نتایج جستجو برای: e6ap

تعداد نتایج: 171  

2013
Virginia P. Ronchi Jennifer M. Klein Daniel J. Edwards Arthur L. Haas

Journal: :Physiological genomics 2000
L E Scarafia A Winter D C Swinney

We evaluated the expression of 28 gene sequences with homology to the carboxy terminal of HECT E3 ubiquitin ligases in nine human cell lines using RT-PCR, to determine whether gene expression could be associated with cell-specific functions (HECT is "homologous to E6AP C-terminus"). In general, HECT-domain E3 ligases are constitutively expressed at low levels with a broad range between cell typ...

Journal: :Journal of virology 2001
Q Gao L Singh A Kumar S Srinivasan D E Wazer V Band

Recent analyses have identified a number of binding partners for E6, including E6AP, ERC55, paxillin, hDlg, p300, interferon regulatory factor 3, hMCM7, Bak, and E6TP1. Notably, association with E6 targets p53, E6TP1, myc, hMCM7, and Bak for degradation. However, the relative importance of the various E6 targets in cellular transformation remains unclear. E6 alone can dominantly immortalize nor...

Journal: :The Journal of biological chemistry 2009
Tomoaki Uchiki Hyoung Tae Kim Bo Zhai Steven P Gygi Jennifer A Johnston John P O'Bryan Alfred L Goldberg

S5a/Rpn10 is a ubiquitin (Ub)-binding protein that is a subunit of the 26S proteasome but also exists free in the cytosol. It binds poly-Ub chains through its two Ub-interacting motifs (UIMs). We discovered that, unlike typical substrates of Ub ligases (E3s), S5a can be ubiquitinated by all E3s tested including multimeric and monomeric Ring finger E3s (MuRF1, Siah2, Parkin, APC, and SCF(betaTRC...

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