Proteomics

Dataset Information

VCP–adaptor interactions are exceptionally dynamic and subject to differential modulation by a VCP inhibitor


ABSTRACT: In this study we use a combination of mass spectrometry-based proteomics and biophysical studies to characterize the interaction of adaptors with VCP. Our results reveal that most VCP–adaptor interactions are characterized by exceptionally rapid dynamics that in some cases are modulated by the VCP inhibitor NMS873. These findings have significant implications for both the regulation of VCP function and the impact of VCP inhibition on different VCP–adaptor complexes.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Liang Xue  

LAB HEAD: Raymond Deshaies

PROVIDER: PXD004105 | Pride | 2016-07-18

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
CS-BJ-LFQ-raw.zip Other
CX-BJ-LFQ-search.zip Other
CX-HEK-SILAC-raw.zip Other
CX-HEK-SILAC-search.zip Other
Exchange-raw.zip Other
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