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Volumn 52, Issue 2, 2005, Pages 443-448

Reconstitution of ventricular myosin with atrial light chains 1 improves its functional properties

Author keywords

Actin activated ATPase activity; Cardiac myosin; Dilated cardiomyopathy; Myosin filaments; Myosin light chains; Reconstituted myosin

Indexed keywords

HALC 1 PROTEIN, HUMAN; HALC-1 PROTEIN, HUMAN; MYOSIN; MYOSIN LIGHT CHAIN;

EID: 23644434584     PISSN: 0001527X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (12)

References (26)
  • 1
    • 85047678359 scopus 로고
    • Cardiac myosin light and heavy chain isotypes in tetralogy of Fallot
    • Auckland LM, Lambert SJ, Cummins P (1986) Cardiac myosin light and heavy chain isotypes in tetralogy of Fallot. Cardiovasc Res 20: 828-863.
    • (1986) Cardiovasc Res , vol.20 , pp. 828-863
    • Auckland, L.M.1    Lambert, S.J.2    Cummins, P.3
  • 2
  • 3
    • 0023042751 scopus 로고
    • ATP binding and crossbridge structure in muscle
    • Clarke ML, Hofmann W, Wray JS (1986) ATP binding and crossbridge structure in muscle. J Mol Biol 191: 581-585.
    • (1986) J Mol Biol , vol.191 , pp. 581-585
    • Clarke, M.L.1    Hofmann, W.2    Wray, J.S.3
  • 5
    • 0024561485 scopus 로고
    • Human ventricular/slow twitch myosin alkali light chain gene characterisation, sequence, and chromosomal location
    • Fodor WL, Darras B, Seharaseyon J, Falkenthal S, Francke U, Vanin EF (1989) Human ventricular/slow twitch myosin alkali light chain gene characterisation, sequence, and chromosomal location. J Biol Chem 264: 2143-2149.
    • (1989) J Biol Chem , vol.264 , pp. 2143-2149
    • Fodor, W.L.1    Darras, B.2    Seharaseyon, J.3    Falkenthal, S.4    Francke, U.5    Vanin, E.F.6
  • 7
    • 0041866669 scopus 로고    scopus 로고
    • Changes of composition of cardiac myosin light chains in dilated cardiomyopathy: Effect on functional properties
    • Khalina Y, Udaltsov SN, Podlubnaya ZA (2002) Changes of composition of cardiac myosin light chains in dilated cardiomyopathy: effect on functional properties. Biofizika 47: 361-366.
    • (2002) Biofizika , vol.47 , pp. 361-366
    • Khalina, Y.1    Udaltsov, S.N.2    Podlubnaya, Z.A.3
  • 8
    • 33750550114 scopus 로고    scopus 로고
    • Atrial myosin light chains in modulation of the functional properties of myocardium
    • Khalina YN, Shpagina MD, Malyshev SL, Podlubnaya ZA (2003) Atrial myosin light chains in modulation of the functional properties of myocardium. Biofizika 48: 900-904.
    • (2003) Biofizika , vol.48 , pp. 900-904
    • Khalina, Y.N.1    Shpagina, M.D.2    Malyshev, S.L.3    Podlubnaya, Z.A.4
  • 9
    • 0021717613 scopus 로고
    • Structure of the myosin projections on native thick filaments from vertebrate skeletal muscle
    • Knight P, Trinick J (1984) Structure of the myosin projections on native thick filaments from vertebrate skeletal muscle. J Mol Biol 177: 461-482.
    • (1984) J Mol Biol , vol.177 , pp. 461-482
    • Knight, P.1    Trinick, J.2
  • 11
    • 0030882063 scopus 로고    scopus 로고
    • Differences in myosin head arrangement on relaxed thick filaments from Lethocerus and rabbit muscles
    • Levine RJC (1997) Differences in myosin head arrangement on relaxed thick filaments from Lethocerus and rabbit muscles. J Muscle Res Cell Motil 18: 529-543.
    • (1997) J Muscle Res Cell Motil , vol.18 , pp. 529-543
    • Levine, R.J.C.1
  • 13
    • 33645174850 scopus 로고    scopus 로고
    • Titin-isoform shift in failing DCM hearts reduces myofibrillar passive stiffness but is independent of hypertrophy signals
    • Makarenko IV, Leake MC, Dussel RJ, Hajjar RJ, Linke WA (2004) Titin-isoform shift in failing DCM hearts reduces myofibrillar passive stiffness but is independent of hypertrophy signals. Biophys J 86: 207a.
    • (2004) Biophys J , vol.86
    • Makarenko, I.V.1    Leake, M.C.2    Dussel, R.J.3    Hajjar, R.J.4    Linke, W.A.5
  • 16
    • 17744416349 scopus 로고    scopus 로고
    • Changes in essential myosin light chain isoform expression provide a molecular basis for isometric force regulation in the failing human heart
