Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Automatic assignment of GO terms using logical inference, based on inter-ontology links
Combined Automated Annotation using Multiple IEA Methods
Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ.
Zinc fingers and thiol-disulfide oxidoreductase activities of chaperone DnaJ.
Systematic search for zinc-binding proteins in Escherichia coli.
The roles of the two zinc binding sites in DnaJ.
Activity of the Hsp70 chaperone complex--DnaK, DnaJ, and GrpE--in initiating phage lambda DNA replication by sequestering and releasing lambda P protein.
Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock transcription factor sigma 32.
Interaction network containing conserved and essential protein complexes in Escherichia coli.
Monitoring protein conformation along the pathway of chaperonin-assisted folding.
Molecular basis for regulation of the heat shock transcription factor sigma32 by the DnaK and DnaJ chaperones.
Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate.
Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK.
The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase.
Isolation and characterization of dnaJ null mutants of Escherichia coli.
Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface.
The binary protein-protein interaction landscape of Escherichia coli.
Purification and properties of the dnaJ replication protein of Escherichia coli.
Escherichia coli dnaJ- and dnaK-gene products: synthesis in minicells and membrane-affinity.
A novel function of Escherichia coli chaperone DnaJ. Protein-disulfide isomerase.
Characterization of twenty-six new heat shock genes of Escherichia coli.
A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32.
Structure-function analysis of the zinc finger region of the DnaJ molecular chaperone.
Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK.
Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ.
UniProtKB entry for Escherichia coli DnaJ (P08622)
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Reviewed record summarizes DnaJ client transfer, DnaK ATPase-cycle stimulation, autonomous chaperone activity, zinc binding, homodimerization, and cytoplasmic localization.
"Unfolded proteins bind initially to DnaJ"
Deep research report for Escherichia coli DnaJ
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Synthesizes DnaJ's J-domain-mediated DnaK regulation, client targeting, cytosolic localization, heat-stress roles, and evidence gaps.
Unfolded protein binding annotation review project
OpenScientist focused report on DnaJ disulfide-isomerase prediction
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Focused computational-prediction audit arguing that the DnaJ protein disulfide isomerase prediction recapitulates a legacy over-annotation, while the reductase assay is at most a non-core in-vitro side activity.
"little, if any, isomerase activity"