Results 191 to 200 of about 51,201 (249)
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Journal of biochemical and molecular toxicology, 2018
Classical antivenom therapy is unable to shield complications of viper bite and has limitations such as anaphylaxis and serum sickness. Snake venom metalloproteinases are responsible for local tissue damage and hemorrhage at the bitten site in viper ...
M. Choudhury +2 more
semanticscholar +1 more source
Classical antivenom therapy is unable to shield complications of viper bite and has limitations such as anaphylaxis and serum sickness. Snake venom metalloproteinases are responsible for local tissue damage and hemorrhage at the bitten site in viper ...
M. Choudhury +2 more
semanticscholar +1 more source
Triacontyl p-coumarate: An inhibitor of snake venom metalloproteinases
Phytochemistry, 2013Snake venom metalloproteinases (SVMPs) participate in a number of important biological, physiological and pathophysiological processes and are primarily responsible for the local tissue damage characteristic of viperid snake envenomations. The use of medicinal plant extracts as antidotes against animal venoms is an old practice, especially against ...
Mendes, M. M. +9 more
openaire +3 more sources
Unraveling the Processing and Activation of Snake Venom Metalloproteinases
Journal of Proteome Research, 2014Snake venom metalloproteinases (SVMPs) are zinc-dependent enzymes responsible for most symptoms of human envenoming. Like matrix metalloproteinases (MMPs) and a disintegrin and metalloproteinase (ADAM) proteins, SVMPs are synthesized as zymogens, and enzyme activation is regulated by hydrolysis of their prodomain, but the processing of SVMPs is still ...
José A, Portes-Junior +9 more
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Angiostatin-like molecules are generated by snake venom metalloproteinases
Biochemical and Biophysical Research Communications, 2002Angiostatin 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 +8 more
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Timeline of key events in snake venom metalloproteinase research
Journal of Proteomics, 2009It 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, 2005For 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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Archives of Biochemistry and Biophysics, 2003
The reprolysin subfamily of metalloproteinases includes snake venom metalloproteinases (SVMP) and mammalian disintegrin/metalloproteinase. These proteins are synthesized as zymogens and undergo proteolytic processing resulting in a variety of multifunctional proteins. Jararhagin is a P-III SVMP isolated from the venom of Bothrops jararaca.
A M, Moura-da-Silva +8 more
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The reprolysin subfamily of metalloproteinases includes snake venom metalloproteinases (SVMP) and mammalian disintegrin/metalloproteinase. These proteins are synthesized as zymogens and undergo proteolytic processing resulting in a variety of multifunctional proteins. Jararhagin is a P-III SVMP isolated from the venom of Bothrops jararaca.
A M, Moura-da-Silva +8 more
openaire +2 more sources