node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
BPI | CAMP | ENSP00000262865 | ENSP00000296435 | Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family | Cathelicidin antimicrobial peptide; Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity; Endogenous ligands | 0.974 |
BPI | CXCL1 | ENSP00000262865 | ENSP00000379110 | Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family | Growth-regulated alpha protein; Has chemotactic activity for neutrophils. May play a role in inflammation and exerts its effects on endothelial cells in an autocrine fashion. In vitro, the processed forms GRO- alpha(4-73), GRO-alpha(5-73) and GRO-alpha(6-73) show a 30-fold higher chemotactic activity; Chemokine ligands | 0.913 |
BPI | DEFA4 | ENSP00000262865 | ENSP00000297435 | Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family | Neutrophil defensin 4; Has antimicrobial activity against Gram-negative bacteria, and to a lesser extent also against Gram-positive bacteria and fungi. Protects blood cells against infection with HIV-1 (in vitro). Inhibits corticotropin (ACTH)-stimulated corticosterone production; Defensins, alpha | 0.984 |
BPI | ELANE | ENSP00000262865 | ENSP00000466090 | Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family | Neutrophil elastase; Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis | 0.982 |
BPI | LCN2 | ENSP00000262865 | ENSP00000362108 | Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family | Neutrophil gelatinase-associated lipocalin; Iron-trafficking protein involved in multiple processes such as apoptosis, innate immunity and renal development. Binds iron through association with 2,5-dihydroxybenzoic acid (2,5- DHBA), a siderophore that shares structural similarities with bacterial enterobactin, and delivers or removes iron from the cell, depending on the context. Iron-bound form (holo-24p3) is internalized following binding to the SLC22A17 (24p3R) receptor, leading to release of iron and subsequent increase of intracellular iron concentration. In contrast, association o [...] | 0.936 |
BPI | LTF | ENSP00000262865 | ENSP00000231751 | Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family | Lactotransferrin; Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors; Transferrins | 0.939 |
BPI | PGLYRP1 | ENSP00000262865 | ENSP00000008938 | Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family | Peptidoglycan recognition protein 1; Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram- negative bacteria, and has bacteriostatic activity towards Gram- negative bacteria. Plays a role in innate immunity; Peptidoglycan recognition proteins | 0.960 |
BPI | PRTN3 | ENSP00000262865 | ENSP00000234347 | Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family | Myeloblastin; Serine protease that degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro). By cleaving and activating receptor F2RL1/PAR-2, enhances endothelial cell barrier function and thus vascular integrity during neutrophil transendothelial migration. May play a role in neutrophil transendothelial migration, probably when associated with CD177; Belongs to the peptidase S1 family. Elastase subfamily | 0.972 |
BPI | SLPI | ENSP00000262865 | ENSP00000342082 | Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family | Antileukoproteinase; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. Modulates the inflammatory and immune responses after bacterial infection, and after infection by the intracellular parasite L.major. Down-regulates responses to bacterial lipopolysaccharide (LPS) (By similarity). Plays a role in regulating the activation of NF-kappa-B and inflammatory responses. Has antimicrobial activity against mycobacteria, but not against salmonella. Contributes to normal resistance against infection by M.tuberculosis. Required for nor [...] | 0.939 |
CAMP | BPI | ENSP00000296435 | ENSP00000262865 | Cathelicidin antimicrobial peptide; Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity; Endogenous ligands | Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family | 0.974 |
CAMP | CXCL1 | ENSP00000296435 | ENSP00000379110 | Cathelicidin antimicrobial peptide; Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity; Endogenous ligands | Growth-regulated alpha protein; Has chemotactic activity for neutrophils. May play a role in inflammation and exerts its effects on endothelial cells in an autocrine fashion. In vitro, the processed forms GRO- alpha(4-73), GRO-alpha(5-73) and GRO-alpha(6-73) show a 30-fold higher chemotactic activity; Chemokine ligands | 0.941 |
