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Ala-Arg-Ser-Val-Val-Arg-Asp-Val-Asn + H2O
Ala-Arg-Ser-Val + Val-Arg-Asp-Val-Asn
azocasein + H2O
low molecular weight acid-soluble azopeptides
Bovine serum albumin + H2O
?
Casein micelles + H2O
?
-
milk assay
-
-
?
Dansyl-Ala-Tyr-Leu-Lys-Lys-Trp-Val-NH2 + H2O
Dansyl-Ala-Tyr + ?
-
cleavage site: Tyr-Leu
-
?
Elastin + H2O
?
-
zymographic assay
-
-
?
kappa-B nuclear factor + H2O
?
Leu-Ile-Ala-Tyr-Leu-Lys-Lys-Ala-Thr + H2O
Leu-Ile-Ala-Tyr + ?
Leu-Ile-Ala-Tyr-Ser-Lys-Lys-Ala-Thr + H2O
?
MARCKS-related protein MRP + H2O
?
myristoylated alanine-rich C kinase substrate MARCKS + H2O
?
Oxidized insulin B-chain + H2O
?
p130Cas + H2O
?
-
phosphorylated adaptor protein of fibroblasts
-
-
?
Peptide 170-182 from CW-3 HLA antigen + H2O
?
Peptide 83-94 from beta-chain of HLA DO + H2O
?
Peptide 97-105 from Leishmanolysin + H2O
?
Peptides from horse cytochrome c + H2O
?
protein tyrosine phosphatase PTP1B + H2O
?
protein tyrosine phosphatase SHP-1 + H2O
?
protein tyrosine phosphatase TCPTP + H2O
?
protein-tyrosine phosphatase-PEST + H2O
?
-
fibroblast protein cleaved upon infection by Leishmania major. cleavage augments its catalytic activity. Cleavage occurs likely near its C-terminal nuclear localization signal. Removal of the nuclear localization signal could allow the phosphatase to access additional substrates and also enhance its catalytic activity
-
-
?
transcription factor AP-1 + H2O
?
-
inactivation and degradation
-
-
?
tyrosine phosphatase + H2O
?
additional information
?
-
Ala-Arg-Ser-Val-Val-Arg-Asp-Val-Asn + H2O
Ala-Arg-Ser-Val + Val-Arg-Asp-Val-Asn
-
i.e. synthetic peptide derived from leishmanolysin
-
-
?
Ala-Arg-Ser-Val-Val-Arg-Asp-Val-Asn + H2O
Ala-Arg-Ser-Val + Val-Arg-Asp-Val-Asn
-
i.e. synthetic peptide derived from leishmanolysin
-
?
Ala-Arg-Ser-Val-Val-Arg-Asp-Val-Asn + H2O
Ala-Arg-Ser-Val + Val-Arg-Asp-Val-Asn
-
covers the last 4 amino acids of the prosequence and the first 5 amino acids of the native Leishmanolysin, cleavage site: Val-Val
-
?
azocasein + H2O
?
-
-
-
?
azocasein + H2O
?
-
-
-
?
azocasein + H2O
low molecular weight acid-soluble azopeptides
-
-
-
?
azocasein + H2O
low molecular weight acid-soluble azopeptides
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
-
radioiodinated
-
-
?
Bovine serum albumin + H2O
?
-
radioiodinated
-
-
?
Bovine serum albumin + H2O
?
-
radioiodinated
-
-
?
casein + H2O
?
fluorescein isothiocyanate-labeled casein
-
-
?
casein + H2O
?
fluorescein isothiocyanate-labeled casein
-
-
?
Fibrinogen + H2O
?
-
-
-
-
?
Fibrinogen + H2O
?
-
-
-
-
?
Fibrinogen + H2O
?
-
ovine fibrinogen, zymographic assay
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
?
Glucagon + H2O
?
-
-
-
-
?
Glucagon + H2O
?
