Zobrazeno 1 - 10
of 10
pro vyhledávání: '"James L. Yen"'
Publikováno v:
Proceedings of the National Academy of Sciences. 117:21319-21327
Organisms can adapt to a broad spectrum of sudden and dramatic changes in their environment. These abrupt changes are often perceived as stress and trigger responses that facilitate survival and eventual adaptation. The ubiquitin-proteasome system (U
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::91e0aefde338fb3661577d6d52ebdef6
https://doi.org/10.1073/pnas.1922891117
https://doi.org/10.1073/pnas.1922891117
Publikováno v:
PLoS Genetics, Vol 11, Iss 12, p e1005727 (2015)
Abundance of substrate receptor subunits of Cullin-RING ubiquitin ligases (CRLs) is tightly controlled to maintain the full repertoire of CRLs. Unbalanced levels can lead to sequestration of CRL core components by a few overabundant substrate recepto
Externí odkaz:
https://doaj.org/article/d4923af01ff5425f9c2081aaf72efc71
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 117, iss 35
Organisms can adapt to a broad spectrum of sudden and dramatic changes in their environment. These abrupt changes are often perceived as stress and trigger responses that facilitate survival and eventual adaptation. The ubiquitin proteasome system (U
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15215f4854313fa88850096e7f209b6b
https://escholarship.org/uc/item/29f845pq
https://escholarship.org/uc/item/29f845pq
Publikováno v:
Proc Natl Acad Sci U S A
Organisms can adapt to a broad spectrum of sudden and dramatic changes in their environment. These abrupt changes are often perceived as stress and trigger responses that facilitate survival and eventual adaptation. The ubiquitin–proteasome system
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c138b937d1a5dbc3175f8aedd8c343c9
https://pubmed.ncbi.nlm.nih.gov/32817489
https://pubmed.ncbi.nlm.nih.gov/32817489
Autor:
James L. Yen, Karin Flick, Peter K. Kaiser, Ikram Ouni, Christie V. Papagiannis, Lan Huang, An Tyrrell, Radhika Mathur, Robyn M. Kaake
Publikováno v:
Molecular Cell. 48(2):288-297
Summary A large group of E3 ubiquitin ligases is formed by the multisubunit SCF complex, whose core complex (Rbx1/Cul1-Cdc53/Skp1) binds one of many substrate recruiting F-box proteins to form an array of SCF ligases with diverse substrate specificit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c180f02e80c016c55ab7c3356018bc16
Publikováno v:
PLoS genetics, vol 11, iss 12
Mathur, R; Yen, JL; & Kaiser, P. (2015). Skp1 Independent Function of Cdc53/Cul1 in F-box Protein Homeostasis. PLoS Genetics, 11(12), e1005727. doi: 10.1371/journal.pgen.1005727. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/4760f11z
PLoS Genetics, Vol 11, Iss 12, p e1005727 (2015)
PLoS Genetics
Mathur, R; Yen, JL; & Kaiser, P. (2015). Skp1 Independent Function of Cdc53/Cul1 in F-box Protein Homeostasis. PLoS Genetics, 11(12), e1005727. doi: 10.1371/journal.pgen.1005727. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/4760f11z
PLoS Genetics, Vol 11, Iss 12, p e1005727 (2015)
PLoS Genetics
Abundance of substrate receptor subunits of Cullin-RING ubiquitin ligases (CRLs) is tightly controlled to maintain the full repertoire of CRLs. Unbalanced levels can lead to sequestration of CRL core components by a few overabundant substrate recepto
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::130b2e7df4aa61cd00bb55f40ddab2f2
https://escholarship.org/uc/item/4760f11z
https://escholarship.org/uc/item/4760f11z
Publikováno v:
Science Signaling. 3
The proteasome plays a pivotal role in the cellular response to oxidative stress. Here, we used biochemical and mass spectrometric methods to investigate structural changes in the 26S proteasomes from yeast and mammalian cells exposed to hydrogen per
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33cbafd241cda56f5201ad0361b610a9
https://doi.org/10.1126/scisignal.2001232
https://doi.org/10.1126/scisignal.2001232
A ubiquitin-interacting motif protects polyubiquitinated Met4 from degradation by the 26S proteasome
Publikováno v:
Nature cell biology. 8(5)
Covalent attachment of ubiquitin to proteins regulates a host of cellular events by proteolysis dependent and independent mechanisms. A variety of protein domains that bind non-covalently to ubiquitin have been described and functionally linked to di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6e908606ea7c2b380742b2194073038
https://pubmed.ncbi.nlm.nih.gov/16604062
https://pubmed.ncbi.nlm.nih.gov/16604062
Publikováno v:
Molecular biology of the cell. 16(4)
Cells have developed a variety of mechanisms to respond to heavy metal exposure. Here, we show that the yeast ubiquitin ligase SCFMet30plays a central role in the response to two of the most toxic environmental heavy metal contaminants, namely, cadmi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::293ae0d6ce95b3959cbebdffc79654d8
https://pubmed.ncbi.nlm.nih.gov/15689486
https://pubmed.ncbi.nlm.nih.gov/15689486
Publikováno v:
Cancer Research. 71:3006-3006
Epigenetic mis-regulation leading to diseases such as cancer is classically understood in terms of aberrant DNA methylation patterns. For decades, 5-methylcytosine (5-mC) has been the focus of epigenetic DNA modification studies. But recently, a nove
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f512854624a914deb614c1be4ee88efe
https://doi.org/10.1158/1538-7445.am2011-3006
https://doi.org/10.1158/1538-7445.am2011-3006