Gene Ontology annotation through association of InterPro records with GO terms

Gene Ontology annotation based on Enzyme Commission mapping

Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity

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

A fine-structure genetic and chemical study of the enzyme alkaline phosphatase of E. coli. I. Purification and characterization of alkaline phosphatase.

RELEASE OF ALKALINE PHOSPHATASE FROM CELLS OF ESCHERICHIA COLI UPON LYSOZYME SPHEROPLAST FORMATION.

Alkaline phosphatase of Escherichia coli: a zinc metalloenzyme.

A new activity for an old enzyme: Escherichia coli bacterial alkaline phosphatase is a phosphite-dependent hydrogenase.

Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR.

Detecting folding intermediates of a protein as it passes through the bacterial translocation channel.

Signal peptides are allosteric activators of the protein translocase.

From cell membrane to nucleotides: the phosphate regulon in Escherichia coli.

Identification of protein phosphatase 1 as a regulator of the LRRK2 phosphorylation cycle.

Control of the phoBR Regulon in Escherichia coli.

Refined structure of alkaline phosphatase from Escherichia coli at 2.8 A resolution.

Specific recognition of coiled coils by infrared spectroscopy: analysis of the three structural domains of type III intermediate filament proteins.

Deep research report: E. coli phoA / bacterial alkaline phosphatase (BAP)