Results 121 to 130 of about 3,418,558 (223)
FEBS Open Bio, 2014 Protein disulfide isomerases (PDIs), a family of thiol-disulfide oxidoreductases that are ubiquitous in all eukaryotes, are the principal catalysts for disulfide bond formation. Here, we investigated three rice (Oryza sativa) PDI family members (PDIL1;1,
Yayoi Onda, Yohei Kobori
doaj +1 more source
Recent Advances in Food Allergens and Emerging Biosensing Technologies
Comprehensive Reviews in Food Science and Food Safety, Volume 25, Issue 5, September 2026.ABSTRACT Food allergies have become a worldwide public health issue, highlighting the critical need for rapid, sensitive, and field‐deployable detection strategies. While traditional detection methods offer high accuracy, their high cost, operational complexity, and lengthy analysis time limit their applicability for rapid screening purposes.
Maojie Hu +6 more
wiley +1 more source
The multidrug resistance IncA/C transferable plasmid encodes a novel domain swapped dimeric protein disulfide isomerase [PDF]
, 2013 Background: Bacterial IncA/C plasmids distribute antibiotic resistance genes and encode a conserved thioredoxin-fold protein (DsbP). Results: DsbP shuffles incorrect disulfide bonds in misfolded proteins, and its structure diverges from previously ...
Neyer, Simon +7 more
core +1 more source
The FEBS Journal, Volume 293, Issue 18, Page 5585-5599, September 2026.Proteostasis ensures proper protein folding, modification, and degradation, while its impairment triggers ER stress. Chronic ER stress and maladaptive UPR via the CHOP–ERO1 axis remodel ERMCs, altering calcium signaling and mitochondrial metabolism.
Giorgia Maria Renna +5 more
wiley +1 more source
Protein disulfide isomerase mediates integrin-dependent adhesion [PDF]
, 2000 Cell adhesion is mediated by the integrin adhesion receptors. Receptor–ligand interaction involves conformational changes in the receptor, but the underlying mechanism remains unclear.
Hess, O. +9 more
core +1 more source
Emerging roles of protein disulfide isomerase in cancer
BMB Reports, 2017 The protein disulfide isomerase (PDI) family is a group of multifunctional endoplasmic reticulum (ER) enzymes that mediate the formation of disulfide bonds, catalyze the cysteine-based redox reactions and assist the quality control of client proteins. Recent structural and functional studies have demonstrated that PDI members not only play an essential
Lee, Eunyoug, Lee, Do Hee
openaire +3 more sources
Biogenesis of TNF‐α‐insights into proteostasis and inflammation
The FEBS Journal, Volume 293, Issue 18, Page 5645-5663, September 2026.TNF‐α biogenesis, trafficking, and signalling are tightly and reciprocally coupled to cellular proteostasis systems, including ER chaperones and endoplasmic reticulum‐associated degradation. This bidirectional crosstalk determines whether TNF‐α responses are adaptive or proteotoxic.
Bailasan Haidar +3 more
wiley +1 more source
Ubiquitin and ubiquitin‐like modifications in the endoplasmic reticulum stress response
The FEBS Journal, Volume 293, Issue 18, Page 5481-5513, September 2026.Endoplasmic reticulum (ER) stress activates various proteostasis control processes, including the unfolded protein response, ribosome‐associated quality control, and ER‐associated degradation. Ubiquitin and ubiquitin‐like modifications dynamically regulate these processes to determine cell fate, promoting adaptation or inducing cell death.
Tony Avril +2 more
wiley +1 more source
Dual IRE1 targets: Determinants of the cell fate?
The FEBS Journal, Volume 293, Issue 18, Page 5423-5432, September 2026.IRE1 is an ER stress sensor that restores protein homeostasis through two signaling activities: XBP1s, which upregulates its target gene expression or RIDD which downregulates its target transcripts. We recently identified Dual IRE1 Targets (DIT) which are modulated by both XBP1s and RIDD activities.
Eva Billat +3 more
wiley +1 more source
Combating ageing beyond the cell: Emerging roles of extracellular proteostasis
The FEBS Journal, Volume 293, Issue 18, Page 5558-5584, September 2026.Ageing challenges the body's ability to maintain a stable and functional proteome, leading to protein damage and aggregation both inside and outside cells. This review focuses on the less well understood mechanisms of extracellular protein quality control and how they become disrupted in ageing, particularly in neurodegenerative diseases.
Siddharth R. Venkatesh +7 more
wiley +1 more source