Sort   by:  
 Page size 
MetabolomicsDiallyl disulfide (DADS) ameliorates intestinal Candida albicans infection by modulating the gut microbiota and metabolites and providing intestinal protection in mice
Diallyl disulfide (DADS), a garlic extract also known as allicin, has been reported to have numerous biological activities, including anticancer, antifungal, and inflammation-inhibiting activities, among others. Although many studies have assessed whether DADS can treat Candida albicans infec...
2022-05-03 | MTBLS3750 | MetaboLights
ProteomicsCharacterization of disulfide linkages in proteins by 193 nm ultraviolet photodissociation (UVPD)
Inter-linked disulfide bonds connecting peptide chains are homolytically cleaved with 193 nm ultraviolet photodissociation (UVPD). Analysis of insulin demonstrates the ability for UVPD to cleave multiple disulfide bonds and provide sequence coverage of multiple peptide chains in the same MS/MS event...
ORGANISM(S): Homo Sapiens (human) Gallus Gallus Bos Taurus 
2018-04-28 | PXD009460 | JPOST Repository
TranscriptomicsThe protein disulfide isomerase AGR2 is essential for the production of intestinal mucus
Protein disulfide isomerases (PDIs) aid protein folding and assembly by catalyzing formation and shuffling of cysteine disulfide bonds in the endoplasmic reticulum (ER). Many members of the PDI family are expressed in mammals but the roles of specific PDIs in vivo are poorly understood. A recent hom...
ORGANISM(S): Mus musculus 
2010-05-19 | E-GEOD-12503 | biostudies-arrayexpress
ProteomicsMultiple disulfide-bonded states confer conformational diversity in fibrinogen
Disulfide bonds constrain the polypeptide backbone and reduce conformational variability in proteins. The blood clotting protein fibrinogen is constitutively produced as multiple partially disulfide-bonded states, suggesting that individual fibrinogen molecules have a variety of conformational forms...
ORGANISM(S): Homo sapiens (Human) 
2026-04-13 | PXD076459 | Pride
Human Fibrinogen Disulfide bonds 
ProteomicsComplete sequences of the velvet worm slime proteins reveal that slime formation is enabled by disulfide bonds and intrinsically disordered regions
The slime of velvet worms (Onychophora) is a strong and fully biodegradable protein material, which upon ejection undergoes a fast liquid-to-solid transition to ensnare prey. However, the molecular mechanisms of slime self-assembly are still not well understood, notably because the primary structure...
ORGANISM(S): Cellular Organisms 
2022-09-20 | PXD031722 | JPOST Repository
ProteomicsDetermination of disulfide bridges of human PGAP4 protein
To determine disulfide bonds of human PGAP4 protein
ORGANISM(S): Homo sapiens (Human) 
2018-01-30 | PXD008137 | Pride
Lc-msms Disulfide bridges Pgap4 
ProteomicsPeriostin is a disulfide bonded homodimer and forms a complex with fibronectin in human skin
The protein periostin is a matricellular protein that is expressed in connective tissue. It is composed of five globular domains arranged in an elongated structure with an extensive disordered C-terminal tail. Periostin contains eleven cysteine residues, of which one is unpaired, and the rest forms ...
ORGANISM(S): Homo sapiens (Human) 
2025-01-22 | PXD045285 | Pride
Wound healing Periostin Fibronectin Extracellular matrix 
ProteomicsA Novel Mechanism Mediated by Allosteric Disulfide Bonds Fine-Tunes Thrombus Formation
Mapping of disulfide bonds and quantification of their redox state in the human histidine rich glycoprotein
ORGANISM(S): Homo sapiens (Human) 
2024-04-11 | PXD050718 | Pride
Histidine rich glycoprotein Hrg Disulfide bonds Redox state 
ProteomicsCysteine oxidation and disulfide formation in the ribosomal exit tunnel
Understanding the conformational sampling of translation-arrested ribosome nascent chain complexes is key to understand co-translational folding. Up to now, coupling of cysteine oxidation, disulfide bond formation and structure formation in nascent chains has remained elusive. Here, we investigate t...
ORGANISM(S): Bos taurus (Bovine) Escherichia coli 
2020-11-09 | PXD021574 | Pride
Glutathione Ribosomal exit tunnel Cysterine oxidation Disulfide formation 
ProteomicsLens Disulfide crosslink
Low glutathione levels are associated with crystallin oxidation in age-related nuclear cataract (ARNC). To understand the role of cysteine residue oxidation, we used the novel approach of comparing human cataracts with glutathione-depleted LEGSKO mouse lenses for intra- vs. intermolecular disulfide ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) Mus Musculus (ncbitaxon:10090) 
2016-07-20 | MSV000079952 | MassIVE
Sort   by:  
 Page size