beta-Arrestin 1 and 2 stabilize the angiotensin II type I receptor in distinct high-affinity conformations

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Standard

beta-Arrestin 1 and 2 stabilize the angiotensin II type I receptor in distinct high-affinity conformations. / Sanni, S J; Hansen, J T; Bonde, M M; Speerschneider, T; Christensen, Gitte Lund; Munk, S; Gammeltoft, S.

I: British Journal of Pharmacology, Bind 161, Nr. 1, 09.2010, s. 150-61.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Sanni, SJ, Hansen, JT, Bonde, MM, Speerschneider, T, Christensen, GL, Munk, S & Gammeltoft, S 2010, 'beta-Arrestin 1 and 2 stabilize the angiotensin II type I receptor in distinct high-affinity conformations', British Journal of Pharmacology, bind 161, nr. 1, s. 150-61. https://doi.org/10.1111/j.1476-5381.2010.00875.x

APA

Sanni, S. J., Hansen, J. T., Bonde, M. M., Speerschneider, T., Christensen, G. L., Munk, S., & Gammeltoft, S. (2010). beta-Arrestin 1 and 2 stabilize the angiotensin II type I receptor in distinct high-affinity conformations. British Journal of Pharmacology, 161(1), 150-61. https://doi.org/10.1111/j.1476-5381.2010.00875.x

Vancouver

Sanni SJ, Hansen JT, Bonde MM, Speerschneider T, Christensen GL, Munk S o.a. beta-Arrestin 1 and 2 stabilize the angiotensin II type I receptor in distinct high-affinity conformations. British Journal of Pharmacology. 2010 sep.;161(1):150-61. https://doi.org/10.1111/j.1476-5381.2010.00875.x

Author

Sanni, S J ; Hansen, J T ; Bonde, M M ; Speerschneider, T ; Christensen, Gitte Lund ; Munk, S ; Gammeltoft, S. / beta-Arrestin 1 and 2 stabilize the angiotensin II type I receptor in distinct high-affinity conformations. I: British Journal of Pharmacology. 2010 ; Bind 161, Nr. 1. s. 150-61.

Bibtex

@article{b7e292be077741f6a5b24fa73c61a728,
title = "beta-Arrestin 1 and 2 stabilize the angiotensin II type I receptor in distinct high-affinity conformations",
abstract = "The angiotensin II type 1 (AT(1)) receptor belongs to family A of 7 transmembrane (7TM) receptors. The receptor has important roles in the cardiovascular system and is commonly used as a drug target in cardiovascular diseases. Interaction of 7TM receptors with G proteins or beta-arrestins often induces higher binding affinity for agonists. Here, we examined interactions between AT(1A) receptors and beta-arrestins to look for differences between the AT(1A) receptor interaction with beta-arrestin1 and beta-arrestin2.",
keywords = "Animals, Arrestins, Cell Line, GTP-Binding Proteins, Humans, Protein Conformation, Receptor, Angiotensin, Type 1, Signal Transduction",
author = "Sanni, {S J} and Hansen, {J T} and Bonde, {M M} and T Speerschneider and Christensen, {Gitte Lund} and S Munk and S Gammeltoft",
year = "2010",
month = sep,
doi = "10.1111/j.1476-5381.2010.00875.x",
language = "English",
volume = "161",
pages = "150--61",
journal = "British Journal of Pharmacology",
issn = "0007-1188",
publisher = "Wiley",
number = "1",

}

RIS

TY - JOUR

T1 - beta-Arrestin 1 and 2 stabilize the angiotensin II type I receptor in distinct high-affinity conformations

AU - Sanni, S J

AU - Hansen, J T

AU - Bonde, M M

AU - Speerschneider, T

AU - Christensen, Gitte Lund

AU - Munk, S

AU - Gammeltoft, S

PY - 2010/9

Y1 - 2010/9

N2 - The angiotensin II type 1 (AT(1)) receptor belongs to family A of 7 transmembrane (7TM) receptors. The receptor has important roles in the cardiovascular system and is commonly used as a drug target in cardiovascular diseases. Interaction of 7TM receptors with G proteins or beta-arrestins often induces higher binding affinity for agonists. Here, we examined interactions between AT(1A) receptors and beta-arrestins to look for differences between the AT(1A) receptor interaction with beta-arrestin1 and beta-arrestin2.

AB - The angiotensin II type 1 (AT(1)) receptor belongs to family A of 7 transmembrane (7TM) receptors. The receptor has important roles in the cardiovascular system and is commonly used as a drug target in cardiovascular diseases. Interaction of 7TM receptors with G proteins or beta-arrestins often induces higher binding affinity for agonists. Here, we examined interactions between AT(1A) receptors and beta-arrestins to look for differences between the AT(1A) receptor interaction with beta-arrestin1 and beta-arrestin2.

KW - Animals

KW - Arrestins

KW - Cell Line

KW - GTP-Binding Proteins

KW - Humans

KW - Protein Conformation

KW - Receptor, Angiotensin, Type 1

KW - Signal Transduction

U2 - 10.1111/j.1476-5381.2010.00875.x

DO - 10.1111/j.1476-5381.2010.00875.x

M3 - Journal article

C2 - 20718747

VL - 161

SP - 150

EP - 161

JO - British Journal of Pharmacology

JF - British Journal of Pharmacology

SN - 0007-1188

IS - 1

ER -

ID: 34167999