-
major cleavage sites: Tyr10-Ser11, Asp15-Ser16, minor site: Trp25-Leu26
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
kappa-B nuclear factor + H2O
?
-
-
-
-
?
kappa-B nuclear factor + H2O
?
-
-
-
?
kappa-B nuclear factor + H2O
?
-
-
-
?
kappa-B nuclear factor + H2O
?
-
-
-
-
?
kappa-B nuclear factor + H2O
?
-
-
-
-
?
Leu-Ile-Ala-Tyr-Leu-Lys-Lys-Ala-Thr + H2O
Leu-Ile-Ala-Tyr + ?
-
from horse cytochrome
-
?
Leu-Ile-Ala-Tyr-Leu-Lys-Lys-Ala-Thr + H2O
Leu-Ile-Ala-Tyr + ?
-
from horse cytochrome
-
-
?
Leu-Ile-Ala-Tyr-Leu-Lys-Lys-Ala-Thr + H2O
Leu-Ile-Ala-Tyr + ?
-
model peptide cytochrome c(94-102)L, cleavage site: Tyr97-Leu98
-
-
?
Leu-Ile-Ala-Tyr-Ser-Lys-Lys-Ala-Thr + H2O
?
-
from horse cytochrome
-
-
?
Leu-Ile-Ala-Tyr-Ser-Lys-Lys-Ala-Thr + H2O
?
-
from horse cytochrome
-
-
?
Leu-Ile-Ala-Tyr-Ser-Lys-Lys-Ala-Thr + H2O
?
-
model peptide cytochrome c(94-102)S, cleavage site: Tyr97-Ser98
-
-
?
MARCKS-related protein MRP + H2O
?
-
-
-
?
MARCKS-related protein MRP + H2O
?
-
-
-
?
myristoylated alanine-rich C kinase substrate MARCKS + H2O
?
-
-
-
?
myristoylated alanine-rich C kinase substrate MARCKS + H2O
?
-
-
-
?
Oxidized insulin B-chain + H2O
?
-
-
-
-
?
Oxidized insulin B-chain + H2O
?
-
major cleavage site: Gly8-Ser9, minor site: Tyr16-Leu17
-
-
?
Peptide 170-182 from CW-3 HLA antigen + H2O
?
-
-
-
-
?
Peptide 170-182 from CW-3 HLA antigen + H2O
?
-
major cleavage site: Lys75-Asn76, minor site: Tyr73-Leu74
-
-
?
Peptide 83-94 from beta-chain of HLA DO + H2O
?
-
-
-
-
?
Peptide 83-94 from beta-chain of HLA DO + H2O
?
-
cleavage site: Arg84-Leu85
-
-
?
Peptide 97-105 from Leishmanolysin + H2O
?
-
-
-
-
?
Peptide 97-105 from Leishmanolysin + H2O
?
-
-
-
-
?
Peptides from horse cytochrome c + H2O
?
-
i.e. peptides 1-25, 39-53 and 81-104
-
-
?
Peptides from horse cytochrome c + H2O
?
-
peptide 81-104 cleavage sites: Gly84-Ile85 and Tyr97-Leu98
-
-
?
Peptides from horse cytochrome c + H2O
?
-
i.e. peptides 1-25, 39-53 and 81-104
-
-
?
protein tyrosine phosphatase PTP1B + H2O
?
-
activation and posttranslationally modification of host enzymes in infected macrophages. The PTP1B cleavage fragments are enzymatically active. The mechanism underlying PTP modulation involves the proteolytic activity of the Leishmania surface protease GP63
-
-
?
protein tyrosine phosphatase PTP1B + H2O
?
-
activation and posttranslationally modification of host enzymes in infected macrophages
-
-
?
protein tyrosine phosphatase SHP-1 + H2O
?
-
activation and posttranslationally modification of host enzymes in infected macrophages. The SHP-1 cleavage fragments are enzymatically active
-
-
?
protein tyrosine phosphatase SHP-1 + H2O
?
