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ProteomicsIdentification of intramolecular disulfide bonds in GrxS12
To investigate whether the conserved Cys residues of Grxs form intramolecular or intermolecular disulfide bonds, the recombinant GrxS12 proteins were purified, and subsequently separated using non-reducing SDS-PAGE. The gel revealed the presence of a monomer band but not a dimer band, indicating the...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2026-01-16 | PXD058877 | Pride
Grxs12 Identification Intramolecular disulfide bond 
ProteomicsAnalysis of reduction capability of GrxS12 on SufB and its cysteine residues
To elucidate the reduction of GrxS12 on SufB, an in vitro reducing system was utilized. The mass spectrometry analysis of the GrxS12-reduced SufB samples identified and quantified a large number of SufB peptides containing a total of eight Cys residues. The Cys-containing peptides of SufB exhibited ...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2026-01-16 | PXD058901 | Pride
Grxs12 Sufb Reduction of cysteine residue 
ProteomicsQuantification of the percentage of oxidized cysteine thiols in GrxS12 under normal and H2O2 treatments.
To evaluate the percentage of oxidized cysteine thiols, the GrxS12 proteins underwent either with or without H2O2 treatment were alkylated by iodoacetamide (IAM), reduced with DTT, and subsequently the newly generated free Cys were alkylated with N-ethylmaleimide (NEM). The spectrometric analysis of...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2026-01-16 | PXD059065 | Pride
Grxs12 H2o2 Oxidized cysteine thiols Quantification 
ProteomicsRedox proteomics analysis of Arabidopsis wild type and grxs12 mutants
For an overall evaluation of the protein redox status in grxs12 leaves, the iodoTMT-based redox proteomics approach was employed. After protein extraction, the free thiols in Cys were NEM-blocked, and then the Cys thiols with reversible oxidations such as sulfenic acids (-SOH), S-glutathionylation (...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2026-01-16 | PXD059068 | Pride
Arabidopsis Redox proteomics Grxs12 mutants Iodotmt label 
UnknownStructure-function relationship of the chloroplastic glutaredoxin S12 with an atypical WCSYS active site.
Not available
S-EPMC2666582 | biostudies-literature
UnknownArabidopsis chloroplastic glutaredoxin C5 as a model to explore molecular determinants for iron-sulfur cluster binding into glutaredoxins.
Not available
S-EPMC3149344 | biostudies-literature
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