The membranotropic activity of N-terminal peptides from the pore-forming proteins sticholysin I and II is modulated by hydrophobic and electrostatic interactions as well as lipid composition (2011)
- Authors:
- USP affiliated authors: ITRI, ROSANGELA - IF ; SCHREIER, SHIRLEY - IQ
- Unidades: IF; IQ
- DOI: 10.1007/s12038-011-9156-4
- Subjects: PEPTÍDEOS; TOXINAS
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Journal of Biosciences
- ISSN: 0250-5991
- Volume/Número/Paginação/Ano: v. 36, n. 5, p. 781-791, 2011
- Este periódico é de assinatura
- Este artigo é de acesso aberto
- URL de acesso aberto
- Cor do Acesso Aberto: green
-
ABNT
ROS, Uris et al. The membranotropic activity of N-terminal peptides from the pore-forming proteins sticholysin I and II is modulated by hydrophobic and electrostatic interactions as well as lipid composition. Journal of Biosciences, v. 36, n. 5, p. 781-791, 2011Tradução . . Disponível em: https://doi.org/10.1007/s12038-011-9156-4. Acesso em: 03 maio 2024. -
APA
Ros, U., Pedrera, L., Díaz, D., Karam, J. C. de, Sudbrack, T. de P., Valiente, P. A., et al. (2011). The membranotropic activity of N-terminal peptides from the pore-forming proteins sticholysin I and II is modulated by hydrophobic and electrostatic interactions as well as lipid composition. Journal of Biosciences, 36( 5), 781-791. doi:10.1007/s12038-011-9156-4 -
NLM
Ros U, Pedrera L, Díaz D, Karam JC de, Sudbrack T de P, Valiente PA, Martinez D, Cilli EM, Pazos F, Itri R, Lanio ME, Schreirer S, Alvarez C. The membranotropic activity of N-terminal peptides from the pore-forming proteins sticholysin I and II is modulated by hydrophobic and electrostatic interactions as well as lipid composition [Internet]. Journal of Biosciences. 2011 ; 36( 5): 781-791.[citado 2024 maio 03 ] Available from: https://doi.org/10.1007/s12038-011-9156-4 -
Vancouver
Ros U, Pedrera L, Díaz D, Karam JC de, Sudbrack T de P, Valiente PA, Martinez D, Cilli EM, Pazos F, Itri R, Lanio ME, Schreirer S, Alvarez C. The membranotropic activity of N-terminal peptides from the pore-forming proteins sticholysin I and II is modulated by hydrophobic and electrostatic interactions as well as lipid composition [Internet]. Journal of Biosciences. 2011 ; 36( 5): 781-791.[citado 2024 maio 03 ] Available from: https://doi.org/10.1007/s12038-011-9156-4 - Estudo do efeito de íons da série de Hofmeister em membranas modelo
- Hofmeister ions effect on model membrane
- Local anesthetic-induced microscopic and mesoscopic effects in micelles. A fluorescence, spin label and SAXS study
- Nitroxide-solvent interaction: evaluation of the contribution of hydrogen bonding and van der waals interactions
- Spin label study of the interaction between lipid membranes and dodecapeptide (terminal portion of the angiotensin ii putative receptor)
- Spin label study of local anesthetic-lipid membrane interactions. Phase separation of the uncharged form and bilayer micellization by the charged form of tetracaine cellization by the charged form of tetracaine
- Synthesis and interaction with membranes of a spin labeled pentadecapeptide contained in the sequence of an angiotensin ii receptor
- Pharmacological applications of spin labels .Involvement of membrane structural changes in the mechanism of drug action
- Esr studies of molecular aspects of the mechanism of drug action: antoxidation of the polyene antibiotic amphotericin b
- Metodo para determinacao do coeficiente de particao atraves da medida de alteracoes estruturais de membranas
Informações sobre o DOI: 10.1007/s12038-011-9156-4 (Fonte: oaDOI API)
Download do texto completo
| Tipo | Nome | Link | |
|---|---|---|---|
 | s12038-011-9156-4.pdf | Direct link |
How to cite
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
