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| Registros recuperados : 77 | |
| 2. |  | MAZONI, I.; NESHICH, G. DIPN: a dictionary of the internal proteins nanoenvironments and their potential for transformation into agricultural assets. 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. 9, p. 165-177.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 3. | | MAZONI, I.; NESHICH, G. DPIN: um dicionário dos nanoambientes internos das proteínas e seu potencial para transformação em ativos para a 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. 9, p. 218-232.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 10. | | 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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| 12. | | MAZONI, I.; JARDINE, J. G.; BORRO, L. C.; ALVARENGA, D.; NESHICH, G. Electrostatic potential at the alpha carbon atoms along the alpha helices and beta strands. In: ANNUAL MEETING OF SBBQ, 37.; CONGRESS OF THE PAN-AMERICAN ASSOCIATION FOR BIOCHEMISTRY AND MOLECULAR BIOLOGY, 11, 2008, Águas de Lindóia. Program and index... Águas de Lindóia, Program and index... Águas de Lindóia: SBBq, 2008. Não paginado. PABMB.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 14. | | SALIM, J. A.; BORRO, L.; MAZONI, I.; YANO, I. H.; JARDINE, J. G.; NESHICH, G. Multiple structure single parameter: analysis of a single protein nano environment descriptor characterizing a shared loci on structurally aligned proteins. Bioinformatics, v. 32, n. 12, p. 1885-1887, 2016.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 16. | | PENA, I.; MANCINI, A. L.; MAZONI, I.; JARDINE, J. G.; NESHICH, G.; ORTEGA, J. M. Identification of philogenetic relationship between GDPD and SMaseD proteins based on active site amino acid physical chemical properties. In: INTERNATIONAL CONFERENCE OF BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 4., 2008, Salvador. Proceedings... Salvador: AB³C, 2008. Não paginado. X-Meeting 2008.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 17. | | BORRO, L. C.; SALIM, J. A.; MAZONI, I.; YANO, I.; JARDINE, J. G.; NESHICH, G. Improving binding affinity prediction by using a rule-based model with physical-chemical and structural descriptors of the nano-environment for protein-ligand interactions. In: CONGRESS OF THE INTERNATIONAL UNION FOR BIOCHEMISTRY AND MOLECULAR BIOLOGY, 23.; ANNUAL MEETING OF THE BRAZILIAN SOCIETY FOR BIOCHEMISTRY AND MOLECULAR BIOLOGY, 44., 2015, Foz do Iguaçu. Biochemistry for a better world: abstracts book. [Foz do Iguaçu]: SBBq, 2015. p. 153. C.047.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 18. | | NESHICH, G.; JARDINE, J. G.; BERNARDES, R.; MAZONI, I.; MANCINI, A. L.; SILVEIRA, C. da. "Cloud computation" na forma de serviços WEB para um banco de dados federativo STING_RDB. In: SIMPÓSIO SOBRE INOVAÇÃO E CRIATIVIDADE CIENTÍFICA NA EMBRAPA, 1., 2008, Brasília, DF. Comunicações Selecionadas. Brasília, DF: Embrapa, 2008. Não paginado.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 19. | | 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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| 20. | | JARDINE, J. G.; MAZONI, I.; BORRO, L. C.; ALVARENGA, D.; NESHICH, G. Signature contact coordination patterns for secondary structure elements in protein structures. In: ANNUAL MEETING OF SBBQ, 37.; CONGRESS OF THE PAN-AMERICAN ASSOCIATION FOR BIOCHEMISTRY AND MOLECULAR BIOLOGY, 11, 2008, Águas de Lindóia. Program and index... Águas de Lindóia: SBBq, 2008. Não paginado. PABMB.| Biblioteca(s): Embrapa Agricultura Digital. |
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| Registros recuperados : 77 | |
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 | Acesso ao texto completo restrito à biblioteca da Embrapa Agricultura Digital. Para informações adicionais entre em contato com cnptia.biblioteca@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Agricultura Digital; Embrapa Recursos Genéticos e Biotecnologia. |
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Data corrente: |
06/08/2008 |
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Data da última atualização: |
24/10/2022 |
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Tipo da produção científica: |
Artigo em Anais de Congresso / Nota Técnica |
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Autoria: |
TOGAWA, R. C.; RIBEIRO, C.; MAZONI, I.; PELLIGRINELLI, T.; JARDINE, J. G.; NESHICH, G. |
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Afiliação: |
