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ProteomicsIdentification of sulfenylation patterns in Plasmodium falciparum using a non-dimedone based probe
Plasmodium falciparum causes the deadliest form of malaria. Adequate redox control is crucial for this protozoan parasite to overcome oxidative and nitrosative challenges, thus enabling its survival. Sulfenylation is an oxidative post-translational modification, which acts as a molecular on/off swit...
ORGANISM(S): Plasmodium Falciparum (ncbitaxon:5833) 
MSV000086125 | MassIVE
UnknownProteomic analysis of peptides tagged with dimedone and related probes.
Not available
S-EPMC4070747 | biostudies-literature
ProteomicsMass spectrometric analyses for the C281-dimedone adduct and the sulfinylated peptide fragments of Orf1
Oxidized cysteine residues are highly reactive and can form functional covalent conjugates, of which the allosteric redox switch formed by the lysine-cysteine NOS bridge is an example. Here, we report a non-canonical FAD-dependent enzyme Orf1 that adds a glycine-derived N-formimidoyl group to glycin...
ORGANISM(S): Escherichia coli 
2023-05-10 | PXD041104 | Pride
N-formimmidolation and iminoacetylation enzyme 
UnknownIdentification of sulfenylation patterns in trophozoite stage Plasmodium falciparum using a non-dimedone based probe.
Not available
S-EPMC8218313 | biostudies-literature
ProteomicsPersulfidome of A549 alveolar epithelial cells
To better define the relationship between persulfidation and the cellular antifungal response, we analyzed the cellular persulfidome (proteome of persulfidated proteins) in A549 and in CTH-/- cells upon challenge with Aspergillus fumigatus conidia and/or the sulfide donor GYY4137. All proteins were ...
ORGANISM(S): Homo sapiens (Human) 
2026-08-17 | PXD076106 | Pride
Aspergillus fumigatus A549 persulfidome Gyy4137 persulfidome Cth-/- 
ProteomicsMass spectrometric analyses of the oxidation state of Cys281 in peptide fragment.
Oxidized cysteine residues are highly reactive and can form functional covalent conjugates, of which the allosteric redox switch formed by the lysine-cysteine NOS bridge is an example. Here, we report a non-canonical FAD-dependent enzyme Orf1 that adds a glycine-derived N-formimidoyl group to glycin...
ORGANISM(S): Escherichia coli 
2023-05-10 | PXD041105 | Pride
N-formimmidolation and iminoacetylation enzyme 
ProteomicsMetabolic dysfunction-associated steatohepatitis reduces hepatic H2S- producing enzymes altering persulfidome composition
Metabolic dysfunction–associated steatohepatitis (MASH) is a progressive disease driven byobesity-related hepatic inflammation and oxidative stress. Recently, cysteine persulfidation (PSSH), a protective post-translational modification by hydrogen sulfide (H2S), was established to play a role in red...
ORGANISM(S): Mus musculus (Mouse) 
2025-09-15 | PXD066952 | Pride
Persulfidome Obesity Mash 
UnknownHeme-thiolate sulfenylation of human cytochrome P450 4A11 functions as a redox switch for catalytic inhibition.
Not available
S-EPMC5500791 | biostudies-literature
ProteomicsLower H2S-generating enzyme levels and persulfidation-mediated protein protection characterize metabolic dysfunction-associated steatohepatitis
Metabolic dysfunction–associated steatohepatitis (MASH), marked by hepatic steatosis and inflammation, is a major risk for cirrhosis and liver cancer. Obesity-induced oxidative stress plays a central role in MASH promoting protein damage and dysfunction. Cysteine persulfidation (PSSH), a post-transl...
ORGANISM(S): Mus musculus (Mouse) 
2025-08-04 | PXD057932 | Pride
Phosphoproteomics Cxcr4 oligomerization Apoptosis Lc-ms/ms 
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 
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