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Importance of snake venom metalloproteinases in cell biology: effects on platelets, inflammatory and endothelial cells

Current pharmaceutical design, 2007-10, Vol.13 (28), p.2893

2007

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Collagen binding is a key factor for the hemorrhagic activity of snake venom metalloproteinases

Biochimie, 2008-03, Vol.90 (3), p.484-492

2008

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Jararhagin, a snake venom metalloproteinase, induces a specialized form of apoptosis (anoikis) selective to endothelial cells

Apoptosis (London), 2005-08, Vol.10 (4), p.851-861

2005

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BnP1, a novel P-I metalloproteinase from Bothrops neuwiedi venom: Biological effects benchmarking relatively to jararhagin, a P-III SVMP

Toxicon (Oxford), 2008, Vol.51 (1), p.54-65

2008

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Immunochemical and biological characterization of monoclonal antibodies against BaP1, a metalloproteinase from Bothrops asper snake venom

Toxicon (Oxford), 2010-11, Vol.56 (6), p.1059-1065

2010

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An alternative method to access in vitro the hemorrhagic activity of snake venoms

Toxicon (Oxford), 2008-03, Vol.51 (4), p.479-487

2008

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A National Implementation Project to Prevent Healthcare-Associated Infections in Intensive Care Units: A Collaborative Initiative Using the Breakthrough Series Model

Open forum infectious diseases, 2023-04, Vol.10 (4), p.ofad129-ofad129

2023

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Horse IgG isotypes and cross-neutralization of two snake antivenoms produced in Brazil and Costa Rica

Toxicon (Oxford), 2000-05, Vol.38 (5), p.633-644

2000

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Characterisation of local inflammatory response induced by Thalassophryne nattereri fish venom in a mouse model of tissue injury

Toxicon (Oxford), 2003-10, Vol.42 (5), p.499-507

2003

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Snake venom metalloproteinases: structure/function relationships studies using monoclonal antibodies

Toxicon (Oxford), 2003-12, Vol.42 (7), p.801-808

2003

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Phylogenetic conservation of a snake venom metalloproteinase epitope recognized by a monoclonal antibody that neutralizes hemorrhagic activity

Toxicon (Oxford), 2003-12, Vol.42 (7), p.809-816

2003

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BnPl, a novel P-I metalloproteinase from Bothrops neuwiedi venom : Biological effects benchmarking relatively to jararhagin, a P-III SVMP

Toxicon (Oxford), 2008, Vol.51 (1), p.54-65

2008

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PND-1186 FAK inhibitor selectively promotes tumor cell apoptosis in three-dimensional environments

Cancer biology & therapy, 2010-05, Vol.9 (10), p.764-777

2010

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Oral delivery of PND-1186 FAK inhibitor decreases tumor growth and spontaneous breast to lung metastasis in pre-clinical models

Cancer biology & therapy, 2010-05, Vol.9 (10), p.778-790

2010

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VEGF-Induced Vascular Permeability Is Mediated by FAK

Developmental cell, 2012-01, Vol.22 (1), p.146-157

2012

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Efficiency in the operational process: reduction of incorrect entries and guarantee of compliance in the rendering of accounts

Einstein (São Paulo, Brazil), 2018-11, Vol.16 (4), p.eGS4200-eGS4200

2018

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p190RhoGEF (Rgnef) Promotes Colon Carcinoma Tumor Progression via Interaction with Focal Adhesion Kinase

Cancer research (Chicago, Ill.), 2011-01, Vol.71 (2), p.360-370

2011

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Different regions of the class P-III snake venom metalloproteinase jararhagin are involved in binding to α2β1 integrin and collagen

Toxicon (Oxford), 2010-06, Vol.55 (6), p.1093-1099

2010

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Abstract 1204: FAK inhibition selectively promotes tumor cell apoptosis in three-dimensional environments and suppresses tumor cell metastasis

Cancer research (Chicago, Ill.), 2010-04, Vol.70 (8_Supplement), p.1204-1204

2010

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221. The Interaction of the Antitoxin DM43 with a Snake Venom Metalloproteinase Analyzed by Mass Spectrometry and Surface Plasmon Resonance

Toxicon (Oxford), 2012-08, Vol.60 (2), p.208-209

2012

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Abstract 389: Mice with kinase-dead FAK mutation in endothelial cells are protected from VEGF-induced permeability and are resistant to tumor cell metastasis

