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Volumn 92, Issue 1 SUPPL., 1997, Pages 63-74

Molecular mechanisms regulating the myofilament response to Ca 2+: Implications of mutations causal for familial hypertrophic cardiomyopathy

Author keywords

Cardiomyopathy myofilament activation; Troponin T tropomyosin; myosin heavy chain

Indexed keywords

CALCIUM ION; TROPOMYOSIN; TROPONIN T;

EID: 0030980831     PISSN: 03008428     EISSN: 14351803     Source Type: Journal    
DOI: 10.1007/bf00794070     Document Type: Article
Times cited : (34)

References (113)
  • 3
    • 0022539779 scopus 로고
    • Complete nucleotide sequence of the fast skeletal troponin T gene
    • Breitbart RE, Nadal-Oinard B (1986) Complete nucleotide sequence of the fast skeletal troponin T gene. J Mol Biol 188: 313-324
    • (1986) J Mol Biol , vol.188 , pp. 313-324
    • Breitbart, R.E.1    Nadal-Oinard, B.2
  • 4
    • 0021819912 scopus 로고
    • Intricate combinatorial patterns of exon splicing generate multiple regulated troponin T isoforms from a single gene
    • Breitbart RE, Nguyen HT, Medford RM, Destree AT, Mahdavi V, Nadal- Ginard B (1985) Intricate combinatorial patterns of exon splicing generate multiple regulated troponin T isoforms from a single gene. Cell 41: 67-82 (Pubitemid 15068426)
    • (1985) Cell , vol.41 , Issue.1 , pp. 67-82
    • Breitbart, R.E.1    Nguyen, H.T.2    Medford, R.M.3
  • 5
    • 0022516655 scopus 로고
    • Interaction of tropomyosin and troponin T: A proton nuclear magnetic resonance study
    • Brisson JR, Golosinska K, Smillie LB, Sykes BD (1986) Interaction of tropomyosin and troponin T: a proton nuclear magnetic resonance study. Biochemisty 25: 45484555
    • (1986) Biochemisty , vol.25 , pp. 45484555
    • Brisson, J.R.1    Golosinska, K.2    Smillie, L.B.3    Sykes, B.D.4
  • 6
    • 0025968808 scopus 로고
    • Sports-related and non-sports-related sudden cardiac death in young adults
    • Burke AP, Farb A, Virmani R, Goodman J, Smialek JE (1991) Sports-related and non-sports-related sudden cardiac death in young adults. Am Heart J 121: 568-575
    • (1991) Am Heart J , vol.121 , pp. 568-575
    • Burke, A.P.1    Farb, A.2    Virmani, R.3    Goodman, J.4    Smialek, J.E.5
  • 8
    • 0014674467 scopus 로고
    • Tropomyosin: Crystal structure, polymorphism and molecular interactions
    • Caspar DLD, Cohen C, Longley W (1969) Tropomyosin: crystal structure, polymorphism and molecular interactions. J Mol Biol41: 87-107
    • (1969) J Mol Biol , vol.41 , pp. 87-107
    • Caspar, D.L.D.1    Cohen, C.2    Longley, W.3
  • 9
    • 0025105127 scopus 로고
    • The amino terminus of muscle tropomyosin is a major determinant for function
    • Cho Y J, Liu J, Hitchcock-DeGregori SE (1990) The amino terminus of muscle tropomyosin is a major determinant for function. J Biol Chem 265: 538-545
    • (1990) J Biol Chem , vol.265 , pp. 538-545
    • Cho, Y.J.1    Liu, J.2    Hitchcock-Degregori, S.E.3
  • 10
    • 0020380464 scopus 로고
    • Photochemical cross-linking between rabbit skeletal troponin subunits
    • Chong PCS, Hodges RS (1982) Photochemical cross-linking between rabbit skeletal troponin subunits. J Biol Chem 257: 11667-11672
    • (1982) J Biol Chem , vol.257 , pp. 11667-11672
    • Chong, P.C.S.1    Hodges, R.S.2
  • 11
    • 0020266001 scopus 로고
    • Photochemical cross-linking between rabbit skeletal troponin and α-tropomyosin
    • Chong PCS, Hodges RS (1982) Photochemical cross-linking between rabbit skeletal troponin and α-tropomyosin. J Biol Chem 257: 9152-9160
    • (1982) J Biol Chem , vol.257 , pp. 9152-9160
    • Chong, P.C.S.1    Hodges, R.S.2
  • 12
    • 17044397426 scopus 로고
    • Optical rotation and helical polypeptide chain configuration in α-proteins
    • Cohen C, Szent-Gyorgyi AG (1957) Optical rotation and helical polypeptide chain configuration in α-proteins. J Amcr Chem Soc 79: 248
    • (1957) J Amcr Chem Soc , vol.79 , pp. 248
    • Cohen, C.1    Szent-Gyorgyi, A.G.2
