Quantitative time-resolved chemoproteomics reveals that stable O-GlcNAc regulates box C/D snoRNP biogenesis

scientific article published on 31 July 2017

Quantitative time-resolved chemoproteomics reveals that stable O-GlcNAc regulates box C/D snoRNP biogenesis is …
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scholarly articleQ13442814

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P819ADS bibcode2017PNAS..114E6749Q
P356DOI10.1073/PNAS.1702688114
P932PMC publication ID5565422
P698PubMed publication ID28760965

P50authorChu WangQ50286856
Xing ChenQ50999642
P2093author name stringYing Chen
Wei Qin
Baiyi Quan
Ke Qin
Yuntao Zhu
Xinqi Fan
Pinou Lv
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P4510describes a project that usesImageJQ1659584
P433issue33
P407language of work or nameEnglishQ1860
P304page(s)E6749-E6758
P577publication date2017-07-31
P1433published inProceedings of the National Academy of Sciences of the United States of AmericaQ1146531
P1476titleQuantitative time-resolved chemoproteomics reveals that stable O-GlcNAc regulates box C/D snoRNP biogenesis
P478volume114

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cites work (P2860)
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Q52578738New use for CETSA: monitoring innate immune receptor stability via post-translational modification by OGT.
Q93161828Next-generation unnatural monosaccharides reveal that ESRRB O-GlcNAcylation regulates pluripotency of mouse embryonic stem cells
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Q64234101Structures and functions of invertebrate glycosylation
Q59715262The Metabolic Chemical Reporter 6-Azido-6-deoxy-glucose Further Reveals the Substrate Promiscuity of O-GlcNAc Transferase and Catalyzes the Discovery of Intracellular Protein Modification by O-Glucose.
Q90185969The O-GlcNAc Modification on Kinases

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