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| Registros recuperados : 31 | |
| 3. |  | BACKES, R. L.; REIS, M. S.; CRUZ, C. D.; SEDIYAMA, T.; SEDIYAMA, C. S. Correlation estimates and assessment of selection strategies in five soybean populations. Crop Breeding and Applied Biotechnology, Londrina, v. 3, n. 2, p. 107-115, June 2003.| Biblioteca(s): Embrapa Arroz e Feijão. |
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| 6. | | VOGT, G. A.; BALBINOT JUNIOR, A. A.; TREZZI, M. M.; BACKES, R. L.; NICKNICH, W. Competitive ability of black Common Bean genotypes with weeds. Ciência e Agrotecnologia, Lavras, v. 37, n. 5, p. 397-403, set./out. 2013.| Biblioteca(s): Embrapa Soja. |
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| 8. | | BACKES, R. L.; BALBINOT JUNIOR, A. A.; SAWAZAKI, E.; GALLOTI, G. J. M.; MIRANDA, G. V. Desempenho de genótipos de milho-pipoca no Planalto Norte Catarinense. Agropecuária Catarinense, Florianopólis, v. 20, n. 1, p. 78-81, mar. 2007| Biblioteca(s): Embrapa Hortaliças. |
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| 9. | | HÖFS, A.; BACKES, R. L.; VOGT, G. A.; BALBINOT JUNIOR, A. A.; ZOLDAN, S. R. Ensaios de avaliação de cultivares de milho em santa catarina - safra 2010/11. In: REUNIÃO TÉCNICA CATARINENSE DE MILHO E FEIJÃO, 8., 2011, Chapecó. Resumos expandidos... Chapecó: Epagri, 2011. 5 p. Seção Milho, 1.7. CD-ROM.| Biblioteca(s): Embrapa Soja. |
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| 10. | | BACKES, R. L.; REIS, M. S.; SEDIYAMA, T.; CRUZ, C. D.; BACKES, F. A. A. L. Reaction of soybean lines to stem canker. Crop Breeding and Applied Biotechnology, Viçosa, MG, v. 5, n. 2, p. 223-228, June 2005. Note.| Biblioteca(s): Embrapa Arroz e Feijão. |
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| 12. | | VOGT, G. A.; ELIAS, H. T.; BACKES, R. L.; NICKNICH, W.; BALBINOT JUNIOR, A. A.; CRISPIM, J. E.; HEMP, S. Avaliação de genótipos de feijão vermelho em Santa Catarina: safras 2009/2010 e 2010/11. In: REUNIÃO TÉCNICA CATARINENSE DE MILHO E FEIJÃO, 8., 2011, Chapecó. Resumos expandidos... Chapecó: Epagri, 2011. 5 p. Seção Feijão, 1.6. CD-ROM.| Biblioteca(s): Embrapa Soja. |
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| 13. | | VOGT, G. A.; BALBINOT JUNIOR, A. A.; BACKES, R. L.; SOUZA, A. M. de; GALLOTTI, G. J. M. Estabilidade e adaptabilidade de genótipos de girassol no Planalto Norte Catarinense. Agropecuária Catarinense, Florianópolis, v. 25, n. 1, p. 69-74, mar. 2012.| Biblioteca(s): Embrapa Soja. |
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| 14. | | EMYGDIO, B. M.; TEIXEIRA, M. C. C.; MEIRELLES, W.; PERERIRA, E. R.; BACKES, R. L.; OLIVEIRA, A. C. B. de. Ensaio preliminar de avaliação de variedades de milho em SC e no PR, safra 2008/09. In: REUNIÃO TÉCNICA ANUAL DO MILHO, 54.; REUNIÃO TÉCNICA ANUAL DO SORGO, 37., 2009, Pelotas. Atas e Resumos...Veranópolis: FEPAGRO, 2009. 1 CD-ROM.| Biblioteca(s): Embrapa Clima Temperado. |
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| 15. | | VOGT, G. A.; BALBINOT JUNIOR, A. A.; BACKES, R. L.; HÖFS, A.; DUFLOTH, J. H.; MÁRIO, A. J.; ALMEIDA, E. X. de. Avaliação de cultivares de milho em Santa Catarina - safra 2009/10. In: REUNIÃO TÉCNICA CATARINENSE DE MILHO E FEIJÃO, 8., 2011, Chapecó. Resumos expandidos... Chapecó: Epagri, 2011. 5 p. Seção Milho, 1.1. CD-ROM.| Biblioteca(s): Embrapa Soja. |
