Evidence for conformation change associated with the membrane damaging activity of bothropstoxin-I (BthTX-I), a 'lysine IND.49' PLA isolated from the venom of Bothrops jararacussu (2000)
- Authors:
- USP affiliated authors: WARD, RICHARD JOHN - FFCLRP ; GIGLIO, JOSE ROBERTO - FMRP ; ESCARSO, SILVIA HELENA ANDRIAO - FMRP
- Unidades: FFCLRP; FMRP
- Subjects: BIOFÍSICA; QUÍMICA
- Language: Inglês
- Imprenta:
- Conference titles: Congresso de Biofísica do Cone-Sul
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ABNT
DE OLIVEIRA, A. H. C. et al. Evidence for conformation change associated with the membrane damaging activity of bothropstoxin-I (BthTX-I), a 'lysine IND.49' PLA isolated from the venom of Bothrops jararacussu. 2000, Anais.. Campinas: Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, 2000. . Acesso em: 21 maio 2024. -
APA
de Oliveira, A. H. C., Giglio, J. R., Andrião-Escarso, S. H., & Ward, R. J. (2000). Evidence for conformation change associated with the membrane damaging activity of bothropstoxin-I (BthTX-I), a 'lysine IND.49' PLA isolated from the venom of Bothrops jararacussu. In . Campinas: Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo. -
NLM
de Oliveira AHC, Giglio JR, Andrião-Escarso SH, Ward RJ. Evidence for conformation change associated with the membrane damaging activity of bothropstoxin-I (BthTX-I), a 'lysine IND.49' PLA isolated from the venom of Bothrops jararacussu. 2000 ;[citado 2024 maio 21 ] -
Vancouver
de Oliveira AHC, Giglio JR, Andrião-Escarso SH, Ward RJ. Evidence for conformation change associated with the membrane damaging activity of bothropstoxin-I (BthTX-I), a 'lysine IND.49' PLA isolated from the venom of Bothrops jararacussu. 2000 ;[citado 2024 maio 21 ] - Dissociation of enzymatic and pharmacological properties of piratoxins-I and -III, two myotoxic phospholipases 'A IND.2' from Bothrops pirajai snake venom
- The effect of resonance energy homotransfer on the intrinsic tryptophan fluorescence emission of the Bothropstoxin-I dimer
- Myotoxic phospholipases 'A IND.2' in Bothrops snake venoms: effect of chemical modifications on the enzymatic and pharmacological properties of bothropstoxins from Bothrops jararacussu
- A pH-induced dissociation of the dimeric form of a Lysine 49-Phospholipase 'A IND.2' abolishes 'Ca POT.2+'-independent membrane damaging activity
- Comparative biochemical studies of myotoxic phospholipase 'A IND.2' from Bothrops venom
- Pathological alterations induced by neuwiedase, a metalloproteinase isolated from bothrops neuwiedi snake venom
- A pH-induced dissociation of the dimeric form of a Lysine 49-Phospholipase 'A IND.2' abolishes 'Ca POT.2+'-independent membrane damaging activity
- Crystal structure of piratoxin-I: a calcium-independent, myotoxic phospholipase 'A IND.2'-homologue from bothrops pirajai venom
- The interation between globular proteins and surfactants
- Crystallization of piratoxin I, a myotoxic LYS49-phospholipase 'A IND. 2' homologue isolated from the venom of bothrops pirajai
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