Zobrazeno 1 - 10
of 10
pro vyhledávání: '"John-Paul Upton"'
Autor:
William F. Forrest, Sumit Prakash, Vickie Tsui, Adam R. Renslo, Richard Pastor, Christiaan Klijn, Frank Peale, Mark McCleland, Lorna Kategaya, Carsten Schwerdtfeger, Zachary Stiffler, Matthias Trost, Frederick Cohen, Priyadarshini Jaishankar, Kevin R Clark, Paola Di Lello, Bradley B. Brasher, Florian Gnad, Michael C. M. Kwok, Johanna Heideker, Jeremy Murray, Jason Drummond, Xiaojing Wang, Maria Stella Ritorto, Till Maurer, Maureen Beresini, Matthew T. Chang, James A. Ernst, Taylur P. Ma, Robert A. Blake, Elizabeth Blackwood, Dario R. Alessi, Michelle R. Arkin, Lionel Rouge, Kebing Yu, Brian R. Hearn, Travis W. Bainbridge, Eva Lin, Tracy Kleinheinz, Yinyan Tang, Chudi Ndubaku, Scott E. Martin, John-Paul Upton, Ingrid E. Wertz
Publikováno v:
Nature. 550:534-538
The development of selective ubiquitin-specific protease-7 (USP7) inhibitors GNE-6640 and GNE-6776, which induce tumour cell death and reveal differential kinetics of Lys-48 and Lys-63-linked ubiquitin chain depolymerization by USP7. Deubiquitinating
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2cc98dd9db2eb6f51008b4a3df458a39
https://doi.org/10.1038/nature24006
https://doi.org/10.1038/nature24006
Autor:
Scott A. Oakes, Myriam Heiman, Simon T. Hui, Nathaniel Heintz, Sarah Shen, Paul Greengard, P. V.K. Praveen, Rajarshi Ghosh, Ala Trusina, Qizhi Tang, Vinh Son Nguyen, Feroz R. Papa, John-Paul Upton, Bradley J. Backes, Alana G. Lerner, Yoshimi Nakagawa, Aeid Igbaria
Publikováno v:
PMC
Cell metabolism, vol 16, iss 2
Cell metabolism, vol 16, iss 2
When unfolded proteins accumulate to irremediably high levels within the endoplasmic reticulum (ER), intracellular signaling pathways called the unfolded protein response (UPR) become hyperactivated tocause programmed cell death. We discovered thatth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e692ca040bb363651f884478dd63b2a7
https://doi.org/10.1016/j.cmet.2012.07.007
https://doi.org/10.1016/j.cmet.2012.07.007
Autor:
Maureen Beresini, Matthew T. Chang, Brian R. Hearn, Bradley B. Brasher, Mark McCleland, Ingrid E. Wertz, Lionel Rouge, Tracy Kleinheinz, Kebing Yu, Yinyan Tang, Richard Pastor, Jason Drummond, Chudi Ndubaku, James A. Ernst, William F. Forrest, Scott E. Martin, Christiaan Klijn, Frederick Cohen, John-Paul Upton, Taylur P. Ma, Dario R. Alessi, Carsten Schwerdtfeger, Paola Di Lello, Robert A. Blake, Eva Lin, Travis W. Bainbridge, Sumit Prakash, Adam R. Renslo, Vickie Tsui, Zachary Stiffler, Frank Peale, Maria Stella Ritorto, Till Maurer, Florian Gnad, Jeremy Murray, Matthias Trost, Elizabeth Blackwood, Michael C. Kwok, Priya Jaishanker, Xiaojing Wang, Lorna Kategaya, Kevin R Clark, Johanna Heideker, Michelle R. Arkin
Publikováno v:
Cancer Research. 78:SY23-03
The ubiquitin system regulates the majority of cellular processes in eukaryotes. Ubiquitin is ligated to substrate proteins as monomers or chains, and the topology of ubiquitin modifications regulates substrate interactions with specific proteins. Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::70f0269e1cff3076b98495531f39e19f
https://doi.org/10.1158/1538-7445.am2018-sy23-03
https://doi.org/10.1158/1538-7445.am2018-sy23-03
Autor:
