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Volumn 58, Issue , 1996, Pages 1-19

A personal view of muscle and motility mechanisms

Author keywords

autobiography; contraction mechanism; electron microscopy; molecular structure; X ray

Indexed keywords

ACTIN; MYOSIN;

EID: 0029917475     PISSN: 00664278     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.ph.58.030196.000245     Document Type: Review
Times cited : (44)

References (50)
  • 1
    • 9244227196 scopus 로고
    • An electron microscope and X-ray study of actin: II. X-rays
    • Astbury WT, Spark C. 1947. An electron microscope and X-ray study of actin: II. X-rays. Biochim. Biophys. Acta 1:388-92
    • (1947) Biochim. Biophys. Acta , vol.1 , pp. 388-392
    • Astbury, W.T.1    Spark, C.2
  • 2
    • 0040852540 scopus 로고
    • X-ray diffraction studies on protein fibers. II. Feather rachis, porcupine quill tip and clam muscle
    • Bear RS. 1944. X-ray diffraction studies on protein fibers. II. Feather rachis, porcupine quill tip and clam muscle. J. Am. Chem. Soc. 66:2043-50
    • (1944) J. Am. Chem. Soc. , vol.66 , pp. 2043-2050
    • Bear, R.S.1
  • 3
    • 1542728587 scopus 로고
    • Small angle X-ray diffraction studies of muscle
    • Bear RS. 1945. Small angle X-ray diffraction studies of muscle. J. Am. Chem. Soc. 67:1625-26
    • (1945) J. Am. Chem. Soc. , vol.67 , pp. 1625-1626
    • Bear, R.S.1
  • 4
    • 0025222347 scopus 로고
    • Bead movement by single kinesin molecules studied by optical tweezers
    • Block SM, Goldstein LSB, Schnapp BJ. 1990. Bead movement by single kinesin molecules studied by optical tweezers. Nature 348:348-52
    • (1990) Nature , vol.348 , pp. 348-352
    • Block, S.M.1    Goldstein, L.S.B.2    Schnapp, B.J.3
  • 5
    • 9244257998 scopus 로고
    • Cold Spring Harbor Symposium on Quantitative Biology
    • Cold Spring Harbor Symposium on Quantitative Biology. 1972. The Mechanism of Muscle Contraction. Vol. 37
    • (1972) The Mechanism of Muscle Contraction , vol.37
  • 6
    • 0000668797 scopus 로고
    • Reconstruction of the three-dimensional structures from electron micrographs
    • DeRosier DJ, Klug A. 1968. Reconstruction of the three-dimensional structures from electron micrographs. Nature 217:130-34
    • (1968) Nature , vol.217 , pp. 130-134
    • DeRosier, D.J.1    Klug, A.2
  • 7
    • 33744818386 scopus 로고
    • An electrostatic focussing system and its application to a fine-focus X-ray tube
    • Ehrenberg W, Spear WE. 1951. An electrostatic focussing system and its application to a fine-focus X-ray tube. Proc. Phys. Soc. B 64:67-71
    • (1951) Proc. Phys. Soc. B , vol.64 , pp. 67-71
    • Ehrenberg, W.1    Spear, W.E.2
  • 8
    • 85025365054 scopus 로고
    • An X-ray and light diffraction study of the filament lattice of striated muscle in the living state and in rigor
    • Elliott GF, Lowy J, Worthington CR. 1963. An X-ray and light diffraction study of the filament lattice of striated muscle in the living state and in rigor. J. Mol. Biol. 6:295-305
    • (1963) J. Mol. Biol. , vol.6 , pp. 295-305
    • Elliott, G.F.1    Lowy, J.2    Worthington, C.R.3
  • 9
    • 0028261701 scopus 로고
    • Single myosin mechanics: Piconewton forces and nanometre steps
    • Finer JT, Simmons RM, Spudich JA. 1994. Single myosin mechanics: piconewton forces and nanometre steps. Nature 368:113-19
    • (1994) Nature , vol.368 , pp. 113-119
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 10
    • 36849124390 scopus 로고
    • The structure of certain muscle fibrils as revealed by the use of electron stains
    • Hall CE, Jakus MA, Schmitt FO. 1945. The structure of certain muscle fibrils as revealed by the use of electron stains. J. Appl. Phys. 16:459-65
    • (1945) J. Appl. Phys. , vol.16 , pp. 459-465
    • Hall, C.E.1    Jakus, M.A.2    Schmitt, F.O.3
  • 11
    • 0000975551 scopus 로고
    • The structural basis of the cross-striations in muscle
