Ceapins are a new class of unfolded protein response inhibitors, selectively targeting the ATF6α branch
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 discover and develop Ceapins, a class of pyrazole amid...
Main Authors: | 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 |
---|---|
Format: | Article |
Language: | English |
Published: |
eLife Sciences Publications Ltd
2016-07-01
|
Series: | eLife |
Subjects: | |
Online Access: | https://elifesciences.org/articles/11878 |
Similar Items
-
Ceapins inhibit ATF6α signaling by selectively preventing transport of ATF6α to the Golgi apparatus during ER stress
by: Ciara M Gallagher, et al.
Published: (2016-07-01) -
Ceapins block the unfolded protein response sensor ATF6α by inducing a neomorphic inter-organelle tether
by: Sandra Elizabeth Torres, et al.
Published: (2019-05-01) -
Establishment and validation of an endoplasmic reticulum stress reporter to monitor zebrafish ATF6 activity in development and disease
by: Eric M. Clark, et al.
Published: (2020-01-01) -
A lifetime of stress: ATF6 in development and homeostasis
by: Robert F. Hillary, et al.
Published: (2018-05-01) -
A novel role of ER stress signal transducer ATF6 in regulating enterovirus A71 viral protein stability
by: Jia-Rong Jheng, et al.
Published: (2018-01-01)