Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
UniProtKB/Swiss-Prot entry P08148 (LMSP_LEIMA, leishmanolysin)
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UniProt annotates three Zn(2+)-binding residues (264, 268, 334) in P08148, each marked catalytic and evidenced to the 1.86 A crystal structure.
"BINDING 334 /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_note="catalytic""
Secreted virulence factors and immune evasion in visceral leishmaniasis.
Impact of Leishmania metalloprotease GP63 on macrophage signaling.
Leishmania promastigotes induce cytokine secretion in macrophages through the degradation of synaptotagmin XI.
Role of the Leishmania surface protease gp63 in complement fixation, cell adhesion, and resistance to complement-mediated lysis.
The crystal structure of the Leishmania major surface proteinase leishmanolysin (gp63).
Posttranslational regulation of a Leishmania HEXXH metalloprotease (gp63). The effects of site-specific mutagenesis of catalytic, zinc binding, N-glycosylation, and glycosyl phosphatidylinositol addition sites on N-terminal end cleavage, intracellular stability, and extracellular exit.
Structure of the glycosyl-phosphatidylinositol membrane anchor of the Leishmania major promastigote surface protease.
Leishmania GP63 alters host signaling through cleavage-activated protein tyrosine phosphatases.
Leishmania repression of host translation through mTOR cleavage is required for parasite survival and infection.
Targeted gene deletion of Leishmania major genes encoding developmental stage-specific leishmanolysin (GP63).
Targeted gene deletion in Leishmania major identifies leishmanolysin (GP63) as a virulence factor.
The major surface-metalloprotease of the parasitic protozoan, Leishmania, protects against antimicrobial peptide-induced apoptotic killing.
Migration through the extracellular matrix by the parasitic protozoan Leishmania is enhanced by surface metalloprotease gp63.