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Volumn 93, Issue 3, 2008, Pages 172-180

A possible mechanism for determining the directionality of myosin molecular motors

Author keywords

Actin; Direction; Molecular motor; Myosin; Processive; Structure

Indexed keywords

ACTIN; MOLECULAR MOTOR; MYOSIN; MYOSIN V; MYOSIN VI;

EID: 48049098532     PISSN: 03032647     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biosystems.2008.03.009     Document Type: Article
Times cited : (10)

References (34)
  • 3
    • 0036421146 scopus 로고    scopus 로고
    • Molecular modeling of averaged rigor crossbridges from tomograms of insect flight muscle
    • Chen L.F., Winkler H., Reedy M.K., Reedy M.C., and Taylor K.A. Molecular modeling of averaged rigor crossbridges from tomograms of insect flight muscle. J. Struct. Biol. 138 (2002) 92-104
    • (2002) J. Struct. Biol. , vol.138 , pp. 92-104
    • Chen, L.F.1    Winkler, H.2    Reedy, M.K.3    Reedy, M.C.4    Taylor, K.A.5
  • 5
    • 33847344645 scopus 로고    scopus 로고
    • Cooperative actions between myosin heads bring effective functions
    • Esaki S., Ishii Y., Nishikawa M., and Yanagida T. Cooperative actions between myosin heads bring effective functions. Biosystems 88 (2007) 293-300
    • (2007) Biosystems , vol.88 , pp. 293-300
    • Esaki, S.1    Ishii, Y.2    Nishikawa, M.3    Yanagida, T.4
  • 6
    • 0037050015 scopus 로고    scopus 로고
    • Stretching the lever-arm theory
    • Geeves M.A. Stretching the lever-arm theory. Nature 415 (2002) 129-131
    • (2002) Nature , vol.415 , pp. 129-131
    • Geeves, M.A.1
  • 7
    • 0032883413 scopus 로고    scopus 로고
    • Structural mechanism of muscle contraction
    • Geeves M.A., and Holmes K.C. Structural mechanism of muscle contraction. Annu. Rev. Biochem. 68 (1999) 687-728
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 687-728
    • Geeves, M.A.1    Holmes, K.C.2
  • 8
    • 0032559298 scopus 로고    scopus 로고
    • Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin
    • Ishijima A., Kojima H., Funatsu T., Tokunaga M., Higuchi H., Tanaka H., and Yanagida T. Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin. Cell 92 (1998) 161-171
    • (1998) Cell , vol.92 , pp. 161-171
    • Ishijima, A.1    Kojima, H.2    Funatsu, T.3    Tokunaga, M.4    Higuchi, H.5    Tanaka, H.6    Yanagida, T.7
  • 9
    • 33750063183 scopus 로고    scopus 로고
    • A point mutation in the SH1 helix alters elasticity and thermal stability of myosin II
    • Iwai S., Hanamoto D., and Chaen S. A point mutation in the SH1 helix alters elasticity and thermal stability of myosin II. J. Biol. Chem. 281 (2006) 30736-30744
    • (2006) J. Biol. Chem. , vol.281 , pp. 30736-30744
    • Iwai, S.1    Hanamoto, D.2    Chaen, S.3
  • 11
    • 33845360185 scopus 로고    scopus 로고
    • Flexible light-chain and helical structure of F-actin explain the movement and step size of myosin-VI
    • Lan G., and Sun S.X. Flexible light-chain and helical structure of F-actin explain the movement and step size of myosin-VI. Biophys. J. 91 (2006) 4002-4013
    • (2006) Biophys. J. , vol.91 , pp. 4002-4013
    • Lan, G.1    Sun, S.X.2
  • 12
    • 34047208553 scopus 로고    scopus 로고
    • Stiffness and fraction of myosin motors responsible for active force in permeabilised muscle fibers from rabbit psoas
    • Linari M., Caremani M., Piperio C., Brandt P., and Lombardi V. Stiffness and fraction of myosin motors responsible for active force in permeabilised muscle fibers from rabbit psoas. Biophys. J. 92 (2007) 2476-2490
    • (2007) Biophys. J. , vol.92 , pp. 2476-2490
    • Linari, M.1    Caremani, M.2    Piperio, C.3    Brandt, P.4    Lombardi, V.5
  • 13
    • 33746129173 scopus 로고    scopus 로고
    • Three-dimensional structure of the myosin V inhibited state by cryoelectron tomography
    • Liu J., Taylor D.W., Krementsova E.B., Trybus K.M., and Taylor K.A. Three-dimensional structure of the myosin V inhibited state by cryoelectron tomography. Nature 442 (2006) 208-211
    • (2006) Nature , vol.442 , pp. 208-211
