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TranscriptomicsRole of thioredoxin reductase in the Yap1p-dependent response to oxidative stress
The Saccharomyces cerevisiae Yap1p transcription factor is required for the H2O2-dependent activation of many antioxidant genes including the TRX2 gene encoding thioredoxin 2. To identify factors that regulate Yap1p activity, we carried out a genetic screen for mutants that show elevated expression ...
ORGANISM(S): Saccharomyces cerevisiae 
2005-07-22 | E-GEOD-2977 | biostudies-arrayexpress
TranscriptomicsTranscription profiling of mutations in the yeast TRR1 gene encoding thioredoxin reductase
The Saccharomyces cerevisiae Yap1p transcription factor is required for the H2O2-dependent activation of many antioxidant genes including the TRX2 gene encoding thioredoxin 2. To identify factors that regulate Yap1p activity, we carried out a genetic screen for mutants that show elevated expression ...
ORGANISM(S): Saccharomyces cerevisiae 
2005-06-30 | E-SMDB-2716 | biostudies-arrayexpress
ProteomicsIdentification of thioredoxin targets in Chlamydomonas reinhardtii using an affinity purification approach
Thiol-based redox post-translational modifications have emerged as important mechanisms of signaling and regulation in all organisms. In this context, the small ubiquitous oxido-reductase thioredoxin plays a key role by controlling the thiol-disulfide status of target proteins. Recent redox proteomi...
ORGANISM(S): Chlamydomonas reinhardtii 
2017-07-28 | PXD006097 | Pride
Chlamydomonas reinhardtii Redox proteomics Disulfide bonds Thioredoxin targets Redox regulation 
TranscriptomicsRetrotransposon Ty1 integration targets specifically positioned asymmetric nucleosomal DNA segments in tRNA hotspots
Using a TIP-seq protocol (specifically isolating transposon insertion junctions) we determined that the Ty1 retrotransposon targets tRNA genes and, in particular, we determined that the transposon inserts into nucleosomal DNA in an asymmetric pattern. TIP-seq recovery of transposon insertion junctio...
ORGANISM(S): Saccharomyces cerevisiae 
2012-01-01 | E-GEOD-33986 | biostudies-arrayexpress
UnknownNew thioredoxin targets in the unicellular photosynthetic eukaryote Chlamydomonas reinhardtii.
Not available
S-EPMC409943 | biostudies-literature
OtherIdentification of targets of the protein disulfide reductase thioredoxin
Identification of targets of the protein disulfide reductase thioredoxin using liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS) and thiol specific differential labeling with isotope-coded affinity tags (ICAT). Reduction of specific target disulfides is quantified by measuring rat...
ORGANISM(S): Hordeum vulgare 
2008-11-20 | GSE11650 | GEO
ProteomicsIdentification of thioredoxin-dependent regulatory cysteines in Chlamydomonas reinhardtii using the reductome approach.
Thiol-based redox post-translational modifications have emerged as important mechanisms of signaling and regulation in all organisms. In this context, the small ubiquitous oxido-reductase thioredoxin (Trx) plays a key role by controlling the thiol-disulfide status of target proteins. Recent redox pr...
ORGANISM(S): Chlamydomonas reinhardtii 
2017-07-28 | PXD006116 | Pride
Isotope-coded affinity tag Chlamydomonas reinhardtii Redox proteomics Disulfide bonds Thioredoxin targets Redox regulation 
TranscriptomicsRole of thioredoxin reductase in the Yap1p-dependent response to oxidative stress
The Saccharomyces cerevisiae Yap1p transcription factor is required for the H2O2-dependent activation of many antioxidant genes including the TRX2 gene encoding thioredoxin 2. To identify factors that regulate Yap1p activity, we carried out a genetic screen for mutants that show elevated expression ...
ORGANISM(S): Saccharomyces cerevisiae 
2005-07-22 | GSE2977 | GEO
UnknownIdentification of S-nitrosylated targets of thioredoxin using a quantitative proteomic approach.
Not available
S-EPMC3008576 | biostudies-literature
UnknownThioredoxin-linked processes in cyanobacteria are as numerous as in chloroplasts, but targets are different.
Not available
S-EPMC307700 | biostudies-literature
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