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GARBELLINI, Carolina Patricia Aires et al. Bacillus subtilis engagement induced via sporulation: a case of bacterial communication. Brazilian Journal of Physics, v. 52, n. 3, p. 88-1-88-4, 2022Tradução . . Disponível em: https://doi.org/10.1007/s13538-022-01079-7. Acesso em: 14 jan. 2025.
APA
Garbellini, C. P. A., Polizello, A. C. M., Caliri, A., & Mascarenhas, S. (2022). Bacillus subtilis engagement induced via sporulation: a case of bacterial communication. Brazilian Journal of Physics, 52( 3), 88-1-88-4. doi:10.1007/s13538-022-01079-7
NLM
Garbellini CPA, Polizello ACM, Caliri A, Mascarenhas S. Bacillus subtilis engagement induced via sporulation: a case of bacterial communication [Internet]. Brazilian Journal of Physics. 2022 ; 52( 3): 88-1-88-4.[citado 2025 jan. 14 ] Available from: https://doi.org/10.1007/s13538-022-01079-7
Vancouver
Garbellini CPA, Polizello ACM, Caliri A, Mascarenhas S. Bacillus subtilis engagement induced via sporulation: a case of bacterial communication [Internet]. Brazilian Journal of Physics. 2022 ; 52( 3): 88-1-88-4.[citado 2025 jan. 14 ] Available from: https://doi.org/10.1007/s13538-022-01079-7
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ANDRADE, Micássio F. et al. The 3-phenylcoumarin derivative 6,7-dihydroxy-3-[3′,4′-methylenedioxyphenyl]-coumarin downmodulates the FcγR- and CR-mediated oxidative metabolism and elastase release in human neutrophils: possible mechanisms underlying inhibition of the formation and release of neutrophil extracellular traps. Free Radical Biology and Medicine, v. 115, p. 421-435, 2018Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2017.12.012. Acesso em: 14 jan. 2025.
APA
Andrade, M. F., Kabeya, L. M., Bortot, L. O., Santos, G. B. dos, Santos, E. O. L., Albiero, L. R., et al. (2018). The 3-phenylcoumarin derivative 6,7-dihydroxy-3-[3′,4′-methylenedioxyphenyl]-coumarin downmodulates the FcγR- and CR-mediated oxidative metabolism and elastase release in human neutrophils: possible mechanisms underlying inhibition of the formation and release of neutrophil extracellular traps. Free Radical Biology and Medicine, 115, 421-435. doi:10.1016/j.freeradbiomed.2017.12.012
NLM
Andrade MF, Kabeya LM, Bortot LO, Santos GB dos, Santos EOL, Albiero LR, Figueiredo-Rinhel ASG, Carvalho CA, Azzolini AECS, Caliri A, Pupo MT, Emery F da S, Lucisano-Valim YM. The 3-phenylcoumarin derivative 6,7-dihydroxy-3-[3′,4′-methylenedioxyphenyl]-coumarin downmodulates the FcγR- and CR-mediated oxidative metabolism and elastase release in human neutrophils: possible mechanisms underlying inhibition of the formation and release of neutrophil extracellular traps [Internet]. Free Radical Biology and Medicine. 2018 ; 115 421-435.[citado 2025 jan. 14 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2017.12.012
Vancouver
Andrade MF, Kabeya LM, Bortot LO, Santos GB dos, Santos EOL, Albiero LR, Figueiredo-Rinhel ASG, Carvalho CA, Azzolini AECS, Caliri A, Pupo MT, Emery F da S, Lucisano-Valim YM. The 3-phenylcoumarin derivative 6,7-dihydroxy-3-[3′,4′-methylenedioxyphenyl]-coumarin downmodulates the FcγR- and CR-mediated oxidative metabolism and elastase release in human neutrophils: possible mechanisms underlying inhibition of the formation and release of neutrophil extracellular traps [Internet]. Free Radical Biology and Medicine. 2018 ; 115 421-435.[citado 2025 jan. 14 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2017.12.012
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SOARES, Ricardo Oliveira dos Santos et al. Membrane vesiculation induced by proteins of the dengue virus envelope studied by molecular dynamics simulations. Journal of Physics: Condensed Matter, v. 29, n. 50, 2017Tradução . . Disponível em: https://doi.org/10.1088/1361-648x/aa99c6. Acesso em: 14 jan. 2025.
