메뉴 건너뛰기




Volumn 78, Issue 3, 2000, Pages 1458-1473

Cross-bridge attachment during high-speed active shortening of skinned fibers of the rabbit psoas muscle: Implications for cross-bridge action during maximum velocity of filament sliding

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATE MAGNESIUM; CALCIUM ION; MYOSIN;

EID: 0034008022     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76699-9     Document Type: Article
Times cited : (37)

References (75)
  • 1
    • 0018881743 scopus 로고
    • Regulation and kinetics of the actin-myosin-ATP interaction
    • Adelstein, R. S., and E. Eisenberg. 1980. Regulation and kinetics of the actin-myosin-ATP interaction. Annu. Rev. Biochem. 49:921-956.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 921-956
    • Adelstein, R.S.1    Eisenberg, E.2
  • 4
    • 0019171105 scopus 로고
    • 2+ concentration on maximum unloaded shortening velocity: Measurements on single glycerinated rabbit psoas fibers
    • 2+ concentration on maximum unloaded shortening velocity: measurements on single glycerinated rabbit psoas fibers. J. Muscle Res. Cell Motil. 1:409-428.
    • (1980) J. Muscle Res. Cell Motil. , vol.1 , pp. 409-428
    • Brenner, B.1
  • 5
    • 0020536686 scopus 로고
    • Technique for stabilizing the striation pattern in maximally calcium-activated skinned rabbit psoas fibers
    • Brenner, B. 1983a. Technique for stabilizing the striation pattern in maximally calcium-activated skinned rabbit psoas fibers. Biophys. J. 41: 99-102.
    • (1983) Biophys. J. , vol.41 , pp. 99-102
    • Brenner, B.1
  • 6
    • 0343919977 scopus 로고
    • Cross-bridge attachment during isotonic shortening in single skinned rabbit psoas fibers
    • Brenner, B. 1983b. Cross-bridge attachment during isotonic shortening in single skinned rabbit psoas fibers. Biophys. J. 41:33a.
    • (1983) Biophys. J. , vol.41
    • Brenner, B.1
  • 7
    • 0022338370 scopus 로고
    • Sarcomeric domain organization within single skinned rabbit psoas fibers and its effects on laser light diffraction patterns
    • Brenner, B. 1985. Sarcomeric domain organization within single skinned rabbit psoas fibers and its effects on laser light diffraction patterns. Biophys. J. 48:967-982.
    • (1985) Biophys. J. , vol.48 , pp. 967-982
    • Brenner, B.1
  • 8
    • 0023006793 scopus 로고
    • The cross-bridge cycle in muscle. Mechanical, biochemical, and structural studies on single skinned rabbit psoas fibers to characterize cross-bridge kinetics in muscle for correlation with the actomyosin-ATPase in solution
    • Brenner, B. 1986. The cross-bridge cycle in muscle. Mechanical, biochemical, and structural studies on single skinned rabbit psoas fibers to characterize cross-bridge kinetics in muscle for correlation with the actomyosin-ATPase in solution. Basic Res. Cardiol. 81:1-15.
    • (1986) Basic Res. Cardiol. , vol.81 , pp. 1-15
    • Brenner, B.1
  • 9
    • 4243834695 scopus 로고
    • An experimental approach to determine cross-bridge turnover kinetics during isometric and isotonic steady-state contraction using skinned skeletal muscles of the rabbit
    • Brenner, B. 1988a. An experimental approach to determine cross-bridge turnover kinetics during isometric and isotonic steady-state contraction using skinned skeletal muscles of the rabbit. Pflügers Arch. 411(Suppl. 1):R186.
