SILAC analysis of proteins enriched from LNCaP cells by ABE
Ontology highlight
ABSTRACT:
INSTRUMENT(S):
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
Dataset's files
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| Sample6004_101.raw | Raw | |||
| Sample6004_102.raw | Raw | |||
| Sample6004_103.raw | Raw | |||
| Sample6004_104.raw | Raw | |||
| Sample6004_105.raw | Raw |
Items per page: 5 1 - 5 of 11 |
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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