APA
Soares, R. O. dos S., Bortot, L. O., Spoel, D. van der, & Caliri, A. (2017). Membrane vesiculation induced by proteins of the dengue virus envelope studied by molecular dynamics simulations. Journal of Physics: Condensed Matter, 29( 50). doi:10.1088/1361-648x/aa99c6
NLM
Soares RO dos S, Bortot LO, Spoel D van der, Caliri A. Membrane vesiculation induced by proteins of the dengue virus envelope studied by molecular dynamics simulations [Internet]. Journal of Physics: Condensed Matter. 2017 ; 29( 50):[citado 2025 jan. 14 ] Available from: https://doi.org/10.1088/1361-648x/aa99c6
Vancouver
Soares RO dos S, Bortot LO, Spoel D van der, Caliri A. Membrane vesiculation induced by proteins of the dengue virus envelope studied by molecular dynamics simulations [Internet]. Journal of Physics: Condensed Matter. 2017 ; 29( 50):[citado 2025 jan. 14 ] Available from: https://doi.org/10.1088/1361-648x/aa99c6
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FIGUEIREDO-RINHEL, Andréa S. G et al. Baccharis dracunculifolia DC (Asteraceae) selectively modulates the effector functions of human neutrophils. Journal of Pharmacy and Pharmacology, v. 69, p. 1829-1845, 2017Tradução . . Disponível em: https://doi.org/10.1111/jphp.12822. Acesso em: 14 jan. 2025.
APA
Figueiredo-Rinhel, A. S. G., Melo, L. L. de, Bortot, L. O., Santos, E. O. L., Andrade, M. F., Azzolini, A. E. C. S., et al. (2017). Baccharis dracunculifolia DC (Asteraceae) selectively modulates the effector functions of human neutrophils. Journal of Pharmacy and Pharmacology, 69, 1829-1845. doi:10.1111/jphp.12822
NLM
Figueiredo-Rinhel ASG, Melo LL de, Bortot LO, Santos EOL, Andrade MF, Azzolini AECS, Kabeya LM, Caliri A, Bastos JK, Lucisano-Valim YM. Baccharis dracunculifolia DC (Asteraceae) selectively modulates the effector functions of human neutrophils [Internet]. Journal of Pharmacy and Pharmacology. 2017 ; 69 1829-1845.[citado 2025 jan. 14 ] Available from: https://doi.org/10.1111/jphp.12822
Vancouver
Figueiredo-Rinhel ASG, Melo LL de, Bortot LO, Santos EOL, Andrade MF, Azzolini AECS, Kabeya LM, Caliri A, Bastos JK, Lucisano-Valim YM. Baccharis dracunculifolia DC (Asteraceae) selectively modulates the effector functions of human neutrophils [Internet]. Journal of Pharmacy and Pharmacology. 2017 ; 69 1829-1845.[citado 2025 jan. 14 ] Available from: https://doi.org/10.1111/jphp.12822
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REIS, Renata Almeida Garcia e BORTOT, Leandro Oliveira e CALIRI, Antônio. In silico assessment of S100A12 monomer and dimer structural dynamics: implications for the understanding of its metal-induced conformational changes. Journal of Biological Inorganic Chemistry, v. 19, n. 7, p. 1113-1120, 2014Tradução . . Disponível em: https://doi.org/10.1007/s00775-014-1149-y. Acesso em: 14 jan. 2025.
APA
Reis, R. A. G., Bortot, L. O., & Caliri, A. (2014). In silico assessment of S100A12 monomer and dimer structural dynamics: implications for the understanding of its metal-induced conformational changes. Journal of Biological Inorganic Chemistry, 19( 7), 1113-1120. doi:10.1007/s00775-014-1149-y
NLM
Reis RAG, Bortot LO, Caliri A. In silico assessment of S100A12 monomer and dimer structural dynamics: implications for the understanding of its metal-induced conformational changes [Internet]. Journal of Biological Inorganic Chemistry. 2014 ; 19( 7): 1113-1120.[citado 2025 jan. 14 ] Available from: https://doi.org/10.1007/s00775-014-1149-y
Vancouver
Reis RAG, Bortot LO, Caliri A. In silico assessment of S100A12 monomer and dimer structural dynamics: implications for the understanding of its metal-induced conformational changes [Internet]. Journal of Biological Inorganic Chemistry. 2014 ; 19( 7): 1113-1120.[citado 2025 jan. 14 ] Available from: https://doi.org/10.1007/s00775-014-1149-y
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DEGREVE, Léo e FUZO, Carlos Alessandro e CALIRI, Antônio. Extended secondary structures in proteins. Biochimica et Biophysica Acta - Proteins and Proteomics, v. 1844, n. 2, p. 384\2013388, 2014Tradução . . Disponível em: https://doi.org/10.1016/j.bbapap.2013.10.005. Acesso em: 14 jan. 2025.