    • (1988) Pflügers Arch. , vol.411 , Issue.SUPPL. 1
    • Brenner, B.1
  • 10
    • 0024007477 scopus 로고
    • 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: Implications for regulation of muscle contraction
    • 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: implications for regulation of muscle contraction. Proc. Natl. Acad. Sci. USA. 85:3265-3269.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3265-3269
    • Brenner, B.1
  • 12
    • 0025748142 scopus 로고
    • Rapid dissociation and reassociation of actomyosin cross-bridges during force generation: A newly observed facet of cross-bridge action in muscle
    • Brenner, B. 1991. Rapid dissociation and reassociation of actomyosin cross-bridges during force generation: a newly observed facet of cross-bridge action in muscle. Proc. Natl. Acad. Sci. USA. 88:10490-10494.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10490-10494
    • Brenner, B.1
  • 13
    • 0343048303 scopus 로고
    • Further analysis of cross-bridge turnover kinetics during isotonic contraction in skinned rabbit psoas fibers
    • Brenner, B. 1993. Further analysis of cross-bridge turnover kinetics during isotonic contraction in skinned rabbit psoas fibers. Biophys. J. 64:345a.
    • (1993) Biophys. J. , vol.64
    • Brenner, B.1
  • 14
    • 0141610223 scopus 로고    scopus 로고
    • Muscle mechanics II: Skinned muscle fibres
    • H. Sugi, editor. Oxford University Press, Oxford, UK
    • Brenner, B. 1998. Muscle mechanics II: skinned muscle fibres. In Current Methods in Muscle Physiology. H. Sugi, editor. Oxford University Press, Oxford, UK. 33-69.
    • (1998) Current Methods in Muscle Physiology , pp. 33-69
    • Brenner, B.1
  • 16
    • 0343919970 scopus 로고
    • Cross-bridge cycling kinetics during isotonic contraction of skinned rabbit psoas fibers
    • abstract
    • Brenner, B., and R. Stehle. 1994. Cross-bridge cycling kinetics during isotonic contraction of skinned rabbit psoas fibers. J. Muscle Res. Cell Motil. 15:202. (abstract).
    • (1994) J. Muscle Res. Cell Motil. , vol.15 , pp. 202
    • Brenner, B.1    Stehle, R.2
  • 17
    • 0022931147 scopus 로고
    • 2+-sensitive cross-bridge dissociation in the presence of magnesium pyrophosphate in skinned rabbit psoas fibers
    • 2+-sensitive cross-bridge dissociation in the presence of magnesium pyrophosphate in skinned rabbit psoas fibers. Biophys. J. 50: 1101-1108.
    • (1986) Biophys. J. , vol.50 , pp. 1101-1108
    • Brenner, B.1    Yu, L.C.2    Greene, L.E.3    Eisenberg, E.4    Schoenberg, M.5
  • 18
    • 0027103829 scopus 로고
    • Myosin step size: Estimates from motility assays and shortening muscle
    • Burton, K. 1992. Myosin step size: estimates from motility assays and shortening muscle. J. Muscle Res. Cell. Motil. 13:590-607.
    • (1992) J. Muscle Res. Cell. Motil. , vol.13 , pp. 590-607
    • Burton, K.1
  • 19
    • 0023889297 scopus 로고
    • Effect of pH on contraction of rabbit fast and slow skeletal muscle fibers
    • Chase, P. B., and M. J. Kushmerick. 1988. Effect of pH on contraction of rabbit fast and slow skeletal muscle fibers. Biophys. J. 53:935-946.
    • (1988) Biophys. J. , vol.53 , pp. 935-946
    • Chase, P.B.1    Kushmerick, M.J.2
  • 20
    • 0020425131 scopus 로고
    • Orientation of spin labels attached to cross-bridges in contracting muscle fibers
    • Cooke, R., M. S. Crowder, and D. D. Thomas. 1982. Orientation of spin labels attached to cross-bridges in contracting muscle fibers. Nature. 300:776-778.
