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Volumn 875, Issue , 2012, Pages 311-334

Single molecule detection approach to muscle study: Kinetics of a single cross-bridge during contraction of muscle

Author keywords

Cardiac muscle; Correlation function; Hearth hypertrophy; Single molecule detection

Indexed keywords

ADENOSINE TRIPHOSPHATASE; MYOSIN;

EID: 84865828044     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-61779-806-1_17     Document Type: Article
Times cited : (6)

References (66)
  • 1
    • 0015948545 scopus 로고
    • Use of fluorescence polarization to observe changes in attitude of S1 moieties in muscle fibers
    • Nihei T, Mendelson RA, Botts J (1974) Use of fluorescence polarization to observe changes in attitude of S1 moieties in muscle fibers. Biophys J 14:236-242
    • (1974) Biophys J , vol.14 , pp. 236-242
    • Nihei, T.1    Mendelson, R.A.2    Botts, J.3
  • 2
    • 0020327766 scopus 로고
    • Cross-bridge orientation in skeletal muscle measured by linear dichroism of an extrinsic chromophore
    • Borejdo J, Assulin O, Ando T, Putnam S (1982) Cross-bridge orientation in skeletal muscle measured by linear dichroism of an extrinsic chromophore. J Mol Biol 158: 391-414
    • (1982) J Mol Biol , vol.158 , pp. 391-414
    • Borejdo, J.1    Assulin, O.2    Ando, T.3    Putnam, S.4
  • 3
    • 0019193255 scopus 로고
    • Orientation of spin-labeled myosin heads in glycerinated muscle fibers
    • Thomas DD, Cooke R (1980) Orientation of spin-labeled myosin heads in glycerinated muscle fibers. Biophys J 32:891-905
    • (1980) Biophys J , vol.32 , pp. 891-905
    • Thomas, D.D.1    Cooke, R.2
  • 4
    • 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 233:533-538
    • (1971) Nature , vol.233 , pp. 533-538
    • Huxley, A.F.1    Simmons, R.M.2
  • 5
    • 0015214368 scopus 로고
    • Mechanism of adenosine triphosphate hydrolysis by actomyosin
    • Lymn RW, Taylor EW (1971) Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry 10:4617-4624
    • (1971) Biochemistry , vol.10 , pp. 4617-4624
    • Lymn, R.W.1    Taylor, E.W.2
  • 6
    • 0010083875 scopus 로고
    • ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle
    • Siemankowski RF, Wiseman MO, White HD (1985) ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle. Proc Natl Acad Sci U S A 82:658-662
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 658-662
    • Siemankowski, R.F.1    Wiseman, M.O.2    White, H.D.3
  • 7
    • 26844566272 scopus 로고    scopus 로고
    • The molecular mechanism of muscle contraction
    • Geeves MA, Holmes KC, Bodis E et al (2005) The molecular mechanism of muscle contraction. Adv Protein Chem 71:161-193
    • (2005) Adv Protein Chem , vol.71 , pp. 161-193
    • Geeves, M.A.1    Holmes, K.C.2    Bodis, E.3
  • 8
    • 0016366591 scopus 로고
    • Fluorescence correlation spectroscopy. II. An experimental realization
    • Magde D, Elson EL, Webb WW (1974) Fluorescence correlation spectroscopy. II. An experimental realization. Biopolymers 13:29-61
    • (1974) Biopolymers , vol.13 , pp. 29-61
    • Magde, D.1    Elson, E.L.2    Webb, W.W.3
  • 9
    • 0036679175 scopus 로고    scopus 로고
    • Concentration fluctuations in a mesoscopic oscillating chemical reaction system
    • Qian H, Saffarian S, Elson EL (2002) Concentration fluctuations in a mesoscopic oscillating chemical reaction system. Proc Natl Acad Sci U S A 99:10376-10381
