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| Registros recuperados : 29 | |
| 2. |  | MELO, R. C.; MAZONI, I.; NESHICH, G.; SANTORO, M. M.; MEIRA JUNIOR, W. Protein structure topology comparison based on contact maps. In: ANNUAL INTERNATIONAL CONFERENCE ON INTELLIGENT SYSTEMS FOR MOLECULAR BIOLOGY, 14.; ANNUAL AB3C CONFERENCE, 2., 2006, Fortaleza. Conference Program... Fortaleza: ISCB, 2006. Não paginado. ISMB, X-MEETING 2006. Poster I-5.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 3. | | MELO, R. C.; MAZONI, I.; NESHICH, G.; SANTORO, M. M.; MEIRA JÚNIOR, W. Contacts as the key elements for comparing two protein structures. In: ANNUAL INTERNATIONAL CONFERENCE ON INTELLIGENT SYSTEMS FOR MOLECULAR BIOLOGY, 14.; ANNUAL AB3C CONFERENCE, 2., 2006, Fortaleza. Conference Program... Fortaleza: ISCB, 2006. Não paginado. ISMB, X-MEETING 2006. Poster I-6.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 4. | | MELO, R. C.; GOMIDE, J. S.; MEIRA JUNIOR, W.; LOPES, J. C. D.; NESHICH, G.; SANTORO, M. M. Mining structural signatures in proteins using intrachain interactions. In: INTERNATIONAL CONFERENCE OF THE BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 3., 2007, São Paulo. Proceedings... Campinas: Embrapa Informática Agropecuária, 2007. p. 133. X-meeting 2007.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 5. | | LIMA, F. L.; CARVALHO, M. A. R. de; APOLÔNIO, A. C. M.; BEMQUERER, M. P.; SANTORO, M. M.; OLIVEIRA, J. S.; ALVIANO, C. S.; FARIAS, L. de M. Actinomycetemcomitin: a new bacteriocin produced by Aggregatibacter (Actinobacillus) actinomycetemcomitans. Journal of Industrial Microbiology and Biotechnology, v. 35, p. 103-110, 2008.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| 6. | | LIMA, F. L.; CARVALHO, M. A. R.; SANTORO, M. M.; BEMQUERER, M. P.; OLIVEIRA, J. S.; APOLÔNIO, A. C. M.; ALVIANO, C. S.; FARIAS, L. M. Actinomycetemcomitin: a new bacteriocin produced by Aggregatibacter (Actinobacillus) Actinomycetemcomitans. In: ANNUAL MEETING OF THE SBBq, 36.; IUBMB CONFERENCE, 10., 2007, Salvador, BA. Infectious diseases: biochemistry of parasites, vectors and hosts: program and abstracts. São Paulo, SP: Brazilian Society for Biochemistry and Molecular Biology, 2007.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| 7. | | VIANA, P. A.; REZENDE, S. T. de; ALVES, A. de A.; MANFRINI, R. M.; ALVES, R. J.; BEMQUERER, M. P.; SANTORO, M. M.; GUIMARÃES, V. M. Activity of Debaryomyces hansenii UFV-1 alfa-galactosidades against alfa-D-galactophyranoside derivatives. Carbohydrate Research, v. 346, p. 602-605, 2011.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| 8. | | PIMENTA, A. M. C.; RATES, B.; BLOCH JUNIOR, C.; GOMES, P. C.; SANTORO, M. M.; LIMA, M. E. de; RICHARDSON, M.; CORDEIRO, M. do N. Electrospray ionization quadrupole time-of-flight and matrix-assisted laser desorption/ionization tandem time-of-flight mass spectrometric analyses to solve micro heterogeneity in post-translationally modified peptides from Phoneutria nigriventer (Aranea, Ctenidae) venom. Rapid Communications in Mass Spectrometry, Chichester, UK, v. 19, p. 31-37, 2005.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| 9. | | MELO, R. C.; RIBEIRO, C.; MURRAY, C. S.; VELOSO, C. J. M.; SILVEIRA, C. H. da; NESHICH, G.; MEIRA JUNIOR, W.; CARCERONI, R. L.; SANTORO, M. M. Finding protein-protein interaction patterns by contact map matching. Genetics and Molecular Research, v. 6, n. 4, p. 946-963, 2007.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 10. | | SANTOS, A. M. C.; OLIVEIRA, J. S. de; BITTAR, E. R.; SILVA, A. L. da; GUIA, M. L. dos; BEMQUERER, M. P.; SANTORO, M. M. Improved purification process of β- and α-tripsin isoforms by ion-exchange choromatography. Brazilian Archives of Biology and technologgy: an International Journal, v.51, n. 4, p. 711-721, jul.-ago., 2008.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| 11. | | GOMIDE, F. T. F.; SANTOS, A. M. C.; BITTAR, E. R.; VASCONCELOS, A. B.; TEIXEIRA, K. N.; SANTANA, M. A. de; BEMQUERER, M. P.; SANTORO, M. M. Thermodynamic characterization of alfa trypsin at acid pH range. In: ANNUAL MEETING OF THE SBBq, 36.; IUBMB CONFERENCE, 10., 2007, Salvador, BA. Infectious diseases: biochemistry of parasites, vectors and hosts: program and abstracts. São Paulo, SP: Brazilian Society for Biochemistry and Molecular Biology, 2007.