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Volumn 103, Issue 1, 2008, Pages

Ca2+-calmodulin-dependent protein kinase phosphorylation of ryanodine receptor may contribute to the β-adrenergic regulation of myocardial contractility independently of increases in heart rate

Author keywords

[No Author keywords available]

Indexed keywords

BETA ADRENERGIC RECEPTOR; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; ISOPRENALINE; RYANODINE RECEPTOR; RYANODINE RECEPTOR 2; CYCLIC AMP DEPENDENT PROTEIN KINASE; SERINE;

EID: 48049095721     PISSN: 00097330     EISSN: 15244571     Source Type: Journal    
DOI: 10.1161/CIRCRESAHA.108.178673     Document Type: Letter
Times cited : (2)

References (7)
  • 1
    • 42549130368 scopus 로고    scopus 로고
    • Adrenergic regulation of cardiac contractility does not involve phosphorylation of the cardiac ryanodine receptor at serine 2808
    • MacDonnell SM, García-Rivas G, Scherman JA, Kubo H, Chen X, Valdivia H, Houser SR. Adrenergic regulation of cardiac contractility does not involve phosphorylation of the cardiac ryanodine receptor at serine 2808. Circ Res. 2008;102:e65-e72.
    • (2008) Circ Res , vol.102
    • MacDonnell, S.M.1    García-Rivas, G.2    Scherman, J.A.3    Kubo, H.4    Chen, X.5    Valdivia, H.6    Houser, S.R.7
  • 2
    • 34548124746 scopus 로고    scopus 로고
    • 2+ release kinetics during beta-adrenergic stimulation. J Mol Cell Cardiol. 2007;43:281-291.
    • 2+ release kinetics during beta-adrenergic stimulation. J Mol Cell Cardiol. 2007;43:281-291.
  • 3
    • 33646771721 scopus 로고    scopus 로고
    • Ser-2030, but not Ser-2808, is the major phosphorylation site in cardiac ryanodine receptors responding to protein kinase A activation upon beta-adrenergic stimulation in normal and failing hearts
    • Xiao B, Zhong G, Obayashi M, Yang D, Chen K, Walsh MP, Shimoni Y, Cheng H, Ter Keurs H, Chen SR. Ser-2030, but not Ser-2808, is the major phosphorylation site in cardiac ryanodine receptors responding to protein kinase A activation upon beta-adrenergic stimulation in normal and failing hearts. Biochem J. 2006;396:7-16.
    • (2006) Biochem J , vol.396 , pp. 7-16
    • Xiao, B.1    Zhong, G.2    Obayashi, M.3    Yang, D.4    Chen, K.5    Walsh, M.P.6    Shimoni, Y.7    Cheng, H.8    Ter Keurs, H.9    Chen, S.R.10
  • 4
    • 0030479505 scopus 로고    scopus 로고
    • Immunodetection of phosphorylation sites gives new insights into the mechanisms underlying phospholamban phosphorylation in the intact heart
    • Mundina-Weilenmann C, Vittone L, Ortale M, Chiappe de Cingolani G, Mattiazzi A. Immunodetection of phosphorylation sites gives new insights into the mechanisms underlying phospholamban phosphorylation in the intact heart. J Biol Chem. 1996;271:33561-33567.
    • (1996) J Biol Chem , vol.271 , pp. 33561-33567
    • Mundina-Weilenmann, C.1    Vittone, L.2    Ortale, M.3    Chiappe de Cingolani, G.4    Mattiazzi, A.5
  • 6
    • 33847058737 scopus 로고    scopus 로고
    • β-Adrenergic enhancement of sarcoplasmic reticulum calcium leak in cardiac myocytes is mediated by calcium/calmodulin-dependent protein kinase
    • Curran J, Hinton MJ, Ríos E, Bers DM, Shannon TR. β-Adrenergic enhancement of sarcoplasmic reticulum calcium leak in cardiac myocytes is mediated by calcium/calmodulin-dependent protein kinase. Circ Res. 2007;100:391-398.
    • (2007) Circ Res , vol.100 , pp. 391-398
    • Curran, J.1    Hinton, M.J.2    Ríos, E.3    Bers, D.M.4    Shannon, T.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.