated myosin V. Biochemistry 46, 6318-6330 (2007). (Pubitemid 46842875)
    • (2007) Biochemistry , vol.46 , Issue.21 , pp. 6318-6330
    • Wu, Y.1    Yi, Q.G.2    Karplus, M.3
  • 49
    • 33847680889 scopus 로고    scopus 로고
    • Dynamics of the unbound head during myosin V processive translocation
    • DOI 10.1038/nsmb1206, PII NSMB1206
    • Dunn A. R., J. A. Spudich: Dynamics of the unbound head during myosin V processive translocation. Nat Struct Mol Biol 14, 246-248 (2007). (Pubitemid 46355576)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.3 , pp. 246-248
    • Dunn, A.R.1    Spudich, J.A.2
  • 53
    • 41349113308 scopus 로고    scopus 로고
    • Understanding mechanochemical coupling in kinesins using first-passage-time processes
    • Kolomeisky A. B., E. B. Stukalin, A. A. Popov: Understanding mechanochemical coupling in kinesins using first-passage-time processes. Phys Rev E 71, 031902 (2005).
    • (2005) Phys Rev E , vol.71 , pp. 031902
    • Kolomeisky, A.B.1    Stukalin, E.B.2    Popov, A.A.3
  • 54
    • 47749142424 scopus 로고    scopus 로고
    • Load and Pi control flux through the branched kinetic cycle of myosin V
    • Kad N. M., K. M. Trybus, D. M. Warshaw: Load and Pi control flux through the branched kinetic cycle of myosin V. J Biol Chem 284, 17477-17484.
    • J Biol Chem , vol.284 , pp. 17477-17484
    • Kad, N.M.1    Trybus, K.M.2    Warshaw, D.M.3
  • 55
    • 34848896360 scopus 로고    scopus 로고
    • Engineering the processive run length of myosin V
    • DOI 10.1074/jbc.M703968200
    • Hodges A. R., E. B. Krementsova, K. M. Trybus: Engineering the processive run length of Myosin V. J Biol Chem 282, 27192-27197 (2007). (Pubitemid 47501930)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.37 , pp. 27192-27197
    • Hodges, A.R.1    Krementsova, E.B.2    Trybus, K.M.3
  • 56
    • 0033600904 scopus 로고    scopus 로고
    • Kinetic characterization of a monomeric unconventional myosin V construct
    • Trybus K. M., E. Krementsova, Y. Freyzon: Kinetic characterization of a monomeric unconventional myosin V construct. J Biol Chem 274, 27448-27456 (1999).
    • (1999) J Biol Chem , vol.274 , pp. 27448-27456
    • Trybus, K.M.1    Krementsova, E.2    Freyzon, Y.3
  • 59
    • 4544232738 scopus 로고    scopus 로고
    • A model of myosin V processivity
    • DOI 10.1074/jbc.M402583200
    • Rosenfeld S. S., H. L. Sweeney: A model of myosin V processivity. J Biol Chem 279, 40100-40111 (2004). (Pubitemid 39258285)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.38 , pp. 40100-40111
    • Rosenfeld, S.S.1    Sweeney, H.L.2
  • 60
    • 1542267772 scopus 로고    scopus 로고
    • Functional Role of Loop 2 in Myosin V
    • DOI 10.1021/bi035510v
    • Yengo C. M., H. L. Sweeney: Functional role of loop 2 in myosin V. Biochemistry 43, 2605-2612 (2004). (Pubitemid 38327856)
    • (2004) Biochemistry , vol.43 , Issue.9 , pp. 2605-2612
    • Yengo, C.M.1    Sweeney, H.L.2
  • 61
    • 38149111237 scopus 로고    scopus 로고
    • Kinetics of ADP dissociation from the trail and lead heads of actomyosin V following the power stroke
    • Forgacs E., S. Cartwright, T. Sakamoto, J. R. Sellers, J. E. T. Corrie, M. R. Webb, H. D. White: Kinetics of ADP dissociation from the trail and lead heads of actomyosin V following the power stroke. J Biol Chem 283, 766-773 (2008).
