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Information on EC 3.4.24.73 - jararhagin and Organism(s) Bothrops jararaca and UniProt Accession P30431
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3.4.24.73 jararhaginSpecify your search results
Word Map
- 3.4.24.73
- bothrops
- jararaca
- metalloproteinases
-
disintegrin-like
-
svmps
-
cysteine-rich
-
envenom
-
disintegrins
- viper
-
collagen-induced
- alpha2beta1
-
snakebite
- antivenoms
- marsupialis
- atrolysin
-
trigramin
- atrox
-
reprolysin
-
didelphis
-
hemorrhagins
- medicine
The taxonomic range for the selected organisms is: Bothrops jararaca
The expected taxonomic range for this enzyme is: Bothrops jararaca
The expected taxonomic range for this enzyme is: Bothrops jararaca
Reaction Schemes
Hydrolysis of -His10-/-Leu-, -Ala14-/-Leu-, -Tyr16-/-Leu-and -Phe24-/-Phe- bonds in insulin B chain
Synonyms
jararhagin, jararhagin-c, piii svmp, hemorrhagic svmp, jar-c, piii snake venom metalloproteinase, snake venom metalloproteinase-disintegrin, piii snake venom metalloprotease, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
HF2-proteinase
jararhagin-c
JF1
additional information
-
snake venom metalloproteinases are members of the reprolysin family of metalloproteinases
HF2-proteinase
-
-
-
-
jararhagin-c
-
consists of the disintegrin-like and cysteine-rich domains of jararhagin only
jararhagin-c
-
lacking the catalytic domain of enzymatically active jararhagin
JF1
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of -His10-/-Leu-, -Ala14-/-Leu-, -Tyr16-/-Leu-and -Phe24-/-Phe- bonds in insulin B chain
degradation of alpha- and beta-chains of fibrin and fibrinogen with very little degradation of the gamma-chains
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
160477-79-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha2 subunit I domain of the platelet surface alpha2beta1 integrin + H2O
?
-
-
-
-
?
alpha2-Plasmin inhibitor + H2O
Inactivated alpha2-plasmin inhibitor
-
-
-
?
FVNQHLCGSHLVEALYVCGERGFFYTPKA + H2O
FVNQHLCGSH + Lys-Val-Glu-Ala + Lys + YVCGERGF + FYTPKA
-
-
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin B-chain
-
cleavage at 4 peptide bonds
-
?
Type I collagen + H2O
?
bovine and chicken substrates, the enzyme binds with high affinity to the intact triple helix collagen structure affecting the collagen suprastructure
-
-
?
collagen XII + H2O
?
-
bovine substrate, the substrate contains Von Willebrand factor A1 domains, which interacts with the enzyme's cysteine-rich domain promoting site-specific proteolysis, jararhagin cleaves the substrate at or near the A1 domains, cleavage pattern, overview
-
-
?
collagen XII + H2O
?
-
the substrate contains Von Willebrand factor A1 domains, which interacts with the enzyme's cysteine-rich domain promoting site-specific proteolysis
-
-
?
collagen XIV + H2O
?
-
bovine substrate, a fibril-associated collagen with interrupted triple helices, the substrate contains Von Willebrand factor A1 domains, which interacts with the enzyme's cysteine-rich domain promoting site-specific proteolysis, jararhagin cleaves the substrate at or near the A1 domains, cleavage pattern, overview
-
-
?
collagen XIV + H2O
?
-
the substrate contains Von Willebrand factor A1 domains, which interacts with the enzyme's cysteine-rich domain promoting site-specific proteolysis
-
-
?
matrilin 1 + H2O
?
-
bovine substrate, the substrate contains Von Willebrand factor A1 domains, which interacts with the enzyme's cysteine-rich domain promoting site-specific proteolysis, jararhagin cleaves the substrate at or near the A1 domains
-
-
?
matrilin 1 + H2O
?
-
the substrate contains Von Willebrand factor A1 domains, which interacts with the enzyme's cysteine-rich domain promoting site-specific proteolysis
-
-
?
matrilin 3 + H2O
?
-
the substrate contains Von Willebrand factor A1 domains, which interacts with the enzyme's cysteine-rich domain promoting site-specific proteolysis
-
-
?
matrilin 3 + H2O
?
-
the substrate contains Von Willebrand factor A1 domains, which interacts with the enzyme's cysteine-rich domain promoting site-specific proteolysis, jararhagin cleaves the substrate at or near the A1 domains, cleavage pattern, overview
-
-
?
matrilin 4 + H2O
?