-
activation and posttranslationally modification of host enzymes in infected macrophages
-
-
?
protein tyrosine phosphatase TCPTP + H2O
?
-
activation and posttranslationally modification of host enzymes in infected macrophages. The TCPTP cleavage fragments are enzymatically active
-
-
?
protein tyrosine phosphatase TCPTP + H2O
?
-
activation and posttranslationally modification of host enzymes in infected macrophages
-
-
?
tyrosine phosphatase + H2O
?
-
-
-
-
?
tyrosine phosphatase + H2O
?
-
-
-
?
tyrosine phosphatase + H2O
?
-
-
-
?
tyrosine phosphatase + H2O
?
-
-
-
-
?
tyrosine phosphatase + H2O
?
-
-
-
-
?
additional information
?
-
-
the enzyme shows a broad substrate spectrum and ability to degrade albumin,hemoglobin, IgG, mucin, casein, and gut proteins obtained from Aedes aegypti
-
-
?
additional information
?
-
-
non-specific endopeptidase
-
-
?
additional information
?
-
-
protects parasite membrane from cytosolic damage during their survival, differentiation and multiplication in the phagolysosomes of macrophages
-
-
?
additional information
?
-
-
non-specific endopeptidase
-
-
?
additional information
?
-
-
protects parasite membrane from cytosolic damage during their survival, differentiation and multiplication in the phagolysosomes of macrophages
-
-
?
additional information
?
-
-
major surface protease is a virulence factor of Leishmania spp. protozoan, virulent Leishmania chagasi undergoes a growth-associated lengthening in the t1/2 of surface-localized MSP, but this does not occur in the attenuated L5 strain, surface-localized MSP isoforms are differently regulated in attenuated and virulent strains, overview
-
-
?
additional information
?
-
-
major surface protease is a virulence factor of Leishmania spp. protozoan, virulent Leishmania chagasi undergoes a growth-associated lengthening in the t1/2 of surface-localized MSP, but this does not occur in the attenuated L5 strain, surface-localized MSP isoforms are differently regulated in attenuated and virulent strains, overview
-
-
?
additional information
?
-
-
role of enzyme in promastigote multiplication connected with its fibronectin-like properties
-
-
?
additional information
?
-
-
specificity is defined by P'-subsites of the substrates
-
-
?
additional information
?
-
-
Leishmania promastigotes reside in the midgut of the phlebotomine sand fly and invade host macrophages during a sand fly bite, infection may result in leishmanolysin-dependent hydrolysis of MRP, a major protein kinase C substrate in macrophages
-
?
additional information
?
-
-
enzyme plays a significant role in association with other surface molecules, especially lipophosphoglycan. Overexpression of enzyme can compensate lipophosphoglycan defect in the vertebrate host but in sand flies both molecules fulfill quite different functions
-
-
?
additional information
?
-
-
the major surface-metalloprotease is a virulence factor which contributes to a variety of functions including evasion of complement-mediated parasite-killing and host intramacrophage survival, the protozoan enzyme protects the parasite against antimicrobial peptide-induced apoptotic killing by the host cell, overview
-
-
?
additional information
?
-
gp63 is an important agent for suppression of natural killer cells during Leishmain infection. Proliferation of interleukin-2-activated purified natural killer cells is suppressed after exposure to the wild-type but not to gp63ko promastigotes. gp63ko Leishmaina major induces no natural killer cell proliferation when natural killer cells are co-cultured with peripheral blood mononuclear cells populations such as CD14+ monocytes or T cells
-
-
?
additional information
?
-
-
gp63 is an important agent for suppression of natural killer cells during Leishmain infection. Proliferation of interleukin-2-activated purified natural killer cells is suppressed after exposure to the wild-type but not to gp63ko promastigotes. gp63ko Leishmaina major induces no natural killer cell proliferation when natural killer cells are co-cultured with peripheral blood mononuclear cells populations such as CD14+ monocytes or T cells
-
-
?
additional information
?
