Gene Ontology annotation through association of InterPro records with GO terms

Annotation inferences using phylogenetic trees

Combined Automated Annotation using Multiple IEA Methods

Reversible thermal transition in GrpE, the nucleotide exchange factor of the DnaK heat-shock system.

Interaction network containing conserved and essential protein complexes in Escherichia coli.

Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth.

Large-scale identification of protein-protein interaction of Escherichia coli K-12.

A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis.

GrpE N-terminal domain contributes to the interaction with Dnak and modulates the dynamics of the chaperone substrate binding domain.

Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK.

Protein abundance profiling of the Escherichia coli cytosol.

Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins.

The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase.

The binary protein-protein interaction landscape of Escherichia coli.

Escherichia coli DnaK and GrpE heat shock proteins interact both in vivo and in vitro.

Characterization of twenty-six new heat shock genes of Escherichia coli.

Initiation of lambda DNA replication. The Escherichia coli small heat shock proteins, DnaJ and GrpE, increase DnaK's affinity for the lambda P protein.

A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32.

Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK.