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Registro Completo |
Biblioteca(s): |
Embrapa Hortaliças; Embrapa Unidades Centrais. |
Data corrente: |
01/04/1997 |
Data da última atualização: |
01/04/1997 |
Autoria: |
GUEDES, A. C.; MOREIRA, H. M.; MENEZES, J. E. |
Afiliação: |
EMBRAPA-CNPH, Brasilia, DF. |
Título: |
Producao e importacao de sementes de hortalicas no Brasil - 1981-1985. |
Ano de publicação: |
1988 |
Fonte/Imprenta: |
Brasilia: EMBRAPA-CNPH, 1988. |
Páginas: |
141p. |
Série: |
(EMBRAPA-CNPH. Documentos, 2). |
Idioma: |
Português |
Conteúdo: |
O presente trabalho é um contribuição do Centro Nacional de Pesquisa de Hortaliças (CNPH) da EMBRAPA à ações de vários setores para o desenvolvimento da olericultura nacional. Mesmo tratando-se de uma coleta quatittiva de dados, muitas informações importantes foram obtidas, sendo a principal delas a revelação do quadro da realidade do setor e o seu consequente registro histórico. A utilização destes dados por pesquisadores, professores, jprodutore, importadores e comerciantes de sementes será o termômetro que marcará a importância deste trabalho que ora é colacado à disposição de todos. |
Palavras-Chave: |
Brasil; Import; Production; Seed; Vegetable. |
Thesagro: |
Hortaliça; Importação; Produção; Semente. |
Thesaurus Nal: |
Brazil. |
Categoria do assunto: |
-- |
Marc: |
LEADER 01300nam a2200277 a 4500 001 1756908 005 1997-04-01 008 1988 bl uuuu 00u1 u #d 100 1 $aGUEDES, A. C. 245 $aProducao e importacao de sementes de hortalicas no Brasil - 1981-1985. 260 $aBrasilia: EMBRAPA-CNPH$c1988 300 $a141p. 490 $a(EMBRAPA-CNPH. Documentos, 2). 520 $aO presente trabalho é um contribuição do Centro Nacional de Pesquisa de Hortaliças (CNPH) da EMBRAPA à ações de vários setores para o desenvolvimento da olericultura nacional. Mesmo tratando-se de uma coleta quatittiva de dados, muitas informações importantes foram obtidas, sendo a principal delas a revelação do quadro da realidade do setor e o seu consequente registro histórico. A utilização destes dados por pesquisadores, professores, jprodutore, importadores e comerciantes de sementes será o termômetro que marcará a importância deste trabalho que ora é colacado à disposição de todos. 650 $aBrazil 650 $aHortaliça 650 $aImportação 650 $aProdução 650 $aSemente 653 $aBrasil 653 $aImport 653 $aProduction 653 $aSeed 653 $aVegetable 700 1 $aMOREIRA, H. M. 700 1 $aMENEZES, J. E.
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Registro original: |
Embrapa Hortaliças (CNPH) |
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Registro Completo
Biblioteca(s): |
Embrapa Recursos Genéticos e Biotecnologia. |
Data corrente: |
05/01/2011 |
Data da última atualização: |
03/06/2024 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Circulação/Nível: |
B - 1 |
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. |
Afiliação: |
CRISTINA RIBEIRO, UFMG; ROBERTO COITI TOGAWA, CENARGEN; IZABELLA A. P. NESHICH; 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. |
Título: |
Analysis of binding properties and specificity through identification of the interface forming residues (IFR) for serine proteases in silico docked to different inhibitors. |
Ano de publicação: |
2010 |
Fonte/Imprenta: |
BMC Structural Biology, London, v. 10, n. 36, p. 1-16, 2010. |
Idioma: |
Inglês |
Notas: |
Disponível em:.Acesso em: 5 jan. 2011. |
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 |
Palavras-Chave: |
Enzimas; Interface Forming Residues; Propriedades ligantes; Proteases. |
Thesaurus NAL: |
Binding properties; Enzymes. |
Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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 005 2024-06-03 008 2010 bl uuuu u00u1 u #d 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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