Ontology highlight
ABSTRACT:
INSTRUMENT(S): Q Exactive
ORGANISM(S): Homo Sapiens (human)
TISSUE(S): Cell Culture
SUBMITTER: Ling Xie
LAB HEAD: Qing Zhang
PROVIDER: PXD015790 | Pride | 2019-11-20
REPOSITORIES: Pride
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20160113_ZhangQ_H1.raw | Raw | |||
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andromeda.zip | Other |
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Nature communications 20191115 1
Protein hydroxylation affects protein stability, activity, and interactome, therefore contributing to various diseases including cancers. However, the transiency of the hydroxylation reaction hinders the identification of hydroxylase substrates. By developing an enzyme-substrate trapping strategy coupled with TAP-TAG or orthogonal GST- purification followed by mass spectrometry, we identify adenylosuccinate lyase (ADSL) as an EglN2 hydroxylase substrate in triple negative breast cancer (TNBC). A ...[more]