-
the substrate contains Von Willebrand factor A1 domains, which interacts with the enzyme's cysteine-rich domain promoting site-specific proteolysis
-
-
?
matrilin 4 + H2O
?
-
the substrate contains Von Willebrand factor A1 domains, which interacts with the enzyme's cysteine-rich domain promoting site-specific proteolysis, jararhagin cleaves the substrate at or near the A1 domains
-
-
?
von Willebrand factor + H2O
?
-
binding between jararhagin cysteine-rich domain and Von Willebrand factor A1 domain leads to inhibition of Von Willebrand factor platelet aggregation activity, overview
-
-
?
von Willebrand factor + H2O
?
-
Von Willebrand factor A1 domain interacts with the enzyme's cysteine-rich domain, which promotes site-specific proteolysis, jararhagin cleaves the substrate at sites adjacent to the A1 domain
-
-
?
von Willebrand factor + H2O
?
-
mapping of Von Willebrand factor A domain binding sites on the enzyme's cysteine-rich domain, binding between jararhagin cysteine-rich domain and Von Willebrand factor A1 domain, protein-protein interactions, molecular modeling, overview
-
-
?
von Willebrand factor + H2O
?
-
Von Willebrand factor A1 domain interacts with the enzyme's cysteine-rich domain, which promotes site-specific proteolysis, jararhagin cleaves the substrate at or near the A1 domains
-
-
?
additional information
?
-
the enzyme is a hemorrhagic P-III snake venom metalloproteinase, collagen binding is a key factor for the hemorrhagic activity of snake venom metalloproteinases, the multidomain enzyme binds to collagen via disintegrin-like and cysteine-rich domains allocate motifs that enable catalytic degradation of extracellular matrix components leading to disruption of capillary vessels
-
-
?
additional information
?
-
the enzyme inhibits collagen-induced platelet aggregation with an IC50 value of 300 nM
-
-
?
additional information
?
-
-
possesses proteolytic and hemorrhagic activity
-
-
?
additional information
?
-
-
possesses proteolytic and hemorrhagic activity
-
-
?
additional information
?
-
-
possesses proteolytic and hemorrhagic activity
-
-
?
additional information
?
-
-
possesses proteolytic and hemorrhagic activity
-
-
?
additional information
?
-
-
in vitro induces strongly fibrinolytic activity in plasma of guinea pig, horse, dog, rabbit and human (not in plasma of rat, mouse, hamster, goat, sheep, pig or bovine), it increases tissue-type plasminogen activator activity by dissociation of a complex of this activator with type 1 plasminogen activator inhibitor and inactivation of alpha2-plasmin inhibitor
-
-
?
additional information
?
-
-
main hemorrhagic metalloproteinase in Bothrops jararaca venom
-
-
?
additional information
?
-
-
jararhagin blocks type I collagen-induced platelet aggregation by binding to the alpha2beta1 integrin and inhibiting collagen-mediated intracellular signaling events, in contrast to observation in platelets enzyme binding to the integrin receptor alpha2beta1 in fibroblasts produces collagen-like cell signaling events such as up-regulation of matrix metalloproteinase-1 and membrane-type matrix metalloproteinase-1, in fibroblasts enzyme functions as a collagen-mimetic substrate that binds to and activates integrins
-
?
additional information
?
-
-
low doses of the toxin jararhagin induce interstitial edema and increase the metabolic rate and red blood cells in Swiss mice, histology of lungs and kidney, overview, at high doses it causes hemorrhage, inflammation, necrosis and edema
-
-
?
additional information
?
-
-
the enzyme is a hemorrhagic P-III snake venom metalloproteinase
-
-
?
additional information
?
-
-
the enzyme is a P-III snake venom metalloproteinase and a potent hemorrhagin
-
-
?
additional information
?
-
-
the enzyme is a P-III snake venom metalloproteinase and a potent hemorrhagin, it causes capillary vessel basement membrane damage in vitro and in vivo, degradation of extracellular matrix components in skeletal muscle cells and endothelial cells, overview
-
-
?
additional information
?
-
-
the enzyme is a P-III snake venom metalloproteinase and a potent hemorrhagin, it induces strong pro-inflammatory response increasing the number of rolling leukocytes within capillary vessels, jararhagin induces apoptosis and release of angiostatin-like peptides in human endothelial cells, overview
-
-
?
additional information
?
