Results 181 to 190 of about 34,979 (216)

Timeline of key events in snake venom metalloproteinase research

Journal of Proteomics, 2009
It is reasonable to state that snake venom toxinology has been actively pursued for at least the past 400 to 500 years. Early on it was appreciated that the venoms of the Viperidae produced profound local effects, notably hemorrhage. For the past 100 years, with the advent of modern chemistry and biochemistry significant progress has been gained ...
Jay W, Fox, Solange M T, Serrano
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Platelets as targets of snake venom metalloproteinases

Toxicon, 2005
For centuries snake venoms have been known to interfere with haemostasis and this is now known basically due either to toxins activating/inhibiting clotting factors, having effects on blood vessels or interfering with platelet function. In this short review, the interaction of one major group of toxins, the snake venom metalloproteinases, with ...
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Molecular characterisation of endogenous snake venom metalloproteinase inhibitors

Biochemical and Biophysical Research Communications, 2008
Viper venoms contain one of the most potent mixtures of proteases in natural existence and yet the venom gland and proteins in this mixture are refractory to degradation. Here we demonstrate that the sub-10-kDa components of venom from two African viper species (Echis ocellatus and Cerastes cerastes cerastes) are predominantly composed of the tri ...
Wagstaff, Simon C., Favreau, Philippe, Cheneval, Olivier, Laing, Gavin D., Wilkinson, Mark C., Miller, Rebecca L., Stöcklin, Reto, Harrison, Robert A.   +7 more
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On the ancestral recruitment of metalloproteinases into the venom of snakes

Toxicon, 2012
Tracing the evolutionary history of proteins can reveal insights into gene alterations responsible for changes in structure and function. Here, the origin of snake venom metalloproteinases was rigorously reassessed using phylogenetics and the reconstruction of ancestral sequences.
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Angiostatin-like molecules are generated by snake venom metalloproteinases

Biochemical and Biophysical Research Communications, 2002
Angiostatin is a plasminogen-derived anti-angiogenic factor composed of its first four kringle structures. This molecule is generated by proteolytic cleavage of plasminogen by some proteolytic enzymes in vitro. Since venoms of viper snakes are a rich source of both serine- and metalloproteinase, we hypothesized that angiostatin-like polypeptides could ...
Paulo Lee, Ho, Solange Maria de Toledo, Serrano, Ana Marisa, Chudzinski-Tavassi, Ana Maria, Moura da Silva, Reinhard, Mentele, Cristina, Caldas, Maria Luiza Vilela, Oliva, Isabel Fátima Correia, Batista, Maria Leonor Sarno de, Oliveira   +8 more
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Insights into the mechanism of haemorrhage caused by snake venom metalloproteinases

Toxicon, 1996
Local and systemic haemorrhage are common consequences of crotaline and viperine envenoming. Several studies carried out using purified toxins have indicated that local haemorrhage can be attributed to a distinct class of venom metalloproteinases. Analyses of their cDNAs predict multi-domain enzymes, with an N-terminal metalloproteinase domain, a ...
A S, Kamiguti, C R, Hay, R D, Theakston, M, Zuzel   +3 more
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Doxycycline-Mediated Inhibition of Snake Venom Phospholipase and Metalloproteinase

Military Medicine
ABSTRACT Introduction Warfighters are exposed to life-threatening injuries daily and according to the Joint Trauma System Military Clinical Practice Guideline—Global Snake Envenomation Management snakebites are a concerning threat in all theaters of operation.
Daniel K Arens, Meaghan A Rose, Emelyn M Salazar, Merideth A Harvey, Eun Y Huh, April A Ford, Daniel W Thompson, Elda E Sanchez, Yoon Y Hwang   +8 more
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A New Family of Proteinases is Defined by Several Snake Venom Metalloproteinases

Biological Chemistry Hoppe-Seyler, 1992
Recently, the complete amino acid sequences have been determined for several snake venom metalloproteinases from the genera Crotalus, Trimeresurus and Lachesis of the Crotalidae family. Among these are both hemorrhagic and nonhemorrhagic metalloproteinases.
L A, Hite, J W, Fox, J B, Bjarnason
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Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases

Toxicon, 2005
The importance of proteinases in the pathologies associated with Viperid envenoming has long been appreciated. Over the past 40 years substantial research has clearly implicated metalloproteinases in the venom (snake venom metalloproteinases; SVMPs) as playing key roles in the development of such symptoms as hemorrhage, edema, hypotension, hypovolemia,
Jay W, Fox, Solange M T, Serrano
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Inhibition of a snake venom hemorrhagic metalloproteinase by human and ratα-macroglobulins

Toxicon, 1998
Jararafibrase I is a hemorrhagic metalloproteinase purified from Bothrops jararaca venom, which induces local hemorrhage by degrading the basement membrane components. The present study was undertaken to investigate the inhibition of jararafibrase I by human and rat serum proteinase inhibitors. The proteolytic activity of jararafibrase I was completely
K, Anai, M, Sugiki, E, Yoshida, M, Maruyama   +3 more
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