Proteomics

Dataset Information

0

Human cholangiocarcinoma LC-MS/MS


ABSTRACT: We studied the effect of Ser30 with or without O-GlcNAc modification on K18 protein and its co-immunoprecipitated proteins in cholangiocarcinoma cells.The lysates from HuCCT1 shK18 stable cell line transfected with FLAG-K18-WT or FLAG-K18-S30A were captured with anti-FLAG beads, and then subjected to in-gel trypsin digestion and LC-MS/MS analysis.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

DISEASE(S): Cholangiocarcinoma

SUBMITTER: xiangfeng Meng  

LAB HEAD: Xiangfeng Meng

PROVIDER: PXD048144 | Pride | 2024-06-22

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
K18-S30A-1.raw Raw
K18-S30A-2.raw Raw
K18-S30A-3.raw Raw
K18-WT-1.raw Raw
K18-WT-2.raw Raw
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Publications

<i>O</i>-GlcNAcylation Facilitates the Interaction between Keratin 18 and Isocitrate Dehydrogenases and Potentially Influencing Cholangiocarcinoma Progression.

Meng Xiangfeng X   Zhou Yue Y   Xu Lei L   Hu Limu L   Wang Changjiang C   Tian Xiao X   Zhang Xiang X   Hao Yi Y   Cheng Bo B   Ma Jing J   Wang Lei L   Liu Jialin J   Xie Ran R  

ACS central science 20240423 5


Glycosylation plays a pivotal role in the intricate landscape of human cholangiocarcinoma (CCA), actively participating in key pathophysiological processes driving tumor progression. Among the various glycosylation modifications, <i>O</i>-linked β-<i>N</i>-acetyl-glucosamine modification (<i>O</i>-GlcNAcylation) emerges as a dynamic regulator influencing diverse tumor-associated biological activities. In this study, we employed a state-of-the-art chemical proteomic approach to analyze intact gly  ...[more]

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