| |
|
|
|
Registro Completo |
|
Biblioteca(s): |
Embrapa Agricultura Digital; Embrapa Milho e Sorgo. |
|
Data corrente: |
06/12/2022 |
|
Data da última atualização: |
06/12/2022 |
|
Tipo da produção científica: |
Resumo em Anais de Congresso |
|
Autoria: |
DART, R. de O.; PINTO, D. M.; MOTA, C.; AMORIM, A.; SIMÕES, M.; DRUCKER, D. P.; CRISCUOLO, C.; CUSTODIO, D. de O.; BORBA, R.; GOVEIA, S. S.; GRIGOLIN, G.; CAMBOIM, S.; LANDAU, E. C.; GARRASTAZU, M. C.; SILVA, M. F. da; BERTIN, P. R. B. |
|
Afiliação: |
RICARDO DE OLIVEIRA DART, CNPS; DANIELA MACIEL PINTO, CNPM; CARLOS MOTA, SERVIÇO GEOLÓGICO DO BRASIL; ALEXANDRE AMORIM, AGÊNCIA NACIONAL DE ÁGUAS E SANEAMENTO BÁSICO; MARGARETH GONCALVES SIMOES, CNPS; DEBORA PIGNATARI DRUCKER, CNPTIA; CRISTINA CRISCUOLO, CNPM; DAVI DE OLIVEIRA CUSTODIO, CNPM; ROGÉRIO BORBA, INSTITUTO BRASILEIRO DE GEOGRAFIA E ESTATÍSTICA; SIDNEY SCHABERLE GOVEIA, GEOSABER / QGIS BR; GIULIANO GRIGOLIN, SISTEMA INTEGRADO DE BASES GEOESPACIAIS DO ESTADO DO ESPÍRITO SANTO GEOBASES; SILVANA CAMBOIM, UNIVERSIDADE FEDERAL DO PARANÁ; ELENA CHARLOTTE LANDAU, CNPMS; MARILICE CORDEIRO GARRASTAZU, CNPF; MAURIELLE FELIX DA SILVA, MINISTÉRIO PÚBLICO DO PARANÁ; PATRICIA ROCHA BELLO BERTIN, DEPI. |
|
Título: |
GeoNode-BR: comunidade brasileira para a colaboração entre usuários do software GeoNode. |
|
Ano de publicação: |
2022 |
|
Fonte/Imprenta: |
In: SIMPÓSIO BRASILEIRO DE INFRAESTRUTURA DE DADOS ESPACIAIS, 3., 2022. Geoinformação aberta para o desenvolvimento sustentável: anais. Rio de Janeiro: IBGE, 2022. p. 185-187. |
|
Idioma: |
Português |
|
Notas: |
Evento online. SBIDE 2002. |
|
Conteúdo: |
O GeoNode é uma solução web para o gerenciamento de recursos espaciais [1], e para a implantação de Infraestruturas de Dados Espaciais (IDEs). É uma solução livre e de código aberto, que oferece suporte aos padrões do Open Geoespatial Consortium (OGC) [2], além de ser extensível e interoperável com outras plataformas. O GeoNode possui uma estrutura de metadados baseada na ISO 19115 [3], essa aplicação Free Open Source Software (FOSS) GIS web tem sido uma ótima alternativa para implantar IDE e, por essa razão, tem sido muito adotada por empresas e instituições que possuem grande acervo de dados espaciais no Brasil e no mundo. Desta forma, visando trocar experiências sobre a aplicação FOSS GeoNode, profissionais de gestão de geoinformação da Embrapa, CPRM, ANA, IBGE e Geobases criaram um Grupo de Trabalho (GT) com reuniões periódicas a partir de 2020. Destas reuniões surgiu o interesse em criar uma comunidade brasileira de usuários GeoNode, e organizar um primeiro evento para disseminar, compartilhar e difundir conhecimentos sobre essa aplicação FOSS GIS, além de identificar outras iniciativas, em curso no país, que também estejam utilizando o GeoNode. |
|
Palavras-Chave: |
Dados espaciais; Geoinformação. |
|
Thesaurus Nal: |
Spatial data. |
|
Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
|
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/doc/1149252/1/GeoNode-BR-2022.pdf
|
|
Marc: |
LEADER 02288nam a2200337 a 4500
001 2149258
005 2022-12-06
008 2022 bl uuuu u01u1 u #d
100 1 $aDART, R. de O.
