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TranscriptomicsLoss of subcellular lipid transport due to ARV1 deficiency disrupts organelle homeostasis and activates the unfolded protein response
The ARV1-encoded protein mediates sterol transport from the endoplasmic reticulum (ER) to the plasma membrane. Yeast ARV1 mutants accumulate multiple lipids in the ER and are sensitive to pharmacological modulators of both sterol and sphingolipid metabolism. Using fluorescent and electron microscopy...
ORGANISM(S): Saccharomyces cerevisiae 
2011-02-17 | E-GEOD-26801 | biostudies-arrayexpress
TranscriptomicsThe unfolded protein response in fission yeast modulates stability of select mRNAs to maintain protein homeostasis
Homeostatic control mechanisms are essentil to life. One such mechanism, the unfolded protein response (UPR) operates in all eukarytic cells to adjust protein folding capacity of the endoplasmic reticulum (ER) according to need. UPR induction in all eurkarytic cells to date involves Ire1 (kinase/end...
ORGANISM(S): Schizosaccharomyces pombe 
2012-11-21 | E-GEOD-40298 | biostudies-arrayexpress
Proteomics5'UTR-mediated retention of eIF3 on 80S ribosomes promotes co-translational folding of ER membrane proteins
Co-translational folding of nascent polypeptides is essential for protein function and cellular homeostasis. Ribosome-associated chaperones assist in this process, but coordination between their recruitment and translation initiation remains poorly understood. We report here that specific binding si...
ORGANISM(S): Homo sapiens (Human) 
2025-10-27 | PXD059488 | Pride
UnknownInhibition of fatty acid oxidation enhances oxidative protein folding and protects hepatocytes from endoplasmic reticulum stress.
Not available
S-EPMC3290641 | biostudies-literature
TranscriptomicsTranslational profiling in the unfolded protein response
The unfolded protein response (UPR) couples cellular translation rates and gene expression to the protein folding status of the endoplasmic reticulum (ER). Upon activation, the UPR machinery elicits a general suppression of protein synthesis and activation of stress gene expression, which act coordi...
ORGANISM(S): Mus musculus 
2014-08-28 | E-GEOD-53743 | biostudies-arrayexpress
Unknown24(S)-Hydroxycholesterol induces ER dysfunction-mediated unconventional cell death.
Not available
S-EPMC6611791 | biostudies-literature
MetabolomicsER stress inhibits liver fatty acid oxidation while unmitigated stress leads to anorexia-induced lipolysis and both liver and kidney steatosis
The unfolded protein response (UPR), induced by endoplasmic reticulum (ER) stress, regulates the expression of factors that restore protein folding homeostasis. However, in the liver and kidney, ER stress also leads to lipid accumulation, accompanied at least in the liver by transcriptional suppress...
2017-06-23 | MTBLS472 | MetaboLights
TranscriptomicsBalancing Protein Folding and Disulfide Bond Formation Rates is Key to Mitigating Secretory Stress
The protein secretory pathway must maintain homoeostasis while producing a wide assortment of proteins in different conditions. It is also used extensively to produce many useful proteins in biotechnology. As such, secretory pathway dysfunction can be highly detrimental to the cell, resulting in ...
ORGANISM(S): Saccharomyces cerevisiae 
2011-12-01 | E-GEOD-27062 | biostudies-arrayexpress
TranscriptomicsSmall molecule-mediated ERO1A inhibition in restraining aggressive breast cancer
Cancer cells adapt to harsh environmental conditions by inducing the Unfolded Protein Response (UPR), of which ERO1A is one of the mediators. ERO1A aids protein folding by acting as a protein disulfide oxidase, and under cancer-related hypoxia conditions, it favors the folding of angiogenic VEGFA, l...
ORGANISM(S): Mus musculus 
2025-02-12 | E-MTAB-14269 | biostudies-arrayexpress
UnknownMost F508del-CFTR is targeted to degradation at an early folding checkpoint and independently of calnexin.
Not available
S-EPMC1140594 | biostudies-literature
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