-
-
the enzyme's disintegrin-like/cysteine-rich domains target it to to key extracellular matrix proteins or cell surface proteins, overview
-
-
?
additional information
?
-
-
the snake venom hemorrhagic metalloproteinase causes capillary vessel basement membrane damage in vitro and in vivo, overview
-
-
?
additional information
?
-
-
jararhagin toxin binding to collagen appears to be sufficient to inhibit collagen-induced platelet aggregation in the human host
-
-
?
additional information
?
-
-
different regions of the class P-III snake venom metalloproteinase jararhagin are involved in binding to alpha2beta1 integrin, a collagen receptor, and collagen from host K-562 cells, analysis using monoclonal antibodies and recombinant jararhagin fragments, jararhagin binding to collagen and alpha2beta1 integrin occurs by two independent motifs located on disintegrin-like and cysteine-rich domains, respectively, detailed overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
von Willebrand factor + H2O
?
-
binding between jararhagin cysteine-rich domain and Von Willebrand factor A1 domain leads to inhibition of Von Willebrand factor platelet aggregation activity, overview
-
-
?
von Willebrand factor + H2O
?
-
Von Willebrand factor A1 domain interacts with the enzyme's cysteine-rich domain, which promotes site-specific proteolysis, jararhagin cleaves the substrate at sites adjacent to the A1 domain
-
-
?
additional information
?
-
the enzyme is a hemorrhagic P-III snake venom metalloproteinase, collagen binding is a key factor for the hemorrhagic activity of snake venom metalloproteinases, the multidomain enzyme binds to collagen via disintegrin-like and cysteine-rich domains allocate motifs that enable catalytic degradation of extracellular matrix components leading to disruption of capillary vessels
-
-
?
additional information
?
-
-
main hemorrhagic metalloproteinase in Bothrops jararaca venom
-
-
?
additional information
?
-
-
jararhagin blocks type I collagen-induced platelet aggregation by binding to the alpha2beta1 integrin and inhibiting collagen-mediated intracellular signaling events, in contrast to observation in platelets enzyme binding to the integrin receptor alpha2beta1 in fibroblasts produces collagen-like cell signaling events such as up-regulation of matrix metalloproteinase-1 and membrane-type matrix metalloproteinase-1, in fibroblasts enzyme functions as a collagen-mimetic substrate that binds to and activates integrins
-
?
additional information
?
-
-
low doses of the toxin jararhagin induce interstitial edema and increase the metabolic rate and red blood cells in Swiss mice, histology of lungs and kidney, overview, at high doses it causes hemorrhage, inflammation, necrosis and edema
-
-
?
additional information
?
-
-
the enzyme is a hemorrhagic P-III snake venom metalloproteinase
-
-
?
additional information
?
-
-
the enzyme is a P-III snake venom metalloproteinase and a potent hemorrhagin
-
-
?
additional information
?
-
-
the enzyme is a P-III snake venom metalloproteinase and a potent hemorrhagin, it causes capillary vessel basement membrane damage in vitro and in vivo, degradation of extracellular matrix components in skeletal muscle cells and endothelial cells, overview
-
-
?
additional information
?
-
-
the enzyme is a P-III snake venom metalloproteinase and a potent hemorrhagin, it induces strong pro-inflammatory response increasing the number of rolling leukocytes within capillary vessels, jararhagin induces apoptosis and release of angiostatin-like peptides in human endothelial cells, overview
-
-
?
additional information
?