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| 13. | | APOLÔNIO, A. C. M.; CARVALHO, M. A. R.; BEMQUERER, M. P.; SANTORO, M. M.; PINTO, S. Q.; OLIVEIRA, J. S.; SANTOS, K. V.; FARIAS, L. M. Purification and partial characterization of a bacteriocin produced by Eikenella corrodens. Journal of Applied Microbiology, v. 104, p. 508-514, 2008.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| 14. | | RIBEIRO, C.; TOGAWA, R. C.; NESHICH, I. A. P.; MAZONI, I.; MANCINI, A. L.; MINARDI, R. C. de M.; SILVEIRA, C. H. da; JARDINE, J. G.; SANTORO, M. M.; NESHICH, G. Analysis of binding properties and specificity through identification of the interface forming residues (IFR) for serine proteases in silico docked to different inhibitors. BMC Structural Biology, London, v. 10, n. 36, p. 1-16, 2010.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 15. | | RIBEIRO; TOGAWA, R. C.; NESHICH, I. A. P.; MAZONI, I.; MANCINI, A. L.; MINARDI, R. C. de M.; SILVEIRA, C. H. da; JARDINE, J. G.; SANTORO, M. M.; NESHICH, G. Analysis of binding properties and specificity through identification of the interface forming residues (IFR) for serine proteases in silico docked to different inhibitors. BMC Structural Biology, London, v. 10, n. 36, p. 1-16, 2010. Disponível em:.Acesso em: 5 jan. 2011.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| 16. | | VERLY, R. M.; RODRIGUES, M. A.; DAGHASTANLI, K. R. P.; DENADAI, A. M. L.; CUCCOVIA, I. M.; BLOCH JÚNIOR, C.; FRÉZARD, F.; SANTORO, M. M.; PILÓ VELOSO, D.; BEMQUERER, M. P. Effect of cholesterol on the interaction of the amphibian antimicrobial peptide DD K with liposomes. Peptides, v. 29, p. 15-24, 2008.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| 17. | | SILVEIRA, C. H. da; PIRES, D. E. V.; MINARDI, R.; RIBEIRO, C.; VELOSO, C. J. M.; LOPES, J. C. D.; MEIRA JÚNIOR, W.; NESHICH, G.; RAMOS, C. H. I.; HABESCH, R.; SANTORO, M. M. Protein cutoff scanning: a comparative analysis of cutoff dependent and cutoff free methods for prospecting contacts in proteins. Proteins, n. 74, p. 727-743, 2009.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 18. | | SANTOS, A. M. C.; SANTANA, M. A.; GOMIDE, F. T. F.; MIRANDA, A. A. C.; OLIVEIRA, J. S.; VILAS BOAS, F. A. S.; VASCONCELOS, A. B.; TEIXERA, K. N.; BIONDI, I.; BEMQUERER, M. P.; SANTORO, M. M. Physical-chemical characterization and stability study of alfa-trypsin at pH 3.0 by differential scanning calorimetry. In: ANNUAL MEETING OF SBBQ, 37.; CONGRESS OF THE PABMB, 11., 2008, Águas de Lindóia, SP. Abstracts... Águas de Lindóia: SBBq, 2008. 1 - CD-ROM.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| 19. | | SANTOS, A. M. C.; SANTANA, M. A.; GOMIDE, F. T. F.; MIRANDA, A. A. C.; OLIVEIRA, J. S.; VILAS BOAS, F. A. S.; VASCONCELOS, A. B.; BEMQUERER, M. P.; SANTORO, M. M. Physical-chemical characterization and stability study of α-trypsin at pH 3.0 by differential scanning calorimetry. International Journal of Biological Macromolecules, v.42, p. 278-284, 2008.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| 20. | | FIGUEIREDO, J. E. F.; COELHO, V. T. da S.; COELHO, E. A. F.; OLIVEIRA, J. S. de; SANTORO, M. M.; ALMEIDA, P. L. B. de; De PAOLI, H. C.; CORREA, G. V.; TEIXEIRA, M. A.; MOTTA, A. C. F. Bioquímica molecular como ferramenta para conservação e uso da biodiversidade agrícola tropical: desenvolvimento de marcador imunoquímico para identificação da bactérias endofíticas do milho. Sete Lagoas: Embrapa Milho e Sorgo, 2005. 12 p. (Embrapa Milho e Sorgo. Boletim de Pesquisa e Desenvolvimento, 2).| Biblioteca(s): Embrapa Milho e Sorgo. |
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| Registros recuperados : 29 | |
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Registro Completo
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Biblioteca(s): |
Embrapa Agricultura Digital. |
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Data corrente: |
24/11/2010 |
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Data da última atualização: |
23/05/2011 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
B - 1 |
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Autoria: |
RIBEIRO, C.; TOGAWA, R. C.; NESHICH, I. A. P.; MAZONI, I.; MANCINI, A. L.; MINARDI, R. C. de M.; SILVEIRA, C. H. da; JARDINE, J. G.; SANTORO, M. M.; NESHICH, G. |
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Afiliação: |