    • (1982) Nature , vol.300 , pp. 776-778
    • Cooke, R.1    Crowder, M.S.2    Thomas, D.D.3
  • 21
    • 0028211178 scopus 로고
    • A model of the release of myosin heads from actin in rapidly contracting muscle fibers
    • Cooke, R., H. White, and E. Pate. 1994. A model of the release of myosin heads from actin in rapidly contracting muscle fibers. Biophys. J. 66: 778-788.
    • (1994) Biophys. J. , vol.66 , pp. 778-788
    • Cooke, R.1    White, H.2    Pate, E.3
  • 22
    • 0018816862 scopus 로고
    • The relation of muscle biochemistry to muscle physiology
    • Eisenberg, E., and L. E. Greene. 1980. The relation of muscle biochemistry to muscle physiology. Annu. Rev. Physiol. 42:293-309.
    • (1980) Annu. Rev. Physiol. , vol.42 , pp. 293-309
    • Eisenberg, E.1    Greene, L.E.2
  • 23
    • 0017851095 scopus 로고
    • A cross-bridge model of muscle contraction
    • Eisenberg, E., and T. L. Hill. 1978. A cross-bridge model of muscle contraction. Prog. Biophys. Mol. Biol. 33:55-82.
    • (1978) Prog. Biophys. Mol. Biol. , vol.33 , pp. 55-82
    • Eisenberg, E.1    Hill, T.L.2
  • 24
    • 0021992946 scopus 로고
    • Muscular contraction and free energy transduction in biological systems
    • Eisenberg, E., and T. L. Hill. 1985. Muscular contraction and free energy transduction in biological systems. Science. 227:999-1006.
    • (1985) Science , vol.227 , pp. 999-1006
    • Eisenberg, E.1    Hill, T.L.2
  • 25
    • 0018877621 scopus 로고
    • Cross-bridge model of muscle contraction. Quantitative analysis
    • Eisenberg, E., T. L. Hill, and Y. Chen. 1980. Cross-bridge model of muscle contraction. Quantitative analysis. Biophys. J. 29:195-227.
    • (1980) Biophys. J. , vol.29 , pp. 195-227
    • Eisenberg, E.1    Hill, T.L.2    Chen, Y.3
  • 26
    • 0021895481 scopus 로고
    • Tension transients during steady shortening of frog muscle fibers
    • Ford, L. E., A. F. Huxley, and R. M. Simmons. 1985. Tension transients during steady shortening of frog muscle fibers. J. Physiol. (Lond.). 361:131-150.
    • (1985) J. Physiol. (Lond.) , vol.361 , pp. 131-150
    • Ford, L.E.1    Huxley, A.F.2    Simmons, R.M.3
  • 27
  • 28
    • 0018975627 scopus 로고
    • Stereochemical aspects of the interaction of myosin and actomyosin with nucleotides
    • Goody, R. S., and W. Hofmann. 1980. Stereochemical aspects of the interaction of myosin and actomyosin with nucleotides. J. Muscle Res. Cell Motil. 1:101-115.
    • (1980) J. Muscle Res. Cell Motil. , vol.1 , pp. 101-115
    • Goody, R.S.1    Hofmann, W.2
  • 29
    • 0020701456 scopus 로고
    • Binding of gizzard smooth muscle myosin subfragment 1 to actin in the presence and absence of adenosine 5′-triphosphate
    • Greene, L. E., J. R. Sellers, E. Eisenberg, and R. S. Adelstein. 1983. Binding of gizzard smooth muscle myosin subfragment 1 to actin in the presence and absence of adenosine 5′-triphosphate. Biochemistry. 22: 530-535.
    • (1983) Biochemistry , vol.22 , pp. 530-535
    • Greene, L.E.1    Sellers, J.R.2    Eisenberg, E.3    Adelstein, R.S.4
  • 30
    • 0027229127 scopus 로고
    • Cross-bridge attachment and stiffness during isotonic shortening of intact single muscle fibers
    • Griffiths, P. J., C. C. Ashley, M. A. Bani, Y. Maéda, and G. Cecchi. 1993. Cross-bridge attachment and stiffness during isotonic shortening of intact single muscle fibers. Biophys. J. 64:1150-1160.
