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Artigo de periodico
The presence of sterols favors sticholysin 'I'-membrane association and pore formation regardless of their ability to form laterally segregated domains (2015)
Pedrera, Lohans; Sanchez, Rafael E.; Ros, Uris; Pazos, Fabiola; Lanio, Maria E.; Alvarez, Carlos; Wilke, Natalia; Fanani, MariaLaura; Gomide, Andreza B.; Itri, Rosangela
Fonte: LANGMUIR. Unidade: IF
Assuntos: TERAPIA FOTODINÂMICA, RPOLÍMEROS (MATERIAIS), FILMES FINOS
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ABNT
PEDRERA, Lohans et al. The presence of sterols favors sticholysin 'I'-membrane association and pore formation regardless of their ability to form laterally segregated domains. LANGMUIR, v. 31, n. 36, p. 9911-9923, 2015Tradução . . Disponível em: https://doi.org/10.1021/acs.langmuir.5b01687. Acesso em: 21 out. 2025.
APA
Pedrera, L., Sanchez, R. E., Ros, U., Pazos, F., Lanio, M. E., Alvarez, C., et al. (2015). The presence of sterols favors sticholysin 'I'-membrane association and pore formation regardless of their ability to form laterally segregated domains. LANGMUIR, 31( 36), 9911-9923. doi:10.1021/acs.langmuir.5b01687
NLM
Pedrera L, Sanchez RE, Ros U, Pazos F, Lanio ME, Alvarez C, Wilke N, Fanani ML, Gomide AB, Itri R. The presence of sterols favors sticholysin 'I'-membrane association and pore formation regardless of their ability to form laterally segregated domains [Internet]. LANGMUIR. 2015 ; 31( 36): 9911-9923.[citado 2025 out. 21 ] Available from: https://doi.org/10.1021/acs.langmuir.5b01687
Vancouver
Pedrera L, Sanchez RE, Ros U, Pazos F, Lanio ME, Alvarez C, Wilke N, Fanani ML, Gomide AB, Itri R. The presence of sterols favors sticholysin 'I'-membrane association and pore formation regardless of their ability to form laterally segregated domains [Internet]. LANGMUIR. 2015 ; 31( 36): 9911-9923.[citado 2025 out. 21 ] Available from: https://doi.org/10.1021/acs.langmuir.5b01687
Artigo de periodico
Solution NMR analysis of the interaction between the actinoporin sticholysin i and DHPC micelles—correlation with backbone dynamics (2014)
López-Castilla, Aracelys; Pazos, Fabiola; Schreier, Shirley ; Pires, José Ricardo
Fonte: Proteins. Unidade: IQ
Assuntos: FOSFOLIPÍDEOS, TOXINAS
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ABNT
LÓPEZ-CASTILLA, Aracelys et al. Solution NMR analysis of the interaction between the actinoporin sticholysin i and DHPC micelles—correlation with backbone dynamics. Proteins, v. 82, n. 6, p. 1022-1034, 2014Tradução . . Disponível em: https://doi.org/10.1002/prot.24475. Acesso em: 21 out. 2025.