    • (2008) J Biol Chem , vol.283 , pp. 766-773
    • Forgacs, E.1    Cartwright, S.2    Sakamoto, T.3    Sellers, J.R.4    Corrie, J.E.T.5    Webb, M.R.6    White, H.D.7
  • 63
    • 26944449015 scopus 로고    scopus 로고
    • Load-dependent kinetics of myosin-V can explain its high processivity
    • DOI 10.1038/ncb1287, PII N1287
    • Veigel C., S. Schmitz, F. Wang, J. R. Sellers: Load-dependent kinetics of myosin-V can explain its high processivity. Nat Cell Biol 7, 861-869 (2005). (Pubitemid 41486286)
    • (2005) Nature Cell Biology , vol.7 , Issue.9 , pp. 861-869
    • Veigel, C.1    Schmitz, S.2    Wang, F.3    Sellers, J.R.4
  • 65
    • 4444384544 scopus 로고    scopus 로고
    • Nanometer localization of single fluorescent proteins: Evidence that myosin V walks hand-over-hand via telemark configuration
    • DOI 10.1529/biophysj.103.036897
    • Snyder G. E., T. Sakamoto, J. A. Hammer, J. R. Sellers, P. R. Selvin: Nanometer localization of single green fluorescent proteins: evidence that myosin V walks handover-hand via telemark configuration. Biophys J 87, 1776-1783 (2004). (Pubitemid 39167033)
    • (2004) Biophysical Journal , vol.87 , Issue.3 , pp. 1776-1783
    • Snyder, G.E.1    Sakamoto, T.2    Hammer III, J.A.3    Sellers, J.R.4    Selvin, P.R.5
  • 67
    • 33646568493 scopus 로고    scopus 로고
    • Adaptability of myosin V studied by simultaneous detection of position and orientation
    • Syed S., G. E. Snyder, C. Franzini-Armstrong, P. R. Selvin, Y. E. Goldman: Adaptability of myosin V studied by simultaneous detection of position and orientation. EMBO J 25, 1795-1803 (2006).
    • (2006) EMBO J , vol.25 , pp. 1795-1803
    • Syed, S.1    Snyder, G.E.2    Franzini-Armstrong, C.3    Selvin, P.R.4    Goldman, Y.E.5
  • 68
    • 0030744142 scopus 로고    scopus 로고
    • Kinesin hydrolyses one ATP per 8-nm step
    • DOI 10.1038/41111
    • Schnitzer M. J., S. M. Block: Kinesin hydrolyses one ATP per 8-nm step. Nature 388, 386-390 (1997). (Pubitemid 27334818)
    • (1997) Nature , vol.388 , Issue.6640 , pp. 386-390
    • Schnitzer, M.J.1    Block, S.M.2
  • 71
    • 19644377414 scopus 로고    scopus 로고
    • Mechanics of the kinesin step
    • DOI 10.1038/nature03528
    • Carter N. J., R. A. Cross: Mechanics of the kinesin step. Nature 435, 308-312 (2005). (Pubitemid 40745535)
    • (2005) Nature , vol.435 , Issue.7040 , pp. 308-312
    • Carter, N.J.1    Cross, R.A.2
  • 73
    • 37249048802 scopus 로고    scopus 로고
    • Myosin V movement: Lessons from molecular dynamics studies of IQ peptides in the lever arm
    • Ganoth A., E. Nachliel, R. Friedman, M. Gutman: Myosin V Movement: Lessons from Molecular Dynamics Studies of IQ Peptides in the Lever Arm. Biochemistry (2007).
