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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 
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
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
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
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 
ProteomicsA-to-I mRNA editing controls disulfide bond formation and the toxicity of the HokB toxin in bacteria
Protein disulfide bonds between cysteine residues serve a prominent role in bacterial protein function, virulence, and viability. Adenosine-to-inosine (A-to-I) mRNA editing changes the genetic information at the RNA level. Previously, we discovered that A-to-I mRNA editing occurs in bacteria (Escher...
ORGANISM(S): Escherichia coli 
2025-07-14 | PXD051162 | Pride
Tada Adenosine-to-inosine rna editing Toxin-antitoxin Disulfide bond Hokb Bacteria Dsba 
ProteomicsMS analysis of an FGE-PDI complex
Multiple Sulfatase Deficiency (MSD) is a fatal, inherited lysosomal storage disorder characterised by reduced activities of all cellular sulfatases in patients. Sulfatases require a unique post-translational modification of an active site cysteine to formylglycine that is catalysed by the Formylglyc...
ORGANISM(S): Homo sapiens (Human) 
2018-07-04 | PXD009758 | Pride
Pdi Multiple sulfatase deficiency Fge 
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
ProteomicsDisulfide bonds are critical for stabilizing cell division, cell envelope biogenesis, and antibiotic resistance proteins in mycobacteria
Mycobacterium, including Mycobacterium tuberculosis, the etiological agent of tuberculosis, have a unique cell envelope critical for their survival and antibacterial resistance. The cell envelope's assembly and maintenance influence permeability, making it a key target against multidrug resistant st...
ORGANISM(S): Mycobacterium Smegmatis Str. Mc2 155 (ncbitaxon:246196) 
2025-01-16 | MSV000096877 | MassIVE
UnknownAC81 Is a Putative Disulfide Isomerase Involved in Baculoviral Disulfide Bond Formation.
Not available
S-EPMC9769380 | biostudies-literature
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