Proteomics

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USP13 dictates RAN turnover and vulnerability to ferroptosis in diffused large B cell lymphoma (DLBCL)


ABSTRACT: To identify the substrates of deubiquitinase USP13, we used a protein label-free quantitation technique, which involves mass spectrometry analysis of peptides from protein digests using liquid chromatography, to identify candidate substrates of USP13 that interact with it from co-immunoprecipitation (Co-IP) of HEK293T cells and candidate substrates of USP13 that are upregulated by its overexpression in HEK293T cells, from the data sets of the full protein profile and protein-protein interactions.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

DISEASE(S): Large B-cell Lymphoma

SUBMITTER: Xuan Qiao  

LAB HEAD: Boheng Li

PROVIDER: PXD056804 | Pride | 2025-12-08

REPOSITORIES: Pride

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Publications

USP13 dictates Ran turnover and vulnerability to ferroptosis in diffuse large B cell lymphoma (DLBCL).

Qiao Xuan X   Yang Xingmeng X   Diao Yuanhao Y   Li Qiuxiang Q   Wang Xianhuo X   Li Chong C   Yang Zailin Z   Chng Wee Joo WJ   Li Boheng B  

Cell death & disease 20251128 1


Diffuse large B-cell lymphoma (DLBCL) is one of the most common and lethal B-cell malignancies worldwide, with high relapse rate after standard treatment, and the relapsed cases are often difficult to treat. Ubiquitination has a pivotal role in cellular protein homeostasis and tumorigenic deubiquitinases (DUBs) stabilize oncoproteins during carcinogenesis. In this study, we have identified USP13 as one of the abnormally-overexpressed and stage-related DUBs in DLBCL critical to disease pathogenes  ...[more]

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