    • (2007) Biochemistry
    • Ganoth, A.1    Nachliel, E.2    Friedman, R.3    Gutman, M.4
  • 74
    • 33845360185 scopus 로고    scopus 로고
    • Flexible light-chain and helical structure of F-actin explain the movement and step size of myosin-VI
    • DOI 10.1529/biophysj.106.089888
    • Lan G., S. X. Sun: Flexible light-chain and helical structure of F-actin explain the movement and step size of myosin-VI. Biophys J 91, 4002-4013 (2006). (Pubitemid 44887260)
    • (2006) Biophysical Journal , vol.91 , Issue.11 , pp. 4002-4013
    • Lan, G.1    Sun, S.X.2
  • 75
    • 33847272113 scopus 로고    scopus 로고
    • Molecular motors: A theorist's perspective
    • DOI 10.1146/annurev.physchem.58.032806.104532
    • Kolomeisky A. B., M. E. Fisher: Molecular motors: a theorist's perspective. Annu Rev Phys Chem 58, 675-695 (2007). (Pubitemid 46877604)
    • (2007) Annual Review of Physical Chemistry , vol.58 , pp. 675-695
    • Kolomeisky, A.B.1    Fisher, M.E.2
  • 76
    • 38049032321 scopus 로고    scopus 로고
    • Kinetic models for mechanoenzymes: Structural aspects under large loads
    • Tsygankov D., M. E. Fisher: Kinetic models for mechanoenzymes: Structural aspects under large loads. J Chem Phys 128, 015102 (2008).
    • (2008) J Chem Phys , vol.128 , pp. 015102
    • Tsygankov, D.1    Fisher, M.E.2
  • 77
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley A. F.: Muscle structure and theories of contraction. Prog Biophys Biophys Chem 7, 255-318 (1957).
    • (1957) Prog Biophys Biophys Chem , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 78
    • 0016180488 scopus 로고
    • Theoretical formalism for the sliding filament model of contraction of striated muscle. Part I
    • Hill T. L.: Theoretical formalism for the sliding filament model of contraction of striated muscle. Part I. Prog Biophys Mol Biol 28, 267-340 (1974).
    • (1974) Prog Biophys Mol Biol , vol.28 , pp. 267-340
    • Hill, T.L.1
  • 79
    • 0042344863 scopus 로고    scopus 로고
    • Instabilities in the transient response of muscle
    • Vilfan A., T. Duke: Instabilities in the transient response of muscle. Biophys J 85, 818-826 (2003).
    • (2003) Biophys J , vol.85 , pp. 818-826
    • Vilfan, A.1    Duke, T.2
  • 80
    • 33646468356 scopus 로고    scopus 로고
    • Insights into the chemomechanical coupling of the myosin motor from simulation of its ATP hydrolysis mechanism
    • Schwarzl S. M., J. C. Smith, S. Fischer: Insights into the chemomechanical coupling of the myosin motor from simulation of its ATP hydrolysis mechanism. Biochemistry 45, 5830-5847 (2006).
    • (2006) Biochemistry , vol.45 , pp. 5830-5847
    • Schwarzl, S.M.1    Smith, J.C.2    Fischer, S.3
  • 81
    • 33746513207 scopus 로고    scopus 로고
    • Simulations of the Myosin II Motor Reveal a Nucleotide-state Sensing Element that Controls the Recovery Stroke
    • DOI 10.1016/j.jmb.2006.06.022, PII S0022283606007650
    • Koppole S., J. C. Smith, S. Fischer: Simulations of the myosin II motor reveal a nucleotide-state sensing element that controls the recovery stroke. J Mol Biol 361, 604-616 (2006). (Pubitemid 44137359)
    • (2006) Journal of Molecular Biology , vol.361 , Issue.3 , pp. 604-616
    • Koppole, S.1    Smith, J.C.2    Fischer, S.3
  • 82
    • 33847278350 scopus 로고    scopus 로고
    • Mechanochemical coupling in the myosin motor domain. I. Insights from equilibrium active-site simulations
    • Yu H., L. Ma, Y. Yang, Q. Cui: Mechanochemical coupling in the myosin motor domain. I. Insights from equilibrium active-site simulations. PLoS Comput Biol 3, e21 (2007).
