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Registros recuperados : 79 | |
25. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | SANTOS, M. T.; FERRAZ, L. F. C.; REIS, F. C.; FALCÃO, P. R. K.; NESHICH, G.; OTTOBONI, L. M. M. Análise estrutural e funcional da proteína CMP quinase de Acidithiobacillus ferrooxidans. In: CONGRESSO BRASILEIRO DE GENÉTICA, 51., 2005, Águas de Lindóia. Resumos... Águas de Lindóias: SBG, 2005. p. 1075. Na publicação: Falcão, PK. Biblioteca(s): Embrapa Agricultura Digital. |
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27. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | SIMÕES, M.; BAHIA, D.; TORRES, K.; ZERLOTINI NETO, A.; ARTIGUENAVE, F.; FALCAO, P. R. K.; NESHICH, G.; OLIVEIRA, G. SNP identification in Schistosoma mansoni expressed genes. In: X-MEETING; INTERNATIONAL CONFERENCE OF THE AB3C, 1., 2005, Caxambu. [Proceedings...]. [S.l.]: Associação Brasileira de Bioinformática e Biologia Computacional, 2005. p. 131. X-meeting 2005. Presented Posters. Na publicação: Paula Kuser. Biblioteca(s): Embrapa Agricultura Digital. |
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28. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | GUELFI, A.; CHABREGAS, S. M.; FALCO, M. C.; FALCAO, P. R. K.; NESHICH, G.; AZEVEDO, R. A. Molecular dynamics analysis of glutathione transferases sugarcane mutants and their interactions with atrazine. In: X-MEETING; INTERNATIONAL CONFERENCE OF THE AB3C, 1., 2005, Caxambu. [Proceedings...]. [S.l.]: Associação Brasileira de Bioinformática e Biologia Computacional, 2005. p. 94. X-meeting 2005. Presented posters. Biblioteca(s): Embrapa Agricultura Digital. |
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29. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | FALCAO, P. R. K.; YAMAGISHI, M. E. B.; BORRO, L.; MANCINI, A. L.; HIGA, R. H.; NESHICH, G. Identification of folding essential residues by looking at an extensive DB of the structure descriptors in Diamond STING. In: ANNUAL INTERNATIONAL CONFERENCE ON INTELLIGENT SYSTEMS FOR MOLECULAR BIOLOGY, 13., 2005, Detroit. Program... Detroit: ISCB, 2005. p. 71. Na publicação: Paula Kuser; Michel Yamagishi; Adauto Mancini; Roberto Higa; Goran Neshich. ISMB 2005. Poster A-47. Biblioteca(s): Embrapa Agricultura Digital. |
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30. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | ZERLOTINI NETO, A.; NHANI JÚNIOR, A.; VIEIRA, F. D.; CINTRA, L. C.; MUDADU, M. de A.; FALCÃO, P. R. K.; GIACHETTO, P. F. Aplicações da bioinformática na agricultura. In: MASSRUHÁ, S. M. F. S.; LEITE, M. A. de A.; OLIVEIRA, S. R. de M.; MEIRA, C. A. A.; LUCHIARI JUNIOR, A.; BOLFE, E. L. (Ed.). Agricultura digital: pesquisa, desenvolvimento e inovação nas cadeias produtivas. Brasília, DF: Embrapa, 2020. cap. 10, p. 234-257. Biblioteca(s): Embrapa Agricultura Digital. |
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31. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | ZERLOTINI NETO, A.; NHANI JÚNIOR, A.; VIEIRA, F. D.; CINTRA, L. C.; MUDADU, M. de A.; FALCÃO, P. R. K.; GIACHETTO, P. F. Applications of bioinformatics in agriculture. In: MASSRUHÁ, S. M. F. S.; LEITE, M. A. de A.; OLIVEIRA, S. R. de M.; MEIRA, C. A. A.; LUCHIARI JUNIOR, A.; BOLFE, E. L. (ed.). Digital agriculture: research, development and innovation in production chains. Brasília, DF: Embrapa, 2023. cap. 10, p. 179-194. Biblioteca(s): Embrapa Agricultura Digital. |
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32. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | NARCISO, M. G.; YAMAGISHI, M. E. B.; QUINAGLIA, T.; SANTOS, E. H. dos; VIEIRA, F. D.; JARDINE, J. G.; MAZONI, I.; FALCAO, P. R. K.; NESHICH, G. Aspectos computacionais da análise da co-evolução de aminoácidos que pertencem a uma proteína qualquer. Campinas: Embrapa Informática Agropecuária, 2006. 4 p. (Embrapa Informática Agropecuária. Comunicado técnico, 77). Na publicação: Goran Neshich. Biblioteca(s): Embrapa Agricultura Digital. |
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33. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | NARCISO, M. G.; YAMAGISHI, M. E. B.; QUINAGLIA, T.; SANTOS, E. H. dos; VIEIRA, F. D.; JARDINE, J. G.; MAZONI, I.; FALCAO, P. R. K.; NESHICH, G. Projeções de superfície 3D no plano para análise de interfaces proteicas através do Sting. Campinas: Embrapa Informática Agropecuária, 2006. 5 p. (Embrapa Informática Agropecuária. Comunicado técnico, 78). Na publicação: Goran Neshich. Biblioteca(s): Embrapa Agricultura Digital. |
