Results 41 to 50 of about 34,979 (216)
Toxins, 2021 Bites from elapid snakes typically result in neurotoxic symptoms in snakebite victims. Neurotoxins are, therefore, often the focus of research relating to understanding the pathogenesis of elapid bites.
Taline D. Kazandjian +7 more
doaj +1 more source
Involvement of Nitric Oxide on Bothropoides insularis Venom Biological Effects on Murine Macrophages In Vitro [PDF]
, 2016 Viperidae venom has several local and systemic effects, such as pain, edema, inflammation, kidney failure and coagulopathy. Additionally, bothropic venom and its isolated components directly interfere on cellular metabolism, causing alterations such as ...
de Menezes, Ramon R. P. P. B. +1 more
core +2 more sources
Journal of Venomous Animals and Toxins including Tropical Diseases, 2022 Background: Several studies have been published on the characterization of Trimeresurus venoms. However, there is still limited information concerning the venom composition of Trimeresurus species distributed throughout Indonesia, which contributes to ...
Syahfitri Anita +11 more
doaj +1 more source
Integrated “omics” profiling indicates that miRNAs are modulators of the ontogenetic venom composition shift in the Central American rattlesnake, [PDF]
, 2013 Background Understanding the processes that drive the evolution of snake venom is a topic of great research interest in molecular and evolutionary toxinology. Recent studies suggest that ontogenetic changes in venom composition are genetically controlled
Angulo, Yamileth +10 more
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49. The Origin and Evolution of Metalloproteinases in the Venom of Snakes
Toxicon, 2012 Background: Snake venom metalloproteinases (SVMPs) are a pathologically-important, often major, toxin component of snake venoms, particularly in the venoms of viperid snakes. The SVMPs are members of the large multi-locus adamalysin gene family alongside ADAM (a disintegrin and metalloproteinase) and ADAMTS (ADAM with thrombospondin motifs) proteins ...
Casewell, N.R. +6 more
openaire +2 more sources
Hemorrhage Caused by Snake Venom Metalloproteinases: A Journey of Discovery and Understanding [PDF]
Toxins, 2016 The historical development of discoveries and conceptual frames for understanding the hemorrhagic activity induced by viperid snake venoms and by hemorrhagic metalloproteinases (SVMPs) present in these venoms is reviewed. Histological and ultrastructural tools allowed the identification of the capillary network as the main site of action of SVMPs ...
José Gutiérrez +3 more
openaire +5 more sources
Transcriptomic basis for an antiserum against Micrurus corallinus (coral snake) venom [PDF]
, 2009 Background Micrurus corallinus (coral snake) is a tropical forest snake belonging to the family Elapidae. Its venom shows a high neurotoxicity associated with pre- and post-synaptic toxins, causing diaphragm paralysis, which may result in death. In spite
Luciana I Leão +2 more
core +2 more sources
Toxins, 2018 Venom composition varies across snakes from all taxonomic levels and is influenced by the snakes’ age, habitat, diet, and sexual dimorphism. The present study reports the first in-depth investigation of venom composition in male and female Bothrops
Fernanda Gobbi Amorim +5 more
doaj +1 more source
The venom gland transcriptome of the Desert Massasauga Rattlesnake (): towards an understanding of venom composition among advanced snakes (Superfamily Colubroidea) [PDF]
, 2007 BACKGROUND: Snake venoms are complex mixtures of pharmacologically active proteins and peptides which belong to a small number of superfamilies. Global cataloguing of the venom transcriptome facilitates the identification of new families of toxins as ...
Kini, R. Manjunatha +2 more
core +4 more sources
Activation of snake venom metalloproteinases by a cysteine switch‐like mechanism [PDF]
FEBS Letters, 1993 The cDNAs of several snake venom zinc endopeptidases code for a putative propeptide, which includes the conserved cysteine‐containing sequence PKMCGVT. It has been suggested that binding of the cysteine thiol function to the active‐site zinc, resulting in inactivation of the catalytic domain, occurs in a mode similar to the ‘cysteine switch’ mechanism ...
Grams, Frank +4 more
openaire +2 more sources