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Alterations in the interactome of serine/threonine protein phosphatase type-1 in atrial fibrillation patients.


ABSTRACT: Data from ProteomeXchange, PXD ID: PXD000697. Exiperiment: PP1_Mouse_raw_IgG, file: OR8_121211_NL_DC_PP1_Gel4_B_labelfree2.mzml. Published as part of J Am Coll Cardiol. 2015 Jan 20;65(2):163-73 . From the Abstract: {{i}} Cardiac lysates were coimmunoprecipitated with anti-PP1c antibody followed by mass spectrometry-based, quantitative profiling of associated R-subunits. Subsequently, label-free quantification (LFQ) was used to evaluate altered R-subunit-PP1c interactions in PAF patients. R-subunits with altered binding to PP1c in PAF were further studied using bioinformatics, Western blotting (WB), immunocytochemistry, and coimmunoprecipitation. {{/i}}

INSTRUMENT(S): Instrument

ORGANISM(S): Mus_musculus_viruses, Mouse

DISEASE(S): Not Available

SUBMITTER: Chiang DY, et al.  

PROVIDER: GPM32320014437 | GPMDB |

REPOSITORIES: GPMDB

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Alterations in the interactome of serine/threonine protein phosphatase type-1 in atrial fibrillation patients.

Chiang David Y DY   Lebesgue Nicolas N   Beavers David L DL   Alsina Katherina M KM   Damen J Mirjam A JM   Voigt Niels N   Dobrev Dobromir D   Wehrens Xander H T XH   Scholten Arjen A  

Journal of the American College of Cardiology 20150101 2


<h4>Background</h4>Atrial fibrillation (AF) is the most common sustained cardiac arrhythmia, yet current pharmacological treatments are limited. Serine/threonine protein phosphatase type-1 (PP1), a major phosphatase in the heart, consists of a catalytic subunit (PP1c) and a large set of regulatory (R)-subunits that confer localization and substrate specificity to the holoenzyme. Previous studies suggest that PP1 is dysregulated in AF, but the mechanisms are unknown.<h4>Objectives</h4>The purpose  ...[more]

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