APA
Degreve, L., Fuzo, C. A., & Caliri, A. (2014). Extended secondary structures in proteins. Biochimica et Biophysica Acta - Proteins and Proteomics, 1844( 2), 384\2013388. doi:10.1016/j.bbapap.2013.10.005
NLM
Degreve L, Fuzo CA, Caliri A. Extended secondary structures in proteins [Internet]. Biochimica et Biophysica Acta - Proteins and Proteomics. 2014 ; 1844( 2): 384\2013388.[citado 2025 jan. 14 ] Available from: https://doi.org/10.1016/j.bbapap.2013.10.005
Vancouver
Degreve L, Fuzo CA, Caliri A. Extended secondary structures in proteins [Internet]. Biochimica et Biophysica Acta - Proteins and Proteomics. 2014 ; 1844( 2): 384\2013388.[citado 2025 jan. 14 ] Available from: https://doi.org/10.1016/j.bbapap.2013.10.005
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MULLER, Vanessa Danielle et al. Phospholipase A2 isolated from the venom of Crotalus durissus terrificus inactivates Dengue virus and other enveloped viruses by disrupting the viral envelope. PLOs One, v. 9, n. 11, p. e112351-1 - e112351-10, 2014Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0112351. Acesso em: 14 jan. 2025.
APA
Muller, V. D., Soares, R. O., Santos-Júnior, N. N. dos, Trabuco, A. C., Cintra, A. C., Figueiredo, L. T. M., et al. (2014). Phospholipase A2 isolated from the venom of Crotalus durissus terrificus inactivates Dengue virus and other enveloped viruses by disrupting the viral envelope. PLOs One, 9( 11), e112351-1 - e112351-10. doi:10.1371/journal.pone.0112351
NLM
Muller VD, Soares RO, Santos-Júnior NN dos, Trabuco AC, Cintra AC, Figueiredo LTM, Caliri A, Sampaio SV, Aquino VH. Phospholipase A2 isolated from the venom of Crotalus durissus terrificus inactivates Dengue virus and other enveloped viruses by disrupting the viral envelope [Internet]. PLOs One. 2014 ; 9( 11): e112351-1 - e112351-10.[citado 2025 jan. 14 ] Available from: https://doi.org/10.1371/journal.pone.0112351
Vancouver
Muller VD, Soares RO, Santos-Júnior NN dos, Trabuco AC, Cintra AC, Figueiredo LTM, Caliri A, Sampaio SV, Aquino VH. Phospholipase A2 isolated from the venom of Crotalus durissus terrificus inactivates Dengue virus and other enveloped viruses by disrupting the viral envelope [Internet]. PLOs One. 2014 ; 9( 11): e112351-1 - e112351-10.[citado 2025 jan. 14 ] Available from: https://doi.org/10.1371/journal.pone.0112351
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SOARES, R. O. S. e CALIRI, Antônio. Stereochemical features of the envelope protein domain III of dengue virus reveals putative antigenic site in the five-fold symmetry axis. Biochimica et Biophysica Acta - Proteins and Proteomics, v. 1834, n. 1, p. 221-230, 2013Tradução . . Disponível em: https://doi.org/10.1016/j.bbapap.2012.09.007. Acesso em: 14 jan. 2025.
