Proteomics

Dataset Information

55

Prolyl hydroxylation regulates protein degradation, synthesis and splicing in human induced pluripotent stem cell-derived cardiomyocytes


ABSTRACT: Protein hydroxylases are oxygen and alpha-ketoglutarate-dependent enzymes that catalyze hydroxylation of amino acids such as proline, thus linking oxygen and metabolism to enzymatic activity. Prolyl hydroxylation is a dynamic post-translational modification that regulates protein stability and protein-protein interactions; however, the extent of this modification is largely uncharacterized. The goals of this study are to investigate the biological consequences of prolyl hydroxylation and to identify new targets which undergo prolyl hydroxylation in human cardiomyocytes.

INSTRUMENT(S): Thermo Scientific instrument model

ORGANISM(S): Homo sapiens  

TISSUE(S): Cell Culture

DISEASE(S): Not Available

SUBMITTER: Andrea Stoehr  

LAB HEAD: Elizabeth (Tish) Murphy

PROVIDER: PXD003621 | Pride | 2016-05-06

REPOSITORIES: Pride

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Publications

Prolyl hydroxylation regulates protein degradation, synthesis, and splicing in human induced pluripotent stem cell-derived cardiomyocytes.

Stoehr Andrea A   Yang Yanqin Y   Patel Sajni S   Evangelista Alicia M AM   Aponte Angel A   Wang Guanghui G   Liu Poching P   Boylston Jennifer J   Kloner Philip H PH   Lin Yongshun Y   Gucek Marjan M   Zhu Jun J   Murphy Elizabeth E  

Cardiovascular research 20160419 3


Protein hydroxylases are oxygen- and α-ketoglutarate-dependent enzymes that catalyse hydroxylation of amino acids such as proline, thus linking oxygen and metabolism to enzymatic activity. Prolyl hydroxylation is a dynamic post-translational modification that regulates protein stability and protein-protein interactions; however, the extent of this modification is largely uncharacterized. The goals of this study are to investigate the biological consequences of prolyl hydroxylation and to identif  ...[more]

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