  • 14
    • 0007055077 scopus 로고
    • A new missense mutation, Arg719Gln, in the β-cardiac heavy chain myosin gene of patients with familial hypertrophic cardiomyopathy
    • Consevage MW, Salada GC, Baylen BG, Ladda RL, Rogan PK (1994) A new missense mutation, Arg719 Gln, in theβ-cardiac heavy chain myosin gene of patients with familial hypertrophic cardiomyopathy. Human Mol Genetics 3: 1025-1026 (Pubitemid 24189987)
    • (1994) Human Molecular Genetics , vol.3 , Issue.6 , pp. 1025-1026
    • Consevage, M.W.1    Salada, G.C.2    Baylen, B.G.3    Ladda, R.L.4    Rogan, P.K.5
  • 17
    • 0029017141 scopus 로고
    • Molecular and clinical aspects of inherited cardiomyopathies
    • Durand JB, Anchee AB, Roberts R (1995) Molecular and clinical aspects of inherited cardiomyopathies. Annals of Medicine 27: 311-317
    • (1995) Annals of Medicine , vol.27 , pp. 311-317
    • Durand, J.B.1    Anchee, A.B.2    Roberts, R.3
  • 18
    • 0026629472 scopus 로고
    • Differences in clinical expression of hypertrophic cardiomyopathy associated with two distinct mutations in the B-myosin heavy chain gene a 908Leu-Val mutation and a 403Arg-Gln mutation
    • Epstein ND, Cohn GM, Cyran F, Fananapazir L (1992) Differences in clinical expression of hypertrophic cardiomyopathy associated with two distinct mutations in the B-myosin heavy chain gene a 908Leu-Val mutation and a 403Arg-Gln mutation. Circulation 86: 345-352
    • (1992) Circulation , vol.86 , pp. 345-352
    • Epstein, N.D.1    Cohn, G.M.2    Cyran, F.3    Fananapazir, L.4
  • 20
    • 0029128024 scopus 로고
    • Prevalence of hypertrophic cardiomyopathy and limitations of screening methods
    • Fananapazir L, Epstein ND (1995) Prevalence of hypertrophic cardiomyopathy and limitations of screening methods. Circulation 92: 700-704
    • (1995) Circulation , vol.92 , pp. 700-704
    • Fananapazir, L.1    Epstein, N.D.2
  • 22
    • 0028140230 scopus 로고
    • Genotype-phenotype correlations in hypertrophic cardiomyopathy
    • Fananapazir L, Epstein ND (1994) Genotype-phenotype correlations in hypertrophic cardiomyopathy. Circulation 89: 22-32
    • (1994) Circulation , vol.89 , pp. 22-32
    • Fananapazir, L.1    Epstein, N.D.2
  • 23
    • 0029031198 scopus 로고
    • The troponin complex and regulation of muscle contraction
    • Farah CS, Reinach FC (1995) The troponin complex and regulation of muscle contraction. Faseb J 9: 755-767
    • (1995) Faseb J , vol.9 , pp. 755-767
    • Farah, C.S.1    Reinach, F.C.2
  • 24
    • 0020475827 scopus 로고
    • Troponin and its interactions with tropomyosin
    • Flicker PF, Phillips GN JR, Cohen C (1982) Troponin and its interactions with tropomyosin. J Mol Biol162: 495-501
    • (1982) J Mol Biol , vol.162 , pp. 495-501
    • Flicker, P.F.1    Phillips, G.N.J.R.2    Cohen, C.3
  • 25
    • 0025604603 scopus 로고
    • Drosophila melanogaster troponin-T mutations engender three distinct syndromes of myofibrillar abnormalities
    • Fryberg E, Fryberg CC, Beall C, Saville DL (1990) Drosophila melanogaster troponin-T mutations engender three distincct syndromes of myofibrillar abnormalities. J Mol Bio 216: 657-675 (Pubitemid 120037397)
    • (1990) Journal of Molecular Biology , vol.216 , Issue.3 , pp. 657-675
    • Fyrberg, E.1    Fyrberg, C.C.2    Beall, C.3    Saville, D.L.4
  • 27
    • 0023258399 scopus 로고
    • Inheritance of hypertrophic cardiomyopathy: A cross sectional and M mode echocardiographic study of 50 families
    • Greaves SC, Roche AHG, Meutze JM, Whitlock RML, Veale AMO (1987) Inheritance of hypertrophic cardiomyopathy: a cross sectional and M mode echocardiographic study of 50 families. Br Heart J 58: 259-66 (Pubitemid 17131907)
    • (1987) British Heart Journal , vol.58 , Issue.3 , pp. 259-266
    • Greaves, S.C.1    Roche, A.H.G.2    Neutze, J.M.3
  • 28
    • 0020533250 scopus 로고
    • Some properties of cardiac troponin T structure