-
-
gp63 is the principal catalyst of proteolysis during infection. It plays a central role in a number of host cell molecular events that likely contribute to the infectivity of Leishmania
-
-
?
additional information
?
-
-
Leishmania promastigotes reside in the midgut of the phlebotomine sand fly and invade host macrophages during a sand fly bite, infection may result in leishmanolysin-dependent hydrolysis of MRP, a major protein kinase C substrate in macrophages
-
?
additional information
?
-
-
protects parasite membrane from cytosolic damage during their survival, differentiation and multiplication in the phagolysosomes of macrophages
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
preferentially cleaves at amino side when hydrophobic residues are in P1'-site, basic amino acids in P2' and P3' and commonly Tyr at P1
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kappa-B nuclear factor + H2O
?
protein tyrosine phosphatase PTP1B + H2O
?
-
activation and posttranslationally modification of host enzymes in infected macrophages. The PTP1B cleavage fragments are enzymatically active. The mechanism underlying PTP modulation involves the proteolytic activity of the Leishmania surface protease GP63
-
-
?
protein tyrosine phosphatase SHP-1 + H2O
?
-
activation and posttranslationally modification of host enzymes in infected macrophages. The SHP-1 cleavage fragments are enzymatically active
-
-
?
protein tyrosine phosphatase TCPTP + H2O
?
-
activation and posttranslationally modification of host enzymes in infected macrophages. The TCPTP cleavage fragments are enzymatically active
-
-
?
transcription factor AP-1 + H2O
?
-
inactivation and degradation
-
-
?
tyrosine phosphatase + H2O
?
additional information
?
-
Fibronectin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
kappa-B nuclear factor + H2O
?
-
-
-
-
?
kappa-B nuclear factor + H2O
?
-
-
-
?
kappa-B nuclear factor + H2O
?
-
-
-
?
kappa-B nuclear factor + H2O
?
-
-
-
-
?
kappa-B nuclear factor + H2O
?
-
-
-
-
?
tyrosine phosphatase + H2O
?
-
-
-
-
?
tyrosine phosphatase + H2O
?
-
-
-
?
tyrosine phosphatase + H2O
?
-
-
-
?
tyrosine phosphatase + H2O
?
-
-
-
-
?
tyrosine phosphatase + H2O
?
-
-
-
-
?
additional information
?
-
-
the enzyme shows a broad substrate spectrum and ability to degrade albumin,hemoglobin, IgG, mucin, casein, and gut proteins obtained from Aedes aegypti
-
-
?
additional information
?
-
-
protects parasite membrane from cytosolic damage during their survival, differentiation and multiplication in the phagolysosomes of macrophages
-
-
?
additional information
?
-
-
protects parasite membrane from cytosolic damage during their survival, differentiation and multiplication in the phagolysosomes of macrophages
-
-
?
additional information
?
-
-
major surface protease is a virulence factor of Leishmania spp. protozoan, virulent Leishmania chagasi undergoes a growth-associated lengthening in the t1/2 of surface-localized MSP, but this does not occur in the attenuated L5 strain, surface-localized MSP isoforms are differently regulated in attenuated and virulent strains, overview
-
-
?
additional information
?
-
-
major surface protease is a virulence factor of Leishmania spp. protozoan, virulent Leishmania chagasi undergoes a growth-associated lengthening in the t1/2 of surface-localized MSP, but this does not occur in the attenuated L5 strain, surface-localized MSP isoforms are differently regulated in attenuated and virulent strains, overview
-
-
?
additional information
?
-
-
role of enzyme in promastigote multiplication connected with its fibronectin-like properties
-
-
?
additional information
?
-
-
Leishmania promastigotes reside in the midgut of the phlebotomine sand fly and invade host macrophages during a sand fly bite, infection may result in leishmanolysin-dependent hydrolysis of MRP, a major protein kinase C substrate in macrophages
-
?
additional information
?