CRISTINA RIBEIRO, UFMG; ROBERTO C. TOGAWA, CENARGEN; IZABELLA A. P. NESHICH, Estagiária/CNPTIA; IVAN MAZONI, CNPTIA; ADAUTO LUIZ MANCINI, CNPTIA; RAQUEL C. DE MELO MINARDI, UFMG; CARLOS H. DA SILVEIRA, UNIFEI; JOSE GILBERTO JARDINE, CNPTIA; MARCELO M. SANTORO, UFMG; GORAN NESHICH, CNPTIA. |
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Título: |
Analysis of binding properties and specificity through identification of the interface forming residues (IFR) for serine proteases in silico docked to different inhibitors. |
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Ano de publicação: |
2010 |
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Fonte/Imprenta: |
BMC Structural Biology, London, v. 10, n. 36, p. 1-16, 2010. |
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Idioma: |
Inglês |
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Conteúdo: |
Background: Enzymes belonging to the same super family of proteins in general operate on variety of substrates and are inhibited by wide selection of inhibitors. In this work our main objective was to expand the scope of studies that consider only the catalytic and binding pocket amino acids while analyzing enzyme specificity and instead, include a wider category which we have named the Interface Forming Residues (IFR). We were motivated to identify those amino acids with decreased accessibility to solvent after docking of different types of inhibitors to sub classes of serine proteases and then create a table (matrix) of all amino acid positions at the interface as well as their respective occupancies. Our goal is to establish a platform for analysis of the relationship between IFR characteristics and binding properties/specificity for bi-molecular complexes. Results: We propose a novel method for describing binding properties and delineating serine proteases specificity by compiling an exhaustive table of interface forming residues (IFR) for serine proteases and their inhibitors. Currently, the Protein Data Bank (PDB) does not contain all the data that our analysis would require. Therefore, an in silico approach was designed for building corresponding complexes The IFRs are obtained by ?rigid body docking? among 70 structurally aligned, sequence wise non-redundant, serine protease structures with 3 inhibitors: bovine pancreatic trypsin inhibitor (BPTI), ecotine and ovomucoid third domain inhibitor. The table (matrix) of all amino acid positions at the interface and their respective occupancy is created. We also developed a new computational protocol for predicting IFRs for those complexes which were not deciphered experimentally so far, achieving accuracy of at least 0.97. Conclusions: The serine proteases interfaces prefer polar (including glycine) residues (with some exceptions). Charged residues were found to be uniquely prevalent at the interfaces between the ?miscellaneous-virus? subfamily and the three inhibitors. This prompts speculation about how important this difference in IFR characteristics is for maintaining virulence of those organisms. Our work here provides a unique tool for both structure/function relationship analysis as well as a compilation of indicators detailing how the specificity of various serine proteases may have been achieved and/or could be altered. It also indicates that the interface forming residues which also determine specificity of serine protease sub-family can not be presented in a canonical way but rather as a matrix of alternative populations of amino acids occupying variety of IFR positions. MenosBackground: Enzymes belonging to the same super family of proteins in general operate on variety of substrates and are inhibited by wide selection of inhibitors. In this work our main objective was to expand the scope of studies that consider only the catalytic and binding pocket amino acids while analyzing enzyme specificity and instead, include a wider category which we have named the Interface Forming Residues (IFR). We were motivated to identify those amino acids with decreased accessibility to solvent after docking of different types of inhibitors to sub classes of serine proteases and then create a table (matrix) of all amino acid positions at the interface as well as their respective occupancies. Our goal is to establish a platform for analysis of the relationship between IFR characteristics and binding properties/specificity for bi-molecular complexes. Results: We propose a novel method for describing binding properties and delineating serine proteases specificity by compiling an exhaustive table of interface forming residues (IFR) for serine proteases and their inhibitors. Currently, the Protein Data Bank (PDB) does not contain all the data that our analysis would require. Therefore, an in silico approach was designed for building corresponding complexes The IFRs are obtained by ?rigid body docking? among 70 structurally aligned, sequence wise non-redundant, serine protease structures with 3 inhibitors: bovine pancreatic trypsin inhibitor (BPTI), ecotine and ovomuco... Mostrar Tudo |