    • Gusev NB, Barskaya NV, Verin AD, Duzhenkova IV, Khuchna ZA, Zheltova AO (1983) Some properties of cardiac troponin T structure. Biophys J 213: 123-129 (Pubitemid 13063439)
    • (1983) Biochemical Journal , vol.213 , Issue.1 , pp. 123-129
    • Gusev, N.B.1    Barskaya, N.V.2    Verin, A.D.3
  • 29
    • 0023733230 scopus 로고
    • Interaction of rabbit skeletal muscle troponin T and F-actin at physiological ionic strength
    • Heeley DH, Smillie LB (1988) Interaction of rabbit skeletal muscle troponin T and F-actin at physiological ionic strength. Biochemistry 27: 8227-8232
    • (1988) Biochemistry , vol.27 , pp. 8227-8232
    • Heeley, D.H.1    Smillie, L.B.2
  • 30
    • 0023664677 scopus 로고
    • The effects of troponin T fragments T1 and T2 on the binding of nonpolymerizable tropomyosin to F-actin in the presence and absence of troponin i and troponin C
    • Heeley DH, Golosinska K, Smillie LB (1987) The effects of troponin T fragments T1 and T2 on the binding of nonpolymerizable tropomyosin to F-actin in the presence and absence of troponin I and troponin C. J Biol Chem 262: 9971-9978
    • (1987) J Biol Chem , vol.262 , pp. 9971-9978
    • Heeley, D.H.1    Golosinska, K.2    Smillie, L.B.3
  • 31
    • 0024513868 scopus 로고
    • Effects of deletion of tropomyosin overlap on regulated actomyosin subfragment 1 ATPase
    • Heeley DH, Smillie LB, Lohmeirer- Vogel EM (1989) Effects of deletion of tropomyosin overlap on regulated actomyosin subfragment 1 ATPase. Biochem J 258: 831-836 (Pubitemid 19083544)
    • (1989) Biochemical Journal , vol.258 , Issue.3 , pp. 831-836
    • Heeley, D.H.1    Smillie, L.B.2    Lohmeier-Vogel, E.M.3
  • 33
    • 0016610748 scopus 로고
    • Regulation of muscle contraction: Binding of troponin and its components to actin and tropomyosin
    • Hitchcock SE (1975) Regulation of muscle contraction: binding of troponin and its components to actin and tropomyosin. Eur J Biochem 52: 255-263
    • (1975) Eur J Biochem , vol.52 , pp. 255-263
    • Hitchcock, S.E.1
  • 36
    • 0021844197 scopus 로고
    • Conformational change of troponin T induced by calcium binding to troponin C
    • IioT(1985) Conformational changes of troponin T induced by calcium binding to troponin C. J Biochem 98: 261-263 (Pubitemid 15038078)
    • (1985) Journal of Biochemistry , vol.98 , Issue.1 , pp. 261-263
    • Iio, T.1
  • 37
    • 0025895385 scopus 로고
    • Two-site attachment of troponin to pyrene-labeled tropomyosin
    • Ishii Y, Lehrer SS (1991) Two-site attachment of troponin to pyrenelabelled tropomyosin. J Biol Chem 266: 6894-6903 (Pubitemid 21906308)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.11 , pp. 6894-6903
    • Ishii, Y.1    Lehrer, S.S.2
  • 39
    • 0024385895 scopus 로고
    • Isolation and characterization of cDNA clones encoding embryonic and adult isoforms of rat cardiac troponin T
    • Jin JR Lin JJC (1989) Isolation and characterization of cDNA clones encoding embryonic and adult isoforms of rat cardiac troponin T. J Biol Chem 264: 14471-14477
    • (1989) J Biol Chem , vol.264 , pp. 14471-14477
    • Jin, J.R.1    Lin, J.J.C.2
  • 41
    • 0028179144 scopus 로고
    • 2+-induced tropomyosin movement in Limulus thin filaments revealed by three dimensional reconstruction
    • 2+-induced tropomyosin movement in Limulus thin filaments revealed by three dimensional reconstruction. Nature 368: 65-67
    • (1994) Nature , vol.368 , pp. 65-67
    • Lehman, W.1    Craig, R.2    Vilbert, P.3
  • 43
    • 0014693726 scopus 로고
    • Substructure of the myosin molecule
    • Baker H
    • Lowey S, Slayter HS, Weeds AG, Baker H (1969) Substructure of the myosin molecule. J Mol Biol42: 1-29
    • (1969) J Mol Biol , vol.42 , pp. 1-29
    • Lowey, S.1    Slayter, H.S.2    Weeds, A.G.3
  • 45
    • 0019862956 scopus 로고
    • Structural interpretation of the two-site binding of troponin on the muscle thin filament
    • DOI 10.1016/0022-2836(81)90486-1
    • Mak AS, Smillie LB (1981) Structural interpretation of the two site binding of troponin on the muscle thin filament. J Mol Bio 149: 541-550 (Pubitemid 11044956)