APA
Soares, R. O. S., & Caliri, A. (2013). Stereochemical features of the envelope protein domain III of dengue virus reveals putative antigenic site in the five-fold symmetry axis. Biochimica et Biophysica Acta - Proteins and Proteomics, 1834( 1), 221-230. doi:10.1016/j.bbapap.2012.09.007
NLM
Soares ROS, Caliri A. Stereochemical features of the envelope protein domain III of dengue virus reveals putative antigenic site in the five-fold symmetry axis [Internet]. Biochimica et Biophysica Acta - Proteins and Proteomics. 2013 ; 1834( 1): 221-230.[citado 2025 jan. 14 ] Available from: https://doi.org/10.1016/j.bbapap.2012.09.007
Vancouver
Soares ROS, Caliri A. Stereochemical features of the envelope protein domain III of dengue virus reveals putative antigenic site in the five-fold symmetry axis [Internet]. Biochimica et Biophysica Acta - Proteins and Proteomics. 2013 ; 1834( 1): 221-230.[citado 2025 jan. 14 ] Available from: https://doi.org/10.1016/j.bbapap.2012.09.007
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DAL MOLIN, J. P. e CALIRI, Antonio. The early events of the protein folding process. Current Physical Chemistry, v. 3, n. 1, p. 69-76, 2013Tradução . . Disponível em: https://doi.org/10.2174/1877946811303010010. Acesso em: 14 jan. 2025.
APA
Dal Molin, J. P., & Caliri, A. (2013). The early events of the protein folding process. Current Physical Chemistry, 3( 1), 69-76. doi:10.2174/1877946811303010010
NLM
Dal Molin JP, Caliri A. The early events of the protein folding process [Internet]. Current Physical Chemistry. 2013 ; 3( 1): 69-76.[citado 2025 jan. 14 ] Available from: https://doi.org/10.2174/1877946811303010010
Vancouver
Dal Molin JP, Caliri A. The early events of the protein folding process [Internet]. Current Physical Chemistry. 2013 ; 3( 1): 69-76.[citado 2025 jan. 14 ] Available from: https://doi.org/10.2174/1877946811303010010
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DAL MOLIN, João Paulo e SILVA, Marco Antonio Alves da e CALIRI, Antônio. The role of entropic index q over protein native structure stability in the stereochemical model context. 2012, Anais.. São Paulo: SBF, 2012. . Acesso em: 14 jan. 2025.
APA
Dal Molin, J. P., Silva, M. A. A. da, & Caliri, A. (2012). The role of entropic index q over protein native structure stability in the stereochemical model context. In Resumos. São Paulo: SBF.
NLM
Dal Molin JP, Silva MAA da, Caliri A. The role of entropic index q over protein native structure stability in the stereochemical model context. Resumos. 2012 ;[citado 2025 jan. 14 ]
Vancouver
Dal Molin JP, Silva MAA da, Caliri A. The role of entropic index q over protein native structure stability in the stereochemical model context. Resumos. 2012 ;[citado 2025 jan. 14 ]
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BORTOT, Leandro Oliveira e CALIRI, Antonio. Dynamic modulation of the S100A12 dimerization process by the presence of different ions in the solution. 2012, Anais.. São Paulo: SBF, 2012. . Acesso em: 14 jan. 2025.
APA
Bortot, L. O., & Caliri, A. (2012). Dynamic modulation of the S100A12 dimerization process by the presence of different ions in the solution. In Resumos. São Paulo: SBF.
NLM
Bortot LO, Caliri A. Dynamic modulation of the S100A12 dimerization process by the presence of different ions in the solution. Resumos. 2012 ;[citado 2025 jan. 14 ]
Vancouver
Bortot LO, Caliri A. Dynamic modulation of the S100A12 dimerization process by the presence of different ions in the solution. Resumos. 2012 ;[citado 2025 jan. 14 ]
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DEGRÈVE, Léo e FUZO, Carlos A. e CALIRI, Antônio. Extensive structural change of the envelope protein of dengue virus induced by a tuned ionic strength: conformational and energetic analyses. Journal of Computer-Aided Molecular Design, v. 26, n. 12, p. 1311-1325, 2012Tradução . . Disponível em: https://doi.org/10.1007/s10822-012-9616-4. Acesso em: 14 jan. 2025.