Cancer research (Chicago, Ill.), 2010-04, Vol.70 (8_Supplement), p.389-389

2010

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Different regions of the class P-III snake venom metalloproteinase jararhagin are involved in binding to a2b1 integrin and collagen

Toxicon (Oxford), 2010-06, Vol.55 (6), p.1093-1099

2010

Volltextzugriff (PDF)

The interaction of the antitoxin DM43 with a snake venom metalloproteinase analyzed by mass spectrometry and surface plasmon resonance

Journal of mass spectrometry., 2012-05, Vol.47 (5), p.567-573

2012

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Different regions of the class P-III snake venom metalloproteinase jararhagin are involved in binding to α 2β 1 integrin and collagen

Toxicon (Oxford), 2010, Vol.55 (6), p.1093-1099

2010

Volltextzugriff (PDF)

Different regions of the class P-III snake venom metalloproteinase jararhagin are involved in binding to alpha2beta1 integrin and collagen

Toxicon (Oxford), 2010-06, Vol.55 (6), p.1093-1099

2010

Volltextzugriff (PDF)

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Metalloproteinase
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Animal Poisons Toxicology. Antivenoms
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Bothrops Jararaca Venom
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Hemorrhage - Chemically Induced
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Amino Acid Sequence
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Importance of snake venom metalloproteinases in cell biology: effects on platelets, inflammatory and endothelial cells

Collagen binding is a key factor for the hemorrhagic activity of snake venom metalloproteinases

Jararhagin, a snake venom metalloproteinase, induces a specialized form of apoptosis (anoikis) selective to endothelial cells

BnP1, a novel P-I metalloproteinase from Bothrops neuwiedi venom: Biological effects benchmarking relatively to jararhagin, a P-III SVMP

Immunochemical and biological characterization of monoclonal antibodies against BaP1, a metalloproteinase from Bothrops asper snake venom

An alternative method to access in vitro the hemorrhagic activity of snake venoms

A National Implementation Project to Prevent Healthcare-Associated Infections in Intensive Care Units: A Collaborative Initiative Using the Breakthrough Series Model

Horse IgG isotypes and cross-neutralization of two snake antivenoms produced in Brazil and Costa Rica

Characterisation of local inflammatory response induced by Thalassophryne nattereri fish venom in a mouse model of tissue injury

Snake venom metalloproteinases: structure/function relationships studies using monoclonal antibodies

Phylogenetic conservation of a snake venom metalloproteinase epitope recognized by a monoclonal antibody that neutralizes hemorrhagic activity

BnPl, a novel P-I metalloproteinase from Bothrops neuwiedi venom : Biological effects benchmarking relatively to jararhagin, a P-III SVMP

PND-1186 FAK inhibitor selectively promotes tumor cell apoptosis in three-dimensional environments

Oral delivery of PND-1186 FAK inhibitor decreases tumor growth and spontaneous breast to lung metastasis in pre-clinical models

VEGF-Induced Vascular Permeability Is Mediated by FAK

Efficiency in the operational process: reduction of incorrect entries and guarantee of compliance in the rendering of accounts

p190RhoGEF (Rgnef) Promotes Colon Carcinoma Tumor Progression via Interaction with Focal Adhesion Kinase

Different regions of the class P-III snake venom metalloproteinase jararhagin are involved in binding to α2β1 integrin and collagen

Abstract 1204: FAK inhibition selectively promotes tumor cell apoptosis in three-dimensional environments and suppresses tumor cell metastasis

221. The Interaction of the Antitoxin DM43 with a Snake Venom Metalloproteinase Analyzed by Mass Spectrometry and Surface Plasmon Resonance

Abstract 389: Mice with kinase-dead FAK mutation in endothelial cells are protected from VEGF-induced permeability and are resistant to tumor cell metastasis

Different regions of the class P-III snake venom metalloproteinase jararhagin are involved in binding to a2b1 integrin and collagen

The interaction of the antitoxin DM43 with a snake venom metalloproteinase analyzed by mass spectrometry and surface plasmon resonance

Different regions of the class P-III snake venom metalloproteinase jararhagin are involved in binding to α 2β 1 integrin and collagen

Different regions of the class P-III snake venom metalloproteinase jararhagin are involved in binding to alpha2beta1 integrin and collagen

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