The effect of resonance energy homotransfer on the intrinsic tryptophan fluorescence emission of the Bothropstoxin-I dimer (2001)
- Authors:
- USP affiliated authors: GIGLIO, JOSE ROBERTO - FMRP ; ESCARSO, SILVIA HELENA ANDRIÃO - FMRP ; WARD, RICHARD JOHN - FFCLRP
- Unidades: FMRP; FFCLRP
- Subjects: BIOQUÍMICA; ESPECTROSCOPIA DA LUZ; VENENOS DE ORIGEM ANIMAL; SERPENTES
- Language: Inglês
- Imprenta:
- Source:
- Título: Biochemical and Biophysical Research Communications
- ISSN: 0006-291X
- Volume/Número/Paginação/Ano: v. 281, p. 1011-1015, 2001
-
ABNT
OLIVEIRA, A. H. C. de et al. The effect of resonance energy homotransfer on the intrinsic tryptophan fluorescence emission of the Bothropstoxin-I dimer. Biochemical and Biophysical Research Communications, v. 281, p. 1011-1015, 2001Tradução . . Acesso em: 29 dez. 2025. -
APA
Oliveira, A. H. C. de, Giglio, J. R., Andrião-Escarso, S. H., & Ward, R. J. (2001). The effect of resonance energy homotransfer on the intrinsic tryptophan fluorescence emission of the Bothropstoxin-I dimer. Biochemical and Biophysical Research Communications, 281, 1011-1015. -
NLM
Oliveira AHC de, Giglio JR, Andrião-Escarso SH, Ward RJ. The effect of resonance energy homotransfer on the intrinsic tryptophan fluorescence emission of the Bothropstoxin-I dimer. Biochemical and Biophysical Research Communications. 2001 ; 281 1011-1015.[citado 2025 dez. 29 ] -
Vancouver
Oliveira AHC de, Giglio JR, Andrião-Escarso SH, Ward RJ. The effect of resonance energy homotransfer on the intrinsic tryptophan fluorescence emission of the Bothropstoxin-I dimer. Biochemical and Biophysical Research Communications. 2001 ; 281 1011-1015.[citado 2025 dez. 29 ] - 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
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- A pH-induced dissociation of the dimeric form of a Lysine 49-Phospholipase 'A IND.2' abolishes 'Ca POT.2+'-independent membrane damaging activity
- 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
- 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
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