CAMP | DEFA4 | ENSP00000296435 | ENSP00000297435 | Cathelicidin antimicrobial peptide; Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity; Endogenous ligands | Neutrophil defensin 4; Has antimicrobial activity against Gram-negative bacteria, and to a lesser extent also against Gram-positive bacteria and fungi. Protects blood cells against infection with HIV-1 (in vitro). Inhibits corticotropin (ACTH)-stimulated corticosterone production; Defensins, alpha | 0.980 |
CAMP | ELANE | ENSP00000296435 | ENSP00000466090 | Cathelicidin antimicrobial peptide; Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity; Endogenous ligands | Neutrophil elastase; Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis | 0.980 |
CAMP | HBB | ENSP00000296435 | ENSP00000333994 | Cathelicidin antimicrobial peptide; Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity; Endogenous ligands | Hemoglobin subunit beta; Involved in oxygen transport from the lung to the various peripheral tissues; Belongs to the globin family | 0.955 |
CAMP | LCN2 | ENSP00000296435 | ENSP00000362108 | Cathelicidin antimicrobial peptide; Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity; Endogenous ligands | Neutrophil gelatinase-associated lipocalin; Iron-trafficking protein involved in multiple processes such as apoptosis, innate immunity and renal development. Binds iron through association with 2,5-dihydroxybenzoic acid (2,5- DHBA), a siderophore that shares structural similarities with bacterial enterobactin, and delivers or removes iron from the cell, depending on the context. Iron-bound form (holo-24p3) is internalized following binding to the SLC22A17 (24p3R) receptor, leading to release of iron and subsequent increase of intracellular iron concentration. In contrast, association o [...] | 0.958 |
CAMP | LTF | ENSP00000296435 | ENSP00000231751 | Cathelicidin antimicrobial peptide; Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity; Endogenous ligands | Lactotransferrin; Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors; Transferrins | 0.946 |
CAMP | PGLYRP1 | ENSP00000296435 | ENSP00000008938 | Cathelicidin antimicrobial peptide; Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity; Endogenous ligands | Peptidoglycan recognition protein 1; Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram- negative bacteria, and has bacteriostatic activity towards Gram- negative bacteria. Plays a role in innate immunity; Peptidoglycan recognition proteins | 0.968 |
CAMP | PRTN3 | ENSP00000296435 | ENSP00000234347 | Cathelicidin antimicrobial peptide; Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity; Endogenous ligands | Myeloblastin; Serine protease that degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro). By cleaving and activating receptor F2RL1/PAR-2, enhances endothelial cell barrier function and thus vascular integrity during neutrophil transendothelial migration. May play a role in neutrophil transendothelial migration, probably when associated with CD177; Belongs to the peptidase S1 family. Elastase subfamily | 0.978 |
CAMP | SLPI | ENSP00000296435 | ENSP00000342082 | Cathelicidin antimicrobial peptide; Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity; Endogenous ligands | Antileukoproteinase; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. Modulates the inflammatory and immune responses after bacterial infection, and after infection by the intracellular parasite L.major. Down-regulates responses to bacterial lipopolysaccharide (LPS) (By similarity). Plays a role in regulating the activation of NF-kappa-B and inflammatory responses. Has antimicrobial activity against mycobacteria, but not against salmonella. Contributes to normal resistance against infection by M.tuberculosis. Required for nor [...] | 0.964 |
CXCL1 | BPI | ENSP00000379110 | ENSP00000262865 | Growth-regulated alpha protein; Has chemotactic activity for neutrophils. May play a role in inflammation and exerts its effects on endothelial cells in an autocrine fashion. In vitro, the processed forms GRO- alpha(4-73), GRO-alpha(5-73) and GRO-alpha(6-73) show a 30-fold higher chemotactic activity; Chemokine ligands | Bactericidal permeability-increasing protein; The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa; Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family | 0.913 |