메뉴 건너뛰기




Volumn 18, Issue 6, 2003, Pages 222-225

Role of Calcium Sensitivity Modulation in Skeletal Muscle Performance

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATASE; CALCIUM; MYOSIN LIGHT CHAIN; MYOSIN LIGHT CHAIN KINASE; TROPONIN C;

EID: 0347623036     PISSN: 08861714     EISSN: None     Source Type: Journal    
DOI: 10.1152/nips.01456.2003     Document Type: Review
Times cited : (82)

References (20)
  • 1
    • 0015505916 scopus 로고
    • Stretch-induced increase in activation of skinned muscle fibres by calcium
    • Endo M. Stretch-induced increase in activation of skinned muscle fibres by calcium. Nature 237: 211-213, 1972.
    • (1972) Nature , vol.237 , pp. 211-213
    • Endo, M.1
  • 2
    • 0032883413 scopus 로고    scopus 로고
    • Structural mechanism of muscle contraction
    • Geeves MA and Holmes KC. Structural mechanism of muscle contraction. Annu Rev Biochem 68: 687-728, 1999.
    • (1999) Annu Rev Biochem , vol.68 , pp. 687-728
    • Geeves, M.A.1    Holmes, K.C.2
  • 3
    • 0029757994 scopus 로고    scopus 로고
    • Myosin light chain phosphorylation affects the structure of rabbit skeletal muscle thick filaments
    • Levine RJC, Kensler RW, Yang ZH, Stull JT, and Sweeney HL. Myosin light chain phosphorylation affects the structure of rabbit skeletal muscle thick filaments. Biophys J 71: 898-907, 1996.
    • (1996) Biophys J , vol.71 , pp. 898-907
    • Levine, R.J.C.1    Kensler, R.W.2    Yang, Z.H.3    Stull, J.T.4    Sweeney, H.L.5
  • 4
    • 0030734902 scopus 로고    scopus 로고
    • Temperature-induced structural changes in the myosin thick filament of skinned rabbit psoas muscle
    • Malinchik S, Xu S, and Yu LC. Temperature-induced structural changes in the myosin thick filament of skinned rabbit psoas muscle. Biophys J 73: 2304-2312, 1997.
    • (1997) Biophys J , vol.73 , pp. 2304-2312
    • Malinchik, S.1    Xu, S.2    Yu, L.C.3
  • 5
    • 0024157190 scopus 로고
    • Length and myofilament spacing-dependent changes in calcium sensitivity of skeletal fibres: Effects of pH and ionic strength
    • Martyn DA and Gordon AM. Length and myofilament spacing-dependent changes in calcium sensitivity of skeletal fibres: effects of pH and ionic strength. J Muscle Res Cell Motil 9: 428-445, 1988.
    • (1988) J Muscle Res Cell Motil , vol.9 , pp. 428-445
    • Martyn, D.A.1    Gordon, A.M.2
  • 6
    • 0035006418 scopus 로고    scopus 로고
    • Influence of length on force and activation-dependent changes in troponin C structure in skinned cardiac and fast skeletal muscle
    • Martyn DA and Gordon AM. Influence of length on force and activation-dependent changes in troponin C structure in skinned cardiac and fast skeletal muscle. Biophys J 80: 2798-2808, 2001.
    • (2001) Biophys J , vol.80 , pp. 2798-2808
    • Martyn, D.A.1    Gordon, A.M.2
  • 7
    • 0025026206 scopus 로고
    • Effects on tension and stiffness due to reduced pH in mammalian fast- and slow-twitch skinned skeletal muscle fibres
    • Metzger JM and Moss RL. Effects on tension and stiffness due to reduced pH in mammalian fast- and slow-twitch skinned skeletal muscle fibres. J Physiol 428: 737-750, 1990.
    • (1990) J Physiol , vol.428 , pp. 737-750
    • Metzger, J.M.1    Moss, R.L.2
  • 8
    • 0031918744 scopus 로고    scopus 로고
    • The filament lattice of striated muscle
    • Millman BM. The filament lattice of striated muscle. Physiol Rev 78: 359-391, 1998.
    • (1998) Physiol Rev , vol.78 , pp. 359-391
    • Millman, B.M.1
  • 10
    • 0029117260 scopus 로고
    • Reduced effect of pH on skinned rabbit psoas muscle mechanics at high temperatures: Implications for fatigue
    • Pate E, Bhimani M, Franks-Skiba K, and Cooke R. Reduced effect of pH on skinned rabbit psoas muscle mechanics at high temperatures: implications for fatigue. J Physiol 486: 689-694, 1995.
    • (1995) J Physiol , vol.486 , pp. 689-694
    • Pate, E.1    Bhimani, M.2    Franks-Skiba, K.3    Cooke, R.4
  • 11
    • 0021961219 scopus 로고
    • The effect of myosin phosphorylation on the contractile properties of skinned rabbit skeletal muscle fibers