245 $aGeoNode-BR$bcomunidade brasileira para a colaboração entre usuários do software GeoNode.$h[electronic resource]
260 $aIn: SIMPÓSIO BRASILEIRO DE INFRAESTRUTURA DE DADOS ESPACIAIS, 3., 2022. Geoinformação aberta para o desenvolvimento sustentável: anais. Rio de Janeiro: IBGE, 2022. p. 185-187.$c2022
500 $aEvento online. SBIDE 2002.
520 $aO GeoNode é uma solução web para o gerenciamento de recursos espaciais [1], e para a implantação de Infraestruturas de Dados Espaciais (IDEs). É uma solução livre e de código aberto, que oferece suporte aos padrões do Open Geoespatial Consortium (OGC) [2], além de ser extensível e interoperável com outras plataformas. O GeoNode possui uma estrutura de metadados baseada na ISO 19115 [3], essa aplicação Free Open Source Software (FOSS) GIS web tem sido uma ótima alternativa para implantar IDE e, por essa razão, tem sido muito adotada por empresas e instituições que possuem grande acervo de dados espaciais no Brasil e no mundo. Desta forma, visando trocar experiências sobre a aplicação FOSS GeoNode, profissionais de gestão de geoinformação da Embrapa, CPRM, ANA, IBGE e Geobases criaram um Grupo de Trabalho (GT) com reuniões periódicas a partir de 2020. Destas reuniões surgiu o interesse em criar uma comunidade brasileira de usuários GeoNode, e organizar um primeiro evento para disseminar, compartilhar e difundir conhecimentos sobre essa aplicação FOSS GIS, além de identificar outras iniciativas, em curso no país, que também estejam utilizando o GeoNode.
650 $aSpatial data
653 $aDados espaciais
653 $aGeoinformação
700 1 $aPINTO, D. M.
700 1 $aMOTA, C.
700 1 $aAMORIM, A.
700 1 $aSIMÕES, M.
700 1 $aDRUCKER, D. P.
700 1 $aCRISCUOLO, C.
700 1 $aCUSTODIO, D. de O.
700 1 $aBORBA, R.
700 1 $aGOVEIA, S. S.
700 1 $aGRIGOLIN, G.
700 1 $aCAMBOIM, S.
700 1 $aLANDAU, E. C.
700 1 $aGARRASTAZU, M. C.
700 1 $aSILVA, M. F. da
700 1 $aBERTIN, P. R. B.
Download
Esconder MarcMostrar Marc Completo |
|
Registro original: |
Embrapa Agricultura Digital (CNPTIA) |
|
|
Biblioteca |
ID |
Origem |
Tipo/Formato |
Classificação |
Cutter |
Registro |
Volume |
Status |
URL |
Voltar
|
|
|
Registro Completo
|
Biblioteca(s): |
Embrapa Agricultura Digital. |
|
Data corrente: |
24/11/2010 |
|
Data da última atualização: |
23/05/2011 |
|
Tipo da produção científica: |
Artigo em Periódico Indexado |
|
Circulação/Nível: |
B - 1 |
|
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. |
|
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. |
|
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 |
|
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
|
|
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.
Download
Esconder MarcMostrar Marc Completo |
|
Registro original: |
Embrapa Agricultura Digital (CNPTIA) |
|
|
Biblioteca |
ID |
Origem |
Tipo/Formato |
Classificação |
Cutter |
Registro |
Volume |
Status |
Fechar
|
| Expressão de busca inválida. Verifique!!! |
|
|