APA
Degrève, L., Fuzo, C. A., & Caliri, A. (2012). Extensive structural change of the envelope protein of dengue virus induced by a tuned ionic strength: conformational and energetic analyses. Journal of Computer-Aided Molecular Design, 26( 12), 1311-1325. doi:10.1007/s10822-012-9616-4
NLM
Degrève L, Fuzo CA, Caliri A. Extensive structural change of the envelope protein of dengue virus induced by a tuned ionic strength: conformational and energetic analyses [Internet]. Journal of Computer-Aided Molecular Design. 2012 ; 26( 12): 1311-1325.[citado 2025 jan. 14 ] Available from: https://doi.org/10.1007/s10822-012-9616-4
Vancouver
Degrève L, Fuzo CA, Caliri A. Extensive structural change of the envelope protein of dengue virus induced by a tuned ionic strength: conformational and energetic analyses [Internet]. Journal of Computer-Aided Molecular Design. 2012 ; 26( 12): 1311-1325.[citado 2025 jan. 14 ] Available from: https://doi.org/10.1007/s10822-012-9616-4
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DEGREVE, Leo e FUZO, Carlos Alessandro e CALIRI, Antônio. Molecular simulation of the E protein from dengue virus type 2. FEBS Journal. Oxford: Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo. . Acesso em: 14 jan. 2025. , 2011
APA
Degreve, L., Fuzo, C. A., & Caliri, A. (2011). Molecular simulation of the E protein from dengue virus type 2. FEBS Journal. Oxford: Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo.
NLM
Degreve L, Fuzo CA, Caliri A. Molecular simulation of the E protein from dengue virus type 2. FEBS Journal. 2011 ; 278( suppl.1): 368.[citado 2025 jan. 14 ]
Vancouver
Degreve L, Fuzo CA, Caliri A. Molecular simulation of the E protein from dengue virus type 2. FEBS Journal. 2011 ; 278( suppl.1): 368.[citado 2025 jan. 14 ]
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FACCIOLI, Rodrigo Antonio et al. Protpred-gromacs: evolutionary algorithm with gromacs for protein structure prediction. 2011, Anais.. Santiago de Chile: Escola de Engenharia de São Carlos, Universidade de São Paulo, 2011. . Acesso em: 14 jan. 2025.
APA
Faccioli, R. A., Silva, I. N. da, Delbem, A. C. B., Brancini, G. T. P., & Caliri, A. (2011). Protpred-gromacs: evolutionary algorithm with gromacs for protein structure prediction. In Proceedings of BIOMAT. Santiago de Chile: Escola de Engenharia de São Carlos, Universidade de São Paulo.
NLM
Faccioli RA, Silva IN da, Delbem ACB, Brancini GTP, Caliri A. Protpred-gromacs: evolutionary algorithm with gromacs for protein structure prediction. Proceedings of BIOMAT. 2011 ;[citado 2025 jan. 14 ]
Vancouver
Faccioli RA, Silva IN da, Delbem ACB, Brancini GTP, Caliri A. Protpred-gromacs: evolutionary algorithm with gromacs for protein structure prediction. Proceedings of BIOMAT. 2011 ;[citado 2025 jan. 14 ]
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DEGREVE, Leo e FUZO, C. A. e CALIRI, Antonio. The ionic strength is also responsible for structural changes in proteins. 2011, Anais.. Madeira: Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo, 2011. . Acesso em: 14 jan. 2025.
APA
Degreve, L., Fuzo, C. A., & Caliri, A. (2011). The ionic strength is also responsible for structural changes in proteins. In Abstract. Madeira: Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo.
NLM
Degreve L, Fuzo CA, Caliri A. The ionic strength is also responsible for structural changes in proteins. Abstract. 2011 ;[citado 2025 jan. 14 ]
Vancouver
Degreve L, Fuzo CA, Caliri A. The ionic strength is also responsible for structural changes in proteins. Abstract. 2011 ;[citado 2025 jan. 14 ]
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DAL MOLIN, João Paulo e SILVA, Marco Antonio Alves da e CALIRI, Antônio. Effect of local thermal fluctuations on folding kinetics: a study from the perspective of nonextensive statistical mechanics. Physical Review E (Statistical, Nonlinear and Soft Matter Physics), v. 84, p. 041903-1-041903-10, 2011Tradução . . Disponível em: https://doi.org/10.1103/physreve.84.041903. Acesso em: 14 jan. 2025.
