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ProteomicsTrypOx, a novel eukaryotic homologue of the redox-regulated chaperone Hsp33 in Trypanosoma brucei
In this study, we describe a novel eukaryotic homologue of Hsp33 in Trypanosoma brucei.Bioinformatics analysis of the Hsp33 family suggested that eukaryotic pathogens belonging to the kinetoplastids, such as Trypanosoma cruzi,Trypanosoma brucei spp, and leishmaniasis had persevered Hsp33 homologues...
ORGANISM(S): Trypanosoma brucei 
2020-07-28 | PXD018965 | Pride
Trypanosoma brucei Lc-ms/ms 
UnknownStructure of Hsp33/YOR391Cp from the yeast Saccharomyces cerevisiae.
Not available
S-EPMC2998354 | biostudies-literature
UnknownThe redox-switch domain of Hsp33 functions as dual stress sensor.
Not available
S-EPMC2782886 | biostudies-literature
UnknownUnfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperone.
Not available
S-EPMC2857002 | biostudies-literature
UnknownPurification, crystallization and preliminary X-ray analysis of Hsp33 from Saccharomyces cerevisiae.
Not available
S-EPMC2330124 | biostudies-literature
UnknownTrypOx, a Novel Eukaryotic Homolog of the Redox-Regulated Chaperone Hsp33 in Trypanosoma brucei.
Not available
S-EPMC7423844 | biostudies-literature
TranscriptomicsExpression profile of hsp31∆, hsp32∆, hsp33∆ during diauxic shift
The yeast Hsp31 mini-family proteins (Hsp31, Hsp32, Hsp33, Hsp34) belong to the highly conserved DJ-1 superfamily. The human DJ-1 protein is associated with cancer and neurodegenerative disorders, such as Parkinson’s disease. However, the precise function of human and yeast DJ-1 proteins is unclear....
ORGANISM(S): Saccharomyces cerevisiae 
2014-03-25 | GSE56124 | GEO
UnknownThe crystal structure of the reduced, Zn2+-bound form of the B. subtilis Hsp33 chaperone and its implications for the activation mechanism.
Not available
S-EPMC3691021 | biostudies-literature
TranscriptomicsAnalyses the expression profile of hsp31∆, hsp32∆, hsp33∆ during diauxic shift
The yeast Hsp31 mini-family proteins (Hsp31, Hsp32, Hsp33, Hsp34) belong to the highly conserved DJ-1 superfamily. The human DJ-1 protein is associated with cancer and neurodegenerative disorders, such as Parkinson’s disease. However, the precise function of human and yeast DJ-1 proteins is unclear....
ORGANISM(S): Saccharomyces cerevisiae 
2014-03-25 | E-GEOD-56124 | biostudies-arrayexpress
ProteomicsCOPPER INDUCES PROTEIN AGGREGATION, A TOXIC PROCESS COMPENSATED BY MOLECULAR CHAPERONES.
Copper is a powerful antimicrobial and antiviral agent, which has interest through several biomedical applications. Nevertheless, how copper induces the cellular damage is not fully understood. Two main mechanisms are claimed to be involved, i.e. Cu catalyzed reactive oxygen species production (ROS...
ORGANISM(S): Escherichia coli 
2022-02-10 | PXD019288 | Pride
Hsp33 Escherichia coli Molecular chaperone Copper Aggregation 
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