    • Hanson J, Huxley HE. 1953. The structural basis of the cross-striations in muscle. Nature 172:530-32
    • (1953) Nature , vol.172 , pp. 530-532
    • Hanson, J.1    Huxley, H.E.2
  • 13
    • 85010916780 scopus 로고
    • The structure of F-actin and of actin filaments isolated from muscle
    • Hanson J, Lowy J. 1963. The structure of F-actin and of actin filaments isolated from muscle. J. Mol. Biol. 6:46-60
    • (1963) J. Mol. Biol. , vol.6 , pp. 46-60
    • Hanson, J.1    Lowy, J.2
  • 14
    • 0000733783 scopus 로고
    • X-ray evidence for a conformational change in the actin-containing filaments of vertebrate striated muscle
    • Haselgrove JC. 1972. X-ray evidence for a conformational change in the actin-containing filaments of vertebrate striated muscle. Cold Spring Harbor Symp. Quant. Biol. 37:341-52
    • (1972) Cold Spring Harbor Symp. Quant. Biol. , vol.37 , pp. 341-352
    • Haselgrove, J.C.1
  • 15
    • 0015801643 scopus 로고
    • X-ray evidence for radial crossbridge movement and for the sliding filament model in actively contracting skeletal muscle
    • Haselgrove JC, Huxley HE. 1973. X-ray evidence for radial crossbridge movement and for the sliding filament model in actively contracting skeletal muscle. J. Mol. Biol. 77:549-68
    • (1973) J. Mol. Biol. , vol.77 , pp. 549-568
    • Haselgrove, J.C.1    Huxley, H.E.2
  • 17
    • 0000219872 scopus 로고
    • Structural changes in muscle during contraction. Interference microscopy of living muscle fibers
    • Huxley AF, Niedergerke R. 1954. Structural changes in muscle during contraction. Interference microscopy of living muscle fibers. Nature 173:971-73
    • (1954) Nature , vol.173 , pp. 971-973
    • Huxley, A.F.1    Niedergerke, R.2
  • 18
    • 0015236610 scopus 로고
    • Proposed mechanism of force generation in striated muscle
    • Huxley AF, Simmons RM. 1971. Proposed mechanism of force generation in striated muscle. Nature 233:533-38
    • (1971) Nature , vol.233 , pp. 533-538
    • Huxley, A.F.1    Simmons, R.M.2
  • 19
    • 0013668565 scopus 로고
    • Low-angle X-ray diffraction studies on muscle
    • Huxley HE. 1951. Low-angle X-ray diffraction studies on muscle. Disc. Faraday Soc. 11:148
    • (1951) Disc. Faraday Soc. , vol.11 , pp. 148
    • Huxley, H.E.1
  • 20
    • 0000700952 scopus 로고
    • Electron microscope studies of the organization of the filaments in striated muscle
    • Huxley HE. 1953a. Electron microscope studies of the organization of the filaments in striated muscle. Biochim. Biophys. Acta 12:387-94
    • (1953) Biochim. Biophys. Acta , vol.12 , pp. 387-394
    • Huxley, H.E.1
  • 21
    • 77049131135 scopus 로고
    • X-ray analysis and the problem of muscle
    • Huxley HE. 1953b. X-ray analysis and the problem of muscle. Proc. R. Soc. London Ser. B 141:59-62
    • (1953) Proc. R. Soc. London Ser. B , vol.141 , pp. 59-62
    • Huxley, H.E.1
  • 23
    • 0001353052 scopus 로고
    • The double array of filaments in cross-striated muscle
    • Huxley HE. 1957. The double array of filaments in cross-striated muscle. J. Biophys. Biochem. Cytol. 3:631-48
    • (1957) J. Biophys. Biochem. Cytol. , vol.3 , pp. 631-648
    • Huxley, H.E.1
  • 24
    • 85012414651 scopus 로고
    • Electron microscope studies of the structure of natural and synthetic protein filaments from muscle
    • Huxley HE. 1963. Electron microscope studies of the structure of natural and synthetic protein filaments from muscle. J. Mol. Biol. 7:281-308
    • (1963) J. Mol. Biol. , vol.7 , pp. 281-308
    • Huxley, H.E.1
  • 25
    • 0014414249 scopus 로고
    • Structural differences between resting and rigor muscle: Evidence from intensity changes in the low-angle equatorial X-ray diagram
    • Huxley HE. 1968. Structural differences between resting and rigor muscle: evidence from intensity changes in the low-angle equatorial X-ray diagram. J. Mol. Biol. 37:507-20
    • (1968) J. Mol. Biol. , vol.37 , pp. 507-520
    • Huxley, H.E.1
  • 26
