Results 61 to 70 of about 19,138 (225)

Activation of the IRE1 RNase through remodeling of the kinase front pocket by ATP-competitive ligands

Nature Communications, 2020
The RNase activity of Inositol-Requiring Enzyme 1 (IRE1) can be allosterically regulated by ATP-competitive inhibitors of the IRE1 kinase domain. Here, the authors identify ATP-competitive IRE1 RNase activators with improved selectivity and cellular ...
Elena Ferri, Adrien Le Thomas, Heidi Ackerly Wallweber, Eric S. Day, Benjamin T. Walters, Susan E. Kaufman, Marie-Gabrielle Braun, Kevin R. Clark, Maureen H. Beresini, Kyle Mortara, Yung-Chia A. Chen, Breanna Canter, Wilson Phung, Peter S. Liu, Alfred Lammens, Avi Ashkenazi, Joachim Rudolph, Weiru Wang   +17 more
doaj   +1 more source

RNA sequencing identifies novel regulated IRE1-dependent decay targets that affect multiple myeloma survival and proliferation

Experimental Hematology & Oncology, 2022
Background IRE1 is an unfolded protein response (UPR) sensor with kinase and endonuclease activity. It plays a central role in the endoplasmic reticulum (ER) stress response through unconventional splicing of XBP1 mRNA and regulated IRE1-dependent decay (
Dalia Quwaider, Luis A. Corchete, Marta Martín-Izquierdo, Jesús M. Hernández-Sánchez, Elizabeta A. Rojas, Ignacio J. Cardona-Benavides, Ramón García-Sanz, Ana B. Herrero, Norma C. Gutiérrez   +8 more
doaj   +1 more source

Modulation of Animal Gut Health by Milk Oligosaccharide

Animal Research and One Health, EarlyView.
This review summarizes the composition and structural characteristics of MOs across different mammalian species, and elucidates their roles and mechanisms in maintaining intestinal homeostasis by regulating gut microbiome and enhancing intestinal chemical, physical and immune barriers.
Ningtao Chen, Nana Jing, Shiyu Tao, Mingyue Fei, Wentao Lv, Hua Yang, Yingping Xiao, Haiqin Wu   +7 more
wiley   +1 more source

Mammalian endoplasmic reticulum stress sensor IRE1 signals by dynamic clustering

, 2010
Accumulation of misfolded proteins in the endoplasmic reticulum (ER) triggers the unfolded protein response (UPR), an intracellular signaling pathway that adjusts the protein folding capacity of the ER according to need.
Shannon L. Behrman, Peter Walter, Alexei V. Korennykh, Han Li   +3 more
core   +1 more source

Chemically-induced degradation of the endoplasmic-reticulum stress sensor IRE1 by a VHL-recruiting chimera

Nature Communications
The endoplasmic-reticulum (ER) transmembrane protein IRE1 mitigates ER stress through kinase-endoribonuclease and scaffolding activities. Cancer cells often co-opt IRE1 to facilitate growth.
Jin Du, Elisia Villemure, Matthew Johnson, Caleigh Azumaya, Catarina J. Gaspar, Scot Marsters, David Lawrence, Scott Foster, Alexis Rohou, Tommy K. Cheung, Christopher M. Rose, Thomas Garner, Soo Ro, Kevin Clark, Maureen H. Beresini, Marie-Gabrielle Braun, Joachim Rudolph, Peter Hsu, Avi Ashkenazi   +18 more
doaj   +1 more source

Bridging the Gap Between Human Toxicology and Ecotoxicology Under One Health Perspective by a Cross‐Species Adverse Outcome Pathway Network for Reproductive Toxicity

Environmental Toxicology and Chemistry, EarlyView.
Cross‐species extrapolation of adverse outcome pathway network on reproductive toxicity under the One Health perspective using new approach methodologies. AOP = adverse outcome pathway. Abstract Although ecotoxicological and toxicological risk assessments are performed separately from each other, recent efforts have been made in both disciplines to ...
Elizabeth Dufourcq Sekatcheff, Jaeseong Jeong, Jinhee Choi   +2 more
wiley   +1 more source

Sensor dimer disruption as a new mode of action to block the IRE1-mediated unfolded protein response

Computational and Structural Biotechnology Journal, 2022
The unfolded protein response (UPR) is activated to cope with an accumulation of improperly folded proteins in the Endoplasmic reticulum (ER). The Inositol requiring enzyme 1α (IRE1α) is the most evolutionary conserved transducer of the UPR.
Kosala N. Amarasinghe, Diana Pelizzari-Raymundo, Antonio Carlesso, Eric Chevet, Leif A. Eriksson, Sayyed Jalil Mahdizadeh   +5 more
doaj   +1 more source

Mitochondria-derived oxidative factor activates IRE1.

, 2013
(a) Effects of Tg, antimycin A (AMA), or rotenone on the activation of ER stress sensors. IRE1 were immunoprecipitated before detection by western blottings.
Tomohisa Mori (474320), Tsung-Ping Su (90695), Teruo Hayashi (90690), Eri Hayashi (474321)   +3 more
core   +1 more source

The Effects of Angiotensin Receptor Neprilysin Inhibitor on Endoplasmic Reticulum Stress in Doxorubicin‐Mediated Cardiomyopathy‐Associated Heart Failure Model in Rats

Journal of Applied Toxicology, EarlyView.
ABSTRACT One of the most serious complications associated with the use of the chemotherapeutic agent doxorubicin (DOX) is cardiomyopathy. Although cardioprotective drugs such as angiotensin receptor‐neprilysin inhibitors (ARNI) are used to prevent cardiomyopathy in DOX patients, no studies have reported the relationship between ARNI and endoplasmic ...
Mert Unvan, Meryem İlkay Karagül, Hatice Oruç Demirbağ, Ebru Balli   +3 more
wiley   +1 more source

A nonenzymatic dependency on inositol-requiring enzyme 1 controls cancer cell cycle progression and tumor growth.

PLoS Biology
Endoplasmic-reticulum resident inositol-requiring enzyme 1α (IRE1) supports protein homeostasis via its cytoplasmic kinase-RNase module. Known cancer dependency on IRE1 entails its enzymatic activation of the transcription factor XBP1s and of regulated ...
Iratxe Zuazo-Gaztelu, David Lawrence, Ioanna Oikonomidi, Scot Marsters, Ximo Pechuan-Jorge, Catarina J Gaspar, David Kan, Ehud Segal, Kevin Clark, Maureen Beresini, Marie-Gabrielle Braun, Joachim Rudolph, Zora Modrusan, Meena Choi, Wendy Sandoval, Mike Reichelt, David C DeWitt, Pekka Kujala, Suzanne van Dijk, Judith Klumperman, Avi Ashkenazi   +20 more
doaj   +1 more source