    • (1993) Biophys. J. , vol.64 , pp. 1150-1160
    • Griffiths, P.J.1    Ashley, C.C.2    Bani, M.A.3    Maéda, Y.4    Cecchi, G.5
  • 31
    • 0025104145 scopus 로고
    • Mechanochemical coupling in actomyosin energy transduction studied by in vitro motility assay
    • Harada, Y., K. Sakurada, T. Aoki, D. D. Thomas, and T. Yanagida. 1990. Mechanochemical coupling in actomyosin energy transduction studied by in vitro motility assay. J. Mol. Biol. 216:49-68.
    • (1990) J. Mol. Biol. , vol.216 , pp. 49-68
    • Harada, Y.1    Sakurada, K.2    Aoki, T.3    Thomas, D.D.4    Yanagida, T.5
  • 32
    • 0023687726 scopus 로고
    • Direct observation of molecular motility by light microscopy
    • Harada, Y., and T. Yanagida. 1988. Direct observation of molecular motility by light microscopy. Cell Motil. Cytoskel. 10:71-76.
    • (1988) Cell Motil. Cytoskel. , vol.10 , pp. 71-76
    • Harada, Y.1    Yanagida, T.2
  • 33
    • 0023803940 scopus 로고
    • The stiffness under isotonic releases during a twitch of a frog muscle fiber
    • Haugen, P. 1986. The stiffness under isotonic releases during a twitch of a frog muscle fiber. Adv. Exp. Med. Biol. 226:461-469.
    • (1986) Adv. Exp. Med. Biol. , vol.226 , pp. 461-469
    • Haugen, P.1
  • 34
    • 0027205560 scopus 로고
    • A structural and kinetic study on myofibrils prevented from shortening by chemical cross-linking
    • Herrmann, C., J. Sleep, P. Chaussepied, F. Travers, and T. Barman. 1993. A structural and kinetic study on myofibrils prevented from shortening by chemical cross-linking. Biochemistry. 32:7255-7263.
    • (1993) Biochemistry , vol.32 , pp. 7255-7263
    • Herrmann, C.1    Sleep, J.2    Chaussepied, P.3    Travers, F.4    Barman, T.5
  • 35
    • 0025874034 scopus 로고
    • Sliding distance between actin and myosin filaments per ATP molecule hydrolyzed in skinned muscle fibers
    • Higuchi, H., and Y. E. Goldman. 1991. Sliding distance between actin and myosin filaments per ATP molecule hydrolyzed in skinned muscle fibers. Nature. 352:352-354.
    • (1991) Nature , vol.352 , pp. 352-354
    • Higuchi, H.1    Goldman, Y.E.2
  • 36
    • 0029095005 scopus 로고
    • Sliding distance per ATP molecule hydrolyzed by myosin heads during isotonic shortening of skinned muscle fibers
    • Higuchi, H., and Y. E. Goldman. 1995. Sliding distance per ATP molecule hydrolyzed by myosin heads during isotonic shortening of skinned muscle fibers. Biophys. J. 69:1491-1507.
    • (1995) Biophys. J. , vol.69 , pp. 1491-1507
    • Higuchi, H.1    Goldman, Y.E.2
  • 37
    • 0029162081 scopus 로고
    • Compliance in thin filaments in skinned fibers of rabbit skeletal muscle
    • Higuchi, H., T. Yanagida, and Y. E. Goldman. 1995. Compliance in thin filaments in skinned fibers of rabbit skeletal muscle. Biophys. J. 69: 1000-1010.
    • (1995) Biophys. J. , vol.69 , pp. 1000-1010
    • Higuchi, H.1    Yanagida, T.2    Goldman, Y.E.3
  • 38
    • 0016180488 scopus 로고
    • Theoretical formalism for the sliding filament model of contraction of striated muscle. Part I
    • Hill, T. L. 1974. Theoretical formalism for the sliding filament model of contraction of striated muscle. Part I. Prog. Biophys. Mol. Biol. 28: 267-340.