APA
López-Castilla, A., Pazos, F., Schreier, S., & Pires, J. R. (2014). Solution NMR analysis of the interaction between the actinoporin sticholysin i and DHPC micelles—correlation with backbone dynamics. Proteins, 82( 6), 1022-1034. doi:10.1002/prot.24475
NLM
López-Castilla A, Pazos F, Schreier S, Pires JR. Solution NMR analysis of the interaction between the actinoporin sticholysin i and DHPC micelles—correlation with backbone dynamics [Internet]. Proteins. 2014 ; 82( 6): 1022-1034.[citado 2025 out. 21 ] Available from: https://doi.org/10.1002/prot.24475
Vancouver
López-Castilla A, Pazos F, Schreier S, Pires JR. Solution NMR analysis of the interaction between the actinoporin sticholysin i and DHPC micelles—correlation with backbone dynamics [Internet]. Proteins. 2014 ; 82( 6): 1022-1034.[citado 2025 out. 21 ] Available from: https://doi.org/10.1002/prot.24475
Artigo de periodico
Functional and topological studies with Trp-containing analogs of the peptide `Stll IND. 1-30´ derived from the N-terminus of the pore forming toxin sticholysin II: contribution to understand its orientation in membrane (2013)
Ros, Uris; Souto, Ana Lucia Carneiro Fernandes; Oliveira, Felipe J. de; Crusca Junior, Edson; Pazos, Fabiola; Cilli, Eduardo Maffud; Lanio, Maria Eliana; Schreier, Shirley ; Alvarez, Carlos
Fonte: Biopolymers. Unidade: IQ
Assuntos: FLUORESCÊNCIA, PEPTÍDEOS
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ABNT
ROS, Uris et al. Functional and topological studies with Trp-containing analogs of the peptide `Stll IND. 1-30´ derived from the N-terminus of the pore forming toxin sticholysin II: contribution to understand its orientation in membrane. Biopolymers, v. 100, n. 4, p. 337-346, 2013Tradução . . Disponível em: https://doi.org/10.1002/bip.22211. Acesso em: 21 out. 2025.
APA
Ros, U., Souto, A. L. C. F., Oliveira, F. J. de, Crusca Junior, E., Pazos, F., Cilli, E. M., et al. (2013). Functional and topological studies with Trp-containing analogs of the peptide `Stll IND. 1-30´ derived from the N-terminus of the pore forming toxin sticholysin II: contribution to understand its orientation in membrane. Biopolymers, 100( 4), 337-346. doi:10.1002/bip.22211
NLM
Ros U, Souto ALCF, Oliveira FJ de, Crusca Junior E, Pazos F, Cilli EM, Lanio ME, Schreier S, Alvarez C. Functional and topological studies with Trp-containing analogs of the peptide `Stll IND. 1-30´ derived from the N-terminus of the pore forming toxin sticholysin II: contribution to understand its orientation in membrane [Internet]. Biopolymers. 2013 ; 100( 4): 337-346.[citado 2025 out. 21 ] Available from: https://doi.org/10.1002/bip.22211
Vancouver
Ros U, Souto ALCF, Oliveira FJ de, Crusca Junior E, Pazos F, Cilli EM, Lanio ME, Schreier S, Alvarez C. Functional and topological studies with Trp-containing analogs of the peptide `Stll IND. 1-30´ derived from the N-terminus of the pore forming toxin sticholysin II: contribution to understand its orientation in membrane [Internet]. Biopolymers. 2013 ; 100( 4): 337-346.[citado 2025 out. 21 ] Available from: https://doi.org/10.1002/bip.22211
Trabalho de evento-resumo
Conformational and functional properties of mutants of the sea anemone cytolsin sticholysin I (2010)
Castro, Iris Arantes de; Paulino, Joana; Valle, A; Pazos, Fabiola; Alvarez, Carlos; Lanio, Maria Eliana; Schreier, Shirley
Fonte: Abstracts. Nome do evento: Annual Meeting of Brazilian Biochemistry and Molecular Biology (SBBq). Unidade: IQ
Assuntos: PROTEÍNAS, BIOQUÍMICA
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ABNT
CASTRO, Iris Arantes de et al. Conformational and functional properties of mutants of the sea anemone cytolsin sticholysin I. 2010, Anais.. São Paulo: SBBq, 2010. . Acesso em: 21 out. 2025.
APA
Castro, I. A. de, Paulino, J., Valle, A., Pazos, F., Alvarez, C., Lanio, M. E., & Schreier, S. (2010). Conformational and functional properties of mutants of the sea anemone cytolsin sticholysin I. In Abstracts. São Paulo: SBBq.
NLM
Castro IA de, Paulino J, Valle A, Pazos F, Alvarez C, Lanio ME, Schreier S. Conformational and functional properties of mutants of the sea anemone cytolsin sticholysin I. Abstracts. 2010 ;[citado 2025 out. 21 ]
Vancouver
Castro IA de, Paulino J, Valle A, Pazos F, Alvarez C, Lanio ME, Schreier S. Conformational and functional properties of mutants of the sea anemone cytolsin sticholysin I. Abstracts. 2010 ;[citado 2025 out. 21 ]
Artigo de periodico
Structural and functional characterization of a recombinant sticholysin I (rSt I) from the sea anemone Stichodactyla helianthus (2007)
Pazos, Fabiola; Valle, A.; Martínez, Diana; Ramírez, A.; Calderon, L.; Puppo, A.; Tejuca, Mayra; Morera, V.; Campos, J.; Fando, R.; Dyszy, F.; Schreier, Shirley ; Horjales, Eduardo ; Alvarez, Carlos; Lanio, M. E.; Lissi, Eduardo
Fonte: Toxicon. Unidade: IQ
Assuntos: BIOQUÍMICA, TOXINAS
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ABNT
PAZOS, Fabiola et al. Structural and functional characterization of a recombinant sticholysin I (rSt I) from the sea anemone Stichodactyla helianthus. Toxicon, v. 48, n. 8, p. 1083-1094, 2007Tradução . . Disponível em: https://doi.org/10.1016/j.toxicon.2006.09.004. Acesso em: 21 out. 2025.
APA
Pazos, F., Valle, A., Martínez, D., Ramírez, A., Calderon, L., Puppo, A., et al. (2007). Structural and functional characterization of a recombinant sticholysin I (rSt I) from the sea anemone Stichodactyla helianthus. Toxicon, 48( 8), 1083-1094. doi:10.1016/j.toxicon.2006.09.004
NLM
Pazos F, Valle A, Martínez D, Ramírez A, Calderon L, Puppo A, Tejuca M, Morera V, Campos J, Fando R, Dyszy F, Schreier S, Horjales E, Alvarez C, Lanio ME, Lissi E. Structural and functional characterization of a recombinant sticholysin I (rSt I) from the sea anemone Stichodactyla helianthus [Internet]. Toxicon. 2007 ; 48( 8): 1083-1094.[citado 2025 out. 21 ] Available from: https://doi.org/10.1016/j.toxicon.2006.09.004
Vancouver
Pazos F, Valle A, Martínez D, Ramírez A, Calderon L, Puppo A, Tejuca M, Morera V, Campos J, Fando R, Dyszy F, Schreier S, Horjales E, Alvarez C, Lanio ME, Lissi E. Structural and functional characterization of a recombinant sticholysin I (rSt I) from the sea anemone Stichodactyla helianthus [Internet]. Toxicon. 2007 ; 48( 8): 1083-1094.[citado 2025 out. 21 ] Available from: https://doi.org/10.1016/j.toxicon.2006.09.004
Artigo de periodico
Sticholysins I and II interaction with cationic micelles promotes toxins' conformational changes and enhanced hemolytic activity (2007)
Lanio, María E.; Alvarez, Carlos; Ochoa, Camila; Ros, Uris; Pazos, Fabiola; Martinez, Diana; Tejuca, Mayra; Eugenio, Luiz Marcelo; Casallanovo, Fábio; Dyszy, Fabio Henrique; Schreier, Shirley ; Lissi, Eduardo
Fonte: Toxicon. Unidade: IQ
Assuntos: FLUORESCÊNCIA, SURFACTANTES
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ABNT
LANIO, María E. et al. Sticholysins I and II interaction with cationic micelles promotes toxins' conformational changes and enhanced hemolytic activity. Toxicon, v. 50, n. 6, p. 731-739, 2007Tradução . . Disponível em: https://doi.org/10.1016/j.toxicon.2007.06.007. Acesso em: 21 out. 2025.
