Gene Ontology annotation through association of InterPro records with GO terms

Annotation inferences using phylogenetic trees

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

Electronic Gene Ontology annotations created by ARBA machine learning models

The delta subunit of DNA polymerase III holoenzyme serves as a sliding clamp unloader in Escherichia coli.

Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III.

Over 1000 genes are involved in the DNA damage response of Escherichia coli.

Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp.

Structural basis for recruitment of translesion DNA polymerase Pol IV/DinB to the beta-clamp.

Interaction of the sliding clamp beta-subunit and Hda, a DnaA-related protein.

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

Mutant forms of the Escherichia colibeta sliding clamp that distinguish between its roles in replication and DNA polymerase V-dependent translesion DNA synthesis.

Two processivity clamp interactions differentially alter the dual activities of UmuC.

The beta sliding clamp binds to multiple sites within MutL and MutS.

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

Protein abundance profiling of the Escherichia coli cytosol.

Transposition into replicating DNA occurs through interaction with the processivity factor.

Benchmarking yeast two-hybrid systems using the interactions of bacterial motility proteins.

Mechanism of the sliding beta-clamp of DNA polymerase III holoenzyme.

DnaA protein DNA-binding domain binds to Hda protein to promote inter-AAA+ domain interaction involved in regulatory inactivation of DnaA.

A direct proofreader-clamp interaction stabilizes the Pol III replicase in the polymerization mode.

Architecture of the Pol III-clamp-exonuclease complex reveals key roles of the exonuclease subunit in processive DNA synthesis and repair.

A replicase clamp-binding dynamin-like protein promotes colocalization of nascent DNA strands and equipartitioning of chromosomes in E. coli.

The binary protein-protein interaction landscape of Escherichia coli.

A second-generation protein-protein interaction network of Helicobacter pylori.

cryo-EM structures of the E. coli replicative DNA polymerase reveal its dynamic interactions with the DNA sliding clamp, exonuclease and τ.

Dynamic assembly of Hda and the sliding clamp in the regulation of replication licensing.

The dimer of the beta subunit of Escherichia coli DNA polymerase III holoenzyme is dissociated into monomers upon binding magnesium(II).

A quest for coordination among activities at the replisome.

DNA polymerase III holoenzyme of Escherichia coli. III. Distinctive processive polymerases reconstituted from purified subunits.

The beta subunit of the Escherichia coli DNA polymerase III holoenzyme interacts functionally with the catalytic core in the absence of other subunits.

DNA polymerase III holoenzyme: structure and function of a chromosomal replicating machine.

Assembly of a chromosomal replication machine: two DNA polymerases, a clamp loader, and sliding clamps in one holoenzyme particle. II. Intermediate complex between the clamp loader and its clamp.

Devoted to the lagging strand-the subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly.

A separate editing exonuclease for DNA replication: the epsilon subunit of Escherichia coli DNA polymerase III holoenzyme.

The polymerase subunit of DNA polymerase III of Escherichia coli. II. Purification of the alpha subunit, devoid of nuclease activities.

The E. coli DNA Replication Fork.