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ProteomicsThe self-association equilibrium of DNAJA2 regulates its interaction with unfolded substrate proteins and with Hsc70
J-domain proteins tune the specificity of Hsp70s, engaging them in precise functions. Despite their essential role, the structure and function of many J-domain proteins remain largely unknown. We explore human DNAJA2, a class A J-domain protein, finding that it reversibly oligomerises into highly-or...
ORGANISM(S): Homo sapiens (Human) 
2023-09-05 | PXD043837 | Pride
Dnaja2 structure Chaperone Hsp70 system J-domain proteins Protein folding 
UnknownThe self-association equilibrium of DNAJA2 regulates its interaction with unfolded substrate proteins and with Hsc70.
Not available
S-EPMC10480186 | biostudies-literature
UnknownHsp70 and DNAJA2 limit CFTR levels through degradation.
Not available
S-EPMC6692068 | biostudies-literature
UnknownThe DNAJA2 substrate release mechanism is essential for chaperone-mediated folding.
Not available
S-EPMC3516741 | biostudies-literature
UnknownDevelopmental origins of disease and determinants of chromatin structure: maternal diet modifies the primate fetal epigenome.
Not available
S-EPMC2959100 | biostudies-literature
UnknownStructural resemblance of the DNAJA-family protein, Tid1, to the DNAJB-family Hsp40.
Not available
S-EPMC9623239 | biostudies-literature
TranscriptomicsGenome-wide ParB2-DNA and RctB-DNA interaction analyses in Vibrio cholerae
Replication and segregation are the two main processes that maintain chromosomes in growing cells. In bacteria, replication and transcription have been proposed to provide motive force in chromosome segregation. Recently, ParB2, a segregation protein, encoded by V. cholerae chromosome II (chrII) wa...
ORGANISM(S): Vibrio cholerae O1 biovar El Tor str. N16961 
2015-09-14 | E-GEOD-72978 | biostudies-arrayexpress
TranscriptomicsChange in gene expression in Chlamydomonas reinhardtii upon heat shock
This was an accompanying experiment. Previously, the expression of genes hsp70A and hsp70B had been established as being tetrapyrrole-dependent (Kropat et al., 1997, 2000). Since both are well-known heat-shock proteins, we performed a one-step heat shock treatment by shifting the temperatures from 2...
ORGANISM(S): Chlamydomonas reinhardtii 
2011-03-02 | E-GEOD-20859 | biostudies-arrayexpress
TranscriptomicsAcetone stress response in Desulfovibrio vulgaris
Desulfovibrio vulgaris has been studied extensively for its potential in the bioremediation of heavy metals and radionuclides. Hydrocarbons and solvents, as frequent environmental co-contaminants, have been reported to inhibit microbial activities and thereby pose a limitation on bioremediation effi...
ORGANISM(S): Desulfovibrio vulgaris str. Hildenborough 
2009-08-08 | E-GEOD-5569 | biostudies-arrayexpress
TranscriptomicsEthanol stress response in Desulfovibrio vulgaris
Desulfovibrio vulgaris has been studied extensively for its potential in the bioremediation of heavy metals and radionuclides. Hydrocarbons and solvents, as frequent environmental co-contaminants, have been reported to inhibit microbial activities and thereby pose a limitation on bioremediation effi...
ORGANISM(S): Desulfovibrio vulgaris str. Hildenborough 
2010-06-24 | E-GEOD-7489 | biostudies-arrayexpress
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