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ProteomicsPDI-catalyzed oxidative protein folding mediates senescence by induction of ER-derived oxidative stress
Protein homeostasis is linked with aging and aging associated diseases. Oxidative protein folding occurs in the endoplasmic reticulum (ER) and produces H2O2 as a byproduct. The role of oxidative protein folding in human stem cells aging remains unknown. Here, we succeed to knockout protein disulfide...
ORGANISM(S): Homo sapiens (Human) 
2023-06-12 | PXD037244 | Pride
Human mesenchymal stem cells (hmscs)  hydrogen peroxide (h2o2)  oxidative 29 protein folding  protein disulfide isomerase (pdi)  senescence 
TranscriptomicsChromatin structure changes upon oxidative stress or UV irradiation in the yeast Saccharomyces cerevisiae
Development of molecular approaches based on chromosome conformation capture (3C) technology such as Hi-C, combined with methods for modeling and interpreting chromatin interaction data, have revolutionized the analysis of chromosome folding. Even if the impact of chromatin structure on gene express...
ORGANISM(S): Saccharomyces cerevisiae 
2020-12-20 | E-MTAB-5825 | biostudies-arrayexpress
TranscriptomicsRole of thioredoxin reductase in the Yap1p-dependent response to oxidative stress
The Saccharomyces cerevisiae Yap1p transcription factor is required for the H2O2-dependent activation of many antioxidant genes including the TRX2 gene encoding thioredoxin 2. To identify factors that regulate Yap1p activity, we carried out a genetic screen for mutants that show elevated expression ...
ORGANISM(S): Saccharomyces cerevisiae 
2005-07-22 | E-GEOD-2977 | biostudies-arrayexpress
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
ProteomicsS-Sulfenylation regulates non-enzymatic oxidative protein folding
The post-translational modification S-Sulfenylation functions as a key sensor of oxidative stress yet the dynamics of sulfenic acids in proteins is largely elusive due to it's fleeting nature. LC-MS/MS analysis has detected the evolution of this modification in oxidative and reducing states.
ORGANISM(S): Homo sapiens (Human) 
2016-12-23 | PXD004514 | Pride
Lc-ms/ms Post-translational modifications Human titin 
UnknownOxidative folding pathway of onconase, a ribonuclease homologue: insight into oxidative folding mechanisms from a study of two homologues.
Not available
S-EPMC2717042 | biostudies-literature
UnknownBeyond Folding Enzymes: A Redox-Active "Solid Chaperone" Unlocks Recyclable, HPLC-Free Oxidative Protein Folding.
Not available
S-EPMC12933366 | biostudies-literature
UnknownHarnessing selenocysteine reactivity for oxidative protein folding.
Not available
S-EPMC5514408 | biostudies-literature
UnknownNucleation of a key beta-turn promotes cyclotide oxidative folding.
Not available
S-EPMC10999817 | biostudies-literature
UnknownA quantitative interpretation of oxidative protein folding activity in Escherichia coli.
Not available
S-EPMC9773447 | biostudies-literature
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