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Antivenoms for Snakebite Envenomings
(2011-10)
Animal-derived antivenoms constitute the mainstay in the therapy of snakebite envenoming. Antivenoms are manufactured by immunizing animals, usually horses, with venoms from a single or several medically-relevant snake ...
Mecanismo de açao dos venenos de cobras corais
(2016)
Os venenos apresentam um importante papel fisiológico para as serpentes: são os fatores responsáveis pela subjugação das presas, iniciam e auxiliam sua digestão e constituem um mecanismo de defesa contra predadores/agressores, ...
Pitfalls to avoid when using phage display for snake toxins
(2017-02)
Antivenoms against bites and stings from snakes, spiders, and scorpions are associated with immunological side effects and high cost of production, since these therapies are still derived from the serum of hyper-immunized ...
The earless monitor lizard Lanthanotus borneensis – a venomous animal?
(2021)
Based on its mandibular gland secretion, the earless monitor lizard, Lanthanotus borneensis, has been considered a venomous animal like other members of the Toxicofera group, including Heloderma. In the present study, the ...
Phospholipases a2 from Viperidae snakes: Differences in membranotropic activity between enzymatically active toxin and its inactive isoforms
(Biochimica et Biophysica Acta - Biomembranes vol 1848: 463–468, 2015-02)
We describe the interaction of various phospholipases A2 (PLA2) from snake venoms of the family Viperidae
(Macrovipera lebetina obtusa, Vipera ursinii renardi, Bothrops asper) with giant unilamellar vesicles (GUVs)
composed ...
The Phospholipase A2 Homologues of Snake Venoms: Biological Activities and Their Possible Adaptive Roles
(2009)
A particular subgroup of toxins with phospholipase A2 (PLA2) structure, but devoid of this enzymatic activity, is commonly found in the venoms of snakes of the family Viperidae, and known as the PLA2 homologues. Among ...
Functional analysis of DM64, an antimyotoxic protein with immunoglobulin-like structure from Didelphis marsupialis serum
(2002-12-11)
Bothrops snake venoms are known to induce local tissue damage such as hemorrhage and myonecrosis. The opossum Didelphis marsupialis is resistant to these snake venoms and has natural venom inhibitors in its plasma. The aim ...
Venomic analysis of the poorly studied desert coral snake, Micrurus tschudii tschudii, supports the 3FTx/PLA2 dichotomy across Micrurus venoms
(2016)
The venom proteome of the poorly studied desert coral snake Micrurus tschudii tschudii
was unveiled using a venomic approach, which identified ¥38 proteins belonging to only four snake
venom protein families. The ...
Inhibition of the myotoxic activity of Bothrops aspermyotoxin II in mice by immunization with its synthetic 13-mer peptide 115-129
(1999)
The region comprising amino acid residues 115±129 of myotoxin II, a Lys49
phospholipase A2 from the venom of Bothrops asper, was previously shown to constitute a
heparin binding site, and to be associated with its toxic ...
Proteomic and toxicological profiling of the venom of Bothrocophias campbelli, a pitviper species from Ecuador and Colombia
(Toxicon 90, 2014)
Detailed snake venom proteomes for nearly a hundred species in different pitviper genera have accumulated using ‘venomics’ methodologies. However, venom composition for some lineages remains poorly known. Bothrocophias ...