Proteomics

Dataset Information

0

Mass spetrometry analysis of FTO-interacting proteins


ABSTRACT: We identified the proteins which interact with fat mass and obesity-associated protein (FTO).

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Bone Marrow-derived Macrophage

SUBMITTER: Lu Zhang  

LAB HEAD: Xiao-Lian Zhang

PROVIDER: PXD047256 | Pride | 2025-07-14

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
2008011_ZL_BMMC.group Other
2008011_ZL_BMMC.wiff Wiff
2008011_ZL_BMMC.wiff.scan Wiff
2008011_ZL_BMMC_MGFPeaklist.mgf Mgf
2008011_ZL_BMMC_PeptideSummary.txt Txt
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Publications

FTO O-GlcNAcylation promotes TRIM21-mediated FTO ubiquitination degradation to sustain the negative feedback control of macrophage inflammation.

Zhang Lu L   Liu Min M   Xie Yan Y   Yuan Bi-Feng BF   Peng Zhiyong Z   Xiong Jun J   Zhang Xiao-Lian XL  

Frontiers in immunology 20250626


<h4>Introduction</h4>The fat mass and obesity-associated protein (FTO), a key RNA N<sup>6</sup>-methyladenosine (m<sup>6</sup>A) demethylase, has been highlighted for its important role in inflammatory response. Emerging evidences link the O-GlcNAcylation to numerous human diseases, particularly inflammation. However, the specific role and underlying mechanism of FTO O-GlcNAcylation in inflammation remain elusive.<h4>Methods</h4>The FTO O-GlcNAcylation modification was determined by co-immunopre  ...[more]

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