-
-
enzyme plays a significant role in association with other surface molecules, especially lipophosphoglycan. Overexpression of enzyme can compensate lipophosphoglycan defect in the vertebrate host but in sand flies both molecules fulfill quite different functions
-
-
?
additional information
?
-
-
the major surface-metalloprotease is a virulence factor which contributes to a variety of functions including evasion of complement-mediated parasite-killing and host intramacrophage survival, the protozoan enzyme protects the parasite against antimicrobial peptide-induced apoptotic killing by the host cell, overview
-
-
?
additional information
?
-
gp63 is an important agent for suppression of natural killer cells during Leishmain infection. Proliferation of interleukin-2-activated purified natural killer cells is suppressed after exposure to the wild-type but not to gp63ko promastigotes. gp63ko Leishmaina major induces no natural killer cell proliferation when natural killer cells are co-cultured with peripheral blood mononuclear cells populations such as CD14+ monocytes or T cells
-
-
?
additional information
?
-
-
gp63 is an important agent for suppression of natural killer cells during Leishmain infection. Proliferation of interleukin-2-activated purified natural killer cells is suppressed after exposure to the wild-type but not to gp63ko promastigotes. gp63ko Leishmaina major induces no natural killer cell proliferation when natural killer cells are co-cultured with peripheral blood mononuclear cells populations such as CD14+ monocytes or T cells
-
-
?
additional information
?
-
-
gp63 is the principal catalyst of proteolysis during infection. It plays a central role in a number of host cell molecular events that likely contribute to the infectivity of Leishmania
-
-
?
additional information
?
-
-
Leishmania promastigotes reside in the midgut of the phlebotomine sand fly and invade host macrophages during a sand fly bite, infection may result in leishmanolysin-dependent hydrolysis of MRP, a major protein kinase C substrate in macrophages
-
?
additional information
?
-
-
protects parasite membrane from cytosolic damage during their survival, differentiation and multiplication in the phagolysosomes of macrophages
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-
-
brenda
-
GP63 is able to act on its substrate proteins within the nucleus of its host cell
brenda
-
Leishmania mexicana amastigotes
-
brenda
the host cell secretory pathway mediates the export of Leishmania virulence factors out of the parasitophorous vacuole
brenda
-
surface molecules are glycosylphosphatidylinositol-anchored
brenda
-
-
brenda
-
major surface protein
brenda
-
major surface protein
-
brenda
-
-
brenda
-
about two-thirds of newly synthesized enzyme becomes surface localized, the rest of enzyme does not reach the cell surface. Surface-localized enzyme is released at different rates from logarithmic and stationary phase virulent promastigotes. Major mechanism regulating enzyme abundance is the rate of loss of surface-localized enzyme from promastigote surface
brenda
-
two-third of MSPs in promastigotes is orientated along the cell surface, whereas most MSPs in amastigotes are localized in the flagellar pocket
brenda
-
-
-
brenda
-
two-third of MSPs in promastigotes is orientated along the cell surface, whereas most MSPs in amastigotes are localized in the flagellar pocket
-
brenda
-
GP63 is able to act on its substrate proteins within the nucleus of its host cell
brenda
-
-
brenda
-
major surface protein
brenda
-
most MSPs in promastigotes are membrane-associated, whereas most MSPs in amastigotes are cytosolic
brenda
-
most MSPs in promastigotes are membrane-associated, whereas most MSPs in amastigotes are cytosolic
-
brenda
metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
-
brenda
metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
-
brenda
metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
-
brenda
metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
-
brenda
metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
-
brenda
metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
-
brenda
metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
-
brenda
-
metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
-
-
brenda
metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
-
brenda
-
the enzyme is secreted. The zinc-metallopeptidase inhibitor 1,10-phenanthroline is able to restrain the secretion of the metallopeptidase in a dose-dependent manner, while the phospholipase C inhibitor 4-chloromercuriphenylsulfonic acid does not alter the secretion pattern
-
brenda
-
-
-
brenda
-
promastigote MSP is shed extracellularly, whereas MSPs from axenic amastigotes are not shed
-
brenda
-
-
-
-
