Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Gary. J. Sibbet"'
Autor:
Helge M. Magnussen, Syed F. Ahmed, Gary. J. Sibbet, Ventzislava A. Hristova, Koji Nomura, Andreas K. Hock, Lewis J. Archibald, Andrew G. Jamieson, David Fushman, Karen H. Vousden, Allan M. Weissman, Danny T. Huang
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
p53 is an important tumor suppressor protein which is regulated by the E3 ubiquitin ligase MDM2. Here the authors reveal that DNA damage-induced Ser429 phosphorylation of MDM2 serve to boost the activity of MDM2 homodimer by stabilizing the active E2
Externí odkaz:
https://doaj.org/article/80e8bf383dda460bb88d16b6b1cd6555
Autor:
Mark A. Nakasone, Karolina A. Majorek, Mads Gabrielsen, Gary J. Sibbet, Brian O. Smith, Danny T. Huang
Publikováno v:
Nature Chemical Biology. 18:422-431
Ubiquitin (Ub) chain types govern distinct biological processes. K48-linked polyUb chains target substrates for proteasomal degradation, but the mechanism of Ub chain synthesis remains elusive due to the transient nature of Ub handover. Here, we pres
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::59b00b065e84f7df0c09e6f054c06098
https://doi.org/10.1038/s41589-021-00952-x
https://doi.org/10.1038/s41589-021-00952-x
E3 ligase-inactivation rewires CBL interactome to elicit oncogenesis by hijacking RTK–CBL–CIN85 axis
Autor:
Danny T. Huang, David Sumpton, Sergio Lilla, Lori Buetow, Syed Feroj Ahmed, William C. Clark, Gary J. Sibbet, Ann Hedley, Sara Zanivan, Mads Gabrielsen
Publikováno v:
Oncogene
Casitas B-lineage lymphoma (CBL) is a ubiquitin ligase (E3) that becomes activated upon Tyr371-phosphorylation and targets receptor protein tyrosine kinases for ubiquitin-mediated degradation. Deregulation of CBL and its E3 activity is observed in my
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9005bbfbdbdd5e0fa9a704a9b8bd131e
https://doi.org/10.1038/s41388-021-01684-x
https://doi.org/10.1038/s41388-021-01684-x
Autor:
Mark A, Nakasone, Karolina A, Majorek, Mads, Gabrielsen, Gary J, Sibbet, Brian O, Smith, Danny T, Huang
Publikováno v:
Nature chemical biology. 18(4)
Ubiquitin (Ub) chain types govern distinct biological processes. K48-linked polyUb chains target substrates for proteasomal degradation, but the mechanism of Ub chain synthesis remains elusive due to the transient nature of Ub handover. Here, we pres
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a423c870b00a52268d7ef3f5190bcd0f
https://pubmed.ncbi.nlm.nih.gov/35027744
https://pubmed.ncbi.nlm.nih.gov/35027744
Autor:
Sara Zanivan, Lori Buetow, Chatrin Chatrin, Danny T. Huang, Sergio Lilla, Syed Feroj Ahmed, Gary J. Sibbet, Mads Gabrielsen
Publikováno v:
Science Advances
The C-terminal domain of DELTEX E3s binds ADP-ribose and promotes ubiquitination of poly-ADP-ribosylated substrates.
Cross-talk between ubiquitination and ADP-ribosylation regulates spatiotemporal recruitment of key players in many signaling pat
Cross-talk between ubiquitination and ADP-ribosylation regulates spatiotemporal recruitment of key players in many signaling pat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af33917f9c6abc0821c6c526665cea28
https://eprints.gla.ac.uk/222684/1/222684.pdf
https://eprints.gla.ac.uk/222684/1/222684.pdf
Autor:
Brian O. Smith, Gary J. Sibbet, Chatrin Chatrin, David Sumpton, Mads Gabrielsen, Syed Feroj Ahmed, Danny T. Huang, Mark A. Nakasone, Lori Buetow
Publikováno v:
Science Advances
The C-terminal RING and DTC domains of mammalian Deltex proteins catalyze ADP-ribosylation at the C terminus of ubiquitin.
Cellular cross-talk between ubiquitination and other posttranslational modifications contributes to the regulation of nume
Cellular cross-talk between ubiquitination and other posttranslational modifications contributes to the regulation of nume
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3f05735803f347e349100b8c131a59d
https://pubmed.ncbi.nlm.nih.gov/32948590
https://pubmed.ncbi.nlm.nih.gov/32948590
Autor:
Syed Faisal Ahmed, Andrew G. Jamieson, Andreas K. Hock, Helge M. Magnussen, Karen H. Vousden, Ventzislava A. Hristova, Lewis J. Archibald, Danny T. Huang, Gary J. Sibbet, Koji Nomura, David Fushman, Allan M. Weissman
Publikováno v:
Nature Communications
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
Phosphorylation of MDM2 by ATM upon DNA damage is an important mechanism for deregulating MDM2, thereby leading to p53 activation. ATM phosphorylates multiple residues near the RING domain of MDM2, but the underlying molecular basis for deregulation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2d3ed69811ec6623d16c2a382921ed6
https://pubmed.ncbi.nlm.nih.gov/32350255
https://pubmed.ncbi.nlm.nih.gov/32350255
Publikováno v:
Journal of Biological Chemistry
The Journal of Biological Chemistry
The Journal of Biological Chemistry
Ubiquitin (Ub)-conjugating enzymes and Ub ligases control protein degradation and regulate many cellular processes in eukaryotes. Cellular inhibitor of apoptosis protein-1 (cIAP1) plays a central role in apoptosis and tumor necrosis factor signaling.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f0ed8fbc72a4ec2f42fb5cf9ce61444
Structural analysis of MDM2 RING separates degradation from regulation of p53 transcription activity
Autor:
Karen H. Vousden, Marta Klejnot, Gary J. Sibbet, Dominika Kowalczyk, Danny T. Huang, Andreas K. Hock, Koji Nomura
Publikováno v:
Nature Structural & Molecular Biology
MDM2-MDMX complexes bind the p53 tumor suppressor protein, inhibiting p53’s transcriptional activity and targeting p53 for proteasomal degradation. Inhibitors that disrupt binding between p53 and MDM2 efficiently activate a p53 response although th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::adf8af8370f62e87a2153f9af3db7e59
Publikováno v:
Nature structural & molecular biology
RING E3 ligases catalyze the transfer of ubiquitin (Ub) from E2 ubiquitin-conjugating enzyme thioesterified with Ub (E2~Ub) to substrate. For RING E3 dimers, the RING domain of one subunit and tail of the second cooperate to prime Ub, but how this is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9be2b86cbf62018d7f2eaab9bca32b86
https://doi.org/10.1038/nsmb.2621
https://doi.org/10.1038/nsmb.2621