Haemostatically active proteins in snake venoms
T Sajevic, A Leonardi, I Križaj - Toxicon, 2011 - Elsevier
Snake venom proteins that affect the haemostatic system can cause (a) lowering of blood
coagulability,(b) damage to blood vessels, resulting in bleeding,(c) secondary effects of …
coagulability,(b) damage to blood vessels, resulting in bleeding,(c) secondary effects of …
Snake venom metalloproteinases: structure, function and relevance to the mammalian ADAM/ADAMTS family proteins
S Takeda, H Takeya, S Iwanaga - … et Biophysica Acta (BBA)-Proteins and …, 2012 - Elsevier
Metalloproteinases are among the most abundant toxins in many Viperidae venoms. Snake
venom metalloproteinases (SVMPs) are the primary factors responsible for hemorrhage and …
venom metalloproteinases (SVMPs) are the primary factors responsible for hemorrhage and …
Domain loss facilitates accelerated evolution and neofunctionalization of duplicate snake venom metalloproteinase toxin genes
NR Casewell, SC Wagstaff, RA Harrison… - Molecular biology …, 2011 - academic.oup.com
Gene duplication is a key mechanism for the adaptive evolution and neofunctionalization of
gene families. Large multigene families often exhibit complex evolutionary histories as a …
gene families. Large multigene families often exhibit complex evolutionary histories as a …
Synergistic strategies of predominant toxins in snake venoms
S Xiong, C Huang - Toxicology letters, 2018 - Elsevier
Synergism is a significant phenomenon present in snake venoms that may be an evolving
strategy to potentiate toxicities. Synergism exists between different toxins or toxin complexes …
strategy to potentiate toxicities. Synergism exists between different toxins or toxin complexes …
Functional proteomic analyses of Bothrops atrox venom reveals phenotypes associated with habitat variation in the Amazon
LF Sousa, JA Portes-Junior, CA Nicolau… - Journal of …, 2017 - Elsevier
Venom variability is commonly reported for venomous snakes including Bothrops atrox.
Here, we compared the composition of venoms from B. atrox snakes collected at Amazonian …
Here, we compared the composition of venoms from B. atrox snakes collected at Amazonian …
The role of platelets in hemostasis and the effects of snake venom toxins on platelet function
MR de Queiroz, BB de Sousa, DF da Cunha Pereira… - Toxicon, 2017 - Elsevier
The human body has a set of physiological processes, known as hemostasis, which keeps
the blood fluid and free of clots in normal vessels; in the case of vascular injury, this process …
the blood fluid and free of clots in normal vessels; in the case of vascular injury, this process …
[HTML][HTML] Batroxase, a new metalloproteinase from B. atrox snake venom with strong fibrinolytic activity
ACO Cintra, LGB De Toni, MA Sartim, JJ Franco… - Toxicon, 2012 - Elsevier
The structures and functional activities of metalloproteinases from snake venoms have been
widely studied because of the importance of these molecules in envenomation. Batroxase …
widely studied because of the importance of these molecules in envenomation. Batroxase …
[HTML][HTML] Insights into the mechanisms involved in strong hemorrhage and dermonecrosis induced by atroxlysin-Ia, a PI-class snake venom metalloproteinase
LA Freitas-de-Sousa, M Colombini, M Lopes-Ferreira… - Toxins, 2017 - mdpi.com
Hemorrhage is the most prominent effect of snake venom metalloproteinases (SVMPs) in
human envenomation. The capillary injury is a multifactorial effect caused by hydrolysis of …
human envenomation. The capillary injury is a multifactorial effect caused by hydrolysis of …
[HTML][HTML] Investigating possible biological targets of Bj-CRP, the first cysteine-rich secretory protein (CRISP) isolated from Bothrops jararaca snake venom
ME Lodovicho, TR Costa, CP Bernardes, DL Menaldo… - Toxicology letters, 2017 - Elsevier
Cysteine-rich secretory proteins (CRISPs) are commonly described as part of the protein
content of snake venoms, nevertheless, so far, little is known about their biological targets …
content of snake venoms, nevertheless, so far, little is known about their biological targets …
Isolation and biological characterization of Batx-I, a weak hemorrhagic and fibrinogenolytic PI metalloproteinase from Colombian Bothrops atrox venom
A hemorrhagic metalloproteinase, named Batx-I, was isolated from the venom of Bothrops
atrox specimens (from Southeastern Colombian region) by a combination of CM-Sephadex …
atrox specimens (from Southeastern Colombian region) by a combination of CM-Sephadex …