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 10376-10381
    • Qian, H.1    Saffarian, S.2    Elson, E.L.3
  • 11
    • 0031212694 scopus 로고    scopus 로고
    • Optical collection efficiency function in single-molecule detection experiments
    • Enderlein J, Ambrose WP (1997) Optical collection efficiency function in single-molecule detection experiments. Appl Opt 36: 5298-5302
    • (1997) Appl Opt , vol.36 , pp. 5298-5302
    • Enderlein, J.1    Ambrose, W.P.2
  • 13
    • 34648813439 scopus 로고    scopus 로고
    • Single-molecule structural dynamics of EF-Gribosome interaction during translocation
    • Wang Y, Qin H, Kudaravalli RD et al (2007) Single-molecule structural dynamics of EF-Gribosome interaction during translocation. Biochemistry 46:10767-10775
    • (2007) Biochemistry , vol.46 , pp. 10767-10775
    • Wang, Y.1    Qin, H.2    Kudaravalli, R.D.3
  • 15
    • 0032493437 scopus 로고    scopus 로고
    • Myosin conformational states determined by single fluorophore polarization
    • Warshaw DM, Hayes E, Gaffney D et al (1998) Myosin conformational states determined by single fluorophore polarization. Proc Natl Acad Sci U S A 95:8034-8039
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 8034-8039
    • Warshaw, D.M.1    Hayes, E.2    Gaffney, D.3
  • 16
    • 23244442264 scopus 로고    scopus 로고
    • Orientation of the myosin light chain region by single molecule total internal reflection fluorescence polarization microscopy
    • Quinlan ME, Forkey JN, Goldman YE (2005) Orientation of the myosin light chain region by single molecule total internal reflection fluorescence polarization microscopy. Biophys J 89: 1132-1142
    • (2005) Biophys J , vol.89 , pp. 1132-1142
    • Quinlan, M.E.1    Forkey, J.N.2    Goldman, Y.E.3
  • 17
    • 0037468838 scopus 로고    scopus 로고
    • Three-dimensional structural dynamics of myosin v by single-molecule fluorescence polarization
    • Forkey JN, Quinlan ME, Shaw MA, Corrie JE, Goldman YE (2003) Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization. Nature 422:399-404
    • (2003) Nature , vol.422 , pp. 399-404
    • Forkey, J.N.1    Quinlan, M.E.2    Shaw, M.A.3    Corrie, J.E.4    Goldman, Y.E.5
  • 18
    • 0037832404 scopus 로고    scopus 로고
    • Myosin v walks hand-over-hand: Single fluorophore imaging with 1.5-nm localization
    • Yildiz A, Forkey JN, McKinney SA, Ha T, Goldman YE, Selvin PR (2003) Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization. Science 300: 2061-2065
    • (2003) Science , vol.300 , 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
  • 19
    • 33646237832 scopus 로고    scopus 로고
    • Defocused orientation and position imaging (DOPI) of myosin v
    • Toprak E, Enderlein J, Syed S et al (2006) Defocused orientation and position imaging (DOPI) of myosin V. Proc Natl Acad Sci U S A 103:6495-6499
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 6495-6499
    • Toprak, E.1    Enderlein, J.2    Syed, S.3
  • 20
    • 0019883893 scopus 로고
    • Effect ofmacromolecular crowding upon the structure and function of an enzyme: Glyceraldehyde-3-phosphate dehydrogenase
    • Minton AP, Wilf J (1981) Effect ofmacromolecular crowding upon the structure and function of an enzyme: glyceraldehyde-3-phosphate dehydrogenase. Biochemistry 20:4821-4826
    • (1981) Biochemistry , vol.20 , pp. 4821-4826
