A pH-induced dissociation of the dimeric form of a Lysine 49-Phospholipase 'A IND.2' abolishes 'Ca POT.2+'-independent membrane damaging activity (2001)
- Authors:
- USP affiliated authors: GIGLIO, JOSE ROBERTO - FMRP ; ESCARSO, SILVIA HELENA ANDRIÃO - FMRP ; ITO, AMANDO SIUITI - FFCLRP ; WARD, RICHARD JOHN - FFCLRP
- Unidades: FMRP; FFCLRP
- Assunto: BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Source:
- Título: Programa e Resumos
- Conference titles: Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular
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ABNT
OLIVEIRA, A. H. C. de et al. A pH-induced dissociation of the dimeric form of a Lysine 49-Phospholipase 'A IND.2' abolishes 'Ca POT.2+'-independent membrane damaging activity. 2001, Anais.. São Paulo: SBBq, 2001. . Acesso em: 29 dez. 2025. -
APA
Oliveira, A. H. C. de, Giglio, J. R., Andrião-Escarso, S. H., Ito, A. S., & Ward, R. J. (2001). A pH-induced dissociation of the dimeric form of a Lysine 49-Phospholipase 'A IND.2' abolishes 'Ca POT.2+'-independent membrane damaging activity. In Programa e Resumos. São Paulo: SBBq. -
NLM
Oliveira AHC de, Giglio JR, Andrião-Escarso SH, Ito AS, Ward RJ. A pH-induced dissociation of the dimeric form of a Lysine 49-Phospholipase 'A IND.2' abolishes 'Ca POT.2+'-independent membrane damaging activity. Programa e Resumos. 2001 ;[citado 2025 dez. 29 ] -
Vancouver
Oliveira AHC de, Giglio JR, Andrião-Escarso SH, Ito AS, Ward RJ. A pH-induced dissociation of the dimeric form of a Lysine 49-Phospholipase 'A IND.2' abolishes 'Ca POT.2+'-independent membrane damaging activity. Programa e Resumos. 2001 ;[citado 2025 dez. 29 ] - The effect of resonance energy homotransfer on the intrinsic tryptophan fluorescence emission of the Bothropstoxin-I dimer
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- Dissociation of enzymatic and pharmacological properties of piratoxins-I and -III, two myotoxic phospholipases 'A IND.2' from Bothrops pirajai snake venom
- Myotoxic phospholipases 'A IND.2' in Bothrops snake venoms: effect of chemical modifications on the enzymatic and pharmacological properties of bothropstoxins from Bothrops jararacussu
- Pathological alterations induced by neuwiedase, a metalloproteinase isolated from bothrops neuwiedi snake venom
- Comparative biochemical studies of myotoxic phospholipase 'A IND.2' from Bothrops venom
- Investigation of the interation between bothropstoxin (BthTX-I), a lysine 49 'PLA ind. 2' isolated from the venom of 'Bothrops jararacussu', and lipossomes
- A pH induced dimer to monomer transition in bothropstoxin-1, a lysine 49 'PLA ind.2'isolated from the venon of Bothrops jararacussu
- The amino acid sequence of ribitol dehydrogenase-F, a mutant enzyme with improved xylitol dehydrogenase activity
- Crystal structure of piratoxin-I: a calcium-independent, myotoxic phospholipase 'A IND.2'-homologue from bothrops pirajai venom
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