Proteomics

Dataset Information

0

Exploring the mechanism of contact-dependent cell-cell communication on chemoresistance based on single-cell high-throughput drug screening platform


ABSTRACT: In this study, we developed a microfluidic chip for single-cell high-throughput combined drug screening, and investigated the molecular mechanisms potentially impacted by CDCCC using quantitative mass spectrometry-based proteomics.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: He Huang  

LAB HEAD: He Huang

PROVIDER: PXD047031 | Pride | 2025-05-06

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
CPTX_proteinGroups.tsv Tabular
CP_proteinGroups.tsv Tabular
PTX_proteinGroups.tsv Tabular
cellcommunity_CPTX_re1.mzXML Mzxml
cellcommunity_CPTX_re2.mzXML Mzxml
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Publications

SIRT3 differentially regulates lysine benzoylation from SIRT2 in mammalian cells.

Peng Panpan P   Lu Ying Y   Ren Xuelian X   Yan Cong C   Guo Xinlong X   Liu Ruilong R   Song Xiaohan X   Huang He H  

iScience 20241016 11


Lysine benzoylation (Kbz), a new type of protein post-translational modification (PTM) we discovered, has garnered significant attention. While we initially identified SIRT2 as a debenzoylase in mammalian cells, recent findings suggest its exclusivity may be questioned. However, other debenzoylases in mammalian cells remain underexplored. Here, our study reveals SIRT3 as an additional debenzoylase. Through quantitative analysis, we identified 1,075 Kbz sites in mammalian cells, with 44 specifica  ...[more]

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