نتایج جستجو برای: conjugating enzyme

تعداد نتایج: 242266  

Journal: :Cell 2011
Derek F. Ceccarelli Xiaojing Tang Benoit Pelletier Stephen Orlicky Weilin Xie Veronique Plantevin Dante Neculai Yang-Chieh Chou Abiodun Ogunjimi Abdallah Al-Hakim Xaralabos Varelas Joanna Koszela Gregory A. Wasney Masoud Vedadi Sirano Dhe-Paganon Sarah Cox Shuichan Xu Antonia Lopez-Girona Frank Mercurio Jeff Wrana Daniel Durocher Sylvain Meloche David R. Webb Mike Tyers Frank Sicheri

In the ubiquitin-proteasome system (UPS), E2 enzymes mediate the conjugation of ubiquitin to substrates and thereby control protein stability and interactions. The E2 enzyme hCdc34 catalyzes the ubiquitination of hundreds of proteins in conjunction with the cullin-RING (CRL) superfamily of E3 enzymes. We identified a small molecule termed CC0651 that selectively inhibits hCdc34. Structure deter...

Journal: :Plant physiology 1993
S Picton J E Gray A Lowe S L Barton D Grierson

Ubiquitin is a small, abundant protein that is seemingly present in a11 eukaryotic cells and that is covalently ligated to specific protein substrates via an ATP-dependent reaction. This ubiquitinous has been demonstrated to target proteins for subsequent cellular degradation. Briefly, the process involves activation of ubiquitin, catalyzed by ubiquitin-activating enzymes, transfer to a family ...

2017
Pearl Magala William E. Bocik Ananya Majumdar Joel R. Tolman

The ubiquitin conjugating enzyme Ube2g2 together with its cognate E3 ligase gp78 catalyzes the synthesis of lysine-48 polyubiquitin chains constituting signals for the proteasomal degradation of misfolded proteins in the endoplasmic reticulum. Here, we employ NMR spectroscopy in combination with single-turnover diubiquitin formation assays to examine the role of the RING domain from gp78 in the...

Journal: :The Journal of biological chemistry 1997
C J Kho G S Huggins W O Endege C M Hsieh M E Lee E Haber

The helix-loop-helix E2A proteins (E12 and E47) govern cellular growth and differentiation. To identify binding partners that regulate the function of these ubiquitous transcription factors, we screened for proteins that interacted with the C terminus of E12 by the yeast interaction trap. UbcE2A, a rat enzyme that is highly homologous to and functionally complements the yeast ubiquitin-conjugat...

Journal: :The EMBO journal 2003
Pei-Ying Wu Mary Hanlon Michael Eddins Colleen Tsui Richard S Rogers Jane P Jensen Michael J Matunis Allan M Weissman Cynthia Wolberger Cecile M Pickart

Ubiquitin (Ub) regulates diverse functions in eukaryotes through its attachment to other proteins. The defining step in this protein modification pathway is the attack of a substrate lysine residue on Ub bound through its C-terminus to the active site cysteine residue of a Ub-conjugating enzyme (E2) or certain Ub ligases (E3s). So far, these E2 and E3 cysteine residues are the only enzyme group...

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