Proteomics

Dataset Information

0

PCP SILAC of apoptosis initiation


ABSTRACT: Protein correlation profiling using size exclusion and blue native page analysis of protein complexes coupled with SILAC to enable the comparsion between conditions

INSTRUMENT(S): LTQ Orbitrap Velos, Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): T Cell, Cell Culture

SUBMITTER: Nichollas Scott  

LAB HEAD: Leonard J Foster

PROVIDER: PXD002892 | Pride | 2017-01-17

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
Apoptosis_combined_libraries_2015_06_08.sky Other
Apoptosis_combined_libraries_2015_06_08.skyd Other
MaxQuantOutput.tar.gz Other
NSco_4hr_Mito_rep3_fraction01.raw Raw
NSco_4hr_Mito_rep3_fraction02.raw Raw
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Publications

Interactome disassembly during apoptosis occurs independent of caspase cleavage.

Scott Nichollas E NE   Rogers Lindsay D LD   Prudova Anna A   Brown Nat F NF   Fortelny Nikolaus N   Overall Christopher M CM   Foster Leonard J LJ  

Molecular systems biology 20170112 1


Protein-protein interaction networks (interactomes) define the functionality of all biological systems. In apoptosis, proteolysis by caspases is thought to initiate disassembly of protein complexes and cell death. Here we used a quantitative proteomics approach, protein correlation profiling (PCP), to explore changes in cytoplasmic and mitochondrial interactomes in response to apoptosis initiation as a function of caspase activity. We measured the response to initiation of Fas-mediated apoptosis  ...[more]

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