Lieselotte Vande Walle, Scott A. Oakes, John-Paul Upton, Dan Han, Alana G. Lerner, Weihong Xu, Bradley J. Backes, Andrew Hagen, Feroz R. Papa
Publikováno v:
Cell. 138:562-575
During endoplasmic reticulum (ER) stress, homeostatic signaling through the unfolded protein response (UPR) augments ER protein-folding capacity. If homeostasis is not restored, the UPR triggers apoptosis. We found that the ER transmembrane kinase/en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a67649ab2911946bb55392ca3b18aafa
https://doi.org/10.1016/j.cell.2009.07.017
https://doi.org/10.1016/j.cell.2009.07.017
Autor:
Mari Nishino, Kristen M. Coakley, Feroz R. Papa, Andrew Hagen, Scott A. Oakes, John-Paul Upton, Dan Han, Kathryn Austgen
Publikováno v:
Molecular and Cellular Biology. 28:3943-3951
The accumulation of misfolded proteins stresses the endoplasmic reticulum (ER) and triggers cell death through activation of the multidomain proapoptotic BCL-2 proteins BAX and BAK at the outer mitochondrial membrane. The signaling events that connec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a7cb51abc55baf7554bfb08559ac679
https://doi.org/10.1128/mcb.00013-08
https://doi.org/10.1128/mcb.00013-08
Publikováno v:
Biochemical Journal. 412:347-357
Bax, a pro-apoptotic Bcl-2 family protein, translocates to mitochondria during apoptosis, where it causes MOMP (mitochondrial outer membrane permeabilization). MOMP releases pro-apoptotic factors, such as cytochrome c and SMAC (second mitochondrial a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::689072b349b86774b99d8d2272c5150e
https://doi.org/10.1042/bj20071548
https://doi.org/10.1042/bj20071548
Publikováno v:
Biochemical and Biophysical Research Communications. 365:777-783
Unfolded proteins in the endoplasmic reticulum (ER) cause trans-autophosphorylation of the bifunctional transmembrane kinase IRE1alpha, inducing its RNase activity to splice XBP1 mRNA, in turn triggering a transcriptional program in the unfolded prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd054f3a606cba628c15ebbf1d4b85ce
https://doi.org/10.1016/j.bbrc.2007.11.040
https://doi.org/10.1016/j.bbrc.2007.11.040
Publikováno v:
Cell Death & Differentiation. 14:932-942
The Bcl-2 protein Bax normally resides in the cytosol, but during apoptosis it translocates to mitochondria where it is responsible for releasing apoptogenic factors. Using anoikis as a model, we have shown that Bax translocation does not commit cell
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22a91796e004b4fab1b0408a08515ee6
https://doi.org/10.1038/sj.cdd.4402092
https://doi.org/10.1038/sj.cdd.4402092
Autor:
Noelle E. Huskey, Scott A. Oakes, Lionel Lim, Eric S. Wang, Morgan L. Truitt, John-Paul Upton, Michael T. McManus, Feroz R. Papa, Andrei Goga, Dan Han, Davide Ruggero, Likun Wang
Publikováno v:
Science (New York, N.Y.), vol 338, iss 6108
To Die For The unfolded protein response (UPR) adjusts the protein folding capacity of the endoplasmic reticulum (ER) to match demand. UPR signaling requires IRE1α, an ER transmembrane kinase-endoribonuclease (RNase) that becomes activated by unfold
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::254569fb9325a837c3da6c82f0791b99
https://escholarship.org/uc/item/87q1790v
https://escholarship.org/uc/item/87q1790v
Publikováno v:
Biochemical Journal; 2008, Vol. 412 Issue 2, p347-357, 11p