    • Liu, J.1    Taylor, D.W.2    Krementsova, E.B.3    Trybus, K.M.4    Taylor, K.A.5
  • 14
    • 0015214368 scopus 로고
    • Mechanism of adenosine triphosphate hydrolysis by actomyosin
    • Lymn R.W., and Taylor E.W. Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry 10 (1971) 4617-4624
    • (1971) Biochemistry , vol.10 , pp. 4617-4624
    • Lymn, R.W.1    Taylor, E.W.2
  • 15
    • 0242522179 scopus 로고    scopus 로고
    • An electromechanical model of myosin molecular motors
    • Masuda T. An electromechanical model of myosin molecular motors. J. Theor. Biol. 225 (2003) 507-515
    • (2003) J. Theor. Biol. , vol.225 , pp. 507-515
    • Masuda, T.1
  • 16
    • 0030878880 scopus 로고    scopus 로고
    • Detection of single-molecule interactions using correlated thermal diffusion
    • Mehta A.D., Finer J.T., and Spucich J.A. Detection of single-molecule interactions using correlated thermal diffusion. Proc. Natl. Acad. Sci. U.S.A. 94 (1997) 7927-7931
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 7927-7931
    • Mehta, A.D.1    Finer, J.T.2    Spucich, J.A.3
  • 19
    • 0030992359 scopus 로고    scopus 로고
    • Scanning force microscopy of the interaction events between a single molecule of heavy meromyosin and actin
    • Nakajima H., Kunioka Y., Nakano K., Shimizu K., Seto M., and Ando T. Scanning force microscopy of the interaction events between a single molecule of heavy meromyosin and actin. Biochem. Biophys. Res. Commun. 234 (1997) 178-182
    • (1997) Biochem. Biophys. Res. Commun. , vol.234 , pp. 178-182
    • Nakajima, H.1    Kunioka, Y.2    Nakano, K.3    Shimizu, K.4    Seto, M.5    Ando, T.6
  • 20
    • 0142122076 scopus 로고    scopus 로고
    • Single molecule processes on the stepwise movement of ATP-driven molecular motors
    • Nishiyama M., Higuchi H., Ishii Y., Taniguchi Y., and Yanagida T. Single molecule processes on the stepwise movement of ATP-driven molecular motors. Biosystems 71 (2003) 145-156
    • (2003) Biosystems , vol.71 , pp. 145-156
    • Nishiyama, M.1    Higuchi, H.2    Ishii, Y.3    Taniguchi, Y.4    Yanagida, T.5
  • 26
    • 0033619228 scopus 로고    scopus 로고
    • Myosin steps backwards
    • Schliwa M. Myosin steps backwards. Nature 401 (1999) 431-432
    • (1999) Nature , vol.401 , pp. 431-432
    • Schliwa, M.1
  • 27
    • 0142026805 scopus 로고    scopus 로고
    • A chemically driven fluctuating ratchet model for actomyosin interaction
    • Shimokawa T., Sato S., Buonocore A., and Ricciardi L.M. A chemically driven fluctuating ratchet model for actomyosin interaction. Biosystems 71 (2003) 179-187
    • (2003) Biosystems , vol.71 , pp. 179-187
    • Shimokawa, T.1    Sato, S.2    Buonocore, A.3    Ricciardi, L.M.4
  • 29
    • 1142286682 scopus 로고    scopus 로고
    • Molecular engineering of a backward-moving myosin motor
    • Tsiavaliaris G., Fujita-Becker S., and Manstein D.J. Molecular engineering of a backward-moving myosin motor. Nature 427 (2004) 558-561
    • (2004) Nature , vol.427 , pp. 558-561
    • Tsiavaliaris, G.1    Fujita-Becker, S.2    Manstein, D.J.3
  • 30
    • 0031656226 scopus 로고    scopus 로고
    • The stiffness of rabbit skeletal actomyosin cross-bridges determined with an optical tweezers transducer
    • Veigel C., Bartoo M.L., White D.C.S., Sparrow J.C., and Molloy J.E. The stiffness of rabbit skeletal actomyosin cross-bridges determined with an optical tweezers transducer. Biophys. J. 75 (1998) 1424-1438
    • (1998) Biophys. J. , vol.75 , pp. 1424-1438
    • Veigel, C.1    Bartoo, M.L.2    White, D.C.S.3    Sparrow, J.C.4    Molloy, J.E.5
  • 32
    • 26944449015 scopus 로고    scopus 로고
    • Load-dependent kinetics of myosin-V can explain its high processivity
    • Veigel C., Schmitz S., Wang F., and Sellers J.R. Load-dependent kinetics of myosin-V can explain its high processivity. Nat. Cell Biol. 7 (2005) 861-869
    • (2005) Nat. Cell Biol. , vol.7 , pp. 861-869
    • Veigel, C.1    Schmitz, S.2    Wang, F.3    Sellers, J.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.