Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Ciara M Gallagher"'
Autor:
Sandra Elizabeth Torres, Ciara M Gallagher, Lars Plate, Meghna Gupta, Christina R Liem, Xiaoyan Guo, Ruilin Tian, Robert M Stroud, Martin Kampmann, Jonathan S Weissman, Peter Walter
Publikováno v:
eLife, Vol 8 (2019)
The unfolded protein response (UPR) detects and restores deficits in the endoplasmic reticulum (ER) protein folding capacity. Ceapins specifically inhibit the UPR sensor ATF6α, an ER-tethered transcription factor, by retaining it at the ER through a
Externí odkaz:
https://doaj.org/article/1385a79477e045e0a8efc889a4a6ac9d
Autor:
Lars Plate, Christina B Cooley, John J Chen, Ryan J Paxman, Ciara M Gallagher, Franck Madoux, Joseph C Genereux, Wesley Dobbs, Dan Garza, Timothy P Spicer, Louis Scampavia, Steven J Brown, Hugh Rosen, Evan T Powers, Peter Walter, Peter Hodder, R Luke Wiseman, Jeffery W Kelly
Publikováno v:
eLife, Vol 5 (2016)
Imbalances in endoplasmic reticulum (ER) proteostasis are associated with etiologically-diverse degenerative diseases linked to excessive extracellular protein misfolding and aggregation. Reprogramming of the ER proteostasis environment through genet
Externí odkaz:
https://doaj.org/article/42f2f67790644b3da9a9b3bdc96ee5c4
Autor:
Ciara M Gallagher, Peter Walter
Publikováno v:
eLife, Vol 5 (2016)
The membrane-bound transcription factor ATF6α is activated by proteolysis during endoplasmic reticulum (ER) stress. ATF6α target genes encode foldases, chaperones, and lipid biosynthesis enzymes that increase protein-folding capacity in response to
Externí odkaz:
https://doaj.org/article/968730e5d484420484fcde61bc827644
Autor:
Ciara M Gallagher, Carolina Garri, Erica L Cain, Kenny Kean-Hooi Ang, Christopher G Wilson, Steven Chen, Brian R Hearn, Priyadarshini Jaishankar, Andres Aranda-Diaz, Michelle R Arkin, Adam R Renslo, Peter Walter
Publikováno v:
eLife, Vol 5 (2016)
The membrane-bound transcription factor ATF6α plays a cytoprotective role in the unfolded protein response (UPR), required for cells to survive ER stress. Activation of ATF6α promotes cell survival in cancer models. We used cell-based screens to di
Externí odkaz:
https://doaj.org/article/44b158715f4e4880ab40be484472e49b
Autor:
Carmela Sidrauski, Diego Acosta-Alvear, Arkady Khoutorsky, Punitha Vedantham, Brian R Hearn, Han Li, Karine Gamache, Ciara M Gallagher, Kenny K-H Ang, Chris Wilson, Voytek Okreglak, Avi Ashkenazi, Byron Hann, Karim Nader, Michelle R Arkin, Adam R Renslo, Nahum Sonenberg, Peter Walter
Publikováno v:
eLife, Vol 2 (2013)
Phosphorylation of the α-subunit of initiation factor 2 (eIF2) controls protein synthesis by a conserved mechanism. In metazoa, distinct stress conditions activate different eIF2α kinases (PERK, PKR, GCN2, and HRI) that converge on phosphorylating
Externí odkaz:
https://doaj.org/article/8e9e1b8dba294563a7f482f53248b47c
Autor:
Jonathan S. Weissman, Ciara M Gallagher, Xiaoyan Guo, Lars Plate, Meghna Gupta, Christina R. Liem, Sandra Elizabeth Torres, Peter Walter, Robert M. Stroud, Martin Kampmann, Ruilin Tian
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a83d8d6d4bf9e8fde389ad182f5dd04e
https://doi.org/10.7554/elife.46595.022
https://doi.org/10.7554/elife.46595.022
Autor:
Christina R. Liem, Jonathan S. Weissman, Lars Plate, Ruilin Tian, Meghna Gupta, Martin Kampmann, Sandra Elizabeth Torres, Xiaoyan Guo, Ciara M Gallagher, Robert M. Stroud, Peter Walter
Publikováno v:
eLife, Vol 8 (2019)
Torres, Sandra Elizabeth; Gallagher, Ciara M; Plate, Lars; Gupta, Meghna; Liem, Christina R; Guo, Xiaoyan; et al.(2019). Ceapins block the unfolded protein response sensor ATF6α by inducing a neomorphic inter-organelle tether.. eLife, 8. doi: 10.7554/elife.46595. UCSF: Retrieved from: http://www.escholarship.org/uc/item/8d84023q
eLife