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| 16. | | BACKES, R. L.; VOGT, G. A.; ZOLDAN, S. R.; DÁVALOS, E. D.; HOFS, A.; STENGER, E. A. F.; EMYGDIO, B. M. Avaliação preliminar de variedades de polinização aberta de milho em Santa Catarina nas safras 2009/10 e 2010/11. In: REUNIÃO TÉCNICA CATARINENSE DE MILHO E FEIJÃO, 8., 2011, Chapecó. Anais. Resumos... Chapecó: EPAGRI, 2011.| Biblioteca(s): Embrapa Clima Temperado. |
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| 17. | | BACKES, F. A. A. L.; BARBOSA, J. G.; CECON, P. R.; GROSSI, J. A. S.; BACKES, R. L.; FINGER, F. L. Cultivo hidropônico de lisianto para flor de corte em sistema de fluxo laminar de nutrientes Pesquisa Agropecuária Brasileira, Brasília, DF, v. 42, n. 11, p. 1561-1566, nov. 2007 Título em inglês: Hydroponic growth of lisianthus as cut flower under nutrient film technique.| Biblioteca(s): Embrapa Unidades Centrais. |
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| 18. | | VOIGT, G. A.; VALENTINI, V. G.; BACKES, R. L.; BALBINOT JUNIOR, A. A.; SOUZA, A. M. de; SILVA, S. D. dos A. e. Comportamento de cultivares de mamona em diferentes épocas de semeadura no oeste catarinense. In: SIMPÓSIO ESTADUAL DE AGROENERGIA, 2.; REUNIÃO TÉCNICA ANUAL DE AGROENERGIA, 2., 2008, Porto Alegre. Anais... Pelotas: Embrapa Clima Temperado, 2008. 1 CD-ROM.| Biblioteca(s): Embrapa Clima Temperado. |
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| 19. | | VALENTINI, G.; VOGT, G. A.; BACKES, R. L.; BALBINOT JUNIOR, A. A.; SOUZA, A. M. de; SILVA, S. D. dos A. e.; MAGRO, J. D. Desempenho de cultivares de girassol no oeste catarinense. In: SIMPÓSIO ESTADUAL DE AGROENERGIA, 2.; REUNIÃO TÉCNICA ANUAL DE AGROENERGIA, 2., 2008, Porto Alegre. Anais... Pelotas: Embrapa Clima Temperado, 2008. 1 CD-ROM.| Biblioteca(s): Embrapa Clima Temperado. |
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| 20. | | VOGT, G. A.; SOUZA, A. M. de; GALLOTTI, G. J. M.; BACKES, R. L.; BALBINOT JUNIOR, A. A.; SILVA, S. D. dos A. e; VALENTINI, G. Desempenho de cultivares de mamona em Santa Catarina. Agropecuária Catarinense, Florianópolis, v. 24, n. 3, p. 89-91, nov. 2011.| Biblioteca(s): Embrapa Soja. |
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| Registros recuperados : 31 | |
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Registro Completo
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Biblioteca(s): |
Embrapa Recursos Genéticos e Biotecnologia. |
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Data corrente: |
05/01/2011 |
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Data da última atualização: |
03/02/2023 |
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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; 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 COITI 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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Notas: |
Disponível em:.Acesso em: 5 jan. 2011. |
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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 03733naa a2200313 a 4500
001 1871662
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100 1 $aRIBEIRO
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
500 $aDisponível em:<http://www.biomedcentral.com/1472-6807/10/36>.Acesso em: 5 jan. 2011.
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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Embrapa Recursos Genéticos e Biotecnologia (CENARGEN) |
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