    • Minton, A.P.1    Wilf, J.2
  • 21
    • 84985735713 scopus 로고
    • Excluded volume as a determinant of macromolecular structure and reactivity
    • Minton AP (1981) Excluded volume as a determinant of macromolecular structure and reactivity. Biopolymers 20:2093-2120
    • (1981) Biopolymers , vol.20 , pp. 2093-2120
    • Minton, A.P.1
  • 22
    • 0028229903 scopus 로고
    • Sorting single molecules: Application to diagnostics and evolutionary biotechnology
    • Eigen M, Rigler R (1994) Sorting single molecules: application to diagnostics and evolutionary biotechnology. Proc Natl Acad Sci U S A 91:5740-5747
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 5740-5747
    • Eigen, M.1    Rigler, R.2
  • 23
    • 10044295196 scopus 로고    scopus 로고
    • Rotation of the lever-arm of myosin in contracting skeletal muscle fiber measured by two-photon anisotropy
    • Borejdo J, Shepard AA, Akopova I, Grudzinski W, Malicka J (2004) Rotation of the lever-arm of myosin in contracting skeletal muscle fiber measured by two-photon anisotropy. Biophys J 87:3912-3921
    • (2004) Biophys J , vol.87 , pp. 3912-3921
    • Borejdo, J.1    Shepard, A.A.2    Akopova, I.3    Grudzinski, W.4    Malicka, J.5
  • 25
    • 0026167312 scopus 로고
    • The optical near-field and cell biology
    • Lewis A (1991) The optical near-field and cell biology. Semin Cell Biol 2:187-192
    • (1991) Semin Cell Biol , vol.2 , pp. 187-192
    • Lewis, A.1
  • 26
    • 0035207438 scopus 로고    scopus 로고
    • Cell biology beyond the diffraction limit: Nearfield scanning optical microscopy
    • de Lange F, Cambi A, Huijbens R et al (2001) Cell biology beyond the diffraction limit: nearfield scanning optical microscopy. J Cell Sci 114:4153-4160
    • (2001) J Cell Sci , vol.114 , pp. 4153-4160
    • De Lange, F.1    Cambi, A.2    Huijbens, R.3
  • 27
    • 33644982036 scopus 로고    scopus 로고
    • Rotations of a few cross-bridges in muscle by confocal total internal reflection microscopy
    • Borejdo J, Talent J, Akopova I, Burghardt TP (2006) Rotations of a few cross-bridges in muscle by confocal total internal reflection microscopy. Biochim Biophys Acta 1763:137-140
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 137-140
    • Borejdo, J.1    Talent, J.2    Akopova, I.3    Burghardt, T.P.4
  • 28
    • 0039644117 scopus 로고
    • Reconvolution analysis in timeresolved fluorescence experiments, an alternative approach: Reference-to-excitationto- fluorescence reconvolution
    • Vecer J, Kowalczyk AA, Davenport L, Dale RE (1993) Reconvolution analysis in timeresolved fluorescence experiments, an alternative approach: reference-to-excitationto- fluorescence reconvolution. Rev Sci Instrum 64:3413-3424
    • (1993) Rev Sci Instrum , vol.64 , pp. 3413-3424
    • Vecer, J.1    Kowalczyk, A.A.2    Davenport, L.3    Dale, R.E.4
  • 29
    • 0030002263 scopus 로고    scopus 로고
    • A study on the mechanism of phalloidin-induced tension changes in skinned rabbit psoas muscle fibres
    • Bukatina AE, Fuchs F, Watkins SC (1996) A study on the mechanism of phalloidin-induced tension changes in skinned rabbit psoas muscle fibres. J Muscle Res Cell Motil 17:365-371
    • (1996) J Muscle Res Cell Motil , vol.17 , pp. 365-371
    • Bukatina, A.E.1    Fuchs, F.2    Watkins, S.C.3
  • 30
    • 0021015221 scopus 로고