-
-
jararhagin toxin binding to collagen appears to be sufficient to inhibit collagen-induced platelet aggregation in the human host
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Zinc
additional information
additional information
the enzyme is a P-III snake venom metalloproteinase
additional information
-
the enzyme is a P-III snake venom metalloproteinase
additional information
-
the enzyme is a P-III snake venom metalloproteinase
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
BJ46a
-
SVMP inhibitor forming a monovalent complex with jararhagin thus inhibiting its hemorrhagic and catalytic activities
-
DM 43
-
SVMP inhibitor isolated from the venom of Didelphis marsupialis forming stable complexes with jararhagin thus inhibiting its hemorrhagic, fibrinolytic and proteolytic activities
-
PO41
-
SVMP inhibitor isolated from the venom of Philander opossum forming stable complexes with jararhagin thus inhibiting its hemorrhagic, fibrinolytic and proteolytic activities
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic evaluation of the interaction of the enzyme with immobilized Von Willebrand factor A1 domains, overview
-
additional information
additional information
-
quantitative analysis of the interaction of enzyme with Von Willebrand factor, VWF, A1 domains, overview
-
additional information
additional information
-
quantitative binding analysis of synthetic peptides designed based on the sequence of the cysteine-rich domain of jararhagin to the substrate Von Willebrand factor, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
analysis of the inhibitory effect of a short cyclic peptide derived from the snake toxin jararhagin, with specific amino acid sequence Arg-Lys-Lys-His, on the ability of alpha2 domain of integrin to bind triple helical collagen
additional information
-
jararhagin stimulates spreading, actin dynamics and neurite outgrowth in neuroblastoma cells, accompanied by the translocation of the Rac1 small GTPase to the cell membrane fraction
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
-
jararhagin toxin binding to collagen appears to be sufficient to inhibit collagen-induced platelet aggregation in the human host
physiological function
jararhagin 0.03 mg/ml upregulated genes TP53, CDKN1A, CDKN2A, CASP3, CASP5, CASP6, CASP8, and E-CDH in SKMel-28, and genes ITGB6, ITGB7, CASP3, TP53, and CDKN1B in mouse fibroblasts
physiological function
jararhagin induces strong hemorrhage accompanied by hydrolysis of collagen fibers in the hypodermis and a marked degradation of type IV collagen at the vascular basement membrane. Toxin accumulation near blood vessels leads to enhanced catalysis of basement membrane components, resulting in the strong hemorrhagic activity of jararhagin
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). VM3JA_BOTJA
571
0
63983
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28000
47000
-
calculation from amino acid sequence, deduced from mature jararhagin
50000
52000
additional information
-
deduced amino acid sequence compared with those of other toxins of the zinc metalloproteinases and disintegrin family
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
three-dimensional structure of jararhagin, structure-function relationship, molecular modeling and dynamics, comparison to berythractivase, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapour-diffusion technique, space group P2(1)2(1)2(1), unit-cell parameters a : 73.7 A, b : 100.3 A, c : 133.4 A
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Hi Trap phenyl Sepharose column chromatography and Mono-Q column chromatography
phenyl Superose column chromatography and Mono-Q column chromatography
synthetic peptides designed based on the sequence of the cysteine-rich domain of jararhagin are purified to homogeneity by gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
appropriate jararhagin concentration can have apoptotic and suppressant effects on SK-Mel-28 cells and can be used to develop potential anti-cancer drugs
medicine
-
useful tool for studying the molecular basis of collagen-induced cellular activities in human skin fibroblasts for comparison and contrast with other cell types
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mandelbaum, F.R.; Reichl, A.P.; Assakura, M.T.
Some physical and biochemical characteristics of HF2, one of the hemorrhagic factors in the venom of Bothrops jararaca
Anim. Plant Microb. Toxins (Proc. Int. Symp. ,4th, Meeting Date 1974) (Ohsaka, A. , Hayashi, K. , Sawai, Y. , eds. ) Plenum Press, N. Y.
1
111-121
1976
Bothrops jararaca
-
Assakura, A.T.; Reichl, A.P.; Mandelbaum, F.R.
Comparison of immunological, biochemical and biophysical properties of three hemorrhagic factors isolated from the venom of Bothrops jararaca (jararaca)
Toxicon
24
943-946
1986
Bothrops jararaca
Paine, M.J.I.; Desmond, H.P.; Theakston, R.D.G.; Crampton, J.M.
Purification, cloning, and molecular characterization of a high molecular weight hemorrhagic metalloprotease, jararhagin, from Bothrops jararaca venom. Insights into the disintegrin gene family
J. Biol. Chem.
267
22869-22876
1992
Bothrops jararaca
Sugiki, M.; Maruyama, M.; Yoshida, E.; Mihara, H.; Kamiguti, A.S.; Theakston, R.D.G.
Enhancement of plasma fibrinolysis in vitro by jararhagin, the main haemorrhagic metalloproteinase in Bothrops jararaca venom
Toxicon
33
1605-1617
1995
Bothrops jararaca
Maruyama, M.; Sugiki, M.; Yoshida, E.; Mihara, H.; Nakajima, N.
Purification and characterization of two fibrinolytic enzymes from Bothrops jararaca (jararaca) venom
Toxicon
30
853-864
1992
Bothrops jararaca
Kamiguti, A.S.; Desmond, H.P.; Theakston, R.D.G.; Hay, C.R.M.; Zuzel, M.
