CaMKII Cardiac Phosphoproteome
Ontology highlight
ABSTRACT:
INSTRUMENT(S): LTQ Orbitrap Velos
ORGANISM(S): Mus Musculus (mouse)
SUBMITTER: 
Arjen Scholten
PROVIDER: PXD000174 | Pride | 2013-08-02
REPOSITORIES: Pride
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| F280631.dat | Other | |||
| F280632.dat | Other | |||
| F281141.dat | Other | |||
| F281232.dat | Other | |||
| F281263.dat | Other |
Items per page: 5 1 - 5 of 191 |
Publications
Phosphoproteomics study based on in vivo inhibition reveals sites of calmodulin-dependent protein kinase II regulation in the heart.
Scholten Arjen A Preisinger Christian C Corradini Eleonora E Bourgonje Vincent J VJ Hennrich Marco L ML van Veen Toon A B TA Swaminathan Paari D PD Joiner Mei-Ling ML Vos Marc A MA Anderson Mark E ME Heck Albert J R AJ
Journal of the American Heart Association 20130807 4
<h4>Background</h4>The multifunctional Ca(2+)- and calmodulin-dependent protein kinase II (CaMKII) is a crucial mediator of cardiac physiology and pathology. Increased expression and activation of CaMKII has been linked to elevated risk for arrhythmic events and is a hallmark of human heart failure. A useful approach to determining CaMKII's role therein is large-scale analysis of phosphorylation events by mass spectrometry. However, current large-scale phosphoproteomics approaches have proved in ...[more]
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