Complex phosphatase regulation of Ca2+-activated Cl- currents in pulmonary arterial smooth muscle cells. - Wikidata - wikimedia - TriplyDB

Complex phosphatase regulation of Ca2+-activated Cl- currents in pulmonary arterial smooth muscle cells.

Complex phosphatase regulation of Ca2+-activated Cl- currents in pulmonary arterial smooth muscle cells.

http://www.wikidata.org/entity/Q37432026

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Calmodulin-dependent activation and inactivation of anoctamin calcium-gated chloride channels Cholesterol depletion alters amplitude and pharmacology of vascular calcium-activated chloride channels International Union of Basic and Clinical Pharmacology. LXXXV: calcium-activated chloride channels.Expression profile and protein translation of TMEM16A in murine smooth muscle.Molecular and functional significance of Ca(2+)-activated Cl(-) channels in pulmonary arterial smooth muscle.Increased TMEM16A-encoded calcium-activated chloride channel activity is associated with pulmonary hypertension.Negative News: Cl- and HCO3- in the Vascular Wall.Molecular, biophysical, and pharmacological properties of calcium-activated chloride channels.

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Complex phosphatase regulation of Ca2+-activated Cl- currents in pulmonary arterial smooth muscle cells.

http://www.wikidata.org/entity/Q37432026

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 18 September 2009

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Complex phosphatase regulation ...... arterial smooth muscle cells.

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Complex phosphatase regulation ...... arterial smooth muscle cells.

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type

label

Complex phosphatase regulation ...... arterial smooth muscle cells.

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Complex phosphatase regulation ...... arterial smooth muscle cells.

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prefLabel

Complex phosphatase regulation ...... arterial smooth muscle cells.

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Complex phosphatase regulation ...... arterial smooth muscle cells.

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JBC.M109.050401

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Journal of Biological Chemistry

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Complex phosphatase regulation ...... arterial smooth muscle cells.

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Abigail S Forrest

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Amy R Sanguinetti

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Michael Wiwchar

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Ramon Ayon

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William Sones

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The C-terminus of NIPP1 (nuclear inhibitor of protein phosphatase-1) contains a novel binding site for protein phosphatase-1 that is controlled by tyrosine phosphorylation and RNA binding

Calcineurin: form and function.

Protein phosphatase 1--targeted in many directions

Bestrophin interacts physically and functionally with protein phosphatase 2A

Molecular physiology of bestrophins: multifunctional membrane proteins linked to best disease and other retinopathies

Substrate selectivity and sensitivity to inhibition by FK506 and cyclosporin A of calcineurin heterodimers composed of the alpha or beta catalytic subunit

Characterization of the phosphatase activity of a baculovirus-expressed calcineurin A isoform

TMEM16A confers receptor-activated calcium-dependent chloride conductance

Cyclic nucleotide dependent relaxation in vascular smooth muscle.

Expression cloning of TMEM16A as a calcium-activated chloride channel subunit.

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32507-32521

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scholarly article

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10.1074/JBC.M109.050401

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47

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284

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Iain A Greenwood

Normand R. Leblanc

Maria L. Valencik

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2009-09-18T00:00:00Z

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19767392

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2781665

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