    • (1981) Journal of Molecular Biology , vol.149 , Issue.3 , pp. 541-550
    • Mak, A.S.1    Smillie, L.B.2
  • 46
    • 0019332511 scopus 로고
    • A comparison of the amino acid of rabbit skeletal muscle α- And β- tropomyosins
    • Mak AS, Smillie LB, Stewart GR (1980) A comparison of the amino acid of rabbit skeletal muscle α- and β- tropomyosins. J Biol Chem 255: 3647-3651
    • (1980) J Biol Chem , vol.255 , pp. 3647-3651
    • Mak, A.S.1    Smillie, L.B.2    Stewart, G.R.3
  • 48
  • 49
    • 0029166817 scopus 로고
    • Recent advances in molecular genetics of hypertrophic cardiomyopathy
    • Marion AJ, Robert R (1995) Recent advances in molecular genetics of hypertrophic cardiomyopathy. Circulation 92: 1336-1347
    • (1995) Circulation , vol.92 , pp. 1336-1347
    • Marion, A.J.1    Robert, R.2
  • 51
    • 0021346026 scopus 로고
    • Patterns of inheritance in hypertrophic cardiomyopathy: Assessment by M-mode and two-dimensional echocardiography
    • Maron B J, Nichols PF III, Pickle LW, Wesley YE, Mulvihill JJ (1984) Patterns of inheritance in hypertrophic cardiomyopathy assessment by M mode and two dimensional echocardiography. Am J Cardiol53: 1087-1094 (Pubitemid 14174258)
    • (1984) American Journal of Cardiology , vol.53 , Issue.8 , pp. 1087-1094
    • Maron, B.J.1    Nichols III, P.F.2    Pickle, L.W.3
  • 52
    • 0024757325 scopus 로고
    • Sudden death in hypertrophic cardiomyopathy
    • McKenna WJ, Carom AJ (1989) Sudden death in hypertrophic cardiomyopathy. Circulation 80: 1489-1492
    • (1989) Circulation , vol.80 , pp. 1489-1492
    • McKenna, W.J.1    Carom, A.J.2
  • 54
    • 0016774265 scopus 로고
    • Tropomyosin coiled-coil interactions: Evidence for an unstaggered structure
    • McLachalan AD, Stewart M (1975) Tropomyosin coiled-coil interactions: evidence for an unstaggered structure. J Mol Biol98: 293-304
    • (1975) J Mol Biol , vol.98 , pp. 293-304
    • McLachalan, A.D.1    Stewart, M.2
  • 55
    • 0021181932 scopus 로고
    • A novel mechanism of alternative RNA splicing for the developmentally regulated generation of troponin T isoforms from a single gene
    • Medford RM, Nguyen HT, Destree AT, Summers E, Nadal-Ginard B (1984) A novel mechanism of alternative RNA splicing for the developmentally regulated generation of troponin Tisoforms from a single gene. Cell 38: 409-421 (Pubitemid 14022035)
    • (1984) Cell , vol.38 , Issue.2 , pp. 409-421
    • Medford, R.M.1    Nguyen, H.T.2    Destree, A.T.3
  • 56
    • 0025251785 scopus 로고
    • The effect of phosphate and calcium on force generation in glycerinated rabbit skeletal muscle fibers: A steady-state and transient kinetic study
    • Millar NC, Homsher E (1990) The effect of phosphate and calcium on force generation in glycerinated rabbit skeletal muscle fibers. J Biol Chem 265: 20234-20240 (Pubitemid 120014000)
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.33 , pp. 20234-20240
    • Millar, N.C.1    Homsher, E.2
  • 57
    • 0021251356 scopus 로고
    • Troponin-Tropomyosin interactions. Fluorescence studies of the binding of troponin, troponin T, and chymotryptic troponin T fragments to specifically labeled tropomyosin
    • Morris ER Lehrer SS (1984)Troponintropomyosin interactions. Flourescence studies of the binding of troponin, troponin T, and chymotryptic troponin T fragments to specifically labeled tropomyosin. Biochemistry 23: 2214-2220 (Pubitemid 14110725)
    • (1984) Biochemistry , vol.23 , Issue.10 , pp. 2214-2220
    • Morris, E.P.1    Lehrer, S.S.2
  • 58
    • 0026611165 scopus 로고
    • 2+ regulation of mechanical properties of striated muscle
    • 2+ regulation of mechanical properties of striated muscle. Cir Res 70: 865-884
    • (1992) Cir Res , vol.70 , pp. 865-884
    • Moss, R.L.1
  • 60
    • 0029164976 scopus 로고
    • Novel missence mutation in α-tropomyosin gene found in japanese patients with hypertrophic cardiomyopathy