    • 0000244537 scopus 로고
    • Structural changes in the actin and myosin-containing filaments during contraction
    • Huxley HE. 1972. Structural changes in the actin and myosin-containing filaments during contraction. Cold Spring Harbor Symp. Quant. Biol. 37:361-76
    • (1972) Cold Spring Harbor Symp. Quant. Biol. , vol.37 , pp. 361-376
    • Huxley, H.E.1
  • 27
    • 85010249552 scopus 로고
    • The low angle X-ray diagram of vertebrate striated muscle and its behavior during contraction and rigor
    • Huxley HE, Brown W. 1967. The low angle X-ray diagram of vertebrate striated muscle and its behavior during contraction and rigor. J. Mol. Biol. 30: 383-434
    • (1967) J. Mol. Biol. , vol.30 , pp. 383-434
    • Huxley, H.E.1    Brown, W.2
  • 28
    • 0020653743 scopus 로고
    • Time-resolved X-ray diffraction studies on vertebrate striated muscle
    • Huxley HE, Faruqi AR. 1983. Time-resolved X-ray diffraction studies on vertebrate striated muscle. Annu. Rev. Biophys. Bioeng. 12:381-417
    • (1983) Annu. Rev. Biophys. Bioeng. , vol.12 , pp. 381-417
    • Huxley, H.E.1    Faruqi, A.R.2
  • 29
    • 0019990501 scopus 로고
    • Time resolved X-ray diffraction studies of the myosin layerline reflections during muscle contraction
    • Huxley HE, Faruqi AR, Kress M, Bordas J, Koch MHJ. 1982. Time resolved X-ray diffraction studies of the myosin layerline reflections during muscle contraction. J. Mol. Biol. 158:637-84
    • (1982) J. Mol. Biol. , vol.158 , pp. 637-684
    • Huxley, H.E.1    Faruqi, A.R.2    Kress, M.3    Bordas, J.4    Koch, M.H.J.5
  • 30
    • 36949093311 scopus 로고
    • Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation
    • Huxley HE, Hanson J. 1954. Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation. Nature 173:973-76
    • (1954) Nature , vol.173 , pp. 973-976
    • Huxley, H.E.1    Hanson, J.2
  • 31
    • 4243837513 scopus 로고
    • Time-course of spacing change of 143 Å meridional crossbridge reflection during rapid shortening
    • Huxley HE, Simmons RM, Faruqi AR. 1989. Time-course of spacing change of 143 Å meridional crossbridge reflection during rapid shortening. Biophys. J. 55:12a
    • (1989) Biophys. J. , vol.55
    • Huxley, H.E.1    Simmons, R.M.2    Faruqi, A.R.3
  • 32
    • 0021104871 scopus 로고
    • Changes in the X-ray reflections from contracting muscle during rapid mechanical transients and their structural implications
    • Huxley HE, Simmons RM, Faruqi AR, Kress M, Bordas J, Koch MHJ. 1983. Changes in the X-ray reflections from contracting muscle during rapid mechanical transients and their structural implications. J. Mol. Biol. 169:469-506
    • (1983) J. Mol. Biol. , vol.169 , pp. 469-506
    • Huxley, H.E.1    Simmons, R.M.2    Faruqi, A.R.3    Kress, M.4    Bordas, J.5    Koch, M.H.J.6
  • 33
    • 85025305661 scopus 로고
    • Electron microscope observations on the structure of microsomal particles from E. coli
    • Huxley HE, Zubay G. 1960a. Electron microscope observations on the structure of microsomal particles from E. coli. J. Mol. Biol. 2:10-18
    • (1960) J. Mol. Biol. , vol.2 , pp. 10-18
    • Huxley, H.E.1    Zubay, G.2
  • 34
    • 85025343606 scopus 로고
    • The structure of the protein shell of turnip yellow mosaic virus
    • Huxley HE, Zubay G. 1960b. The structure of the protein shell of turnip yellow mosaic virus. J. Mol. Biol. 2:189-96
    • (1960) J. Mol. Biol. , vol.2 , pp. 189-196
    • Huxley, H.E.1    Zubay, G.2
  • 35
    • 0026534392 scopus 로고
    • Myosin head movements are synchronous with the elementary force-generating process in muscle
    • Irving M, Lombardi V, Piazzesi G, Ferenczi M. 1992. Myosin head movements are synchronous with the elementary force-generating process in muscle. Nature 357:156-58
    • (1992) Nature , vol.357 , pp. 156-158
    • Irving, M.1    Lombardi, V.2    Piazzesi, G.3    Ferenczi, M.4
  • 38
    • 0023919181 scopus 로고
    • Force measurements by micromanipulation of a single actin filament by glass needles
