Proteomics

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Proteomic and ubiquitinomics of HUH7 cells after treatment of A1

ABSTRACT: Protein ubiquitination is a crucial post-translational modification that regulates diversecellular processes, including protein degradation and signal transduction. This study employs proteomic and ubiquitinomic analyses to systematically profile the alterations in protein expression and ubiquitination sites in Huh7 cells after treatment with 10 µM DUBTAC A1.We utilized high-resolution tandem mass spectrometry (LC-MS/MS) followed by extensive bioinformatic analysis. The dataset comprises raw mass spectrometry data, processed search results including protein identification and quantification, and a comprehensive list of identified ubiquitination sites. Our data provides a valuable resource for understanding the crosstalk between proteomic and ubiquitinomic alterations. This repository contains the complete proteomic and ubiquitinomic dataset supporting the findings of the related manuscript.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hepatocyte, Cell Culture

SUBMITTER: Chen He  

LAB HEAD: He Chen

PROVIDER: PXD069676 | Pride | 2025-11-24

REPOSITORIES: Pride

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Dataset's files

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Action DRS
FWMS20252397_DMSO1.raw Raw
FWMS20252397_DMSO2.raw Raw
FWMS20252397_DMSO3.raw Raw
FWMS20252397_Q1.raw Raw
FWMS20252397_Q2.raw Raw
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Publications

Construction of Small-Molecule Deubiquitinase-Targeting Chimeras to Reactivate and Stabilize Mutant p53 Y220C in Vitro and in Vivo.

He Chen C   Li Junda J   Cui Chenxi C   Xie Jia J   Feng Jiajie J   Zhang Baixue B   Huang Xingting X   Ma Ruoping R   Zheng Lufeng L   Xu Jinyi J   Yao Hong H   Xu Shengtao S  

Angewandte Chemie (International ed. in English) 20251117 3

Wild-type p53 is a tumor suppressor protein that is crucial in various pathological processes. The predominant strategy for p53 Y220C mutant involves binding reactivators to mutation-induced pocket to stabilize the protein thermally and restore wild-type structure. However, the corrected p53 Y220C remains vulnerable to ubiquitination, reducing protein levels and impairing function. Herein, we report the development of p53 Y220C-specific deubiquitinase-targeting chimeras (DUBTACs)-bifunctional sm  ...[more]

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