brenda
-
promastigote MSP is shed extracellularly, whereas MSPs from axenic amastigotes are not shed
-
-
brenda
the host cell secretory pathway mediates the export of Leishmania virulence factors out of the parasitophorous vacuole. The enzyme is released from the parasite surface following phagocytosis and is redistributed to the endoplasmic reticulum of macrophages
-
brenda
-
two-third of MSPs in promastigotes is orientated along the cell surface, whereas most MSPs in amastigotes are localized in the flagellar pocket
-
brenda
-
two-third of MSPs in promastigotes is orientated along the cell surface, whereas most MSPs in amastigotes are localized in the flagellar pocket
-
-
brenda
-
-
brenda
-
about two-thirds of newly synthesized enzyme becomes surface localized, the rest of enzyme does not reach the cell surface. Internal enzyme is stable without detectable decrease in abundance up to 6 days after biosynthesis
brenda
-
-
-
brenda
-
-
brenda
-
-
brenda
-
-
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membrane-bound
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glycosylphosphatidylinositol-anchored
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membrane-bound
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most MSPs in promastigotes are membrane-associated, whereas most MSPs in amastigotes are cytosolic
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most MSPs in promastigotes are membrane-associated, whereas most MSPs in amastigotes are cytosolic
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additional information
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leishmanolysin-like molecules are distributed in different cellular compartments, immunocytochemic analysis, overview. The expression of leishmanolysin-like molecules is not modulated during either temperature- or dimethylsulfoxide-elicited differentiation
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additional information
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three pools of MSP, located either internally within the parasite, anchored to the surface membrane, or released into the extracellular environment, promastigotes incubation with Matrigel matrix, a soluble basement membrane extract of Engelbreth-Holm-Swarm tumor cells, stimulates the release of internal MSP but not of surface-located MSP, at 37°C, overview
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additional information
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three pools of MSP, located either internally within the parasite, anchored to the surface membrane, or released into the extracellular environment, promastigotes incubation with Matrigel matrix, a soluble basement membrane extract of Engelbreth-Holm-Swarm tumor cells, stimulates the release of internal MSP but not of surface-located MSP, at 37°C, overview
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additional information
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GP63 is located in punctuated structures along the cell periphery in infected macrophages, with partial colocalization with the lipid raft marker cholera toxin B
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evolution
GP63 belongs to the metzincin class, encoded by a series of tandemly linked genes usually in a single chromosome that are highly sequence-conserved among different species of Leishmania
evolution
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GP63 belongs to the metzincin class, encoded by a series of tandemly linked genes usually in a single chromosome that are highly sequence-conserved among different species of Leishmania
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malfunction
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a leishmanolysin knockout strain of Leishmania major Seidman strain lacks the GP63 surface metalloprotease
malfunction
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a leishmanolysin knockout strain of Leishmania major Seidman strain lacks the GP63 surface metalloprotease
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physiological function
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GP63 is a key Leishmania virulence factor. Leishmania GP63 alters the profile of protein tyrosine phosphatases associated with JAK-2 at the host cell plasma membrane
physiological function
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Leishmania-induced inactivation of the macrophage transcription factor AP-1 is mediated by the parasite metalloprotease GP63 at the cell surface, overview. GP63 but not LPG is highly involved in the mechanism responsible for the inactivation of AP-1 transcription factor. GP63 action requires macrophage lipid raft and is not dependent on parasite phagocytosis