    • (2007) PLoS Comput Biol , vol.3
    • Yu, H.1    Ma, L.2    Yang, Y.3    Cui, Q.4
  • 84
    • 34447276474 scopus 로고    scopus 로고
    • The Structural Coupling between ATPase Activation and Recovery Stroke in the Myosin II Motor
    • DOI 10.1016/j.str.2007.06.008, PII S0969212607002146
    • Koppole S., J. C. Smith, S. Fischer: The structural coupling between ATPase activation and recovery stroke in the myosin II motor. Structure 15, 825-837 (2007). (Pubitemid 47042437)
    • (2007) Structure , vol.15 , Issue.7 , pp. 825-837
    • Koppole, S.1    Smith, J.C.2    Fischer, S.3
  • 85
    • 4444230478 scopus 로고    scopus 로고
    • How processive is the myosin-V motor?
    • Smith D. A.: How processive is the myosin-V motor? J Muscle Res Cell Motil 25, 215-217 (2004).
    • (2004) J Muscle Res Cell Motil , vol.25 , pp. 215-217
    • Smith, D.A.1
  • 86
    • 33746132537 scopus 로고    scopus 로고
    • An elastically tethered viscous load imposes a regular gait on the motion of myosin-V. Simulation of the effect of transient force relaxation on a stochastic process
    • DOI 10.1098/rsif.2005.0098
    • Schilstra M. J., S. R. Martin: An elastically tethered viscous load imposes a regular gait on the motion of myosin-V. Simulation of the effect of transient force relaxation on a stochastic process. J R Soc Interface 3, 153-165 (2006). (Pubitemid 46682214)
    • (2006) Journal of the Royal Society Interface , vol.3 , Issue.6 , pp. 153-165
    • Schilstra, M.J.1    Martin, S.R.2
  • 90
    • 0030606512 scopus 로고    scopus 로고
    • Is the lever arm of myosin a molecular elastic element?
    • Howard J., J. A. Spudich: Is the lever arm of myosin a molecular elastic element? Proc Natl Acad Sci USA 93, 4462-4464 (1996).
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4462-4464
    • Howard, J.1    Spudich, J.A.2
  • 91
    • 28944448143 scopus 로고    scopus 로고
    • Influence of fluctuations in actin structure on myosin V step size
    • DOI 10.1021/ci050182m
    • Vilfan A.: Influence of fluctuations in actin structure on myosin V step size. J Chem Inf Model 45, 1672-1675 (2005). (Pubitemid 41784738)
    • (2005) Journal of Chemical Information and Modeling , vol.45 , Issue.6 , pp. 1672-1675
    • Vilfan, A.1
  • 94
    • 0035312384 scopus 로고    scopus 로고
    • Myosin motors: Missing structures and hidden springs
    • DOI 10.1016/S0959-440X(00)00188-3
    • Houdusse A., H. L. Sweeney: Myosin motors: missing structures and hidden springs. Curr Opin Struct Biol 11, 182-194 (2001). (Pubitemid 32289420)
    • (2001) Current Opinion in Structural Biology , vol.11 , Issue.2 , pp. 182-194
    • Houdusse, A.1    Sweeney, H.L.2
  • 95
    • 0141843643 scopus 로고    scopus 로고
    • Elechron cryo-microscopy shows how strong binding of myosin to actin releases nucleotide
    • DOI 10.1038/nature02005
    • Holmes K. C., I. Angert, F. J. Kull, W. Jahn, R. R. Schroder: Electron cryo-microscopy shows how strong binding of myosin to actin releases nucleotide. Nature 425, 423-427 (2003). (Pubitemid 37187274)
    • (2003) Nature , vol.425 , Issue.6956 , pp. 423-427
    • Holmes, K.C.1    Angert, I.2    Kull, F.J.3    Jahn, W.4    Schroder, R.R.5
  • 98
    • 10644225267 scopus 로고    scopus 로고
    • Three myosin V structures delineate essential features of chemo-mechanical transduction
    • DOI 10.1038/sj.emboj.7600458
    • Coureux P. D., H. L. Sweeney, A. Houdusse: Three myosin V structures delineate essential features of chemomechanical transduction. EMBO J 23, 4527-4537 (2004). (Pubitemid 39657853)
    • (2004) EMBO Journal , vol.23 , Issue.23 , pp. 4527-4537
    • Coureux, P.-D.1    Sweeney, H.L.2    Houdusse, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.