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Phosphorylation of the purified CaCB-receptor.

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Phosphorylation of the purified CaCB-receptor. / Röhrkasten, A; Nastainczyk, W; Sieber, M; Jahn, Holger; Regulla, S; Hofmann, F.

In: J CARDIOVASC PHARM, Vol. 12, No. 5, 5, 1988, p. 43-46.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Röhrkasten, A, Nastainczyk, W, Sieber, M, Jahn, H, Regulla, S & Hofmann, F 1988, 'Phosphorylation of the purified CaCB-receptor.', J CARDIOVASC PHARM, vol. 12, no. 5, 5, pp. 43-46. <http://www.ncbi.nlm.nih.gov/pubmed/2469877?dopt=Citation>

APA

Röhrkasten, A., Nastainczyk, W., Sieber, M., Jahn, H., Regulla, S., & Hofmann, F. (1988). Phosphorylation of the purified CaCB-receptor. J CARDIOVASC PHARM, 12(5), 43-46. [5]. http://www.ncbi.nlm.nih.gov/pubmed/2469877?dopt=Citation

Vancouver

Röhrkasten A, Nastainczyk W, Sieber M, Jahn H, Regulla S, Hofmann F. Phosphorylation of the purified CaCB-receptor. J CARDIOVASC PHARM. 1988;12(5):43-46. 5.

Bibtex

@article{3c9633d18f194c22bc999d03f1518fec,
title = "Phosphorylation of the purified CaCB-receptor.",
abstract = "The purified receptor for calcium channel blockers (CaCB-receptor) from rabbit skeletal muscle contains three polypeptides within a molecular mass of 165, 55, and 32 kDa. cAMP-dependent protein kinase was shown to phosphorylate preferentially the 165-kDa protein. The major phosphorylation site was identified and compared with the recently published primary sequence of the CaCB-receptor. It is concluded that serine 687 is the phosphorylation site. Phosphorylation of serine 687 may regulate the open-state probability of the CaCB-receptor.",
author = "A R{\"o}hrkasten and W Nastainczyk and M Sieber and Holger Jahn and S Regulla and F Hofmann",
year = "1988",
language = "Deutsch",
volume = "12",
pages = "43--46",
journal = "J CARDIOVASC PHARM",
issn = "0160-2446",
publisher = "Lippincott Williams and Wilkins",
number = "5",

}

RIS

TY - JOUR

T1 - Phosphorylation of the purified CaCB-receptor.

AU - Röhrkasten, A

AU - Nastainczyk, W

AU - Sieber, M

AU - Jahn, Holger

AU - Regulla, S

AU - Hofmann, F

PY - 1988

Y1 - 1988

N2 - The purified receptor for calcium channel blockers (CaCB-receptor) from rabbit skeletal muscle contains three polypeptides within a molecular mass of 165, 55, and 32 kDa. cAMP-dependent protein kinase was shown to phosphorylate preferentially the 165-kDa protein. The major phosphorylation site was identified and compared with the recently published primary sequence of the CaCB-receptor. It is concluded that serine 687 is the phosphorylation site. Phosphorylation of serine 687 may regulate the open-state probability of the CaCB-receptor.

AB - The purified receptor for calcium channel blockers (CaCB-receptor) from rabbit skeletal muscle contains three polypeptides within a molecular mass of 165, 55, and 32 kDa. cAMP-dependent protein kinase was shown to phosphorylate preferentially the 165-kDa protein. The major phosphorylation site was identified and compared with the recently published primary sequence of the CaCB-receptor. It is concluded that serine 687 is the phosphorylation site. Phosphorylation of serine 687 may regulate the open-state probability of the CaCB-receptor.

M3 - SCORING: Zeitschriftenaufsatz

VL - 12

SP - 43

EP - 46

JO - J CARDIOVASC PHARM

JF - J CARDIOVASC PHARM

SN - 0160-2446

IS - 5

M1 - 5

ER -