Ineffectiveness of the inhibition of the main haemorrhagic metalloproteinase from Bothrops jararaca venom by its only plasma inhibitor, alpha 2-macroglobulin
Biochim. Biophys. Acta
1200
307-314
1994
Bothrops jararaca
Souza, D.H.; Selistre-de-Araujo, H.S.; Moura-da-Silva, A.M.; Della-Casa, M.S.; Oliva, G.; Garratt, R.C.
Crystallization and preliminary X-ray analysis of jararhagin, a metalloproteinase/disintegrin from Bothrops jararaca snake venom
Acta Crystallogr. Sect. D
57
1135-1137
2001
Bothrops jararaca
Zigrino, P.; Kamiguti, A.S.; Eble, J.; Drescher, C.; Nischt, R.; Fox, J.W.; Mauch, C.
The reprolysin jararhagin, a snake venom metalloproteinase, functions as a fibrillar collagen agonist involved in fibroblast cell adhesion and signaling
J. Biol. Chem.
277
40528-40535
2002
Bothrops jararaca
Tanjoni, I.; Weinlich, R.; Della-Casa, M.S.; Clissa, P.B.; Saldanha-Gama, R.F.; de Freitas, M.S.; Barja-Fidalgo, C.; Amarante-Mendes, G.P.; Moura-da-Silva, A.M.
Jararhagin, a snake venom metalloproteinase, induces a specialized form of apoptosis (anoikis) selective to endothelial cells
Apoptosis
10
851-861
2005
Bothrops jararaca
Gallagher, P.; Bao, Y.; Serrano, S.M.; Laing, G.D.; Theakston, R.D.; Gutierrez, J.M.; Escalante, T.; Zigrino, P.; Moura-da-Silva, A.M.; Nischt, R.; Mauch, C.; Moskaluk, C.; Fox, J.W.
Role of the snake venom toxin jararhagin in proinflammatory pathogenesis: in vitro and in vivo gene expression analysis of the effects of the toxin
Arch. Biochem. Biophys.
441
1-15
2005
Bothrops jararaca
Schattner, M.; Fritzen, M.; Ventura, J.d.e.S.; de Albuquerque Modesto, J.C.; Pozner, R.G.; Moura-da-Silva, A.M.; Chudzinski-Tavassi, A.M.
The snake venom metalloproteases berythractivase and jararhagin activate endothelial cells
Biol. Chem.
386
369-374
2005
Bothrops jararaca
Garcia, L.T.; Parreiras e Silva, L.T.; Ramos, O.H.; Carmona, A.K.; Bersanetti, P.A.; Selistre-de-Araujo, H.S.
The effect of post-translational modifications on the hemorrhagic activity of snake venom metalloproteinases
Comp. Biochem. Physiol. C
138
23-32
2004
Bothrops jararaca
Laing, G.D.; Paine, M.J.
Jararhagin
Handbook of Proteolytic Enzymes (Barrett,A. J. ;Rawlings,N. D. ,Woessner)
1
654-656
2004
Bothrops jararaca
-
Costa, E.P.; Santos, M.F.
Jararhagin, a snake venom metalloproteinase-disintegrin, stimulates epithelial cell migration in an in vitro restitution model
Toxicon
44
861-870
2004
Bothrops jararaca
Laing, G.D.; Moura-da-Silva, A.M.
Jararhagin and its multiple effects on hemostasis
Toxicon
45
987-996
2005
Bothrops jararaca
Clissa, P.B.; Lopes-Ferreira, M.; Della-Casa, M.S.; Farsky, S.H.; Moura-da-Silva, A.M.
Importance of jararhagin disintegrin-like and cysteine-rich domains in the early events of local inflammatory response
Toxicon
47
591-596
2006
Bothrops jararaca
Pereira, A.L.; Fritzen, M.; Faria, F.; da Motta, G.; Chudzinski-Tavassi, A.M.
Releasing or expression modulating mediator involved in hemostasis by Berythractivase and Jararhagin (SVMPs)
Toxicon
47
788-796
2006
Bothrops jararaca
Escalante, T.; Shannon, J.; Moura-da-Silva, A.M.; Gutierrez, J.M.; Fox, J.W.
Novel insights into capillary vessel basement membrane damage by snake venom hemorrhagic metalloproteinases: a biochemical and immunohistochemical study
Arch. Biochem. Biophys.
455
144-153
2006
Bothrops jararaca
Pinto, A.F.; Terra, R.M.; Guimaraes, J.A.; Fox, J.W.
Mapping von Willebrand factor A domain binding sites on a snake venom metalloproteinase cysteine-rich domain
Arch. Biochem. Biophys.