    • Studies on conformation of F-actin in muscle fibers in the relaxed state, rigor, and during contraction using fluorescent phalloidin
    • Prochniewicz-Nakayama E, Yanagida T, Oosawa F (1983) Studies on conformation of F-actin in muscle fibers in the relaxed state, rigor, and during contraction using fluorescent phalloidin. J Cell Biol 97:1663-1667
    • (1983) J Cell Biol , vol.97 , pp. 1663-1667
    • Prochniewicz-Nakayama, E.1    Yanagida, T.2    Oosawa, F.3
  • 31
    • 1542267782 scopus 로고    scopus 로고
    • Correlation between mechanical and enzymatic events in contracting skeletal muscle fiber
    • Shepard A, Borejdo J (2004) Correlation between mechanical and enzymatic events in contracting skeletal muscle fiber. Biochemistry 43:2804-2811
    • (2004) Biochemistry , vol.43 , pp. 2804-2811
    • Shepard, A.1    Borejdo, J.2
  • 32
    • 0027716901 scopus 로고
    • The binding of fluorescent phallotoxins to actin in myofibrils
    • Szczesna D, Lehrer SS (1993) The binding of fluorescent phallotoxins to actin in myofibrils. J Muscle Res Cell Motil 14:594-597
    • (1993) J Muscle Res Cell Motil , vol.14 , pp. 594-597
    • Szczesna, D.1    Lehrer, S.S.2
  • 33
    • 0019218670 scopus 로고
    • Conformational changes of F-actin-epsilon-ADP in thin filaments in myosin-free muscle fibers induced by Ca2+
    • Yanagida T, Oosawa F (1980) Conformational changes of F-actin-epsilon-ADP in thin filaments in myosin-free muscle fibers induced by Ca2+. J Mol Biol 140:313-320
    • (1980) J Mol Biol , vol.140 , pp. 313-320
    • Yanagida, T.1    Oosawa, F.2
  • 34
    • 0018196447 scopus 로고    scopus 로고
    • Polarized fluorescence from epsilon-ADP incorporated into F-actin in a myosin-free single fiber: Conformation of F-actin and changes induced in it by heavy meromyosin
    • Yanagida T, Oosawa F (1998) Polarized fluorescence from epsilon-ADP incorporated into F-actin in a myosin-free single fiber: conformation of F-actin and changes induced in it by heavy meromyosin. J Mol Biol 126:507-524
    • (1998) J Mol Biol , vol.126 , pp. 507-524
    • Yanagida, T.1    Oosawa, F.2
  • 35
    • 0026048670 scopus 로고
    • Polarization microfluorimetry study of interaction between myosin head and F-actin in muscle fibers
    • Borovikov YS, Kuleva NV, Khoroshev MI (1991) Polarization microfluorimetry study of interaction between myosin head and F-actin in muscle fibers. Gen Physiol Biophys 10: 441-459
    • (1991) Gen Physiol Biophys , vol.10 , pp. 441-459
    • Borovikov, Y.S.1    Kuleva, N.V.2    Khoroshev, M.I.3
  • 36
    • 1942423276 scopus 로고    scopus 로고
    • Changes in orientation of actin during contraction of muscle
    • Borejdo J, Shepard A, Dumka D et al (2004) Changes in orientation of actin during contraction of muscle. Biophys J 86:2308-2317
    • (2004) Biophys J , vol.86 , pp. 2308-2317
    • Borejdo, J.1    Shepard, A.2    Dumka, D.3
  • 37
    • 0015257784 scopus 로고
    • Polarization of tryptophan fluorescence from single striated muscle fibers. A molecular probe of contractile state
    • Dos Remedios CG, Millikan RG, Morales MF (1972) Polarization of tryptophan fluorescence from single striated muscle fibers. A molecular probe of contractile state. J Gen Physiol 59: 103-120
    • (1972) J Gen Physiol , vol.59 , pp. 103-120
    • Dos Remedios, C.G.1    Millikan, R.G.2    Morales, M.F.3
  • 39
    • 0016756968 scopus 로고
    • Polarization from a helix of fluorophores and its relation to that obtained from muscle