    • (1974) Prog. Biophys. Mol. Biol. , vol.28 , pp. 267-340
    • Hill, T.L.1
  • 39
    • 0026028022 scopus 로고
    • What is the true ATPase activity of contracting myofibrils
    • Houadjeto, M., T. Barman, and F. Travers. 1991. What is the true ATPase activity of contracting myofibrils. FEBS Lett. 281:105-107.
    • (1991) FEBS Lett. , vol.281 , pp. 105-107
    • Houadjeto, M.1    Barman, T.2    Travers, F.3
  • 40
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley, A. F. 1957. Muscle structure and theories of contraction. Prog. Biophys. Biophys. Chem. 7:255-318.
    • (1957) Prog. Biophys. Biophys. Chem. , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 41
    • 0015236610 scopus 로고
    • Proposed mechanism of force generation in striated muscle
    • Huxley, A. F., and R. M. Simmons. 1971. Proposed mechanism of force generation in striated muscle. Nature. 233:533-538.
    • (1971) Nature , vol.233 , pp. 533-538
    • Huxley, A.F.1    Simmons, R.M.2
  • 43
    • 0014685163 scopus 로고
    • The mechanism of muscular contraction
    • Huxley, H. E. 1969. The mechanism of muscular contraction. Science. 164:1356-1366.
    • (1969) Science , vol.164 , pp. 1356-1366
    • Huxley, H.E.1
  • 44
    • 0025368569 scopus 로고
    • Sliding filaments and molecular motile systems
    • Huxley, H. E. 1990. Sliding filaments and molecular motile systems. J. Biol. Chem. 265:8347-8350.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8347-8350
    • Huxley, H.E.1
  • 45
    • 0028081493 scopus 로고
    • X-ray diffraction measurements of the extensibility of actin and myosin filaments in contracting muscle
    • Huxley, H. E., A. Stewart, H. Sosa, and T. Irving. 1994. X-ray diffraction measurements of the extensibility of actin and myosin filaments in contracting muscle. Biophys. J. 67:2411-2421.
    • (1994) Biophys. J. , vol.67 , pp. 2411-2421
    • Huxley, H.E.1    Stewart, A.2    Sosa, H.3    Irving, T.4
  • 46
    • 0019393860 scopus 로고
    • Variation of muscle stiffness with tension during tension transients and constant velocity shortening in the frog
    • Julian, F. J., and D. L. Morgan. 1981. Variation of muscle stiffness with tension during tension transients and constant velocity shortening in the frog. J. Physiol. (Lond.). 319:193-203.
    • (1981) J. Physiol. (Lond.) , vol.319 , pp. 193-203
    • Julian, F.J.1    Morgan, D.L.2
  • 47
    • 0016815857 scopus 로고
    • Variation of muscle stiffness with force at increasing speeds of shortening
    • Julian, F. J., and M. R. Sollins. 1975. Variation of muscle stiffness with force at increasing speeds of shortening. J. Gen. Physiol. 66:287-302.
