Results 1 to 10 of about 1,858 (50)

A small molecule UPR modulator for diabetes identified by high throughput screening

open access: yesActa Pharmaceutica Sinica B, 2021
Unfolded protein response (UPR) is a stress response that is specific to the endoplasmic reticulum (ER). UPR is activated upon accumulation of unfolded (or misfolded) proteins in the ER's lumen to restore protein folding capacity by increasing the ...
Valeria Marrocco   +15 more
doaj   +1 more source

ROS and Endoplasmic Reticulum Stress in Pulmonary Disease

open access: yesFrontiers in Pharmacology, 2022
Pulmonary diseases are main causes of morbidity and mortality worldwide. Current studies show that though specific pulmonary diseases and correlative lung-metabolic deviance own unique pathophysiology and clinical manifestations, they always tend to ...
Xiangning Cui   +3 more
doaj   +1 more source

Insights Into the Role of Endoplasmic Reticulum Stress in Infectious Diseases

open access: yesFrontiers in Immunology, 2020
The endoplasmic reticulum (ER) is the major organelle in the cell for protein folding and plays an important role in cellular functions. The unfolded protein response (UPR) is activated in response to misfolded or unfolded protein accumulation in the ER.
Ji-Ae Choi   +5 more
doaj   +1 more source

Crosstalk Between ER Stress, Autophagy and Inflammation

open access: yesFrontiers in Medicine, 2021
The endoplasmic reticulum (ER) is not only responsible for protein synthesis and folding but also plays a critical role in sensing cellular stress and maintaining cellular homeostasis.
Sandhya Chipurupalli   +2 more
doaj   +1 more source

The Unfolded Protein Response: An Overview

open access: yesBiology, 2021
The unfolded protein response is the mechanism by which cells control endoplasmic reticulum (ER) protein homeostasis. Under normal conditions, the UPR is not activated; however, under certain stresses, such as hypoxia or altered glycosylation, the UPR ...
Adam Read, Martin Schröder
doaj   +1 more source

The unfolded protein response reverses the effects of glucose on lifespan in chemically-sterilized C. elegans

open access: yesNature Communications, 2022
Endoplasmic reticulum stress activates the unfolded protein response (UPR). The authors show that glucose extends the lifespan of aged animals by activating the otherwise quiescent UPR while causing a UPR-dependent reduced longevity in young ...
Caroline Beaudoin-Chabot   +9 more
doaj   +1 more source

Gcn4p and novel upstream activating sequences regulate targets of the unfolded protein response. [PDF]

open access: yesPLoS Biology, 2004
Eukaryotic cells respond to accumulation of unfolded proteins in the endoplasmic reticulum (ER) by activating the unfolded protein response (UPR), a signal transduction pathway that communicates between the ER and the nucleus.
Christopher K Patil   +2 more
doaj   +1 more source

The Protective Effect of a Newly Developed Molecular Chaperone– Inducer Against Mouse Ischemic Acute Kidney Injury

open access: yesJournal of Pharmacological Sciences, 2009
Activation of the unfolded protein response (UPR) has been suggested to attenuate renal ischemia-reperfusion (I/R) injury. We recently found a compound, namely BIX, that activated the UPR selectively through the activating transcription factor 6 pathway.
Worapat Prachasilchai   +6 more
doaj   +1 more source

Endoplasmic reticulum stress and liver diseases

open access: yesLiver Research, 2019
Endoplasmic reticulum (ER) stress occurs when ER homeostasis is perturbed with accumulation of unfolded/misfolded protein or calcium depletion. The unfolded protein response (UPR), comprising of inositol-requiring enzyme 1α (IRE1α), double-stranded RNA ...
Xiaoying Liu, Richard M. Green
doaj   +1 more source

Long-chain ceramides are cell non-autonomous signals linking lipotoxicity to endoplasmic reticulum stress in skeletal muscle

open access: yesNature Communications, 2022
Endoplasmic Reticulum stress induces cell non-autonomous Unfolded Protein Response (UPR) activation. Here the authors show that long-chain ceramides are secreted from muscle cells in extracellular vesicles and induce cell non-autonomous UPR activation in
Ben D. McNally   +15 more
doaj   +1 more source

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