    • Tregear RT, Mendelson RA (1975) Polarization from a helix of fluorophores and its relation to that obtained from muscle. Biophys J 15:455-467
    • (1975) Biophys J , vol.15 , pp. 455-467
    • Tregear, R.T.1    Mendelson, R.A.2
  • 40
    • 0021367313 scopus 로고
    • Calculation of the polarized fluorescence from a labeled muscle fiber
    • Morales MF (1984) Calculation of the polarized fluorescence from a labeled muscle fiber. Proc Nat Acad Sci U S A 81:145-149
    • (1984) Proc Nat Acad Sci U S A , vol.81 , pp. 145-149
    • Morales, M.F.1
  • 41
    • 0034702926 scopus 로고    scopus 로고
    • Epidemiology of hypertrophic cardiomyopathy- related death: Revisited in a large nonreferral- based patient population
    • Maron BJ, Olivotto I, Spirito P et al (2000) Epidemiology of hypertrophic cardiomyopathy- related death: revisited in a large nonreferral- based patient population. Circulation 102: 858-864
    • (2000) Circulation , vol.102 , pp. 858-864
    • Maron, B.J.1    Olivotto, I.2    Spirito, P.3
  • 43
    • 33847013578 scopus 로고
    • A hypothesis for the mechanism of contraction of muscle
    • Huxley AF (1957) A hypothesis for the mechanism of contraction of muscle. Prog Biophys Biophys Chem 7:255-318
    • (1957) Prog Biophys Biophys Chem , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 44
    • 0020425131 scopus 로고
    • Orientation of spin labels attached to crossbridges in contracting muscle fibres
    • Cooke R, Crowder MS, Thomas DD (1982) Orientation of spin labels attached to crossbridges in contracting muscle fibres. Nature 300:776-778
    • (1982) Nature , vol.300 , pp. 776-778
    • Cooke, R.1    Crowder, M.S.2    Thomas, D.D.3
  • 45
    • 0028946841 scopus 로고
    • The mechanism of force generation in myosin: A disorderto- order transition, coupled to internal structural changes
    • Thomas DD, Ramachandran S, Roopnarine O, Hayden DW, Ostap EM (1995) The mechanism of force generation in myosin: a disorderto- order transition, coupled to internal structural changes. Biophys J 68:135S-141S
    • (1995) Biophys J , vol.68
    • Thomas, D.D.1    Ramachandran, S.2    Roopnarine, O.3    Hayden, D.W.4    Ostap, E.M.5
  • 46
    • 0033748377 scopus 로고    scopus 로고
    • Visualizing myosin's power stroke in muscle contraction
    • Reedy MC (2000) Visualizing myosin's power stroke in muscle contraction. J Cell Sci 113: 3551-3562
    • (2000) J Cell Sci , vol.113 , pp. 3551-3562
    • Reedy, M.C.1
  • 47
    • 13444304331 scopus 로고    scopus 로고
    • The motor mechanism of myosin V: Insights for muscle contraction
    • Sweeney HL, Houdusse A (2004) The motor mechanism of myosin V: insights for muscle contraction. Philos Trans R Soc Lond B Biol Sci 359:1829-1841
    • (2004) Philos Trans R Soc Lond B Biol Sci , vol.359 , pp. 1829-1841
    • Sweeney, H.L.1    Houdusse, A.2
  • 48
    • 13444280378 scopus 로고    scopus 로고
    • Coupling between phosphate release and force generation in muscle actomyosin
    • Takagi Y, Shuman H, Goldman YE (2004) Coupling between phosphate release and force generation in muscle actomyosin. Philos Trans R Soc Lond B Biol Sci 359:1913-1920
    • (2004) Philos Trans R Soc Lond B Biol Sci , vol.359 , pp. 1913-1920
    • Takagi, Y.1    Shuman, H.2    Goldman, Y.E.3
  • 49
    • 15844400653 scopus 로고    scopus 로고