APA
Lanio, M. E., Alvarez, C., Ochoa, C., Ros, U., Pazos, F., Martinez, D., et al. (2007). Sticholysins I and II interaction with cationic micelles promotes toxins' conformational changes and enhanced hemolytic activity. Toxicon, 50( 6), 731-739. doi:10.1016/j.toxicon.2007.06.007
NLM
Lanio ME, Alvarez C, Ochoa C, Ros U, Pazos F, Martinez D, Tejuca M, Eugenio LM, Casallanovo F, Dyszy FH, Schreier S, Lissi E. Sticholysins I and II interaction with cationic micelles promotes toxins' conformational changes and enhanced hemolytic activity [Internet]. Toxicon. 2007 ; 50( 6): 731-739.[citado 2025 out. 21 ] Available from: https://doi.org/10.1016/j.toxicon.2007.06.007
Vancouver
Lanio ME, Alvarez C, Ochoa C, Ros U, Pazos F, Martinez D, Tejuca M, Eugenio LM, Casallanovo F, Dyszy FH, Schreier S, Lissi E. Sticholysins I and II interaction with cationic micelles promotes toxins' conformational changes and enhanced hemolytic activity [Internet]. Toxicon. 2007 ; 50( 6): 731-739.[citado 2025 out. 21 ] Available from: https://doi.org/10.1016/j.toxicon.2007.06.007
Artigo de periodico
Model peptides mimic the structure and function of the N-terminus of the pore-forming toxin sticholysin II (2006)
Casallanovo, Fábio; Oliveira, Felipe Jun Fukimoto de; Souza, Fernando César de; Ros, Uris; Martínez, Yohanka; Pentón, David; Tejuca, Mayra; Martínez, Diana; Pazos, Fabiola; Pertinhez, Thelma de Aguiar; Spisni, Alberto; Cilli, Eduardo Maffud; Lanio, María E.; Alvarez, Carlos; Schreier, Shirley
Fonte: Biopolymers (Peptide Science). Unidade: IQ
Assuntos: BIOQUÍMICA, ANTICORPOS MONOCLONAIS
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ABNT
CASALLANOVO, Fábio et al. Model peptides mimic the structure and function of the N-terminus of the pore-forming toxin sticholysin II. Biopolymers (Peptide Science), v. 84, n. 2, p. 169-180, 2006Tradução . . Disponível em: https://doi.org/10.1002/bip.20374. Acesso em: 21 out. 2025.
APA
Casallanovo, F., Oliveira, F. J. F. de, Souza, F. C. de, Ros, U., Martínez, Y., Pentón, D., et al. (2006). Model peptides mimic the structure and function of the N-terminus of the pore-forming toxin sticholysin II. Biopolymers (Peptide Science), 84( 2), 169-180. doi:10.1002/bip.20374
NLM
Casallanovo F, Oliveira FJF de, Souza FC de, Ros U, Martínez Y, Pentón D, Tejuca M, Martínez D, Pazos F, Pertinhez T de A, Spisni A, Cilli EM, Lanio ME, Alvarez C, Schreier S. Model peptides mimic the structure and function of the N-terminus of the pore-forming toxin sticholysin II [Internet]. Biopolymers (Peptide Science). 2006 ; 84( 2): 169-180.[citado 2025 out. 21 ] Available from: https://doi.org/10.1002/bip.20374
Vancouver
Casallanovo F, Oliveira FJF de, Souza FC de, Ros U, Martínez Y, Pentón D, Tejuca M, Martínez D, Pazos F, Pertinhez T de A, Spisni A, Cilli EM, Lanio ME, Alvarez C, Schreier S. Model peptides mimic the structure and function of the N-terminus of the pore-forming toxin sticholysin II [Internet]. Biopolymers (Peptide Science). 2006 ; 84( 2): 169-180.[citado 2025 out. 21 ] Available from: https://doi.org/10.1002/bip.20374

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