    • Nakajima-Taniguchi C, Matsue H, Nagata S, Kishmoto T, Yamauchi- Takihara K (1995) Novel missence mutation in α-tropomyosin gene found in japanese patients with hypertrophic cardiomyopathy. J Mol Cell Cardiol27: 2053-2058
    • (1995) J Mol Cell Cardiol , vol.27 , pp. 2053-2058
    • Nakajima-Taniguchi, C.1    Matsue, H.2    Nagata, S.3    Kishmoto, T.4    Yamauchi-Takihara, K.5
  • 61
    • 0026463002 scopus 로고
    • Novel missence mutation in cardiac B-myosin heavy chain gene found in a japanese patient with hypertrophic cardiomyopathy
    • Nishi H, Kimura A, Harada H, Toshima H, Sasazuki T (1992) Novel missence mutation in cardiac B-myosin heavy chain gene found in a japanese patient with hypertrophic cardiomyopathy. Biochem Biophys Res Comm 188: 379-387
    • (1992) Biochem Biophys Res Comm , vol.188 , pp. 379-387
    • Nishi, H.1    Kimura, A.2    Harada, H.3    Toshima, H.4    Sasazuki, T.5
  • 62
    • 0018695446 scopus 로고
    • Molecular arrangement of troponin-T in the thin filament
    • Ohtsuki I (1979) Molecular arrangement of troponin T in the thin filament. J Biochem 86: 491-497 (Pubitemid 10251093)
    • (1979) Journal of Biochemistry , vol.86 , Issue.2 , pp. 491-497
    • Ohtsuki, I.1
  • 64
    • 0026496306 scopus 로고
    • Two genetically expressed troponin T fragments representing α and β isoforms exhibit functional differences
    • Pan B, Potter JD (1992) Two genetically expressed troponin T fragments representing α and β isoforms exhibit functional differences. J Biol Chem 267: 23052-23056
    • (1992) J Biol Chem , vol.267 , pp. 23052-23056
    • Pan, B.1    Potter, J.D.2
  • 65
    • 0025887097 scopus 로고
    • 2-terminal residues of rabbit skeletal troponin T strengthens binding of troponin to immobilized tropomyosin
    • Pan B, Gordon AM, Potter JD (1991) Deletion of the first 45 NH2-terminal residures of rabbit skeletal troponin T strengthens binding of troponin to immobilized tropomyosin. J Biol Chem 266: 12432-12438 (Pubitemid 21907112)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.19 , pp. 12432-12438
    • Pan, B.-S.1    Gordon, A.M.2    Potter, J.D.3
  • 66
    • 0024349096 scopus 로고
    • Removal of tropomyosin overlap modifies cooperative binding of myosin S1 to reconstituted thin filaments of rabbit striated muscle
    • Pan BS, GordonAM, Luo Z (1989) Removal of tropomyosin overlap modifies cooperative binding of myosin S1 to reconstituted thin filaments of rabbit striated muscle. J Biol Chem 264: 8495-8498
    • (1989) J Biol Chem , vol.264 , pp. 8495-8498
    • Pan, B.S.1    Gordonam Luo, Z.2
  • 67
    • 0019887719 scopus 로고
    • Analysis of the amino acid sequence of α-tropomyosin- binding fragment from troponinT
    • Parry DAD (1981) Analysis of the amino acid sequence of α-tropomyosin- binding fragment from troponinT. J Mol Biol 146: 259-263
    • (1981) J Mol Biol , vol.146 , pp. 259-263
    • Parry, D.A.D.1
  • 68
    • 0016777712 scopus 로고
    • Analysis of the primary sequence of α-tropomyosin from rabbit skeletal muscle
    • Parry DAD (1975) Analysis of the primary sequence of α-tropomyosin from rabbit skeletal muscle. J Mol Biol 98: 519-535
    • (1975) J Mol Biol , vol.98 , pp. 519-535
    • Parry, D.A.D.1
  • 69
    • 0017235497 scopus 로고
    • Movement of tropomyosin during regulation of vertebrate skeletal muscle: A simple physical model
    • Parry DAD (1976) Movement of tropomyosin during regulation of vertebrate skeletal muscle: a simple physical model. Biochem Biophys Res Corn 68: 323-328
    • (1976) Biochem Biophys Res Corn , vol.68 , pp. 323-328
    • Parry, D.A.D.1
  • 70
    • 0019462166 scopus 로고
    • Fragments of rabbit striated muscle atropomyosin
    • Pato MD, Mak AS, Smillie LB (1981) Fragments of rabbit striated muscle atropomyosin. J Biol Chem 256: 602-607
    • (1981) J Biol Chem , vol.256 , pp. 602-607
    • Pato, M.D.1    Mak, A.S.2    Smillie, L.B.3
  • 71
    • 0019424237 scopus 로고
    • Fragments of rabbit striated muscle - Tropomyosin