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Palavras-Chave: |
Enzimas; Interface Forming Residues; Propriedades ligantes; Proteases. |
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Thesaurus NAL: |
Binding properties; Enzymes. |
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Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/23695/1/1472-6807-10-36.pdf
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Marc: |
LEADER 03631naa a2200301 a 4500
001 1867859
005 2011-05-23
008 2010 bl uuuu u00u1 u #d
100 1 $aRIBEIRO, C.
245 $aAnalysis of binding properties and specificity through identification of the interface forming residues (IFR) for serine proteases in silico docked to different inhibitors.$h[electronic resource]
260 $c2010
520 $aBackground: Enzymes belonging to the same super family of proteins in general operate on variety of substrates and are inhibited by wide selection of inhibitors. In this work our main objective was to expand the scope of studies that consider only the catalytic and binding pocket amino acids while analyzing enzyme specificity and instead, include a wider category which we have named the Interface Forming Residues (IFR). We were motivated to identify those amino acids with decreased accessibility to solvent after docking of different types of inhibitors to sub classes of serine proteases and then create a table (matrix) of all amino acid positions at the interface as well as their respective occupancies. Our goal is to establish a platform for analysis of the relationship between IFR characteristics and binding properties/specificity for bi-molecular complexes. Results: We propose a novel method for describing binding properties and delineating serine proteases specificity by compiling an exhaustive table of interface forming residues (IFR) for serine proteases and their inhibitors. Currently, the Protein Data Bank (PDB) does not contain all the data that our analysis would require. Therefore, an in silico approach was designed for building corresponding complexes The IFRs are obtained by ?rigid body docking? among 70 structurally aligned, sequence wise non-redundant, serine protease structures with 3 inhibitors: bovine pancreatic trypsin inhibitor (BPTI), ecotine and ovomucoid third domain inhibitor. The table (matrix) of all amino acid positions at the interface and their respective occupancy is created. We also developed a new computational protocol for predicting IFRs for those complexes which were not deciphered experimentally so far, achieving accuracy of at least 0.97. Conclusions: The serine proteases interfaces prefer polar (including glycine) residues (with some exceptions). Charged residues were found to be uniquely prevalent at the interfaces between the ?miscellaneous-virus? subfamily and the three inhibitors. This prompts speculation about how important this difference in IFR characteristics is for maintaining virulence of those organisms. Our work here provides a unique tool for both structure/function relationship analysis as well as a compilation of indicators detailing how the specificity of various serine proteases may have been achieved and/or could be altered. It also indicates that the interface forming residues which also determine specificity of serine protease sub-family can not be presented in a canonical way but rather as a matrix of alternative populations of amino acids occupying variety of IFR positions.
650 $aBinding properties
650 $aEnzymes
653 $aEnzimas
653 $aInterface Forming Residues
653 $aPropriedades ligantes
653 $aProteases
700 1 $aTOGAWA, R. C.
700 1 $aNESHICH, I. A. P.
700 1 $aMAZONI, I.
700 1 $aMANCINI, A. L.
700 1 $aMINARDI, R. C. de M.
700 1 $aSILVEIRA, C. H. da
700 1 $aJARDINE, J. G.
700 1 $aSANTORO, M. M.
700 1 $aNESHICH, G.
773 $tBMC Structural Biology, London$gv. 10, n. 36, p. 1-16, 2010.
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