Source: Journal of Biosciences. Unidades: IF, IQ
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 set. 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/s12038-011-9156-4NLM
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 set. 03 ] Available from: https://doi.org/10.1007/s12038-011-9156-4Vancouver
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 set. 03 ] Available from: https://doi.org/10.1007/s12038-011-9156-4