Inflammatory effects of snake venom myotoxic phospholipases A2
Snake venom phospholipases A2 (PLA2) show a remarkable functional diversity. Among
their toxic activities, some display the ability to cause rapid necrosis of skeletal muscle fibers …
their toxic activities, some display the ability to cause rapid necrosis of skeletal muscle fibers …
Chemical modifications of phospholipases A2 from snake venoms: effects on catalytic and pharmacological properties
AM Soares, JR Giglio - Toxicon, 2003 - Elsevier
Phospholipases A2 (PLA2s) constitute major components of snake venoms and have been
extensively investigated not only because they are very abundant in these venoms but …
extensively investigated not only because they are very abundant in these venoms but …
Structural and functional characterization of BnSP-7, a Lys49 myotoxic phospholipase A2 homologue from Bothrops neuwiedi pauloensis venom
AM Soares, R Guerra-Sá, CR Borja-Oliveira… - Archives of Biochemistry …, 2000 - Elsevier
BnSP-7, a Lys49 myotoxic phospholipase A2 homologue from Bothrops neuwiedi
pauloensis venom, was structurally and functionally characterized. Several biological …
pauloensis venom, was structurally and functionally characterized. Several biological …
Effects of aqueous extract of Casearia sylvestris (Flacourtiaceae) on actions of snake and bee venoms and on activity of phospholipases A2
The crude aqueous extract from the leaves of Casearia sylvestris, a plant found in Brazilian
open pastures, was assayed for its ability to inhibit phospholipase A2 (PLA2) activity and …
open pastures, was assayed for its ability to inhibit phospholipase A2 (PLA2) activity and …
Gallic acid anti-myotoxic activity and mechanism of action, a snake venom phospholipase A2 toxin inhibitor, isolated from the medicinal plant Anacardium humile
TR Costa, AF Francisco, FF Cardoso… - International journal of …, 2021 - Elsevier
Snakebite envenoming is the cause of an ongoing health crisis in several regions of the
world, particularly in tropical and neotropical countries. This scenario creates an urgent …
world, particularly in tropical and neotropical countries. This scenario creates an urgent …
Phospholipase A2 myotoxins from Bothrops snake venoms: structure-function relationship
AM Soares, MRM Fontes… - Current Organic Chemistry, 2004 - ingentaconnect.com
Phospholipases A2 constitute the major components from Bothrops snake venoms and have
been extensively investigated not only because they are relatively very abundant in these …
been extensively investigated not only because they are relatively very abundant in these …
[HTML][HTML] Size Matters: An Evaluation of the Molecular Basis of Ontogenetic Modifications in the Composition of Bothrops jararacussu Snake Venom
LA Freitas-de-Sousa, PG Nachtigall, JA Portes-Junior… - Toxins, 2020 - mdpi.com
Ontogenetic changes in venom composition have been described in Bothrops snakes, but
only a few studies have attempted to identify the targeted paralogues or the molecular …
only a few studies have attempted to identify the targeted paralogues or the molecular …
Systemic and local myotoxicity induced by snake venom group II phospholipases A2: comparison between crotoxin, crotoxin B and a Lys49 PLA2 homologue
The patterns of myotoxicity induced in mice by crotoxin, crotoxin B and a Lys49
phospholipase A2 (PLA2) homologue were compared. Lys49 PLA2-induced local …
phospholipase A2 (PLA2) homologue were compared. Lys49 PLA2-induced local …
Identification of the myotoxic site of the Lys49 phospholipase A2 from Agkistrodon piscivorus piscivorus snake venom: synthetic C-terminal peptides from Lys49, but …
CE Núñez, Y Angulo, B Lomonte - Toxicon, 2001 - Elsevier
Group II phospholipase A2 (PLA2) myotoxins found in the venoms of Crotalidae snakes can
be divided into 'Asp49'and 'Lys49'isoforms, the latter being considered catalytically-inactive …
be divided into 'Asp49'and 'Lys49'isoforms, the latter being considered catalytically-inactive …
Structural and functional characterization of an acidic platelet aggregation inhibitor and hypotensive phospholipase A2 from Bothrops jararacussu snake venom
SH Andrião-Escarso, AM Soares, MRM Fontes… - Biochemical …, 2002 - Elsevier
An acidic (pI∼ 4.5) phospholipase A2 (BthA-I-PLA2) was isolated from Bothrops jararacussu
snake venom by ion-exchange chromatography on a CM-Sepharose column followed by …
snake venom by ion-exchange chromatography on a CM-Sepharose column followed by …