    • Mutations in either the essential or regulatory light chains of myosin are associated with a rare myopathy in human heart and skeletal muscle
    • Poetter K, Jiang H, Hassanzadeh S et al (1996) Mutations in either the essential or regulatory light chains of myosin are associated with a rare myopathy in human heart and skeletal muscle. Nat Genet 13:63-69
    • (1996) Nat Genet , vol.13 , pp. 63-69
    • Poetter, K.1    Jiang, H.2    Hassanzadeh, S.3
  • 50
    • 15644366960 scopus 로고    scopus 로고
    • Identification of two novel mutations in the ventricular regulatory myosin light chain gene (MYL2) associated with familial and classical forms of hypertrophic cardiomyopathy
    • Flavigny J, Richard P, Isnard R et al (1998) Identification of two novel mutations in the ventricular regulatory myosin light chain gene (MYL2) associated with familial and classical forms of hypertrophic cardiomyopathy. J Mol Med 76:208-214
    • (1998) J Mol Med , vol.76 , pp. 208-214
    • Flavigny, J.1    Richard, P.2    Isnard, R.3
  • 51
    • 0035651366 scopus 로고    scopus 로고
    • Myosin light chain mutations in familial hypertrophic cardiomyopathy: Phenotypic presentation and frequency in Danish and South African populations
    • Andersen PS, Havndrup O, Bundgaard H et al (2001) Myosin light chain mutations in familial hypertrophic cardiomyopathy: phenotypic presentation and frequency in Danish and South African populations. J Med Genet 38:E43
    • (2001) J Med Genet , vol.38
    • Andersen, P.S.1    Havndrup, O.2    Bundgaard, H.3
  • 52
    • 18744415680 scopus 로고    scopus 로고
    • Systematic analysis of the regulatory and essential myosin light chain genes: Genetic variants and mutations in hypertrophic cardiomyopathy
    • Kabaeva ZT, Perrot A, Wolter B et al (2002) Systematic analysis of the regulatory and essential myosin light chain genes: genetic variants and mutations in hypertrophic cardiomyopathy. Eur J Hum Genet 10:741-748
    • (2002) Eur J Hum Genet , vol.10 , pp. 741-748
    • Kabaeva, Z.T.1    Perrot, A.2    Wolter, B.3
  • 54
    • 0038125906 scopus 로고    scopus 로고
    • Identification of the genotypes causing hypertrophic cardiomyopathy in northern Sweden
    • Morner S, Richard P, Kazzam E et al (2003) Identification of the genotypes causing hypertrophic cardiomyopathy in northern Sweden. J Mol Cell Cardiol 35:841-849
    • (2003) J Mol Cell Cardiol , vol.35 , pp. 841-849
    • Morner, S.1    Richard, P.2    Kazzam, E.3
  • 55
    • 13544249951 scopus 로고    scopus 로고
    • One third of Danish hypertrophic cardiomyopathy patients have mutations in MYH7 rod region
    • Hougs L, Havndrup O, Bundgaard H et al (2005) One third of Danish hypertrophic cardiomyopathy patients have mutations in MYH7 rod region. Eur J Hum Genet 13:161-165
    • (2005) Eur J Hum Genet , vol.13 , pp. 161-165
    • Hougs, L.1    Havndrup, O.2    Bundgaard, H.3
  • 56
    • 0036200885 scopus 로고    scopus 로고
    • The young competitive athlete with cardiovascular abnormalities: Causes of sudden death, detection by preparticipation screening, and standards for disqualification
    • Maron BJ (2002) The young competitive athlete with cardiovascular abnormalities: causes of sudden death, detection by preparticipation screening, and standards for disqualification. Card Electrophysiol Rev 6:100-103
    • (2002) Card Electrophysiol Rev , vol.6 , pp. 100-103
    • Maron, B.J.1
  • 57