    • Morano I, Hädicke K, Haase H, Böhm M, Erdmann E, Schaub MC (1997) Changes in essential myosin light chain isoform expression provide a molecular basis for isometric force regulation in the failing human heart. J Mol Cell Cardiol 29: 1177-1187.
    • (1997) J Mol Cell Cardiol , vol.29 , pp. 1177-1187
    • Morano, I.1    Hädicke, K.2    Haase, H.3    Böhm, M.4    Erdmann, E.5    Schaub, M.C.6
  • 17
    • 0032853632 scopus 로고    scopus 로고
    • Tuning the human heart molecular motors by myosin light chains
    • Morano I (1999) Tuning the human heart molecular motors by myosin light chains. J Mol Med 77: 544-555.
    • (1999) J Mol Med , vol.77 , pp. 544-555
    • Morano, I.1
  • 19
    • 0015924821 scopus 로고
    • A new protein of thick filaments of vertebrate skeletal myofibrils. Extraction, purification and characterization
    • Offer G, Moos C, Starr R (1973) A new protein of thick filaments of vertebrate skeletal myofibrils. Extraction, purification and characterization. J Mol Biol 74: 653-676.
    • (1973) J Mol Biol , vol.74 , pp. 653-676
    • Offer, G.1    Moos, C.2    Starr, R.3
  • 20
    • 0020021878 scopus 로고
    • Purification of muscle actin
    • Pardee JD, Spudich JA (1982) Purification of muscle actin. Methods Enzymol 85(B): 164-181.
    • (1982) Methods Enzymol , vol.85 , Issue.B , pp. 164-181
    • Pardee, J.D.1    Spudich, J.A.2
  • 21
    • 0344132598 scopus 로고    scopus 로고
    • Calcium-induced structural changes in synthetic myosin filaments of striated muscles
    • Podlubnaya Z, Kakol I, Moczarska A, Stepkowski D, Udaltsov S (1999) Calcium-induced structural changes in synthetic myosin filaments of striated muscles. J Struct Biol 127: 1-15.
    • (1999) J Struct Biol , vol.127 , pp. 1-15
    • Podlubnaya, Z.1    Kakol, I.2    Moczarska, A.3    Stepkowski, D.4    Udaltsov, S.5
  • 23
    • 0032731630 scopus 로고    scopus 로고
    • Expression of atrial myosin light chains but not alpha-myosin heavy chains correlate with increased ventricular function in patients with HOCM in vivo
    • Ritter O, Luther HP, Haase H, Baltas LG, Balzereit D, Baumann G, Schulte HD, Morano I (1999) Expression of atrial myosin light chains but not alpha-myosin heavy chains correlate with increased ventricular function in patients with HOCM in vivo. J Mol Med 77: 677-685.
    • (1999) J Mol Med , vol.77 , pp. 677-685
    • Ritter, O.1    Luther, H.P.2    Haase, H.3    Baltas, L.G.4    Balzereit, D.5    Baumann, G.6    Schulte, H.D.7    Morano, I.8
  • 24
    • 0026608619 scopus 로고
    • Hemodynamic performance and myosin light chain 1 expression in the hypertrophied left ventricle in aortic valve disease before and after valve replacement
    • Sütsch G, Brunner UT, Von Schulthess C, Hirzel HO, Hess OM, Turina M, Krayenbuehl HP, Schaub MC (1992) Hemodynamic performance and myosin light chain 1 expression in the hypertrophied left ventricle in aortic valve disease before and after valve replacement. Circ Res 70: 1035-1043.
    • (1992) Circ Res , vol.70 , pp. 1035-1043
    • Sütsch, G.1    Brunner, U.T.2    Von Schulthess, C.3    Hirzel, H.O.4    Hess, O.M.5    Turina, M.6    Krayenbuehl, H.P.7    Schaub, M.C.8
  • 25
    • 0017577042 scopus 로고
    • Studies on the role of myosin alkali light chains. Recombination and hybridization of light chains and heavy chains in subfragment-1 preparations
    • Wagner PD, Weeds AG (1977) Studies on the role of myosin alkali light chains. Recombination and hybridization of light chains and heavy chains in subfragment-1 preparations. J Mol Biol 109: 455-473.
    • (1977) J Mol Biol , vol.109 , pp. 455-473
    • Wagner, P.D.1    Weeds, A.G.2
  • 26
    • 0025218669 scopus 로고
    • Heterogenic mRNAs with an identical protein-coding region of the human embryonic myosin alkali light chain in skeletal muscle cells
    • Zimmermann K, Kautz S, Hajdu G, Winter C, Whalen RG, Starzinski-Powitz A (1990) Heterogenic mRNAs with an identical protein-coding region of the human embryonic myosin alkali light chain in skeletal muscle cells. J Mol Biol 211: 505-513.
    • (1990) J Mol Biol , vol.211 , pp. 505-513
    • Zimmermann, K.1    Kautz, S.2    Hajdu, G.3    Winter, C.4    Whalen, R.G.5    Starzinski-Powitz, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.