    • (1975) J. Gen. Physiol. , vol.66 , pp. 287-302
    • Julian, F.J.1    Sollins, M.R.2
  • 48
    • 0028607563 scopus 로고
    • Direct measurement of stiffness of single actin filaments with and without tropomyosin by in vitro nanomanipulation
    • Kojima, H., A. Ishijima, and T. Yanagida. 1994. Direct measurement of stiffness of single actin filaments with and without tropomyosin by in vitro nanomanipulation. Proc. Natl. Acad. Sci. USA. 91:12962-12966.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12962-12966
    • Kojima, H.1    Ishijima, A.2    Yanagida, T.3
  • 49
    • 0026613697 scopus 로고
    • 2+ on weak cross-bridge interaction with actin in the presence of adenosine 5′-[γ-thio]triphosphate
    • 2+ on weak cross-bridge interaction with actin in the presence of adenosine 5′-[γ-thio]triphosphate. Proc. Natl. Acad. Sci. USA. 89:11362-11366.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11362-11366
    • Kraft, T.1    Yu, L.C.2    Kuhn, H.J.3    Brenner, B.4
  • 50
    • 0031958205 scopus 로고    scopus 로고
    • The stiffness of skeletal muscle in isometric contraction and rigor: The fraction of myosin heads bound to actin
    • Linari, M., I. Dobbi, M. Reconditi, N. Koubassova, M. Irving, G. Piazzesi, and V. Lombardi. 1998. The stiffness of skeletal muscle in isometric contraction and rigor: the fraction of myosin heads bound to actin. Biophys. J. 74:2459-2473.
    • (1998) Biophys. J. , vol.74 , pp. 2459-2473
    • Linari, M.1    Dobbi, I.2    Reconditi, M.3    Koubassova, N.4    Irving, M.5    Piazzesi, G.6    Lombardi, V.7
  • 51
    • 0028928124 scopus 로고
    • Time resolved measurements show that phosphate release is the rate limiting step on myofibrillar ATPases
    • Lionne, C., M. Brune, M. R. Webb, F. Travers, and T. Barman. 1995. Time resolved measurements show that phosphate release is the rate limiting step on myofibrillar ATPases. FEBS Lett. 164:59-62.
    • (1995) FEBS Lett. , vol.164 , pp. 59-62
    • Lionne, C.1    Brune, M.2    Webb, M.R.3    Travers, F.4    Barman, T.5
  • 52
    • 0026571428 scopus 로고
    • Rapid regeneration of the actin-myosin power stroke in contracting muscle
    • Lombardi, V., G. Piazzesi, and M. Linari. 1992. Rapid regeneration of the actin-myosin power stroke in contracting muscle. Nature. 355:638-641.
    • (1992) Nature , vol.355 , pp. 638-641
    • Lombardi, V.1    Piazzesi, G.2    Linari, M.3
  • 53
    • 0015214368 scopus 로고
    • Mechanism of adenosine triphosphate hydrolysis by actomyosin
    • Lymn, R. W., and E. W. Taylor. 1971. Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry. 10:4617-4624.
    • (1971) Biochemistry , vol.10 , pp. 4617-4624
    • Lymn, R.W.1    Taylor, E.W.2
  • 54
    • 0028210495 scopus 로고
    • Kinetic mechanism of myofibril ATPase
    • Ma. Y-Z., and E. W. Taylor. 1994. Kinetic mechanism of myofibril ATPase. Biophys. J. 66:1542-1553.
    • (1994) Biophys. J. , vol.66 , pp. 1542-1553
    • Ma, Y.-Z.1    Taylor, E.W.2
  • 55
    • 0029002428 scopus 로고
    • Resolution of three structural states of spin-labeled myosin in contracting muscle
    • Ostap, E. M., V. A. Barnett, and D. D. Thomas. 1995. Resolution of three structural states of spin-labeled myosin in contracting muscle. Biophys. J. 69:177-188.
    • (1995) Biophys. J. , vol.69 , pp. 177-188
    • Ostap, E.M.1    Barnett, V.A.2    Thomas, D.D.3
  • 56
    • 0027478173 scopus 로고
    • Determination of the myosin step size from mechanical and kinetic data
    • Pate, E., H. White, and R. Cooke. 1993. Determination of the myosin step size from mechanical and kinetic data. Proc. Natl. Acad. Sci. USA. 90:2451-2455.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2451-2455
    • Pate, E.1    White, H.2    Cooke, R.3
  • 57
    • 0026567953 scopus 로고
    • Tension transients during steady lengthening of tetanized muscle fibers from the frog
    • Piazzesi, G., F. Francini, M. Linari, and V. Lombardi. 1992. Tension transients during steady lengthening of tetanized muscle fibers from the frog. J. Physiol. (Lond.). 445:659-711.
