메뉴 건너뛰기




Volumn 545, Issue 3, 2002, Pages 887-901

Determinants of relaxation rate in rabbit skinned skeletal muscle fibres

Author keywords

[No Author keywords available]

Indexed keywords

1,6 HEXANEDIAMINE; ADENOSINE TRIPHOSPHATE; BIOLOGICAL MARKER; CALCIUM CHLORIDE; CALCIUM ION; CHELATING AGENT; CREATINE PHOSPHATE; EGTAZIC ACID; GLYCEROL; IMIDAZOLE; MAGNESIUM CHLORIDE; MUTANT PROTEIN; POTASSIUM CHLORIDE; TROPONIN C; CALCIUM CHELATING AGENT; DIAZO 2; PHOSPHATE; UNCLASSIFIED DRUG;

EID: 0037115194     PISSN: 00223751     EISSN: None     Source Type: Journal    
DOI: 10.1113/jphysiol.2002.031757     Document Type: Review
Times cited : (31)

References (30)
  • 3
    • 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. Proceedings of the National Academy of Sciences of the USA 85, 3265-3269.
    • (1988) Proceedings of the National Academy of Sciences of the USA , vol.85 , pp. 3265-3269
    • Brenner, B.1
  • 4
    • 0028098798 scopus 로고
    • Direct real time measurements of rapid inorganic phosphate release using a novel fluorescent probe and its application to actomyosin subfragment 1 ATPase
    • BRUNE, M., HUNTER, J. L., CORRIE, E. T. & WEBB, M. R. (1994). Direct real time measurements of rapid inorganic phosphate release using a novel fluorescent probe and its application to actomyosin subfragment 1 ATPase. Biochemistry 33, 8262-8271.
    • (1994) Biochemistry , vol.33 , pp. 8262-8271
    • Brune, M.1    Hunter, J.L.2    Corrie, E.T.3    Webb, M.R.4
  • 6
    • 0023889297 scopus 로고
    • Effects of pH on contraction of rabbit fast and slow skeletal muscle fibers
    • CHASE, P. B. & KUSHMERICK, M. J. (1988). Effects of pH on contraction of rabbit fast and slow skeletal muscle fibers. Biophysical Journal 53, 935-946.
    • (1988) Biophysical Journal , vol.53 , pp. 935-946
    • Chase, P.B.1    Kushmerick, M.J.2
  • 7
    • 0024201809 scopus 로고
    • Computer programs for calculating total from specified free or free from specified total ionic concentration in aqueous solutions containing multiple metals and ligands
    • ed. FLEISCHER, S. & FLEISCHER, B., 157, Academic Press, New York
    • FABIATO, A. (1988). Computer programs for calculating total from specified free or free from specified total ionic concentration in aqueous solutions containing multiple metals and ligands. In Methods in Enzymology, Biomembranes, ed. FLEISCHER, S. & FLEISCHER, B., pp. 157, 378-417. Academic Press, New York.
    • (1988) Methods in Enzymology, Biomembranes , pp. 378-417
    • Fabiato, A.1
  • 9
    • 0023645610 scopus 로고
    • 2+-specific regulatory sites in skinned rabbit psoas fibers
    • 2+-specific regulatory sites in skinned rabbit psoas fibers. Journal of Biological Chemistry 262, 13627-13635.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 13627-13635
    • Guth, K.1    Potter, J.D.2
  • 10
    • 0025918658 scopus 로고
    • 2+ dissociation rates correlated with changes in relaxation rate of frog muscle fibres
    • 2+ dissociation rates correlated with changes in relaxation rate of frog muscle fibres. Journal of Physiology 441, 285-304.
    • (1991) Journal of Physiology , vol.441 , pp. 285-304
    • Hou, T.1    Johnson, J.D.2    Rall, J.A.3
  • 11
    • 0030935930 scopus 로고    scopus 로고
    • Troponin I phosphorylation does not increase the rate of relaxation following laser flash photolysis of diazo-2 in guinea-pig skinned trabeculae
    • JOHNS, E. C., SIMNETT, S. J., MULLIGAN, I. P. & ASHLEY, C. C. (1997). Troponin I phosphorylation does not increase the rate of relaxation following laser flash photolysis of diazo-2 in guinea-pig skinned trabeculae. Pflügers Archiv 433, 842-844.
    • (1997) Pflügers Archiv. , vol.433 , pp. 842-844
    • Johns, E.C.1    Simnett, S.J.2    Mulligan, I.P.3    Ashley, C.C.4
  • 13
    • 0027089992 scopus 로고
    • Relaxation rate of intact striated muscle fibers after flash photolysis of a caged calcium chelator (diazo-2)
    • LANNERGREN, J. & ARNER, A. (1992). Relaxation rate of intact striated muscle fibers after flash photolysis of a caged calcium chelator (diazo-2). Journal of Muscle Research and Cell Motility 13, 630-634.
    • (1992) Journal of Muscle Research and Cell Motility , vol.13 , pp. 630-634
    • Lannergren, J.1    Arner, A.2
  • 14
    • 0032510810 scopus 로고    scopus 로고
    • Structural coupling of troponin C and actomyosin in muscle fibers
    • LI, H. C. & FAJER, P. G. (1998). Structural coupling of troponin C and actomyosin in muscle fibers. Biochemistry 37, 6628-6635.
    • (1998) Biochemistry , vol.37 , pp. 6628-6635
    • Li, H.C.1    Fajer, P.G.2
  • 15
    • 0032589143 scopus 로고    scopus 로고
    • 2+ and cross-bridge-induced changes in troponin C in skinned skeletal muscle fibers: Effects of force inhibition
