Proteomics

Dataset Information

38

RPE-1 and RPE-1 trisomic AHA p-c and steady state data


ABSTRACT: We developed a pulse-chase method in where fully SILAC (heavy, medium-heavy and Light) labelled cells were pulsed with Azidohomoalanine (AHA) and then chased for different length of times. In addition, steady state protein levels comparing the RPE- and RPE-1 trisomic cells by standard SILAC labeling was also acquired. These datasets contain data for the human RPE-1 and RPE-1 trisomic cell lines.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo sapiens  

TISSUE(S): Tissue Not Applicable To Dataset

DISEASE(S): Not Available

SUBMITTER: Erik McShane  

PROVIDER: PXD004915 | Pride | 2016-10-06

REPOSITORIES: Pride

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Publications


Do young and old protein molecules have the same probability to be degraded? We addressed this question using metabolic pulse-chase labeling and quantitative mass spectrometry to obtain degradation profiles for thousands of proteins. We find that >10% of proteins are degraded non-exponentially. Specifically, proteins are less stable in the first few hours of their life and stabilize with age. Degradation profiles are conserved and similar in two cell types. Many non-exponentially degraded (NED)  ...[more]

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