    • (1992) J. Physiol. (Lond.) , vol.445 , pp. 659-711
    • Piazzesi, G.1    Francini, F.2    Linari, M.3    Lombardi, V.4
  • 58
    • 0028907268 scopus 로고
    • A cross-bridge model that is able to explain mechanical and energetical properties of a shortening muscle
    • Piazzesi, G., and V. Lombardi. 1995. A cross-bridge model that is able to explain mechanical and energetical properties of a shortening muscle. Biophys. J. 68:1966-1979.
    • (1995) Biophys. J. , vol.68 , pp. 1966-1979
    • Piazzesi, G.1    Lombardi, V.2
  • 60
    • 0023664678 scopus 로고
    • The mechanism of regulation of actomyosin subfragment 1 ATPase
    • Rosenfeld, S. S., and E. W. Taylor. 1984. The mechanism of regulation of actomyosin subfragment 1 ATPase. J. Biol. Chem. 262:9984-9993.
    • (1984) J. Biol. Chem. , vol.262 , pp. 9984-9993
    • Rosenfeld, S.S.1    Taylor, E.W.2
  • 61
    • 0018474787 scopus 로고
    • Interpretation of light diffraction by cross-striated muscle as Bragg reflexion of light by the lattice of contractile proteins
    • Rüdel, R., and F. Zite-Ferenczi. 1979. Interpretation of light diffraction by cross-striated muscle as Bragg reflexion of light by the lattice of contractile proteins. J. Physiol. (Lond.). 290:317-330.
    • (1979) J. Physiol. (Lond.) , vol.290 , pp. 317-330
    • Rüdel, R.1    Zite-Ferenczi, F.2
  • 62
    • 0032486127 scopus 로고    scopus 로고
    • Orientation changes of fluorescent probes at five sites on the myosin regulatory light chain during contraction of single skeletal muscle fibers
    • Sabido-David, C., S. C. Hopkins, L. D. Saraswat, S. Lowey, Y. E. Goldman, and M. Irving. 1998. Orientation changes of fluorescent probes at five sites on the myosin regulatory light chain during contraction of single skeletal muscle fibers. J. Mol. Biol. 279:387-402.
    • (1998) J. Mol. Biol. , vol.279 , pp. 387-402
    • Sabido-David, C.1    Hopkins, S.C.2    Saraswat, L.D.3    Lowey, S.4    Goldman, Y.E.5    Irving, M.6
  • 63
    • 0028347113 scopus 로고
    • Movement of single myosin filaments and myosin step size on an actin filament suspended in solution by a laser trap
    • Saito, K., Ta. Aoki, To. Aoki, and T. Yanagida. 1994. Movement of single myosin filaments and myosin step size on an actin filament suspended in solution by a laser trap. Biophys. J. 66:769-777.
    • (1994) Biophys. J. , vol.66 , pp. 769-777
    • Saito, K.1    Aoki, T.2    Aoki, T.3    Yanagida, T.4
  • 64
    • 0022117773 scopus 로고
    • Equilibrium muscle cross-bridge behavior. Theoretical considerations
    • Schoenberg, M. 1985. Equilibrium muscle cross-bridge behavior. Theoretical considerations. Biophys. J. 48:467-475.
    • (1985) Biophys. J. , vol.48 , pp. 467-475
    • Schoenberg, M.1
  • 65
    • 0023912174 scopus 로고
    • Characterization of the myosin adenosine triphosphate (M.ATP) cross-bridge in rabbit and frog skeletal muscle fibers
    • Schoenberg, M. 1988. Characterization of the myosin adenosine triphosphate (M.ATP) cross-bridge in rabbit and frog skeletal muscle fibers. Biophys. J. 54:135-148.
