Results 141 to 150 of about 32,635 (169)

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
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

BJ46a, a snake venom metalloproteinase inhibitor

European Journal of Biochemistry, 2001
Fractionation of the serum of the venomous snake Bothrops jararaca with (NH4)2SO4, followed by phenyl‐Sepharose and C4‐reversed phase chromatographies, resulted in the isolation of the anti‐hemorrhagic factor BJ46a. BJ46a is a potent inhibitor of the SVMPs atrolysin C (class P‐I) and jararhagin (P‐III) proteolytic activities and B.
R H, Valente, B, Dragulev, J, Perales, J W, Fox, G B, Domont   +4 more
openaire   +2 more sources

Snake Venom Metalloproteinases

2021
Charlotte A. Dawson, Stuart Ainsworth, Laura-Oana Albulescu, Nicholas R. Casewell   +3 more
openaire   +1 more source

Synthetic and endogenous inhibitors of snake venom metalloproteinases.

Biomedica biochimica acta, 1992
The venoms of most Crotalidae snakes contain metalloproteinases which are the agents responsible for the production of venom-induced hemorrhage via proteolytic destruction of capillary basement membranes. Prevention of hemorrhage by administration of antiserum is generally not totally effective against damage at the site of envenomation.
A, Robeva, V, Politi, J D, Shannon, J B, Bjarnason, J W, Fox   +4 more
openaire   +1 more source

Snake Venom Matrix Metalloproteinases (svMMPs)

2021
Inácio L. M. Junqueira-de-Azevedo, Juan David Bayona-Serrano   +1 more
openaire   +1 more source

BthMP: a new weakly hemorrhagic metalloproteinase from Bothrops moojeni snake venom

Toxicon, 2009
Carolina Petri Bernardes, Fabio Oliveira, Andreimar M Soares   +2 more
exaly  

Inflammatory effects of BaP1 a metalloproteinase isolated from Bothrops asper snake venom: Leukocyte recruitment and release of cytokines

Toxicon, 2006
Cristina Fernandes, JOSÉ Maria Gutierrez, Stella Zamuner   +2 more
exaly