Results 151 to 160 of about 15,652 (205)

QM/MM Free Energy Calculations of IRE1 Reveal a Unique Protonation State of the Catalytic Lys599. [PDF]

open access: yesJ Comput Chem
Carlesso A   +5 more
europepmc   +1 more source

Enhancing Yeast Surface Display: UPR, ERAD, and ER Dynamics in Recombinant Protein Production. [PDF]

open access: yesFood Technol Biotechnol
Martinić Cezar T   +5 more
europepmc   +1 more source

FGF1 orchestrates circadian hepatic triglyceride secretion. [PDF]

open access: yesNat Commun
Sermikli BP   +17 more
europepmc   +1 more source

Pyrazolylpyrimidinamines Decorated via Petasis Reaction as Small-Molecule Activators of the RNA-Degrading Ribonuclease IRE1α. [PDF]

open access: yesACS Bio Med Chem Au
Avathan Veettil AK   +7 more
europepmc   +1 more source

Assays to Study IRE1 Activation and Signaling

2022
The endoplasmic reticulum (ER) stress sensor IRE1 is a a major player of the unfolded protein response (UPR), the main pathway driving adaptation processes to restore proteostasis.  In addition, overactivation of IRE1 signaling contributes to a variety of pathologies including diabetes, neurodegenerative diseases, and cancer. Under ER stress, IRE1 auto-
Paloma, Moraga   +3 more
openaire   +2 more sources

Structural and molecular bases to IRE1 activity modulation

Biochemical Journal, 2021
The Unfolded Protein response is an adaptive pathway triggered upon alteration of endoplasmic reticulum (ER) homeostasis. It is transduced by three major ER stress sensors, among which the Inositol Requiring Enzyme 1 (IRE1) is the most evolutionarily conserved.
Timothy Langlais   +7 more
openaire   +2 more sources

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