Results 121 to 130 of about 32,635 (169)

Enhancing Deinagkistrodon acutus antivenom potency through acutolysin A-targeted antibody supplementation. [PDF]

PLoS Negl Trop Dis
Liu CC, Chou YS, Yang YX, Hsiao YC, Chu LJ, Yang C, Yan Z, Peng R, Chao HY, Li MX, Wu CJ.   +10 more
europepmc   +1 more source

Snakebite-induced severe varicella: Exploring venom-related immune dysregulation in a case report. [PDF]

JAAD Case Rep
Wang Y, Wu Y, Ma Y.
europepmc   +1 more source

Snake envenomation in veterinary medicine: comparative insights and emerging therapies. [PDF]

Front Vet Sci
Migliorisi A, Johnson T, Nelson T, Elane GL, Ueda Y, Hobbs KJ.   +5 more
europepmc   +1 more source

Comparative in vitro immunoreactivity and protein analysis of Trimeresurus albolabris and Tropidolaemus wagleri venoms. [PDF]

Sci Rep
Reamtong O, Pearngam P, Laoungbua P, Sitprija S, Thiangtrongjit T, Srisuk G, Vasaruchapong T, Khow O, Noiphrom J, Chaiyabutr N, Chanhome L, Kumkate S.   +11 more
europepmc   +1 more source

Epitope-based antibody development against metalloproteinases and phospholipases A₂ from <i>Deinagkistrodon acutus</i> venom. [PDF]

J Venom Anim Toxins Incl Trop Dis
Zhu H, Pan Y, Tai Z, Wang M, Liu X, Yu X, He Q.   +6 more
europepmc   +1 more source

Biochemical characterisation and substrate-specific proteolytic diversity of venom metalloproteinases in African puff adders. [PDF]

Toxicon X
Wilkinson MC, Modahl CM, Waterhouse DTK, Saviola A, Albulescu LO, Tianyi FL, Kazandjian TD, Wüster W, Theart F, Oluoch GO, Harrison RA, Casewell NR.   +11 more
europepmc   +1 more source

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Evidence for heterogeneous forms of the snake venom metalloproteinase jararhagin: a factor contributing to snake venom variability

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.
Solange M T Serrano, Anthony Sion David, Ana Maria Moura-Da-Silva   +2 more
exaly   +3 more sources

Isolation and cloning of a metalloproteinase from king cobra snake venom

Toxicon, 2007
A 50 kDa fibrinogenolytic protease, ohagin, from the venom of Ophiophagus hannah was isolated by a combination of gel filtration, ion-exchange and heparin affinity chromatography. Ohagin specifically degraded the alpha-chain of human fibrinogen and the proteolytic activity was completely abolished by EDTA, but not by PMSF, suggesting it is a ...
Wen-Hui Lee
exaly   +3 more sources

Snake venom metalloproteinases

Toxicon, 2013
Recent proteomic analyses of snake venoms show that metalloproteinases represent major components in most of the Crotalid and Viperid venoms. In this chapter we discuss the multiple activities of the SVMPs. In addition to hemorrhagic activity, members of the SVMP family also have fibrin(ogen)olytic activity, act as prothrombin activators, activate ...
Francis S, Markland, Stephen, Swenson
openaire   +2 more sources

Hemorrhagic metalloproteinases from snake venoms

Pharmacology & Therapeutics, 1994
One of the more significant consequences of crotalid envenomation is hemorrhage. Over the past 50 years of investigation, it is clear that the primary factors responsible for hemorrhage are metalloproteinases present in the venom of these snakes.
J B, Bjarnason, J W, Fox
openaire   +2 more sources