Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 17, Issue 6, Pages 726-735Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2007.08.018
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Funding
- NCRR NIH HHS [P41 RR000862, P41 RR000862-310201] Funding Source: Medline
- NIGMS NIH HHS [R01 GM065872-07, R01 GM065872, F32 GM075695, GM075695, GM65872] Funding Source: Medline
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Ubiquitin (Ub) and ubiquitin-like (Ubl) proteins regulate a diverse array of cellular pathways through post-translational attachment to protein substrates. Ub/Ubl-mediated signaling is initiated through E1, E2, and E3-mediated conjugation, transduced by proteins that recognize Ub/Ubl-modified substrates, and terminated by proteases which remove the Ub/Ubl from the substrate. Recent structural studies have elucidated mechanisms pertinent to Ub/Ubl conjugation, recognition, and deconjugation, highlighting essential steps during Ub/Ubl modification that illustrate common and divergent mechanistic themes within this important process.
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