    • Pato MD, Mak AS, Smillie LB (1981) Fragments of rabbit striated muscle α- tropomyosin. J Biol Chem 256: 593-598
    • (1981) J Biol Chem , vol.256 , pp. 593-598
    • Pato, M.D.1    Mak, A.S.2    Smillie, L.B.3
  • 72
    • 0020424306 scopus 로고
    • Binding of troponin-T fragments to several types of tropomyosin
    • Pearlstone JR, Smillie LB (1982) Binding of troponin-T fragments to several types of tropomyosin. J Biol Chem 257: 10587-10592
    • (1982) J Biol Chem , vol.257 , pp. 10587-10592
    • Pearlstone, J.R.1    Smillie, L.B.2
  • 73
    • 0020584517 scopus 로고
    • 2+ sensitivity and cooperativity
    • Pearlstone JR, Smillie LB (1983) Effects of troponin-I plus -C on the binding of troponin-T and its fragments to α-tropomyosin. J Biol Chem 258: 2534-2542 (Pubitemid 13118453)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.4 , pp. 2534-2542
    • Pearlstone, J.R.1    Smillie, L.B.2
  • 74
    • 0019573953 scopus 로고
    • Identification of a second binding region on rabbit skeletal troponin-T for - Tropomyosin
    • Pearlstone JR, Smillie LB (1981) Identification of a second binding region on rabbit skeletal troponin-T for α- tropomyosin. FEBS Letters 128: 119-122
    • (1981) FEBS Letters , vol.128 , pp. 119-122
    • Pearlstone, J.R.1    Smillie, L.B.2
  • 75
    • 0017540699 scopus 로고
    • The binding site of rabbit skeletal α-tropomyosin on troponin-T
    • Pearlstone JR, Smillie LB (1977) The binding site of rabbit skeletal α- tropomyosin on troponin T. Can J Biochem 55: 1032-1038 (Pubitemid 8203579)
    • (1977) Canadian Journal of Biochemistry , vol.55 , Issue.10 , pp. 1032-1038
    • Pearlstone, J.R.1    Smillie, L.B.2
  • 76
    • 0019156523 scopus 로고
    • The binding sites of rabbit skeletal troponin-I on troponin-T
    • Pearlstone JR, Smillie LB (1980) The binding sites of rabbit skeletal troponin- I on troponin-T. Can J Biochem 58: 649-654 (Pubitemid 11218242)
    • (1980) Canadian Journal of Biochemistry , vol.58 , Issue.8 , pp. 649-654
    • Pearlstone, J.R.1    Smillie, L.B.2
  • 78
    • 0018193791 scopus 로고
    • Troponin T fragments: Physical properties and binding to troponin C
    • Pearlstone JR, Smillie LB (1978) Troponin T fragments: physical properties and binding to troponin C. Can J Biochem Cell Biol56: 521-527 (Pubitemid 8386001)
    • (1978) Canadian Journal of Biochemistry , vol.56 , Issue.6 , pp. 521-527
    • Pearlstone, J.R.1    Smillie, L.B.2
  • 79
    • 0017369378 scopus 로고
    • Primary structure of rabbit skeletal muscle troponin-T
    • Pearlstone JR, Carpenter MR, Smillie LB (1977) Primary structure of rabbit skeletal muscle troponin-T. J Biol Chem 252: 971-977
    • (1977) J Biol Chem , vol.252 , pp. 971-977
    • Pearlstone, J.R.1    Carpenter, M.R.2    Smillie, L.B.3
  • 80
    • 0011514921 scopus 로고
    • Aminoacid sequence of tropomyosin-binding component of rabbit skeletal muscle troponin
    • Pearlstone JR, Carpenter MR, Johnson R Smillie LB (1976) Aminoacid sequence of tropomyosin-binding component of rabbit skeletal muscle troponin. Proc Nat Acad Sci USA 73: 1902-1906
    • (1976) Proc Nat Acad Sci USA , vol.73 , pp. 1902-1906
    • Pearlstone, J.R.1    Carpenter, M.R.2    Johnson, R.3    Smillie, L.B.4
  • 81
    • 0023042847 scopus 로고
    • Tropomyosin crystal structure and muscle regulation
    • Phillips GN Jr, Fillers JR Cohen C (1986) Tropomyosin crystal structure and muscle regulation. J Mol Bio 192: 111-131
    • (1986) J Mol Biol , vol.92 , pp. 111-131
    • Phillips Jr., G.N.1    Fillers, J.R.2    Cohen, C.3
  • 83
    • 0020483742 scopus 로고
    • Cooperative blocks in tropomyosin
    • Potekhin SA, Privalov PL (1982) Cooperative blocks in tropomyosin. J Mol Biol 159: 519-535
    • (1982) J Mol Biol , vol.159 , pp. 519-535
    • Potekhin, S.A.1    Privalov, P.L.2
  • 84
  • 86
    • 0009020850 scopus 로고
    • Double-stranded coiled coils: Tropomyosin, paramyosin, and the myosin rod