| ![Visualizar detalhes do registro](/consulta/web/img/visualizar.png) ![Acesso ao objeto digital](/consulta/web/img/pdf.png) ![Imprime registro no formato completo](/consulta/web/img/print.png) |
34. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | FALCÃO, P. R. K.; MAZONI, I.; YAMAGISHI, M. E. B.; BORRO, L. C.; JARDINE, J. G.; SANTOS, E. H. dos; OLIVEIRA, S. R. de M.; NESHICH, G. Protein ligand contacts analyzed in an integrated environment with the other sequence and structure related parameters. In: ANNUAL INTERNATIONAL CONFERENCE ON INTELLIGENT SYSTEMS FOR MOLECULAR BIOLOGY, 14.; ANNUAL AB3C CONFERENCE, 2., 2006, Fortaleza. Conference Program... Fortaleza: ISCB, 2006. Não paginado. Na publicação: Paula Kuser, Stanley R. M. Oliveira. ISMB, X-MEETING 2006. Poster I-49. Biblioteca(s): Embrapa Agricultura Digital. |
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36. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | MANCINI, A. L.; HIGA, R. H.; OLIVEIRA, A.; DOMINIQUINI, F.; FALCAO, P. R. K.; YAMAGISHI, M. E. B.; TOGAWA, R. C.; NESHICH, G. Sting contacts: a web-based application for identification and analysis of amino acid contacts within protein structure and across protein interfaces. Bioinformatics, v. 20, n. 13, p. 2145-2147, 2004. Na publicação: P. R. Kuser. Biblioteca(s): Embrapa Agricultura Digital. |
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39. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | SOUZA, M. I. F.; VISOLI, M. C.; TORRES, T. Z.; OSAWA, C. C.; SILVA, A. R. da; GIACHETTO, P. F.; NHANI JUNIOR, A.; FALCAO, P. R. K. Catalogação de datasets ômicos no Repositório de Dados de Pesquisa da Embrapa. Revista Brasileira de Biblioteconomia e Documentação, v. 18, p. 1-28, 2022. Biblioteca(s): Embrapa Agricultura Digital; Embrapa Unidades Centrais. |
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40. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | HERAI, R. H.; VIDAL, R. O.; CARAZZOLLE, M. F.; COSTA, G. G. L.; FALCAO, P. R. K.; YAMAGISHI, M. E. B.; FRANCHINI, K. G.; PEREIRA, G. G. A. CNBi: the new Brazilian National Consortium for Bioinformatics. In: INTERNATIONAL CONFERENCE OF THE BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 6., 2010, Ouro Preto. Abstracts... [S.l.: s.n.], 2010. p. 110. X-meeting 2010. Biblioteca(s): Embrapa Agricultura Digital. |
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Registros recuperados : 79 | |
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![](/consulta/web/img/deny.png) | Acesso ao texto completo restrito à biblioteca da Embrapa Agricultura Digital. Para informações adicionais entre em contato com cnptia.biblioteca@embrapa.br. |
Registro Completo
Biblioteca(s): |
Embrapa Agricultura Digital. |
Data corrente: |
25/04/2006 |
Data da última atualização: |
17/01/2020 |
Tipo da produção científica: |
Resumo em Anais de Congresso |
Autoria: |
HIGA, R. H.; CRUZ, S. A. B. da; FALCAO, P. R. K.; YAMAGISHI, M. E. B.; FILETO, R.; MANCINI, A. L.; NESHICH, G. |
Afiliação: |
ROBERTO HIROSHI HIGA, CNPTIA; SERGIO APARECIDO BRAGA DA CRUZ, CNPTIA; PAULA REGINA KUSER FALCAO, CNPTIA; MICHEL EDUARDO BELEZA YAMAGISHI, CNPTIA; RENATO FILETO, CNPTIA; ADAUTO LUIZ MANCINI, CNPTIA; GORAN NESIC, CNPTIA. |
Título: |
Building multiple sequence alignments with a flavour of HSSP alignments. |
Ano de publicação: |
2005 |
Fonte/Imprenta: |
In: X-MEETING; INTERNATIONAL CONFERENCE OF THE AB3C, 1., 2005, Caxambu. [Proceedings...]. [S.l.]: Associação Brasileira de Bioinformática e Biologia Computacional, 2005. |
Páginas: |
p. 28. |
Idioma: |
Inglês |
Notas: |
X-meeting 2005. Presented Posters. Na publicação: Paula Regina Kuser. |
Conteúdo: |
HSSP is a well-know database of MSAs which merges information of protein sequences and their three-dimensional structures. It is available for all proteins whose structure is deposited in the PDB databank. It is also used by STING and JavaProtein Dossier to calculate and present relative entropy as a measurement of a degree of conservation for each residue of proteins whose structure has been solved and deposited in the PDB. However, if the STING and JavaProtein Dossier are to provide support for analysis of protein structures modeled in computers or being experimentally solved but not yet deposited in the PDB, then we have to have a new method for building alignments having a flavour of HSSP alignments (myMSAr). This work presents this new method and its corresponding databank (SH2Qs - database of Sequences Homologue to the Query [Structure-having] Sequence). Our main interest on making myMSAr was to measure the degree of residue conservation for a given query sequence, regardless if it has a corresponding structure deposited in the PDB