457
41-46
2007
Bothrops jararaca
Moura-da-Silva, A.M.; Ramos, O.H.; Baldo, C.; Niland, S.; Hansen, U.; Ventura, J.S.; Furlan, S.; Butera, D.; Della-Casa, M.S.; Tanjoni, I.; Clissa, P.B.; Fernandes, I.; Chudzinski-Tavassi, A.M.; Eble, J.A.
Collagen binding is a key factor for the hemorrhagic activity of snake venom metalloproteinases
Biochimie
90
484-492
2008
Bothrops jararaca (P30431)
Serrano, S.M.; Wang, D.; Shannon, J.D.; Pinto, A.F.; Polanowska-Grabowska, R.K.; Fox, J.W.
Interaction of the cysteine-rich domain of snake venom metalloproteinases with the A1 domain of von Willebrand factor promotes site-specific proteolysis of von Willebrand factor and inhibition of von Willebrand factor-mediated platelet aggregation
FEBS J.
274
3611-3621
2007
Bothrops jararaca
Serrano, S.M.; Kim, J.; Wang, D.; Dragulev, B.; Shannon, J.D.; Mann, H.H.; Veit, G.; Wagener, R.; Koch, M.; Fox, J.W.
The cysteine-rich domain of snake venom metalloproteinases is a ligand for von Willebrand factor A domains: role in substrate targeting
J. Biol. Chem.
281
39746-39756
2006
Bothrops jararaca
Francisco, G.; Zara, F.J.; Maria, D.A.; Cruz-Neto, A.P.
Toxin jararhagin in low doses induces interstitial edema and increases the metabolic rate and red blood cells in mice
Toxicon
48
1060-1067
2006
Bothrops jararaca
Baldo, C.; Tanjoni, I.; Leon, I.R.; Batista, I.F.; Della-Casa, M.S.; Clissa, P.B.; Weinlich, R.; Lopes-Ferreira, M.; Lebrun, I.; Amarante-Mendes, G.P.; Rodrigues, V.M.; Perales, J.; Valente, R.H.; Moura-da-Silva, A.M.
BnP1, a novel P-I metalloproteinase from Bothrops neuwiedi venom: biological effects benchmarking relatively to jararhagin, a P-III SVMP
Toxicon
51
54-65
2008
Bothrops jararaca
Lambert, L.J.; Bobkov, A.A.; Smith, J.W.; Marassi, F.M.
Competitive interactions of collagen and a jararhagin-derived disintegrin peptide with the integrin alpha2-I domain
J. Biol. Chem.
283
16665-16672
2008
Bothrops jararaca
Costa, E.P.; Del Debbio, C.B.; Cintra, L.C.; da Fontoura Costa, L.; Hamassaki, D.E.; Santos, M.F.
Jararhagin, a snake venom metalloprotease-disintegrin, activates the Rac1 GTPase and stimulates neurite outgrowth in neuroblastoma cells
Toxicon
52
380-384
2008
Bothrops jararaca
Tanjoni, I.; Evangelista, K.; Della-Casa, M.S.; Butera, D.; Magalhaes, G.S.; Baldo, C.; Clissa, P.B.; Fernandes, I.; Eble, J.; Moura-da-Silva, A.M.
Different regions of the class P-III snake venom metalloproteinase jararhagin are involved in binding to alpha2beta1 integrin and collagen
Toxicon
55
1093-1099
2010
Bothrops jararaca
Baldo, C.; Jamora, C.; Yamanouye, N.; Zorn, T.M.; Moura-da-Silva, A.M.
Mechanisms of vascular damage by hemorrhagic snake venom metalloproteinases: tissue distribution and in situ hydrolysis
PLoS Negl. Trop. Dis.
4
e727
2010
Bothrops jararaca (P30431)
Klein, A.; Capitanio, J.S.; Maria, D.A.; Ruiz, I.R.
Gene expression in SK-Mel-28 human melanoma cells treated with the snake venom jararhagin
Toxicon
57
1-8
2011
Bothrops jararaca (P30431), Bothrops jararaca
Ferreira, B.A.; Deconte, S.R.; de Moura, F.B.R.; Tomiosso, T.C.; Clissa, P.B.; Andrade, S.P.; Araujo, F.A.
Inflammation, angiogenesis and fibrogenesis are differentially modulated by distinct domains of the snake venom metalloproteinase jararhagin
Int. J. Biol. Macromol.
119
1179-1187
2018
Bothrops jararaca (P30431), Bothrops jararaca
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