Results 11 to 20 of about 167,289 (308)
IRE1 phosphatase PP2Ce regulates adaptive ER stress response in the postpartum mammary gland. [PDF]
We recently reported that the PPM1l gene encodes an endoplasmic reticulum (ER) membrane targeted protein phosphatase (named PP2Ce) with highly specific activity towards Inositol-requiring protein-1 (IRE1) and regulates the functional outcome of ER stress.
Lane, Timothy F +6 more
core +9 more sources
IRE1β negatively regulates IRE1α signaling in response to endoplasmic reticulum stress [PDF]
IRE1β is an ER stress sensor uniquely expressed in epithelial cells lining mucosal surfaces. Here, we show that intestinal epithelial cells expressing IRE1β have an attenuated unfolded protein response to ER stress.
Acosta-Alvear +54 more
core +1 more source
An unfolded protein-induced conformational switch activates mammalian IRE1. [PDF]
The unfolded protein response (UPR) adjusts the cell's protein folding capacity in the endoplasmic reticulum (ER) according to need. IRE1 is the most conserved UPR sensor in eukaryotic cells.
Acosta-Alvear, Diego +5 more
core +3 more sources
UPR Signal Activation by Luminal Sensor Domains [PDF]
The unfolded protein response (UPR) is a cell-signaling system that detects the accumulation of unfolded protein within the endoplasmic reticulum (ER) and initiates a number of cellular responses to restore ER homeostasis.
Ali, Maruf +2 more
core +1 more source
Gcn4p and novel upstream activating sequences regulate targets of the unfolded protein response. [PDF]
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.
Li, Hao +2 more
core +4 more sources
Mitochondria Retrograde Signaling and the UPR mt: Where Are We in Mammals? [PDF]
Mitochondrial unfolded protein response is a form of retrograde signaling that contributes to ensuring the maintenance of quality control of mitochondria, allowing functional integrity of the mitochondrial proteome. When misfolded proteins or unassembled
Arnould, T., Michel, S., Renard, P.
core +3 more sources
Wolfram Syndrome protein, Miner1, regulates sulphydryl redox status, the unfolded protein response, and Ca2+ homeostasis. [PDF]
Miner1 is a redox-active 2Fe2S cluster protein. Mutations in Miner1 result in Wolfram Syndrome, a metabolic disease associated with diabetes, blindness, deafness, and a shortened lifespan.
Andreyev, Alexander Y +12 more
core +1 more source
Eukaryotic cells possess a variety of signaling pathways that prevent accumulation of unfolded and misfolded proteins. Chief among these is the heat shock response (HSR), which is assumed to respond to unfolded proteins in the cytosol and nucleus alike ...
Yusuke Miyazaki +4 more
doaj +1 more source
Background Multiple myeloma, a malignancy of the antibody-secreting plasma cells, remains incurable by current therapy. However, the proteasome inhibitor bortezomib and other new drugs are revolutionizing its treatment.
Silvia C. W. Ling +11 more
doaj +1 more source
Tidy up - The unfolded protein response in sepsis
Pathogens, their toxic byproducts, and the subsequent immune reaction exert different forms of stress and damage to the tissue of the infected host. This stress can trigger specific transcriptional and post-transcriptional programs that have evolved to ...
Wolfgang Vivas +5 more
doaj +1 more source