physiological function
A0A3Q9STI6, A0A3Q9STK3, A0A3Q9STL5, A0A3Q9SVM5, A0A3Q9SVN4, A0A3Q9SVP4, A0A3Q9SYY1, A0A3Q9SYY8, A0A3Q9SYZ2, A0A3Q9SZ12, A0A3Q9SZ15, A0A3Q9SZ21, A0A3Q9SZ22, A0A3Q9SZ29, A0A3Q9SZ30, A0A3Q9SZ36, A0A3Q9SZ41, A0A3Q9SZQ4, A0A3Q9SZR5, A0A3Q9SZS8, A0A3Q9SZT6, A0A3Q9SZX9, A0A3Q9SZY6, A0A3Q9SZZ7, A0A3Q9T1P4, A0A3Q9T1Q3, A0A3T0NKY9, A0A3T0NKZ0, A0A3T0NKZ1, A0A3T0NKZ2, A0A3T0NKZ3, A0A3T0NKZ5, A0A3T0NKZ7, A0A3T0NKZ9, A0A3T0NL00, A0A3T0NL27 metalloprotease GP63 is the major Leishmania surface antigen. It has multiple functions required for the survival of the parasite. Metalloprotease GP63 is encoded by multiple genes and their copy numbers vary considerably between different species. A greater role for the sequence variation found among the chromosome 10 GP63 genes is possibly related to the pathogenesis of Leishmania braziliensis and closely related species within the mammalian host
physiological function
the enzyme is involved in the degradation and cleavage of many biological molecules as kappa-B nuclear factor, fibronectin, tyrosine phosphatases. GP63 is capable of inhibiting the activity of the complement system and reduces the host's immune functions, allowing the survival of the parasite and its dissemination
physiological function
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the enzyme is involved in the degradation and cleavage of many biological molecules as kappa-B nuclear factor, fibronectin, tyrosine phosphatases. GP63 is capable of inhibiting the activity of the complement system and reduces the host's immune functions, allowing the survival of the parasite and its dissemination
physiological function
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the enzyme is involved in the degradation and cleavage of many biological molecules as kappa-B nuclear factor, fibronectin, tyrosine phosphatases. GP63 is capable of inhibiting the activity of the complement system and reduces the immune functions of the host, allowing the survival of the parasite and its dissemination
physiological function
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the enzyme is involved in the degradation and cleavage of many biological molecules as kappa-B nuclear factor, fibronectin, tyrosine phosphatases. GP63 is capable of inhibiting the activity of the complement system and reduces the immune functions of the host, allowing the survival of the parasite and its dissemination
physiological function
the enzyme is involved in the degradation and cleavage of many biological molecules as kappa-B nuclear factor, fibronectin, tyrosine phosphatases. GP63 is capable of inhibiting the activity of the complement system and reduces the immune functions of the host, allowing the survival of the parasite and its dissemination
additional information
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Herpetomonas samuelpessoai cells are able to colonize the gut of Aedes aegypti, but the pretreatment of gut cells with purified leishmanolysin-like protein drastically diminishes the adhesion, overview. The expression of surface leishmanolysin in Herpetomonas samuelpessoai cells is drastically enhanced after passage in Aedes aegypti
additional information
homology modeling and structure-function relationship of GP63, overview
additional information
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the cathelicidin bovine myeloid antimicrobial peptide 28, BMAP-28, has broad antimicrobial activities and confers protection in animal models of bacterial infection or sepsis. BMAP-28 isomers,i.e. the D-amino acid form D-BMAP-28 and the retro-inverso form RI-BMAP-28, are resistant against GP63 protease activity and act as anti-leishmanial agents against the promastigote and amastigote intracellular Leishmania major lifecycle stages, overview
additional information
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homology modeling and structure-function relationship of GP63, overview
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additional information
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the cathelicidin bovine myeloid antimicrobial peptide 28, BMAP-28, has broad antimicrobial activities and confers protection in animal models of bacterial infection or sepsis. BMAP-28 isomers,i.e. the D-amino acid form D-BMAP-28 and the retro-inverso form RI-BMAP-28, are resistant against GP63 protease activity and act as anti-leishmanial agents against the promastigote and amastigote intracellular Leishmania major lifecycle stages, overview
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brenda
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brenda
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Leishmania major (P08148)
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