Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Larissa A. Durfee"'
Publikováno v:
Molecular Cell. 50:368-378
Previous studies have indicated that 6%-30% of newly synthesized proteins are rapidly degraded by the ubiquitin-proteasome system; however, the relationship of ubiquitination to translation for these proteins has been unclear. We report that cotransl
Autor:
Larissa A. Durfee, Jon M. Huibregtse
Publikováno v:
Subcellular Biochemistry
Conjugation and Deconjugation of Ubiquitin Family Modifiers
Subcellular Biochemistry ISBN: 9781441966759
Conjugation and Deconjugation of Ubiquitin Family Modifiers
Subcellular Biochemistry ISBN: 9781441966759
ISG15 is an interferon-induced ubiquitin-like protein (Ubl) that has antiviral properties. The core E1, E2 and E3 enzymes for conjugation of human ISG15 are Ube1L, UbcH8 and Herc5, all of which are induced at the transcriptional level by Type 1 inter
Autor:
Larissa A. Durfee, Radmila Hrdličková, Jiang Wu, Rashmi Rajendra, Guang Gao, Karen Artzt, Eva Benito, Mariam Kuruvilla, Andrew S. Liss, Julius C. Barsi
Publikováno v:
genesis. 45:722-727
Mib1 and Mib2 ubiquitin ligases are very similar in their domain construction. They partake in the Notch signaling pathway by ubiquitinating the Notch receptors Delta and Jagged prior to endocytosis. We have created a targeted mutation of Mib2 and sh
Autor:
Jon M. Huibregtse, Larissa A. Durfee
Publikováno v:
Methods in Molecular Biology ISBN: 9781617794735
Methods in Molecular Biology
Ubiquitin Family Modifiers and the Proteasome
Methods in Molecular Biology
Ubiquitin Family Modifiers and the Proteasome
ISG15 is a ubiquitin-like modifier that is expressed in response to type 1 interferon signaling (IFN-α/β) and plays a role in antiviral responses. The core E1, E2, and E3 enzymes for ISG15 are Ube1L, UbcH8, and Herc5, respectively, and these are al
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5375c18cbf3c39cf382d8672ab5b7c49
https://europepmc.org/articles/PMC5912894/
https://europepmc.org/articles/PMC5912894/
Publikováno v:
Molecular Cell
ISG15 is an interferon-induced and anti-viral ubiquitin-like protein (Ubl). Herc5, the major E3 enzyme for ISG15, mediates the ISGylation of over 300 proteins in interferon-stimulated cells. In addressing this broad substrate selectivity of Herc5, we
E1 and E2 enzymes coordinate the first steps in conjugation of ubiquitin (Ub) and ubiquitin-like proteins (Ubls). ISG15 is an interferon-alpha/beta-induced Ubl, and the E1 and E2 enzymes for ISG15 conjugation are Ube1L and UbcH8, respectively. UbcH7
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62edf8610a9d0963d5e86a9b274a28e5
https://europepmc.org/articles/PMC2527107/
https://europepmc.org/articles/PMC2527107/
Autor:
Susan Young, Staci D. Schwantz, Jimmy L. Spearow, Karen Artzt, Jonathan Scolnick, M. A. Centilli, Larissa A. Durfee, Jiang Wu, Gabriela Vasquez, Gabriela Rennebeck
At the proximal part of mouse chromosome 17 there are three well-defined genes affecting the axis of the embryo and consequently tail length: Brachyury, Brachyury the second, and the t-complex tail interaction (T1, T2, and tct). The existence of T1 a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::399c1a890ad376073db857f3845779cb
https://europepmc.org/articles/PMC2034620/
https://europepmc.org/articles/PMC2034620/