Zobrazeno 1 - 10
of 178
pro vyhledávání: '"Raymond J Deshaies"'
Autor:
Min-Kyung Sung, Tanya R Porras-Yakushi, Justin M Reitsma, Ferdinand M Huber, Michael J Sweredoski, André Hoelz, Sonja Hess, Raymond J Deshaies
Publikováno v:
eLife, Vol 5 (2016)
Overproduced yeast ribosomal protein (RP) Rpl26 fails to assemble into ribosomes and is degraded in the nucleus/nucleolus by a ubiquitin-proteasome system quality control pathway comprising the E2 enzymes Ubc4/Ubc5 and the ubiquitin ligase Tom1. tom1
Externí odkaz:
https://doaj.org/article/44ad927e6bbf49ea8eb9522bc2eca76c
Autor:
Ruzbeh Mosadeghi, Kurt M Reichermeier, Martin Winkler, Anne Schreiber, Justin M Reitsma, Yaru Zhang, Florian Stengel, Junyue Cao, Minsoo Kim, Michael J Sweredoski, Sonja Hess, Alexander Leitner, Ruedi Aebersold, Matthias Peter, Raymond J Deshaies, Radoslav I Enchev
Publikováno v:
eLife, Vol 5 (2016)
The COP9-Signalosome (CSN) regulates cullin–RING ubiquitin ligase (CRL) activity and assembly by cleaving Nedd8 from cullins. Free CSN is autoinhibited, and it remains unclear how it becomes activated. We combine structural and kinetic analyses to
Externí odkaz:
https://doaj.org/article/687ae2c8181c46b19f44a743b621a9d9
Publikováno v:
eLife, Vol 3 (2014)
Proteasome inhibition elicits an evolutionarily conserved response wherein proteasome subunit mRNAs are upregulated, resulting in recovery (i.e., ‘bounce-back’) of proteasome activity. We previously demonstrated that the transcription factor Nrf1
Externí odkaz:
https://doaj.org/article/f71819adaedc44278dbd74e527365e4b
Publikováno v:
eLife, Vol 2 (2013)
Ubiquitin-dependent proteolysis can initiate at ribosomes for myriad reasons including misfolding of a nascent chain or stalling of the ribosome during translation of mRNA. Clearance of a stalled complex is required to recycle the ribosome for future
Externí odkaz:
https://doaj.org/article/0e9700d971ba403f9a2606c83465e45d
Publikováno v:
PLoS Biology, Vol 4, Iss 8, p e267 (2006)
The 26S proteasome contains a 19S regulatory particle that selects and unfolds ubiquitinated substrates for degradation in the 20S catalytic particle. To date there are no high-resolution structures of the 19S assembly, nor of the lid or base subcomp
Externí odkaz:
https://doaj.org/article/3052dae93af941eaa6935c7d78c588a9
Publikováno v:
PLoS Biology, Vol 2, Iss 1, p E2 (2004)
The JAMM (JAB1/MPN/Mov34 metalloenzyme) motif in Rpn11 and Csn5 underlies isopeptidase activities intrinsic to the proteasome and signalosome, respectively. We show here that the archaebacterial protein AfJAMM possesses the key features of a zinc met
Externí odkaz:
https://doaj.org/article/925701d1c95c403d8e24da88cc6d57b5
Autor:
Yaru Zhang, Marco Jost, Ryan A. Pak, Daniel Lu, Jing Li, Brett Lomenick, Spiros D. Garbis, Chi-Ming Li, Jonathan S. Weissman, James Russell Lipford, Raymond J. Deshaies
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 119(36)
Cop9 signalosome (CSN) regulates the function of cullin–RING E3 ubiquitin ligases (CRLs) by deconjugating the ubiquitin-like protein NEDD8 from the cullin subunit. To understand the physiological impact of CSN function on the CRL network and cell p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc36e57f6f93f9157316c013a44750ab
https://pubmed.ncbi.nlm.nih.gov/36037385
https://pubmed.ncbi.nlm.nih.gov/36037385
Autor:
Raymond J. Deshaies
Publikováno v:
Signal Transduction and Targeted Therapy
The modern biopharmaceutical industry traces its roots to the dawn of the twentieth century, coincident with marketing of aspirin—a signature event in the history of modern drug development. Although the archetypal discovery process did not change
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3a6be08f060009c36e5457b02efdaa1
https://doi.org/10.1038/s41586-020-2168-1
https://doi.org/10.1038/s41586-020-2168-1
Autor:
Jennifer Cable, Eilika Weber‐Ban, Tim Clausen, Kylie J. Walters, Michal Sharon, Daniel J. Finley, Yangnan Gu, John Hanna, Yue Feng, Sascha Martens, Anne Simonsen, Malene Hansen, Hong Zhang, Jonathan M. Goodwin, Alessio Reggio, Chunmei Chang, Liang Ge, Brenda A. Schulman, Raymond J. Deshaies, Ivan Dikic, J. Wade Harper, Ingrid E. Wertz, Nicolas H. Thomä, Mikołaj Słabicki, Judith Frydman, Ursula Jakob, Della C. David, Eric J. Bennett, Carolyn R. Bertozzi, Richa Sardana, Vinay V. Eapen, Serena Carra
Publikováno v:
Annals of the New York Academy of Sciences 1510(1), 79-99 (2022). doi:10.1111/nyas.14745
Targeted protein degradation is critical for proper cellular function and development. Protein degradation pathways, such as the ubiquitin proteasomes system, autophagy, and endosome-lysosome pathway, must be tightly regulated to ensure proper elimin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88110e83b56645cb723743deb2706a33
Autor:
Raymond J. Deshaies, James A. Johnston, J. R. Lipford, Jixi Li, D. J. Sherman, Jennifer L. Mamrosh, Annie Moradian, Rati Verma, Michael J. Sweredoski
The adaptive immune system distinguishes self from non-self by surveying peptides generated from degradation of intracellular proteins that are loaded onto MHC Class I molecules for display on the cell surface. While early studies reported that the b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::481ee2f255b1caa71fa9b6429cac8dce
https://doi.org/10.1101/2021.10.07.463289
https://doi.org/10.1101/2021.10.07.463289