Phospholipases A2inhibitors (PLIs) produced by venomous and non-venomous snakes play essentialrole in this resistance. These endogenous inhibitors may be classified by their fold in PLI , PLI andPLI . Phospholipases A2(PLA2s) develop myonecrosis in snake envenomation, a consequence that isnot efficiently neutralized by antivenom treatment. This work aimed to identify and characterize twoPLIs from Amazonian snake species, Bothrops atrox and Micrurus lemniscatus. Liver tissues RNA of speci-mens from each species were isolated and amplified by RT-PCR using PCR primers based on known PLI gene sequences, followed by cloning and sequencing of amplified fragments. Sequence similarity studiesshowed elevated identity with inhibitor PLI gene sequen...
Bothrops snake venoms contain a variety of phospholipases (PLA(2)) some of which are myotoxic. In th...
A new phospholipase A2 (PLA2)-inhibitory protein was isolated from the plasma of Atropoides nummifer...
Snake venom phospholipases A2 (PLA2) share high sequence identities and a conserved structural scaff...
Phospholipases A(2) (PLA(2)s) are important components of Bothrops snake venoms, that can induce sev...
Phospholipases A(2) (PLA(2)s) are important components of Bothrops snake venoms, that can induce sev...
Phospholipases A(2) (PLA(2)s) are important components of Bothrops snake venoms, that can induce sev...
Abstract The blood plasma of numerous snake species naturally comprises endogenous phospholipase A2 ...
Plasma in several organisms has components that promote resistance to envenomation by inhibiting spe...
Bothrops diporus, previously considered a subspecies of the B. neuwiedi complex, is a medically rele...
Bothrops mattogrossensis snake is widely distributed throughout eastern South America and is respons...
Phospholipases A(2) (PLA(2)s) are commonly found in snake venoms from Viperidae, Hydrophidae and Ela...
Phospholipases A2 (PLA2) are enzymes acting on the cell membrane phospholipids resulting in fatty ac...
Myotoxic phospholipases A2 (PLA2s; group II) account for most of the muscle-tissue damage that resul...
Secretory phospholipase A2 (sPLA2) is known as a major component of snake venoms and displays higher...
Secretory phospholipase A2 (sPLA2) is known as a major component of snake venoms and displays higher...
Bothrops snake venoms contain a variety of phospholipases (PLA(2)) some of which are myotoxic. In th...
A new phospholipase A2 (PLA2)-inhibitory protein was isolated from the plasma of Atropoides nummifer...
Snake venom phospholipases A2 (PLA2) share high sequence identities and a conserved structural scaff...
Phospholipases A(2) (PLA(2)s) are important components of Bothrops snake venoms, that can induce sev...
Phospholipases A(2) (PLA(2)s) are important components of Bothrops snake venoms, that can induce sev...
Phospholipases A(2) (PLA(2)s) are important components of Bothrops snake venoms, that can induce sev...
Abstract The blood plasma of numerous snake species naturally comprises endogenous phospholipase A2 ...
Plasma in several organisms has components that promote resistance to envenomation by inhibiting spe...
Bothrops diporus, previously considered a subspecies of the B. neuwiedi complex, is a medically rele...
Bothrops mattogrossensis snake is widely distributed throughout eastern South America and is respons...
Phospholipases A(2) (PLA(2)s) are commonly found in snake venoms from Viperidae, Hydrophidae and Ela...
Phospholipases A2 (PLA2) are enzymes acting on the cell membrane phospholipids resulting in fatty ac...
Myotoxic phospholipases A2 (PLA2s; group II) account for most of the muscle-tissue damage that resul...
Secretory phospholipase A2 (sPLA2) is known as a major component of snake venoms and displays higher...
Secretory phospholipase A2 (sPLA2) is known as a major component of snake venoms and displays higher...
Bothrops snake venoms contain a variety of phospholipases (PLA(2)) some of which are myotoxic. In th...
A new phospholipase A2 (PLA2)-inhibitory protein was isolated from the plasma of Atropoides nummifer...
Snake venom phospholipases A2 (PLA2) share high sequence identities and a conserved structural scaff...