Quercetin Affects Hsp70/IRE1α Mediated Protection from Death Induced by Endoplasmic Reticulum Stress
Relative to their normal counterparts, tumor cells generally exhibit a greater “stress phenotype” and express heat shock proteins (Hsp) that represent candidate targets for anticancer therapy. Here we investigated the role of Hsp70 in survival induced by endoplasmic reticulum (ER) stressors in human...
Main Authors: | Antonello Storniolo, Marisa Raciti, Alessandra Cucina, Mariano Bizzarri, Livia Di Renzo |
---|---|
Format: | Article |
Language: | English |
Published: |
Hindawi Limited
2015-01-01
|
Series: | Oxidative Medicine and Cellular Longevity |
Online Access: | http://dx.doi.org/10.1155/2015/645157 |
Similar Items
-
IRE1α Implications in Endoplasmic Reticulum Stress-Mediated Development and Pathogenesis of Autoimmune Diseases
by: Raghu Patil Junjappa, et al.
Published: (2018-06-01) -
CHIP, a carboxy terminus HSP-70 interacting protein, prevents cell death induced by endoplasmic reticulum stress in the central nervous system
by: Felipe eCabral Miranda, et al.
Published: (2015-01-01) -
Endoplasmic Reticulum Stress Sensor IRE1α Enhances IL-23 Expression by Human Dendritic Cells
by: Saioa Márquez, et al.
Published: (2017-06-01) -
Endoplasmic Reticulum Lumenal Indicators in Drosophila Reveal Effects of HSP-Related Mutations on Endoplasmic Reticulum Calcium Dynamics
by: Megan K. Oliva, et al.
Published: (2020-08-01) -
IRES-dependent translational control during virus-induced endoplasmic reticulum stress and apoptosis
by: Paul eHanson, et al.
Published: (2012-03-01)