    • (1988) Biophys. J. , vol.54 , pp. 135-148
    • Schoenberg, M.1
  • 67
    • 0010083875 scopus 로고
    • ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle
    • Siemanowsky, R. F., M. O. Wiseman, and H. D. White. 1985. ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle. Proc. Natl. Acad. Sci. USA. 82:658-662.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 658-662
    • Siemanowsky, R.F.1    Wiseman, M.O.2    White, H.D.3
  • 69
    • 0343919944 scopus 로고
    • Stiffness-speed relations for isometric and isotonic contraction. Significance for occupancy of strong-binding states during high-speed shortening
    • Stehle, R., T. Kraft, and B. Brenner. 1993. Stiffness-speed relations for isometric and isotonic contraction. Significance for occupancy of strong-binding states during high-speed shortening. Biophys. J. 64:250a.
    • (1993) Biophys. J. , vol.64
    • Stehle, R.1    Kraft, T.2    Brenner, B.3
  • 70
    • 0025769652 scopus 로고
    • Activation of skeletal S-1 ATPase activity by actin-tropomyosin-troponin
    • Stein, L. A., and J. M. Chalovich. 1991. Activation of skeletal S-1 ATPase activity by actin-tropomyosin-troponin. Biophys. J. 60:399-407.
    • (1991) Biophys. J. , vol.60 , pp. 399-407
    • Stein, L.A.1    Chalovich, J.M.2
  • 71
    • 0026065141 scopus 로고
    • A physical model of ATP-induced actin myosin movement in vitro
    • Tawada, K., and K. Sekimoto. 1991. A physical model of ATP-induced actin myosin movement in vitro. Biophys. J. 59:343-356.
    • (1991) Biophys. J. , vol.59 , pp. 343-356
    • Tawada, K.1    Sekimoto, K.2
  • 72
    • 0024991350 scopus 로고
    • Myosin step size. Estimation from slow sliding movement of actin over low densities of heavy meromyosin
    • Uyeda, T. Q. P., S. J. Kron, and J. A. Spudich. 1990. Myosin step size. Estimation from slow sliding movement of actin over low densities of heavy meromyosin. J. Mol. Biol. 214:699-710.
    • (1990) J. Mol. Biol. , vol.214 , pp. 699-710
    • Uyeda, T.Q.P.1    Kron, S.J.2    Spudich, J.A.3
  • 73
    • 0025900542 scopus 로고
    • Quantized velocities at low myosin densities in an in vitro motility assay
    • Uyeda, T. Q. P., H. M. Warrick, S. J. Kron, and J. A. Spudich. 1991. Quantized velocities at low myosin densities in an in vitro motility assay. Nature. 352:307-311.
    • (1991) Nature , vol.352 , pp. 307-311
    • Uyeda, T.Q.P.1    Warrick, H.M.2    Kron, S.J.3    Spudich, J.A.4
  • 74
    • 0028081494 scopus 로고
    • X-ray diffraction evidence for the extensibility of actin and myosin filaments during muscle contraction
    • Wakabayashi, K., Y. Sugimoto, H. Tanaka, Y. Ueno, Y. Takezawa, and Y. Amemiya. 1994. X-ray diffraction evidence for the extensibility of actin and myosin filaments during muscle contraction. Biophys. J. 67: 2422-2435.
    • (1994) Biophys. J. , vol.67 , pp. 2422-2435
    • Wakabayashi, K.1    Sugimoto, Y.2    Tanaka, H.3    Ueno, Y.4    Takezawa, Y.5    Amemiya, Y.6
  • 75
    • 0024518455 scopus 로고
    • Structures of actomyosin cross-bridges in relaxed and rigor muscle fibers
    • Yu, L. C., and B. Brenner. 1989. Structures of actomyosin cross-bridges in relaxed and rigor muscle fibers. Biophys. J. 55:441-453.
    • (1989) Biophys. J. , vol.55 , pp. 441-453
    • Yu, L.C.1    Brenner, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.