Torres, Sandra Elizabeth; Gallagher, Ciara M; Plate, Lars; Gupta, Meghna; Liem, Christina R; Guo, Xiaoyan; et al.(2019). Ceapins block the unfolded protein response sensor ATF6α by inducing a neomorphic inter-organelle tether.. eLife, 8. doi: 10.7554/elife.46595. UCSF: Retrieved from: http://www.escholarship.org/uc/item/8d84023q
eLife
The unfolded protein response (UPR) detects and restores deficits in the endoplasmic reticulum (ER) protein folding capacity. Ceapins specifically inhibit the UPR sensor ATF6α, an ER-tethered transcription factor, by retaining it at the ER through a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba1679c1542d76cfc90ed9b7c0d32548
https://escholarship.org/uc/item/8d84023q
https://escholarship.org/uc/item/8d84023q
Publikováno v:
Journal of Cell Science
Selective autophagy of damaged or redundant organelles is an important mechanism for maintaining cell homeostasis. We found previously that endoplasmic reticulum (ER) stress in the yeast Saccharomyces cerevisiae causes massive ER expansion and trigge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77b9b65024bc07dbc26384c644dc373a
http://europepmc.org/articles/PMC4163648
http://europepmc.org/articles/PMC4163648
Autor:
Brian R. Hearn, Michelle R. Arkin, Andrés Aranda-Díaz, Erica L Cain, Adam R. Renslo, Steven Chen, Priyadarshini Jaishankar, Kenny K. H. Ang, Carolina Garri, Christopher G. Wilson, Ciara M Gallagher, Peter Walter
Publikováno v:
eLife, Vol 5 (2016)
Walter, Peter; Arkin, Michelle; Gallagher, CM; Garri, C; Cain, EL; Ang, KKH; et al.(2016). Ceapins are a new class of unfolded protein response inhibitors, selectively targeting the ATF6α branch. UC San Francisco: Retrieved from: http://www.escholarship.org/uc/item/2cp6b7k0
eLife
Walter, Peter; Arkin, Michelle; Gallagher, CM; Garri, C; Cain, EL; Ang, KKH; et al.(2016). Ceapins are a new class of unfolded protein response inhibitors, selectively targeting the ATF6α branch. UC San Francisco: Retrieved from: http://www.escholarship.org/uc/item/2cp6b7k0
eLife
The membrane-bound transcription factor ATF6α plays a cytoprotective role in the unfolded protein response (UPR), required for cells to survive ER stress. Activation of ATF6α promotes cell survival in cancer models. We used cell-based screens to di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::37cf58f6c26edb03119de96f4e06aa5b
https://doi.org/10.7554/elife.11878
https://doi.org/10.7554/elife.11878
Autor:
Hugh Rosen, Evan T. Powers, Steven J. Brown, Ryan J Paxman, Peter Walter, Lars Plate, John J. Chen, Ciara M Gallagher, Franck Madoux, Wesley Dobbs, Louis Scampavia, Christina B. Cooley, Joseph C. Genereux, Jeffery W. Kelly, R. Luke Wiseman, Timothy P. Spicer, Peter Hodder, Dan Garza
Publikováno v:
eLife, Vol 5 (2016)
eLife, vol 5, iss 2016JULY
Plate, L; Cooley, CB; Chen, JJ; Paxman, RJ; Gallagher, CM; Madoux, F; et al.(2016). Small molecule proteostasis regulators that reprogram the ER to reduce extracellular protein aggregation. eLife, 5(2016JULY). doi: 10.7554/eLife.15550. UC Riverside: Retrieved from: http://www.escholarship.org/uc/item/6dt069qj
eLife
eLife, vol 5, iss 2016JULY
Plate, L; Cooley, CB; Chen, JJ; Paxman, RJ; Gallagher, CM; Madoux, F; et al.(2016). Small molecule proteostasis regulators that reprogram the ER to reduce extracellular protein aggregation. eLife, 5(2016JULY). doi: 10.7554/eLife.15550. UC Riverside: Retrieved from: http://www.escholarship.org/uc/item/6dt069qj
eLife
Imbalances in endoplasmic reticulum (ER) proteostasis are associated with etiologically-diverse degenerative diseases linked to excessive extracellular protein misfolding and aggregation. Reprogramming of the ER proteostasis environment through genet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b42133e79e8a3f18ac8f641a246df7f8
https://elifesciences.org/articles/15550
https://elifesciences.org/articles/15550