    • Privalov PL (1982) Double-stranded coiled coils: tropomyosin, paramyosin, and the myosin rod. Advan Protein Chem 35: 31-55
    • (1982) Advan Protein Chem , vol.35 , pp. 31-55
    • Privalov, P.L.1
  • 88
    • 0021993040 scopus 로고
    • Comparison of the structure of two cardiac troponin T isoforms
    • Risnik VV, Verin AD, Gusev NB (1985) Comparison of the structure of two cardiac troponin T isoforms. Biochem J 225: 549-552 (Pubitemid 15162203)
    • (1985) Biochemical Journal , vol.225 , Issue.2 , pp. 549-552
    • Risnik, V.V.1    Verin, A.D.2    Gusev, N.B.3
  • 89
    • 0015463470 scopus 로고
    • Amino-acid sequence of rabbit skeletal tropomyosin and its coiled-coil structure
    • Sodek J, Hodges RS, Smillie LB, Jurasek L (1972) Amino-acid sequence of rabbit skeletal tropomyosin and its coiled-coil structure. Proc Nat Acad Sci USA 69: 3800-3804
    • (1972) Proc Nat Acad Sci USA , vol.69 , pp. 3800-3804
    • Sodek, J.1    Hodges, R.S.2    Smillie, L.B.3    Jurasek, L.4
  • 90
    • 0029920689 scopus 로고    scopus 로고
    • Altered interactions among thin filament proteins modulate cardiac function
    • DOI 10.1006/jmcc.1996.0021
    • Solaro RJ, VanEyk JI (1996) Altered interactions among thin filament protein modulate cardiac function. J Mol Cell Cardio 28: 217-230 (Pubitemid 26110467)
    • (1996) Journal of Molecular and Cellular Cardiology , vol.28 , Issue.2 , pp. 217-230
    • Solaro, R.J.1    Van Eyk, J.2
  • 94
    • 0022542030 scopus 로고
    • Developmental and functional adaptation of contractile proteins in cardiac and skeletal muscles
    • Swynghedauw B (1986) Developmental and functional adaptation of contractile proteins in cardiac and skeletal muscles. Physiol Reviews 66: 710-771 (Pubitemid 16074022)
    • (1986) Physiological Reviews , vol.66 , Issue.3 , pp. 710-771
    • Swynghedauw, B.1
  • 95
    • 0025164036 scopus 로고
    • A molecular basis for familial hypertrophic cardiomyopathy: An a/B-cardiac myosin heavy chain hybrid gene
    • Tanigawa G, Jarcho JA, Kass S, Solomon SD, Vosberg H, Seidman JG, Seidman CE (1990) A molecular basis for familial hypertrophic cardiomyopathy: an a/B-cardiac myosin heavy chain hybrid gene. Cell 62: 991-998
    • (1990) Cell , vol.62 , pp. 991-998
    • Tanigawa, G.1    Jarcho, J.A.2    Kass, S.3    Solomon, S.D.4    Vosberg, H.5    Seidman, J.G.6    Seidman, C.E.7
  • 96
    • 0020290646 scopus 로고
    • Location of troponin I-binding on troponin T sequence
    • DOI 10.1016/0014-5793(82)81224-6
    • Tanokura M, Ohtsuki I (1982) Location of troponin I-binding on troponin T sequence. FEBS Letters 145: 147-149 (Pubitemid 12002288)
    • (1982) FEBS Letters , vol.145 , Issue.1 , pp. 147-149
    • Tanokura, M.1    Ohtsuki, I.2
  • 97
    • 0019415765 scopus 로고
    • Primary structure of chymotryptic subfragments from rabbit skeletal troponin T
    • Tanokura M, Tawada Y, Onoyama Y, Nakamura S, Ohtsuki I (1981) Primary structure of chymotryptic subfragments from rabbit skeletal troponin T. J Biochem 90: 263-265 (Pubitemid 11063129)
    • (1981) Journal of Biochemistry , vol.90 , Issue.1 , pp. 263-265
    • Tanokura, M.1    Tawada, Y.2    Onoyama, Y.3
  • 98
    • 0025356099 scopus 로고
    • Calcium- induced movement of troponin i relative to actin in skeletal muscle thin filaments
    • Tao T, Gong B J, Leavis PC (1990) Calcium- induced movement of troponin I relative to actin in skeletal muscle thin filaments. Science 2: 1339-134I
    • (1990) Science , vol.2 , pp. 1339-1341
    • Tao, T.1    Gong, B.J.2    Leavis, P.C.3
  • 100
    • 0028178083 scopus 로고
    • Tropomyosin and cardiac troponin T mutations cause familial hypertrophic cardiomyopathy; A disease of the sarcomere
    • Thierfelder L, Watkins H, MacRae C, Lamas R, McKenna W, Vosberg H, Seidman JG, Seidman CE (1994) α- Tropomyosin and cardiac troponin T mutations cause familial hypertrophic cardiomyopathy; a disease of the sarcomere. Cell 77: 701-712
    • (1994) Cell , vol.77 , pp. 701-712
