Proteomics

Dataset Information

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SILAC analysis of proteins enriched from LNCaP cells by ABE


ABSTRACT: The study was to identify candidate S-acylated proteins from LNCaP cells by coupling SILAC quantification with ABE enrichment of S-acylated proteins and GeLC-MS/MS analysis. Another goal is to determine the ratio of candidate S-acylated proteins versus of co-isolated non-S-acylated proteins.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Bile

DISEASE(S): Prostate Adenocarcinoma

SUBMITTER: Wei Yang  

LAB HEAD: Wei Yang

PROVIDER: PXD013189 | Pride | 2021-09-08

REPOSITORIES: Pride

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Publications

Low-Background Acyl-Biotinyl Exchange Largely Eliminates the Coisolation of Non-<i>S</i>-Acylated Proteins and Enables Deep <i>S</i>-Acylproteomic Analysis.

Zhou Bo B   Wang Yang Y   Yan Yiwu Y   Mariscal Javier J   Di Vizio Dolores D   Freeman Michael R MR   Yang Wei W  

Analytical chemistry 20190711 15


Protein <i>S</i>-acylation (also called palmitoylation) is a common post-translational modification whose deregulation plays a key role in the pathogenesis of many diseases. Acyl-biotinyl exchange (ABE), a widely used method for the enrichment of <i>S</i>-acylated proteins, has the potential of capturing the entire <i>S</i>-acylproteome in any type of biological sample. Here, we showed that current ABE methods suffer from a high background arising from the coisolation of non-<i>S</i>-acylated pr  ...[more]

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