    • 0028811462 scopus 로고
    • Phalloidin unzips nebulin from thin filaments in skeletal myofibrils
    • Ao X, Lehrer SS (1995) Phalloidin unzips nebulin from thin filaments in skeletal myofibrils. J Cell Sci 108:3397-3403
    • (1995) J Cell Sci , vol.108 , pp. 3397-3403
    • Ao, X.1    Lehrer, S.S.2
  • 58
    • 0018751254 scopus 로고
    • Studies on conformational changes in F-actin of glycerinated muscle fibers during relaxation by means of polarized ultraviolet fluorescence microscopy
    • Borovikov YS, Chernogriadskaia NA (1979) Studies on conformational changes in F-actin of glycerinated muscle fibers during relaxation by means of polarized ultraviolet fluorescence microscopy. Microsc Acta 81:383-392
    • (1979) Microsc Acta , vol.81 , pp. 383-392
    • Borovikov, Y.S.1    Chernogriadskaia, N.A.2
  • 59
    • 0035312384 scopus 로고    scopus 로고
    • Myosin motors: Missing structures and hidden springs
    • Houdusse A, Sweeney HL (2001) Myosin motors: missing structures and hidden springs. Curr Opin Struct Biol 11:182-194
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 182-194
    • Houdusse, A.1    Sweeney, H.L.2
  • 62
    • 0034007895 scopus 로고    scopus 로고
    • Detection of fluorescently labeled actinbound cross-bridges in actively contracting myofibrils
    • Cooper WC, Chrin LR, Berger CL (2000) Detection of fluorescently labeled actinbound cross-bridges in actively contracting myofibrils. Biophys J 78:1449-1457
    • (2000) Biophys J , vol.78 , pp. 1449-1457
    • Cooper, W.C.1    Chrin, L.R.2    Berger, C.L.3
  • 63
    • 0024595913 scopus 로고
    • Binding of myosin to actin in myofibrils during ATP hydrolysis
    • Duong AM, Reisler E (1989) Binding of myosin to actin in myofibrils during ATP hydrolysis. Biochemistry 28:1307-1313
    • (1989) Biochemistry , vol.28 , pp. 1307-1313
    • Duong, A.M.1    Reisler, E.2
  • 64
    • 0035868666 scopus 로고    scopus 로고
    • Effects of sarcomere length and temperature on the rate of ATP utilisation by rabbit psoas muscle fibres
    • Hilber K, Sun YB, Irving M (2001) Effects of sarcomere length and temperature on the rate of ATP utilisation by rabbit psoas muscle fibres. J Physiol 531:771-780
    • (2001) J Physiol , vol.531 , pp. 771-780
    • Hilber, K.1    Sun, Y.B.2    Irving, M.3
  • 65
    • 61449250645 scopus 로고    scopus 로고
    • Malignant familial hypertrophic cardiomyopathy D166V mutation in the ventricular myosin regulatory light chain causes profound effects in skinned and intact papillary muscle fibers from transgenic mice
    • Kerrick WG, Kazmierczak K, Xu Y, Wang Y, Szczesna-Cordary D (2009) Malignant familial hypertrophic cardiomyopathy D166V mutation in the ventricular myosin regulatory light chain causes profound effects in skinned and intact papillary muscle fibers from transgenic mice. FASEB J 23:855-865
    • (2009) FASEB J , vol.23 , pp. 855-865
    • Kerrick, W.G.1    Kazmierczak, K.2    Xu, Y.3    Wang, Y.4    Szczesna-Cordary, D.5
  • 66
    • 0024381428 scopus 로고
    • Propagation of Acto-S-1 ATPase reaction-coupled conformational change in actin along the filament
    • Tokyo
    • Ando T (1987) Propagation of Acto-S-1 ATPase reaction-coupled conformational change in actin along the filament. J Biochem (Tokyo) 105:818-822
    • (1987) J Biochem , vol.105 , pp. 818-822
    • Ando, T.1


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