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Processo de obtenção dos peptídeos dímericos desCys11, Lys12, Lys13-(pBthTXI) K, [Trp3,5] des-Cys11, Lys12, Lys13- (pBthTX-I)K E [Trp3,5,10] des-Cys11, Lys12, Lys13- (pBthTX-I)K E SEUS usos como antimicrobiano
(2018-12-26)
Trata-se de um processo de obtenção de peptídeos antibacterianos pela dimerização e modificações pontuais no peptídeo p-BthTX-I que, por sua vez, é derivado da região Cterminal da Lys49 PLA2s homóloga bothropstoxina I ...
Comparison between apo and complexed structures of bothropstoxin-I reveals the role of Lys122 and Ca2+-binding loop region for the catalytically inactive Lys49-PLA(2)s
(Academic Press Inc. Elsevier B.V., 2010-07-01)
Phospholipases A(2) (Asp49-PLA(2)s) are enzymes responsible for cellular membrane disruption through Ca2+-dependent hydrolysis of phospholipids. A class of these proteins (Lys49-PLA(2)s) does not show catalytic activity ...
Comparison between apo and complexed structures of bothropstoxin-I reveals the role of Lys122 and Ca2+-binding loop region for the catalytically inactive Lys49-PLA(2)s
(Academic Press Inc. Elsevier B.V., 2010-07-01)
Phospholipases A(2) (Asp49-PLA(2)s) are enzymes responsible for cellular membrane disruption through Ca2+-dependent hydrolysis of phospholipids. A class of these proteins (Lys49-PLA(2)s) does not show catalytic activity ...
Structural bases for a complete myotoxic mechanism: Crystal structures of two non-catalytic phospholipases A(2)-like from Bothrops brazili venom
(Elsevier Science BvAmsterdamHolanda, 2013)
Crystal structure of myotoxin II, a monomeric Lys49-Phospholipase A(2) homologue isolated from the venom of Cerrophidion (Bothrops) godmani
(Academic Press Inc., 1999-06-15)
Lys49-Phospholipase A(2) (Lys49-PLA(2)) homologues damage membranes by a Ca2+-independent mechanism which does not involve catalytic activity. With the aim of determining the structural basis for this novel activity, we ...
Crystal structure of myotoxin II, a monomeric Lys49-Phospholipase A(2) homologue isolated from the venom of Cerrophidion (Bothrops) godmani
(Academic Press Inc., 1999-06-15)
Lys49-Phospholipase A(2) (Lys49-PLA(2)) homologues damage membranes by a Ca2+-independent mechanism which does not involve catalytic activity. With the aim of determining the structural basis for this novel activity, we ...
Snake venom Lys49 myotoxins: from phospholipases A2 to non-enzymatic membrane disruptors
(2012-09)
Snake venoms often contain toxins that cause a rapid necrosis of skeletal muscle fibers,
referred to as myotoxins. The most common among them are phospholipases A2 (PLA2s),
enzymes that have two independent evolutionary ...
Snake venom Lys49 myotoxins: from phospholipases A2 to non-enzymatic membrane disruptors
(2012-09)
Snake venoms often contain toxins that cause a rapid necrosis of skeletal muscle fibers,
referred to as myotoxins. The most common among them are phospholipases A2 (PLA2s),
enzymes that have two independent evolutionary ...
Crystal structure of myotoxin II, a monomeric Lys49-phospholipase A2 homologue isolated from the venom of Cerrophidion (Bothrops) godmani
(1999-06-15)
Lys49-Phospholipase A2 (Lys49-PLA2) homologues damage membranes by a Ca2+-independent mechanism which does not involve catalytic activity. With the aim of determining the structural basis for this novel activity, we have ...
Antimicrobial and antibiofilm activity of Lys-[Trp6]hy-a1 combined with ciprofloxacin against gram-negative bacteria
(2020-01-01)
Background: Ciprofloxacin (Cip) is the most commonly used quinolone in clinical prac-tice; however large-scale use has favored the increase of multiresistant pathogenic microorganisms. Antimicrobial peptides (AMPs) appear ...