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Registro Completo |
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Biblioteca(s): |
Embrapa Pesca e Aquicultura. |
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Data corrente: |
08/01/2013 |
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Data da última atualização: |
08/01/2013 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
MARTINEZ, E. R. M.; ALVES, A. L.; SILVEIRA, S. M.; FORESTI, F.; OLIVEIRA, C. |
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Afiliação: |
EMANUEL R. M. MARTINEZ, UNESP Botucatu-SP; ANDERSON LUIS ALVES, CNPASA; SARA M. SILVEIRA, UNESP Botucatu-SP; FAUSTO FORESTI, UNESP Botucatu-SP; CLAUDIO OLIVEIRA, UNESP Botucatu-SP. |
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Título: |
Cytogenetic analysis in the incertae sedis species Astyanax altiparanae Garutti and Britzki, 2000 and Hyphessobrycon eques Steindachner, 1882 (Characiformes, Characidae) from the upper Paraná river basin. |
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Ano de publicação: |
2012 |
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Fonte/Imprenta: |
Comparative Cytogenetics, Sofia, v. 6, n. 1, p. 41-51, 2012. |
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DOI: |
doi: 10.3897/CompCytogen.v6i1.1873 |
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Idioma: |
Inglês |
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Conteúdo: |
Cytogenetic analyses were accomplished in two populations of Astyanax altiparanae Garutti & Britzki, 2000 and one population of Hyphessobrycon eques Steindachner, 1882, considered incertae sedis in Characidae family. Two populations of A. altiparanae (Mogi-Guaçu and Tietê rivers) presented 2n=50, with the same karyotype formula: 6M+12SM+20ST+12A (FN=88). H. eques from Capivara river presented 2n=52 and karyotype formula 14M+16SM+4ST+18A (FN=86). In each karyotype, the nucleolus organizer regions were detected at the end of the short arm of a single medium-sized subtelocentric chromosome. The Chromomycin A3 (CMA3) marking is coincident for the NORs in chromosomes of the two species and present additionally in two different chromosomes of A. altiparanae thus showing interpopulation differences in this species. In H. eques, weak heterochromatic blocks in the position of centromeres and telomeres of most chromosomes and negative C-banding for the NOR bearing chromosome were visualized. The obtained results contribute both to the understanding of karyotype evolution of these species and to the clarifying their phylogenetic relationships. |
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Thesagro: |
Citogenética; Cromossoma; Peixe. |
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Thesaurus Nal: |
Cytogenetic analysis. |
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Categoria do assunto: |
L Ciência Animal e Produtos de Origem Animal |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/73450/1/martinez.pdf
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Marc: |
LEADER 01959naa a2200229 a 4500
001 1944447
005 2013-01-08
008 2012 bl uuuu u00u1 u #d
024 7 $adoi: 10.3897/CompCytogen.v6i1.1873$2DOI
100 1 $aMARTINEZ, E. R. M.
245 $aCytogenetic analysis in the incertae sedis species Astyanax altiparanae Garutti and Britzki, 2000 and Hyphessobrycon eques Steindachner, 1882 (Characiformes, Characidae) from the upper Paraná river basin.$h[electronic resource]
260 $c2012
520 $aCytogenetic analyses were accomplished in two populations of Astyanax altiparanae Garutti & Britzki, 2000 and one population of Hyphessobrycon eques Steindachner, 1882, considered incertae sedis in Characidae family. Two populations of A. altiparanae (Mogi-Guaçu and Tietê rivers) presented 2n=50, with the same karyotype formula: 6M+12SM+20ST+12A (FN=88). H. eques from Capivara river presented 2n=52 and karyotype formula 14M+16SM+4ST+18A (FN=86). In each karyotype, the nucleolus organizer regions were detected at the end of the short arm of a single medium-sized subtelocentric chromosome. The Chromomycin A3 (CMA3) marking is coincident for the NORs in chromosomes of the two species and present additionally in two different chromosomes of A. altiparanae thus showing interpopulation differences in this species. In H. eques, weak heterochromatic blocks in the position of centromeres and telomeres of most chromosomes and negative C-banding for the NOR bearing chromosome were visualized. The obtained results contribute both to the understanding of karyotype evolution of these species and to the clarifying their phylogenetic relationships.
650 $aCytogenetic analysis
650 $aCitogenética
650 $aCromossoma
650 $aPeixe
700 1 $aALVES, A. L.
700 1 $aSILVEIRA, S. M.
700 1 $aFORESTI, F.
700 1 $aOLIVEIRA, C.
773 $tComparative Cytogenetics, Sofia$gv. 6, n. 1, p. 41-51, 2012.
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Registro original: |
Embrapa Pesca e Aquicultura (CNPASA) |
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Registro Completo
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Biblioteca(s): |
Embrapa Agricultura Digital. |
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Data corrente: |
24/11/2010 |
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Data da última atualização: |
23/05/2011 |
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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, 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. |
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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. |
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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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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 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.
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Embrapa Agricultura Digital (CNPTIA) |
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