Nonhydrolyzable Ubiquitin−Isopeptide Isosteres as Deubiquitinating Enzyme Probes.

2010 ◽  
Vol 132 (26) ◽  
pp. 8834-8835 ◽  
Author(s):  
Anitha Shanmugham ◽  
Alexander Fish ◽  
Mark P. A. Luna-Vargas ◽  
Alex C. Faesen ◽  
Farid El Oualid ◽  
...  
Keyword(s):  
Deubiquitinating Enzyme ◽  
Enzyme Probes

777: The Von Hippel-Lindau Protein-Interacting Deubiquitinating Enzyme 2 Deubiquitinates and Stabilizes Hypoxia-Inducible Factor-1α

2004 ◽  
Vol 171 (4S) ◽  
pp. 206-206
Author(s):  
Guan Wu ◽  
Zaibo Li ◽  
Dakun Wang ◽  
Edward M. Messing
Keyword(s):  
Hypoxia Inducible Factor ◽  
Deubiquitinating Enzyme ◽  
Von Hippel Lindau ◽  
Hypoxia Inducible Factor 1Α

Function of Deubiquitinating Enzyme USP1 in Adipogenesis

Diabetes ◽  
2018 ◽  
Vol 67 (Supplement 1) ◽  
pp. 284-LB
Author(s):  
JINAH LEE
Keyword(s):  
Deubiquitinating Enzyme

scholarly journals Role of Virally-Encoded Deubiquitinating Enzymes in Regulation of the Virus Life Cycle

2021 ◽  
Vol 22 (9) ◽  
pp. 4438
Author(s):  
Jessica Proulx ◽  
Kathleen Borgmann ◽  
In-Woo Park
Keyword(s):  
Immune Response ◽  
Life Cycle ◽  
Deubiquitinating Enzyme ◽  
Deubiquitinating Enzymes ◽  
Antiviral Immune Response ◽  
Cellular Processes ◽  
Virus Life Cycle ◽  
Infected Cells ◽  
Dependent Processes

The ubiquitin (Ub) proteasome system (UPS) plays a pivotal role in regulation of numerous cellular processes, including innate and adaptive immune responses that are essential for restriction of the virus life cycle in the infected cells. Deubiquitination by the deubiquitinating enzyme, deubiquitinase (DUB), is a reversible molecular process to remove Ub or Ub chains from the target proteins. Deubiquitination is an integral strategy within the UPS in regulating survival and proliferation of the infecting virus and the virus-invaded cells. Many viruses in the infected cells are reported to encode viral DUB, and these vial DUBs actively disrupt cellular Ub-dependent processes to suppress host antiviral immune response, enhancing virus replication and thus proliferation. This review surveys the types of DUBs encoded by different viruses and their molecular processes for how the infecting viruses take advantage of the DUB system to evade the host immune response and expedite their replication.

scholarly journals Activity-based protein profiling reveals deubiquitinase and aldehyde dehydrogenase targets of a cyanopyrrolidine probe

2021 ◽  
Author(s):  
Nattawadee Panyain ◽  
Aurélien Godinat ◽  
Aditya Raymond Thawani ◽  
Sofía Lachiondo-Ortega ◽  
Katie Mason ◽  
...  
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Lung Fibrosis ◽  
Drug Target ◽  
Protein Profiling ◽  
Deubiquitinating Enzyme ◽  
Potential Drug Target ◽  
Potential Drug ◽  
Bona Fide ◽  
Carboxy Terminal

Ubiquitin carboxy-terminal hydrolase L1 (UCHL1), a deubiquitinating enzyme (DUB), is a potential drug target in various cancers, and liver and lung fibrosis. However, bona fide functions and substrates of UCHL1...

scholarly journals Interaction of the Deubiquitinating Enzyme Ubp2 and the E3 Ligase Rsp5 Is Required for Transporter/Receptor Sorting in the Multivesicular Body Pathway

PLoS ONE ◽  
2009 ◽  
Vol 4 (1) ◽  
pp. e4259 ◽  
Author(s):  
Mandy H. Y. Lam ◽  
Danièle Urban-Grimal ◽  
Amandine Bugnicourt ◽  
Jack F. Greenblatt ◽  
Rosine Haguenauer-Tsapis ◽  
...  
Keyword(s):  
E3 Ligase ◽  
Multivesicular Body ◽  
Deubiquitinating Enzyme

scholarly journals The Endosome-associated Deubiquitinating Enzyme USP8 Regulates BACE1 Enzyme Ubiquitination and Degradation

2016 ◽  
Vol 291 (30) ◽  
pp. 15753-15766 ◽  
Author(s):  
Eniola Funmilayo Aduke Yeates ◽  
Giuseppina Tesco
Keyword(s):  
Deubiquitinating Enzyme

scholarly journals HAUSP, a deubiquitinating enzyme for p53, is polyubiquitinated, polyneddylated, and dimerized

FEBS Letters ◽  
2005 ◽  
Vol 579 (21) ◽  
pp. 4867-4872 ◽  
Author(s):  
Hye-Jin Lee ◽  
Myung-Sun Kim ◽  
Yu-Kyung Kim ◽  
Yu-Kyoung Oh ◽  
Kwang-Hyun Baek
Keyword(s):  
Deubiquitinating Enzyme
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