    • 2+ and cross-bridge-induced changes in troponin C in skinned skeletal muscle fibers: effects of force inhibition. Biophysical Journal 76, 1480-1493.
    • (1999) Biophysical Journal , vol.76 , pp. 1480-1493
    • Martyn, D.A.1    Freitag, C.J.2    Chase, P.B.3    Gordon, A.M.4
  • 16
    • 0024312136 scopus 로고
    • Variations in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers
    • METZGER, J. M., GREASER, M. L. & MOSS, R. L. (1989). Variations in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers. Journal of General Physiology 93, 855-883.
    • (1989) Journal of General Physiology , vol.93 , pp. 855-883
    • Metzger, J.M.1    Greaser, M.L.2    Moss, R.L.3
  • 17
    • 77956925456 scopus 로고
    • Disaccharide Phosphorylases
    • Academic Press, New York
    • MIEYAL, J. J. & ABELES, R. H. (1972). Disaccharide Phosphorylases. The Enzymes, Vol. 7, pp. 515-532. Academic Press, New York.
    • (1972) The Enzymes , vol.7 , pp. 515-532
    • Mieyal, J.J.1    Abeles, R.H.2
  • 18
    • 0025251785 scopus 로고
    • The effects of phosphate and calcium on force generation in glycerinated rabbit skeletal muscle fibers
    • MILLAR, N. C. & HOMSHER, E. (1990). The effects of phosphate and calcium on force generation in glycerinated rabbit skeletal muscle fibers. Journal of Biological Chemistry 265, 20234-20240.
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 20234-20240
    • Millar, N.C.1    Homsher, E.2
  • 20
    • 4243215051 scopus 로고    scopus 로고
    • The effect of phosphate on the relaxation of single myofibrils from fast and slow skeletal muscle
    • NENCINI, S., COLOMO, F., PIRODDI, N., TESI, C. & POGGESI, C. (2000). The effect of phosphate on the relaxation of single myofibrils from fast and slow skeletal muscle. Biophysical Journal 78, A791.
    • (2000) Biophysical Journal , vol.78
    • Nencini, S.1    Colomo, F.2    Piroddi, N.3    Tesi, C.4    Poggesi, C.5
  • 21
    • 0031972659 scopus 로고    scopus 로고
    • Depletion of phosphate in active muscle fibers probes actomyosin states within the powerstroke
    • PATE, E., FRANKS-SKIBA, K. & COOKE, R. (1998). Depletion of phosphate in active muscle fibers probes actomyosin states within the powerstroke. Biophysical Journal 74, 369-380.
    • (1998) Biophysical Journal , vol.74 , pp. 369-380
    • Pate, E.1    Franks-Skiba, K.2    Cooke, R.3
  • 22
    • 0031972823 scopus 로고    scopus 로고
    • Phosphorylation of myosin regulatory light chain eliminates force-dependent changes in relaxation rates in skeletal muscle
    • PATEL, J. R., DIFFEE, G. M., HUANG, X. P. & MOSS, R. L. (1998). Phosphorylation of myosin regulatory light chain eliminates force-dependent changes in relaxation rates in skeletal muscle. Biophysical Journal 74, 360-368.
    • (1998) Biophysical Journal , vol.74 , pp. 360-368
    • Patel, J.R.1    Diffee, G.M.2    Huang, X.P.3    Moss, R.L.4
  • 26
    • 0034084354 scopus 로고    scopus 로고
    • The effects of inorganic phosphate on force generation in single myofibrils from rabbit skeletal muscle
    • TESI, C., COLOMO, F., NENCINI, S., PIRODDI, N. & POGGESI, C. (2000). The effects of inorganic phosphate on force generation in single myofibrils from rabbit skeletal muscle. Biophysical Journal 78, 3081-3092.
    • (2000) Biophysical Journal , vol.78 , pp. 3081-3092
    • Tesi, C.1    Colomo, F.2    Nencini, S.3    Piroddi, N.4    Poggesi, C.5
  • 28
    • 0031799047 scopus 로고    scopus 로고
    • Determinants of relaxation rate in skinned frog skeletal muscle fibers
    • WAHR, P. A., JOHNSON, J. D. & RALL, J. A. (1998). Determinants of relaxation rate in skinned frog skeletal muscle fibers. American Journal of Physiology 274, C1608-1615.
    • (1998) American Journal of Physiology , vol.274
    • Wahr, P.A.1    Johnson, J.D.2    Rall, J.A.3
  • 29
    • 0031002397 scopus 로고    scopus 로고
    • Role of calcium and cross bridges in determining rate of force development in frog muscle fibers
    • WAHR, P. A. & RALL, J. A. (1997). Role of calcium and cross bridges in determining rate of force development in frog muscle fibers. American Journal of Physiology 272, C1664-1671.
    • (1997) American Journal of Physiology , vol.272
    • Wahr, P.A.1    Rall, J.A.2
  • 30
    • 0029037870 scopus 로고
    • Cardiac troponin I phosphorylation increased the rate of cardiac muscle relaxation
    • ZHANG, R., ZHAO, J., MANDVENO, A. & POTTER, J. D. (1995). Cardiac troponin I phosphorylation increased the rate of cardiac muscle relaxation. Circulation Research 76, 1028-1035.
    • (1995) Circulation Research , vol.76 , pp. 1028-1035
    • Zhang, R.1    Zhao, J.2    Mandveno, A.3    Potter, J.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.