    • Thierfelder, L.1    Watkins, H.2    MacRae, C.3    Lamas, R.4    McKenna, W.5    Vosberg, H.6    Seidman, J.G.7    Seidman, C.E.8
  • 101
    • 0023845153 scopus 로고
    • Structure-function studies of the amino-terminal region of bovine cardiac troponin T
    • Tobacman LS (1988) Structure-function studies of the amino-terminal region of bovine cardiac troponin T. J Biol Chem 263: 2668-2672 (Pubitemid 18062908)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.6 , pp. 2668-2672
    • Tobacman, L.S.1
  • 102
    • 0023664228 scopus 로고
    • Isolation and functional comparison of bovine cardiac troponin T isoforms
    • Tobacman 1S, Lee R (1987) Isolation and functional comparison of bovine cardiac troponin T isoforms. J Biol Chem 262: 4059-4064
    • (1987) J Biol Chem , vol.262 , pp. 4059-4064
    • Tobacman, I.S.1    Lee, R.2
  • 103
    • 0028792519 scopus 로고
    • Molecular cloning of human cardiac troponin T isoforms: Expression in developing and failing heart
    • Townsend PJ, Barton PJR, Yacoub MH, Farza H (1995) Molecular cloning of human cardiac troponin T isoforms: expression in developing and failing heart. J Mol Cell Cardiol 27: 2223-2236
    • (1995) J Mol Cell Cardiol , vol.27 , pp. 2223-2236
    • Townsend, P.J.1    Barton, P.J.R.2    Yacoub, M.H.3    Farza, H.4
  • 104
    • 0021174871 scopus 로고
    • Local structural changes in tropomyosin detected by a trypsin-probe method
    • DOI 10.1021/bi00315a040
    • Ueno H (1984) Local structural changes in tropomyosin detected by a trypsin-probe method. Biochemistry 23: 4791-4798 (Pubitemid 14012286)
    • (1984) Biochemistry , vol.23 , Issue.20 , pp. 4791-4798
    • Ueno, H.1
  • 107
    • 0026573969 scopus 로고
    • Characteristics and prognostic implications of myosin missense mutations in familial hypertrophic cardiomyopathy
    • Watkins H, Rosenzweig A, Hwang D, Levi T, McKenna W, Seidman CE, Seidman JG (1992) Characteristics and prognostic implications of myosin missense mutations in familial hypertrophic cardiomyopathy. N Engl J Med 326: 1108-14
    • (1992) N Engl J Med , vol.326 , pp. 1108-1114
    • Watkins, H.1    Rosenzweig, A.2    Hwang, D.3    Levi, T.4    McKenna, W.5    Seidman, C.E.6    Seidman, J.G.7
  • 109
    • 0023091230 scopus 로고
    • Structure of co-crystals of tropomyosin and troponin
    • DOI 10.1038/325826a0
    • White SE Cohen C, Phillips GN Jr (1987) Structure of co-crystals of tropomyosin and troponin. Nature 325: 826-828 (Pubitemid 17056484)
    • (1987) Nature , vol.325 , Issue.6107 , pp. 826-828
    • White, S.P.1    Cohen, C.2    Phillips Jr., G.N.3
  • 110
    • 84891668074 scopus 로고    scopus 로고
    • Wieczorek DE Muthuchamy M in production
    • Wieczorek DE Muthuchamy M in production
  • 111
    • 0027082784 scopus 로고
    • Effects of the amino-terminal regions of tropomyosin and troponin T on thin filament assembly
    • Willadsen KA, Butters CA, Hill LE, Tobacman LS (1992) Effects of the amino-terminal regions of tropomyosin and troponin T on thin filament assembly. J BioI Chem 267: 23746-23752 (Pubitemid 23088181)
    • (1992) Journal of Biological Chemistry , vol.267 , Issue.33 , pp. 23746-23752
    • Willadsen, K.A.1    Butters, C.A.2    Hill, L.E.3    Tobacman, L.S.4
  • 112
    • 0029037870 scopus 로고
    • Cardiac troponin i phosphorylation increases the rate of cardiac muscle relaxation
    • Zhang R, Zhao J, MandvenoA, Potter JD (1995) Cardiac troponin I phosphorylation increases the rate of cardiac muscle relaxation. Cir Res 76: 1028-1035
    • (1995) Cir Res , vol.76 , pp. 1028-1035
    • Zhang, R.1    Zhao, J.2    Mandveno, A.3    Potter, J.D.4
  • 113
    • 0023071735 scopus 로고
    • Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction
    • ZotAS, Potter JD (1987) Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction. Ann Rev Biophys Chem 16: 535-559
    • (1987) Ann Rev Biophys Chem , vol.16 , pp. 535-559
    • Zot, A.S.1    Potter, J.D.2


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