    • Kishino A, Yanagida T. 1988. Force measurements by micromanipulation of a single actin filament by glass needles. Nature 334:74-76
    • (1988) Nature , vol.334 , pp. 74-76
    • Kishino, A.1    Yanagida, T.2
  • 39
    • 0023042009 scopus 로고
    • Structural changes during activation of frog muscle studied by time-resolved X-ray diffraction
    • Kress M, Huxley HE, Faruqi AR, Hendrix J. 1986. Structural changes during activation of frog muscle studied by time-resolved X-ray diffraction. J. Mol. Biol. 188:325-42
    • (1986) J. Mol. Biol. , vol.188 , pp. 325-342
    • Kress, M.1    Huxley, H.E.2    Faruqi, A.R.3    Hendrix, J.4
  • 40
    • 0001675681 scopus 로고
    • Fluorescent actin filaments move on myosin fixed to a glass surface
    • Kron SJ, Spudich JA. 1986. Fluorescent actin filaments move on myosin fixed to a glass surface. Proc. Natl. Acad. Sci. USA 83:6272-76
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6272-6276
    • Kron, S.J.1    Spudich, J.A.2
  • 41
    • 0015214368 scopus 로고
    • Mechanism of adenosine triphosphate hydrolysis by actomyosin
    • Lymn RW, Taylor EW. 1971. Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry 10: 4617-24
    • (1971) Biochemistry , vol.10 , pp. 4617-4624
    • Lymn, R.W.1    Taylor, E.W.2
  • 42
    • 0014966071 scopus 로고
    • Electron microscope observations of actomyosin and actin preparations from Physarum polycephalum
    • Nachmias VT, Huxley HE, Kessler D. 1970. Electron microscope observations of actomyosin and actin preparations from Physarum polycephalum. J. Mol. Biol. 50:83-90
    • (1970) J. Mol. Biol. , vol.50 , pp. 83-90
    • Nachmias, V.T.1    Huxley, H.E.2    Kessler, D.3
  • 43
    • 0027226230 scopus 로고
    • Structure of the actin-myosin complex and its implications for muscle contraction
    • Rayment I, Holden HM, Whittaker M, Yohn CB, Lorenz M, et al. 1993a. Structure of the actin-myosin complex and its implications for muscle contraction. Science 261:58-65
    • (1993) Science , vol.261 , pp. 58-65
    • Rayment, I.1    Holden, H.M.2    Whittaker, M.3    Yohn, C.B.4    Lorenz, M.5
  • 45
    • 0000105113 scopus 로고
    • Synchrotron radiation as a source for X-ray diffraction
    • Rosenbaum G, Holmes KC, Witz J. 1971. Synchrotron radiation as a source for X-ray diffraction. Nature 230:434-37
    • (1971) Nature , vol.230 , pp. 434-437
    • Rosenbaum, G.1    Holmes, K.C.2    Witz, J.3
  • 46
    • 0020586332 scopus 로고
    • Movement of myosin-coated fluorescent beads on actin cables in vitro
    • Sheetz MP, Spudich JA. 1983. Movement of myosin-coated fluorescent beads on actin cables in vitro. Nature 303:31-35
    • (1983) Nature , vol.303 , pp. 31-35
    • Sheetz, M.P.1    Spudich, J.A.2
  • 47
    • 0028362281 scopus 로고
    • Ultrastructure of skeletal muscle fibers studied by a plunge quick-freezing method: Myofilament lengths
    • Sosa H, Popp D, Ouyang G, Huxley HE. 1994. Ultrastructure of skeletal muscle fibers studied by a plunge quick-freezing method: myofilament lengths. Biophys. J. 67:283-92
    • (1994) Biophys. J. , vol.67 , pp. 283-292
    • Sosa, H.1    Popp, D.2    Ouyang, G.3    Huxley, H.E.4
  • 48
    • 0022385727 scopus 로고
    • Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility
    • Vale RD, Reese TS, Sheetz MP. 1985. Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility. Cell 42:39-50
    • (1985) Cell , vol.42 , pp. 39-50
    • Vale, R.D.1    Reese, T.S.2    Sheetz, M.P.3
  • 50
    • 0021261156 scopus 로고
    • Direct observation of movement of single F-actin filaments in the presence of myosin
    • Yanagida T, Nakase M, Nishiyama K, Oosawa F. 1984. Direct observation of movement of single F-actin filaments in the presence of myosin. Nature 307:58-60
    • (1984) Nature , vol.307 , pp. 58-60
    • Yanagida, T.1    Nakase, M.2    Nishiyama, K.3    Oosawa, F.4


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