Roberto Coiti Togawa, Embrapa Recursos Genéticos e Biotecnologia; Cristina Ribeiro, UFMG; Ivan Mazoni, Embrapa Informação Tecnógica; Thais Vital Pelligrinelli, Embrapa Informação Tecnógica; José Gilberto Jardine, Embrapa Informação Tecnógica; Goran Neshich, Embrapa Informação Tecnógica. |
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Título: |
The table of interface forming residues as the specificity indicator for serine proteases bound to different inhibitors. |
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Ano de publicação: |
2008 |
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Fonte/Imprenta: |
In: INTERNATIONAL CONFERENCE ON BIOINFORMATICS & COMPUTATIONAL BIOLOGY, 2008, Georgia. Las Vegas Nevada: CSREA, 2008, p. 811-817. |
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Idioma: |
Inglês |
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Notas: |
BIOCOMP 2008. WORLDCOMP'08 |
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Conteúdo: |
We propose a novel method for defining the exclusive and exhaustive table of serine proteases specificity determining interface forming residues (IFR). The IFR are obtained by "hard body docking" among 73 structurally aligned, sequence wise non redundant, serine protease structures, with 3 inhibitors: ecotine, ovomucoid third domain inhibitor and basic pancreatic trypsin inhibitors. In silico constructed complexes offered a condition for determining which residues are participating, from both enzyme and inhibitor side, in the ensemble of amino acids that upon biding loose contact with a solvent. Our focus is on offering a thorough study on how the specificity is achieved among serine proteases even though they have very little difference in their tertiary structure (specifically if the position of catalytic triad residues is considered). Presented table of serine protease specificity based on IFR position occupation show clear variations among sub families such as: trypsines, chymotrypsines, elastases and thrombines. |
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Palavras-Chave: |
Aminoácidos; Enzyme specificity; Especificidade enzimática; Hard body docking; Interface formando resíduos; Interface forming residues; Proteases de serina. |
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Thesagro: |
Enzima. |
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Thesaurus NAL: |
Enzymes; Serine proteinases. |
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Categoria do assunto: |
-- |
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Marc: |
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001 1191302
005 2022-10-24
008 2008 bl uuuu u00u1 u #d
100 1 $aTOGAWA, R. C.
245 $aThe table of interface forming residues as the specificity indicator for serine proteases bound to different inhibitors.$h[electronic resource]
260 $aIn: INTERNATIONAL CONFERENCE ON BIOINFORMATICS & COMPUTATIONAL BIOLOGY, 2008, Georgia. Las Vegas Nevada: CSREA, 2008, p. 811-817.$c2008
500 $aBIOCOMP 2008. WORLDCOMP'08
520 $aWe propose a novel method for defining the exclusive and exhaustive table of serine proteases specificity determining interface forming residues (IFR). The IFR are obtained by "hard body docking" among 73 structurally aligned, sequence wise non redundant, serine protease structures, with 3 inhibitors: ecotine, ovomucoid third domain inhibitor and basic pancreatic trypsin inhibitors. In silico constructed complexes offered a condition for determining which residues are participating, from both enzyme and inhibitor side, in the ensemble of amino acids that upon biding loose contact with a solvent. Our focus is on offering a thorough study on how the specificity is achieved among serine proteases even though they have very little difference in their tertiary structure (specifically if the position of catalytic triad residues is considered). Presented table of serine protease specificity based on IFR position occupation show clear variations among sub families such as: trypsines, chymotrypsines, elastases and thrombines.
650 $aEnzymes
650 $aSerine proteinases
650 $aEnzima
653 $aAminoácidos
653 $aEnzyme specificity
653 $aEspecificidade enzimática
653 $aHard body docking
653 $aInterface formando resíduos
653 $aInterface forming residues
653 $aProteases de serina
700 1 $aRIBEIRO, C.
700 1 $aMAZONI, I.
700 1 $aPELLIGRINELLI, T.
700 1 $aJARDINE, J. G.
700 1 $aNESHICH, G.
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Embrapa Recursos Genéticos e Biotecnologia (CENARGEN) |
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