Ontology highlight
ABSTRACT:
INSTRUMENT(S): Orbitrap Fusion
ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)
SUBMITTER: Duc Duong
LAB HEAD: Jun Yin
PROVIDER: PXD023688 | Pride | 2022-10-13
REPOSITORIES: Pride
Action | DRS | |||
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Rsp5_Geng_dataset_2.xlsx | Xlsx | |||
Rsp5_Geng_dataset_3.xlsx | Xlsx | |||
Wang_Supplemental_table_1_proteomics_5.xlsx | Xlsx | |||
geng_ctl_c.raw | Raw | |||
geng_ctl_c_b.raw | Raw |
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Wang Yiyang Y Wang Yiyang Y Fang Shuai S Chen Geng G Ganti Rakhee R Chernova Tatiana A TA Zhou Li L Duong Duc D Kiyokawa Hiroaki H Li Ming M Zhao Bo B Shcherbik Natalia N Chernoff Yury O YO Yin Jun J
Cell chemical biology 20210304 9
Attachment of the ubiquitin (UB) peptide to proteins via the E1-E2-E3 enzymatic machinery regulates diverse biological pathways, yet identification of the substrates of E3 UB ligases remains a challenge. We overcame this challenge by constructing an "orthogonal UB transfer" (OUT) cascade with yeast E3 Rsp5 to enable the exclusive delivery of an engineered UB (xUB) to Rsp5 and its substrate proteins. The OUT screen uncovered new Rsp5 substrates in yeast, such as Pal1 and Pal2, which are partners ...[more]