databank. In this work, we compare the measurement of residue conservation provided by corresponding alignments produced by the HSSP and SH2Qs. As a case study, we also present two biologically relevant examples, the former one highlighting the equivalence of analysis of a degree of residue conservation by using HSSP or SH2Qs alignments, and the later one presenting the degree of residue conservation for a structure modeled in a computer and, as a consequence, which does not have alignment reported by HSSP. MenosHSSP is a well-know database of MSAs which merges information of protein sequences and their three-dimensional structures. It is available for all proteins whose structure is deposited in the PDB databank. It is also used by STING and JavaProtein Dossier to calculate and present relative entropy as a measurement of a degree of conservation for each residue of proteins whose structure has been solved and deposited in the PDB. However, if the STING and JavaProtein Dossier are to provide support for analysis of protein structures modeled in computers or being experimentally solved but not yet deposited in the PDB, then we have to have a new method for building alignments having a flavour of HSSP alignments (myMSAr). This work presents this new method and its corresponding databank (SH2Qs - database of Sequences Homologue to the Query [Structure-having] Sequence). Our main interest on making myMSAr was to measure the degree of residue conservation for a given query sequence, regardless if it has a corresponding structure deposited in the PDB databank. In this work, we compare the measurement of residue conservation provided by corresponding alignments produced by the HSSP and SH2Qs. As a case study, we also present two biologically relevant examples, the former one highlighting the equivalence of analysis of a degree of residue conservation by using HSSP or SH2Qs alignments, and the later one presenting the degree of residue conservation for a structure modeled in a computer and... Mostrar Tudo |
Palavras-Chave: |
Entropia relativa; Multiple sequence alignment; Relative entropy; Residue conservation. |
Thesagro: |
Proteina. |
Thesaurus NAL: |
Sequence alignment. |
Categoria do assunto: |
-- |
Marc: |
LEADER 02541nam a2200277 a 4500 001 1008967 005 2020-01-17 008 2005 bl uuuu u00u1 u #d 100 1 $aHIGA, R. H. 245 $aBuilding multiple sequence alignments with a flavour of HSSP alignments.$h[electronic resource] 260 $aIn: X-MEETING; INTERNATIONAL CONFERENCE OF THE AB3C, 1., 2005, Caxambu. [Proceedings...]. [S.l.]: Associação Brasileira de Bioinformática e Biologia Computacional$c2005 300 $ap. 28. 500 $aX-meeting 2005. Presented Posters. Na publicação: Paula Regina Kuser. 520 $aHSSP is a well-know database of MSAs which merges information of protein sequences and their three-dimensional structures. It is available for all proteins whose structure is deposited in the PDB databank. It is also used by STING and JavaProtein Dossier to calculate and present relative entropy as a measurement of a degree of conservation for each residue of proteins whose structure has been solved and deposited in the PDB. However, if the STING and JavaProtein Dossier are to provide support for analysis of protein structures modeled in computers or being experimentally solved but not yet deposited in the PDB, then we have to have a new method for building alignments having a flavour of HSSP alignments (myMSAr). This work presents this new method and its corresponding databank (SH2Qs - database of Sequences Homologue to the Query [Structure-having] Sequence). Our main interest on making myMSAr was to measure the degree of residue conservation for a given query sequence, regardless if it has a corresponding structure deposited in the PDB databank. In this work, we compare the measurement of residue conservation provided by corresponding alignments produced by the HSSP and SH2Qs. As a case study, we also present two biologically relevant examples, the former one highlighting the equivalence of analysis of a degree of residue conservation by using HSSP or SH2Qs alignments, and the later one presenting the degree of residue conservation for a structure modeled in a computer and, as a consequence, which does not have alignment reported by HSSP. 650 $aSequence alignment 650 $aProteina 653 $aEntropia relativa 653 $aMultiple sequence alignment 653 $aRelative entropy 653 $aResidue conservation 700 1 $aCRUZ, S. A. B. da 700 1 $aFALCAO, P. R. K. 700 1 $aYAMAGISHI, M. E. B. 700 1 $aFILETO, R. 700 1 $aMANCINI, A. L. 700 1 $aNESHICH, G.
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