Impact of site-specific phosphorylation of protein kinase A sites Ser(23) and Ser(24) of cardiac troponin I in human cardiomyocytes

P.J.M. Wijnker; D.B. Foster; A.L. Tsao; A.H. Frazier; C.G. dos Remedios; A.M. Murphy; G.J.M. Stienen; J. van der Velden

doi:10.1152/ajpheart.00498.2012

Impact of site-specific phosphorylation of protein kinase A sites Ser(23) and Ser(24) of cardiac troponin I in human cardiomyocytes

P.J.M. Wijnker, D.B. Foster, A.L. Tsao, A.H. Frazier, C.G. dos Remedios, A.M. Murphy, G.J.M. Stienen, J. van der Velden

Physics of Living Systems

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

PKA-mediated phosphorylation of contractile proteins upon β-adrenergic stimulation plays an important role in the regulation of cardiac performance. Phosphorylation of the PKA sites (Ser

Original language	English
Pages (from-to)	H260-H268
Journal	American Journal of Physiology. Heart and Circulatory Physiology
Volume	304
Issue number	2
DOIs	https://doi.org/10.1152/ajpheart.00498.2012
Publication status	Published - 2013

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10.1152/ajpheart.00498.2012

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Wijnker, P. J. M., Foster, D. B., Tsao, A. L., Frazier, A. H., dos Remedios, C. G., Murphy, A. M., Stienen, G. J. M., & van der Velden, J. (2013). Impact of site-specific phosphorylation of protein kinase A sites Ser(23) and Ser(24) of cardiac troponin I in human cardiomyocytes. American Journal of Physiology. Heart and Circulatory Physiology, 304(2), H260-H268. https://doi.org/10.1152/ajpheart.00498.2012

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title = "Impact of site-specific phosphorylation of protein kinase A sites Ser(23) and Ser(24) of cardiac troponin I in human cardiomyocytes",

abstract = "PKA-mediated phosphorylation of contractile proteins upon β-adrenergic stimulation plays an important role in the regulation of cardiac performance. Phosphorylation of the PKA sites (Ser",

author = "P.J.M. Wijnker and D.B. Foster and A.L. Tsao and A.H. Frazier and {dos Remedios}, C.G. and A.M. Murphy and G.J.M. Stienen and {van der Velden}, J.",

year = "2013",

doi = "10.1152/ajpheart.00498.2012",

language = "English",

volume = "304",

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journal = "American Journal of Physiology. Heart and Circulatory Physiology",

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Wijnker, PJM, Foster, DB, Tsao, AL, Frazier, AH, dos Remedios, CG, Murphy, AM, Stienen, GJM & van der Velden, J 2013, 'Impact of site-specific phosphorylation of protein kinase A sites Ser(23) and Ser(24) of cardiac troponin I in human cardiomyocytes', American Journal of Physiology. Heart and Circulatory Physiology, vol. 304, no. 2, pp. H260-H268. https://doi.org/10.1152/ajpheart.00498.2012

Impact of site-specific phosphorylation of protein kinase A sites Ser(23) and Ser(24) of cardiac troponin I in human cardiomyocytes. / Wijnker, P.J.M.; Foster, D.B.; Tsao, A.L. et al.
In: American Journal of Physiology. Heart and Circulatory Physiology, Vol. 304, No. 2, 2013, p. H260-H268.

Research output: Contribution to Journal › Article › Academic › peer-review

TY - JOUR

T1 - Impact of site-specific phosphorylation of protein kinase A sites Ser(23) and Ser(24) of cardiac troponin I in human cardiomyocytes

AU - Wijnker, P.J.M.

AU - Foster, D.B.

AU - Tsao, A.L.

AU - Frazier, A.H.

AU - dos Remedios, C.G.

AU - Murphy, A.M.

AU - Stienen, G.J.M.

AU - van der Velden, J.

PY - 2013

Y1 - 2013

N2 - PKA-mediated phosphorylation of contractile proteins upon β-adrenergic stimulation plays an important role in the regulation of cardiac performance. Phosphorylation of the PKA sites (Ser

AB - PKA-mediated phosphorylation of contractile proteins upon β-adrenergic stimulation plays an important role in the regulation of cardiac performance. Phosphorylation of the PKA sites (Ser

U2 - 10.1152/ajpheart.00498.2012

DO - 10.1152/ajpheart.00498.2012

M3 - Article

SN - 0363-6135

VL - 304

SP - H260-H268

JO - American Journal of Physiology. Heart and Circulatory Physiology

JF - American Journal of Physiology. Heart and Circulatory Physiology

IS - 2

ER -

Impact of site-specific phosphorylation of protein kinase A sites Ser(23) and Ser(24) of cardiac troponin I in human cardiomyocytes

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