Results 141 to 150 of about 83,408 (297)

The MIA pathway: a key regulator of mitochondrial oxidative protein folding and biogenesis [PDF]

open access: yes, 2015
Mitochondria are fundamental intracellular organelles with key roles in important cellular processes like energy production, Fe/S cluster biogenesis, and homeostasis of lipids and inorganic ions.
Mordas, Amelia, Tokatlidis, Konstantinos
core   +2 more sources

The C-terminal CGHC motif of protein disulfide isomerase supports thrombosis.

open access: yesJournal of Clinical Investigation, 2015
Protein disulfide isomerase (PDI) has two distinct CGHC redox-active sites; however, the contribution of these sites during different physiologic reactions, including thrombosis, is unknown.
Junsong Zhou   +6 more
semanticscholar   +1 more source

Oxidative Stress: Signaling Pathways, Biological Functions, and Disease

open access: yesMedComm, Volume 6, Issue 7, July 2025.
Oxidative stress causes cellular damage across multiple systems, contributing to neurodegeneration (Alzheimer's, Parkinson's, Huntington's), cancer progression and resistance, cardiovascular diseases (atherosclerosis, heart failure), liver and kidney injury, metabolic disorders (diabetes, obesity), autoimmune diseases, musculoskeletal decline, retinal ...
Sixuan Liu   +4 more
wiley   +1 more source

Protein Disulfide Isomerases Control the Secretion of Wnt proteins [PDF]

open access: yes, 2018
SummaryAppropriate Wnt morphogen secretion is required to control animal development and homeostasis. Although correct Wnt globular structure is essential for secretion, proteins that directly mediate Wnt folding and maturation are incompletely characterized.
Torpe, Nanna   +6 more
openaire   +2 more sources

Therapeutic implications of protein disulfide isomerase inhibition in thrombotic disease.

open access: yesArteriosclerosis, Thrombosis and Vascular Biology, 2015
The study of thrombus formation has increasingly applied in vivo tools such as genetically modified mice and intravital microscopy to the evaluation of molecular and cellular mechanisms of thrombosis.
R. Flaumenhaft, B. Furie, J. Zwicker
semanticscholar   +1 more source

Lactate Metabolism and Lactylation Modification: New Opportunities and Challenges in Cardiovascular Disease

open access: yesMedComm, Volume 6, Issue 7, July 2025.
Lactate, beyond a metabolic byproduct, regulates immunity and inflammation, linked to cardiovascular diseases (CVD) via metabolic reprogramming. Lactylation, a lactate‐driven epigenetic mark, modulates gene expression in fibrosis, lipid disorders, and CVD progression.
Mengyang Song   +3 more
wiley   +1 more source

Impaired Cleavage of Preproinsulin Signal Peptide Linked to Autosomal-Dominant Diabetes [PDF]

open access: yes, 2012
Recently, missense mutations upstream of preproinsulin’s signal peptide (SP) cleavage site were reported to cause mutant INS gene-induced diabetes of youth (MIDY).
Arvan, Peter   +8 more
core   +1 more source

Differential activity of rice protein disulfide isomerase family members for disulfide bond formation and reduction

open access: yesFEBS 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

Phase Separation Regulates Metabolism, Mitochondria, and Diseases

open access: yesMedComm, Volume 6, Issue 7, July 2025.
Mitochondrion‐related liquid–liquid phase separation. (1) Phase separation mediates the self‐assembly of mitochondrial nucleoids (mt‐nucleoids). (2) Phase segregation mediates the formation of mitochondrial RNA granules (MRGs). (3) Phase separation mediates the formation of mitochondrial degradosomes.
Chuan Gao   +3 more
wiley   +1 more source

Lack of an efficient endoplasmic reticulum-localized recycling system protects peroxiredoxin IV from hyperoxidation [PDF]

open access: yes, 2014
Typical 2-cys peroxiredoxins are required to remove hydrogen peroxide from several different cellular compartments. Their activity can be regulated by hyperoxidation and consequent inactivation of the active site peroxidatic cysteine.
Bulleid, Neil J.   +2 more
core   +1 more source

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