    • Persechini A, Stull JT, and Cooke R. The effect of myosin phosphorylation on the contractile properties of skinned rabbit skeletal muscle fibers. J Biol Chem 260: 7951-7954, 1985.
    • (1985) J Biol Chem , vol.260 , pp. 7951-7954
    • Persechini, A.1    Stull, J.T.2    Cooke, R.3
  • 12
    • 0344132598 scopus 로고    scopus 로고
    • Calcium-induced structural changes in synthetic myosin filaments of vertebrate striated muscles
    • Podlubnaya Z, Kakol I, Moczarska A, Stepkowski D, and Udaltsov S. Calcium-induced structural changes in synthetic myosin filaments of vertebrate striated muscles. J Struct Biol 127: 1-15, 1999.
    • (1999) J Struct Biol , vol.127 , pp. 1-15
    • Podlubnaya, Z.1    Kakol, I.2    Moczarska, A.3    Stepkowski, D.4    Udaltsov, S.5
  • 13
    • 0036089851 scopus 로고    scopus 로고
    • Effects of pH on the length-dependent twitch potentiation in skeletal muscle
    • Rassier DE and Herzog W. Effects of pH on the length-dependent twitch potentiation in skeletal muscle. J Appl Physiol 92: 1293-1299, 2002.
    • (2002) J Appl Physiol , vol.92 , pp. 1293-1299
    • Rassier, D.E.1    Herzog, W.2
  • 14
    • 34248356347 scopus 로고    scopus 로고
    • Sarcomere length-dependence of activity-dependent twitch potentiation in mouse skeletal muscle
    • Rassier DE and MacIntosh BR. Sarcomere length-dependence of activity-dependent twitch potentiation in mouse skeletal muscle. BMC Physiol 2: 19, 2002.
    • (2002) BMC Physiol , vol.2 , pp. 19
    • Rassier, D.E.1    MacIntosh, B.R.2
  • 15
    • 0021895461 scopus 로고
    • Temperature-dependent calcium sensitivity changes in skinned muscle fibres of rat and toad
    • Stephenson DG and Williams DA. Temperature-dependent calcium sensitivity changes in skinned muscle fibres of rat and toad. J Physiol 360: 1-12, 1985.
    • (1985) J Physiol , vol.360 , pp. 1-12
    • Stephenson, D.G.1    Williams, D.A.2
  • 16
    • 0025061076 scopus 로고
    • Alteration of cross-bridge kinetics by myosin light chain phosphorylation in rabbit skeletal muscle: Implications for regulation of actin-myosin interaction
    • Sweeney HL and Stull JT. Alteration of cross-bridge kinetics by myosin light chain phosphorylation in rabbit skeletal muscle: implications for regulation of actin-myosin interaction. Proc Natl Acad Sci USA 87: 414-418, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 414-418
    • Sweeney, H.L.1    Stull, J.T.2
  • 17
    • 0033807642 scopus 로고    scopus 로고
    • Length-dependent effects of osmotic compression on skinned rabbit psoas muscle fibers
    • Wang YP and Fuchs F. Length-dependent effects of osmotic compression on skinned rabbit psoas muscle fibers. J Muscle Res Cell Motil 21: 313-319, 2000.
    • (2000) J Muscle Res Cell Motil , vol.21 , pp. 313-319
    • Wang, Y.P.1    Fuchs, F.2
  • 18
    • 0027974349 scopus 로고
    • 2+-troponin C affinity in cardiac and slow skeletal muscle
    • 2+-troponin C affinity in cardiac and slow skeletal muscle. Am J Physiol Cell Physiol 266: C1077-C1082, 1994.
    • (1994) Am J Physiol Cell Physiol , vol.266
    • Wang, Y.P.1    Fuchs, F.2
  • 19
    • 0037457814 scopus 로고    scopus 로고
    • Temperature and ligand dependence of conformation and helical order in myosin filaments
    • Xu S, Offer G, Gu J, White HD, and Yu LC. Temperature and ligand dependence of conformation and helical order in myosin filaments. Biochemistry 42: 390-401, 2003.
    • (2003) Biochemistry , vol.42 , pp. 390-401
    • Xu, S.1    Offer, G.2    Gu, J.3    White, H.D.4    Yu, L.C.5
  • 20
    • 0031692828 scopus 로고    scopus 로고
    • Changes in interfilament spacing mimic the effects of myosin regulatory light chain phosphorylation in rabbit psoas fibers
    • Yang Z, Stull JT, Levine RJ, and Sweeney HL. Changes in interfilament spacing mimic the effects of myosin regulatory light chain phosphorylation in rabbit psoas fibers. J Struct Biol 122: 139-148, 1998.
    • (1998) J Struct Biol , vol.122 , pp. 139-148
    • Yang, Z.1    Stull, J.T.2    Levine, R.J.3    Sweeney, H.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.