APA
Dal Molin, J. P., Silva, M. A. A. da, & Caliri, A. (2011). Effect of local thermal fluctuations on folding kinetics: a study from the perspective of nonextensive statistical mechanics. Physical Review E (Statistical, Nonlinear and Soft Matter Physics), 84, 041903-1-041903-10. doi:10.1103/physreve.84.041903
NLM
Dal Molin JP, Silva MAA da, Caliri A. Effect of local thermal fluctuations on folding kinetics: a study from the perspective of nonextensive statistical mechanics [Internet]. Physical Review E (Statistical, Nonlinear and Soft Matter Physics). 2011 ; 84 041903-1-041903-10.[citado 2025 jan. 14 ] Available from: https://doi.org/10.1103/physreve.84.041903
Vancouver
Dal Molin JP, Silva MAA da, Caliri A. Effect of local thermal fluctuations on folding kinetics: a study from the perspective of nonextensive statistical mechanics [Internet]. Physical Review E (Statistical, Nonlinear and Soft Matter Physics). 2011 ; 84 041903-1-041903-10.[citado 2025 jan. 14 ] Available from: https://doi.org/10.1103/physreve.84.041903
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DEGREVE, Leo et al. The stability of extended secondary protein structures: the Dengue virus E protein case. 2011, Anais.. Santiago de Compostela: Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, 2011. . Acesso em: 14 jan. 2025.
APA
Degreve, L., Fuzo, C. A., Silva, G. M. da, & Caliri, A. (2011). The stability of extended secondary protein structures: the Dengue virus E protein case. In Abstracts. Santiago de Compostela: Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo.
NLM
Degreve L, Fuzo CA, Silva GM da, Caliri A. The stability of extended secondary protein structures: the Dengue virus E protein case. Abstracts. 2011 ;[citado 2025 jan. 14 ]
Vancouver
Degreve L, Fuzo CA, Silva GM da, Caliri A. The stability of extended secondary protein structures: the Dengue virus E protein case. Abstracts. 2011 ;[citado 2025 jan. 14 ]
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DAL MOLIN, J. P. e SILVA, Marco Antonio Alves da e CALIRI, Antônio. The role of nonextensive statistical mechanics on the search stage of the protein native state. 2011, Anais.. Ribeirão Preto: FCFRP, Associação Brasileira de Ciências Farmacêuticas, 2011. . Acesso em: 14 jan. 2025.
APA
Dal Molin, J. P., Silva, M. A. A. da, & Caliri, A. (2011). The role of nonextensive statistical mechanics on the search stage of the protein native state. In Abstracts. Ribeirão Preto: FCFRP, Associação Brasileira de Ciências Farmacêuticas.
NLM
Dal Molin JP, Silva MAA da, Caliri A. The role of nonextensive statistical mechanics on the search stage of the protein native state. Abstracts. 2011 ;[citado 2025 jan. 14 ]
Vancouver
Dal Molin JP, Silva MAA da, Caliri A. The role of nonextensive statistical mechanics on the search stage of the protein native state. Abstracts. 2011 ;[citado 2025 jan. 14 ]
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DAL MOLIN, João Paulo e SILVA, Marco Antonio Alves da e CALIRI, Antônio. Characteristic folding time evaluated by nonextensive statistical mechanics. 2011, Anais.. São Paulo: Sociedade Brasileira de Física, 2011. . Acesso em: 14 jan. 2025.
APA
Dal Molin, J. P., Silva, M. A. A. da, & Caliri, A. (2011). Characteristic folding time evaluated by nonextensive statistical mechanics. In Resumo. São Paulo: Sociedade Brasileira de Física.
NLM
Dal Molin JP, Silva MAA da, Caliri A. Characteristic folding time evaluated by nonextensive statistical mechanics. Resumo. 2011 ;[citado 2025 jan. 14 ]
Vancouver
Dal Molin JP, Silva MAA da, Caliri A. Characteristic folding time evaluated by nonextensive statistical mechanics. Resumo. 2011 ;[citado 2025 jan. 14 ]
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MOLIN, João Paulo Dal e CALIRI, Antônio. The nonextensive parameter q and the topology of native structure of globular proteins. 2010, Anais.. São Paulo: Sociedade Brasileira de Física - SBF, 2010. . Acesso em: 14 jan. 2025.
APA
Molin, J. P. D., & Caliri, A. (2010). The nonextensive parameter q and the topology of native structure of globular proteins. In Resumos. São Paulo: Sociedade Brasileira de Física - SBF.
NLM
Molin JPD, Caliri A. The nonextensive parameter q and the topology of native structure of globular proteins. Resumos. 2010 ;[citado 2025 jan. 14 ]
Vancouver
Molin JPD, Caliri A. The nonextensive parameter q and the topology of native structure of globular proteins. Resumos. 2010 ;[citado 2025 jan. 14 ]
; Polizello, Ana Cristina Morseli 
