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  • publication . Article . Other literature type . 2019
    Structural basis for adenylation and thioester bond formation in the ubiquitin E1
    Open Access English
    Authors:
    Derek S. Tan; Derek S. Tan; Christopher D. Lima; Christopher D. Lima; Zachary S. Hann; Zachary S. Hann; Xuequan Lu; Michaelyn C. Lux; Michaelyn C. Lux; Shaun K. Olsen; ...
    doi: 10.1073/pnas.1905488116
    Publisher: National Academy of Sciences
    Project: NIH | Structural and Functional... (5R01GM079196-07), NIH | Structural studies of RNA... (1R35GM118080-01), NIH | Structural Studies of SUM... (5R01GM065872-12), NIH | Tri-Institutional PhD Pro... (1T32GM115327-01), NIH | MOUSE GENETICS (2P30CA008748-43), NIH | Rational Design of Adenyl... (5R01GM100477-08), NIH | Pixel Array Detector for ... (1S10RR029205-01), NIH | NE-CAT Center for Advance... (4P41GM103403-14)

    Significance Posttranslational protein modification by ubiquitin (Ub) regulates aspects of biology, including protein turnover and the cell cycle. Proteins and enzymes that promote Ub conjugation are therapeutic targets because they are sometimes dysregulated in cancer,...

1 research outcomes, page 1 of 1