| |
|
|
|
Registro Completo |
|
Biblioteca(s): |
Embrapa Soja. |
|
Data corrente: |
21/12/2000 |
|
Data da última atualização: |
09/03/2006 |
|
Autoria: |
CORSO, I. C.; HOFFMANN-CAMPO, C.B. |
|
Título: |
Control of Sternechus subsignatus (Col.: Curculionidae) with insecticides applied on soybean plants. |
|
Ano de publicação: |
2000 |
|
Fonte/Imprenta: |
In: INTERNATIONAL CONGRESS OF ENTOMOLOGY, 21., 2000, Foz do Iguassu. Abstracts... Londrina: Embrapa Soja, 2000. |
|
Volume: |
v.2 |
|
Páginas: |
p.671. |
|
Idioma: |
Inglês |
|
Conteúdo: |
Sternechus subsignatus Boheman (Col.: Curculionidae), a stem borer gall maker, is a weevil that damage soybean plants by scraping stems and petioles, sometimes causing total loss of soybean fields. Aiming to test some insecticides and dosages for controling the weevil, two field experiments were carried out in 1998, in Maua da Serra and Pinhao, Parana State, Brazil. The experiment was in a randomized complete block desing, with four replicates per treatment. The plots measured 4x8m and 6x7m, respectivelly for each location; plants were at the V6 and V3 growing stage. Treatments e evaluated were: beta-cyfluthrin, in the emulsifiable concentrate (EC) and flowable (FW) formulations (10ga.i.ha -1), ethophenprox (45ga.i.ha -1), fipronil (32, 48 e 64 ga.i.ha -1), methamidophos (480ga.i.ha -1), thiamethoxan (210ga.i.ha -1) and a control (without spraying). Alive adults were sampled at 0, 2, 5 ou 6, and 12 or 14 days after application (DAA) of the insecticides in 12m (Maua da Serra) and 5m (Pinhao) os soybean row. In this last site, the initial stand of healthy plants and the number of plants attacked by the insect were also evaluated. Beta-cyfluthrin FW, fipronil (at the 3 tested doses), methamidophos and thiamethoxanwere efficient, reaching at least 80% of control until 5-6 DAA, inthe first experiment. Fipronil (at the 3 doses) and thiamethoxan were also efficient in the second experiment. According the data, the insecticides fipronil and thiamethoxan showed a larger residual power for controling S. subsignatus, providing a lesses final number of attacked plants. MenosSternechus subsignatus Boheman (Col.: Curculionidae), a stem borer gall maker, is a weevil that damage soybean plants by scraping stems and petioles, sometimes causing total loss of soybean fields. Aiming to test some insecticides and dosages for controling the weevil, two field experiments were carried out in 1998, in Maua da Serra and Pinhao, Parana State, Brazil. The experiment was in a randomized complete block desing, with four replicates per treatment. The plots measured 4x8m and 6x7m, respectivelly for each location; plants were at the V6 and V3 growing stage. Treatments e evaluated were: beta-cyfluthrin, in the emulsifiable concentrate (EC) and flowable (FW) formulations (10ga.i.ha -1), ethophenprox (45ga.i.ha -1), fipronil (32, 48 e 64 ga.i.ha -1), methamidophos (480ga.i.ha -1), thiamethoxan (210ga.i.ha -1) and a control (without spraying). Alive adults were sampled at 0, 2, 5 ou 6, and 12 or 14 days after application (DAA) of the insecticides in 12m (Maua da Serra) and 5m (Pinhao) os soybean row. In this last site, the initial stand of healthy plants and the number of plants attacked by the insect were also evaluated. Beta-cyfluthrin FW, fipronil (at the 3 tested doses), methamidophos and thiamethoxanwere efficient, reaching at least 80% of control until 5-6 DAA, inthe first experiment. Fipronil (at the 3 doses) and thiamethoxan were also efficient in the second experiment. According the data, the insecticides fipronil and thiamethoxan showed a larger residual powe... Mostrar Tudo |
|
Palavras-Chave: |
Brasil; Controle integrado de praga. |
|
Thesagro: |
Controle Químico; Inseto; Pesticida. |
|
Thesaurus Nal: |
Brazil; chemical control; Insecta; integrated pest management; pesticides. |
|
Categoria do assunto: |
-- |
|
Marc: |
LEADER 02401naa a2200277 a 4500
001 1462608
005 2006-03-09
008 2000 bl uuuu u00u1 u #d
100 1 $aCORSO, I. C.
245 $aControl of Sternechus subsignatus (Col.$bCurculionidae) with insecticides applied on soybean plants.
260 $c2000
300 $ap.671. v.2
490 $vv.2
520 $aSternechus subsignatus Boheman (Col.: Curculionidae), a stem borer gall maker, is a weevil that damage soybean plants by scraping stems and petioles, sometimes causing total loss of soybean fields. Aiming to test some insecticides and dosages for controling the weevil, two field experiments were carried out in 1998, in Maua da Serra and Pinhao, Parana State, Brazil. The experiment was in a randomized complete block desing, with four replicates per treatment. The plots measured 4x8m and 6x7m, respectivelly for each location; plants were at the V6 and V3 growing stage. Treatments e evaluated were: beta-cyfluthrin, in the emulsifiable concentrate (EC) and flowable (FW) formulations (10ga.i.ha -1), ethophenprox (45ga.i.ha -1), fipronil (32, 48 e 64 ga.i.ha -1), methamidophos (480ga.i.ha -1), thiamethoxan (210ga.i.ha -1) and a control (without spraying). Alive adults were sampled at 0, 2, 5 ou 6, and 12 or 14 days after application (DAA) of the insecticides in 12m (Maua da Serra) and 5m (Pinhao) os soybean row. In this last site, the initial stand of healthy plants and the number of plants attacked by the insect were also evaluated. Beta-cyfluthrin FW, fipronil (at the 3 tested doses), methamidophos and thiamethoxanwere efficient, reaching at least 80% of control until 5-6 DAA, inthe first experiment. Fipronil (at the 3 doses) and thiamethoxan were also efficient in the second experiment. According the data, the insecticides fipronil and thiamethoxan showed a larger residual power for controling S. subsignatus, providing a lesses final number of attacked plants.
650 $aBrazil
650 $achemical control
650 $aInsecta
650 $aintegrated pest management
650 $apesticides
650 $aControle Químico
650 $aInseto
650 $aPesticida
653 $aBrasil
653 $aControle integrado de praga
700 1 $aHOFFMANN-CAMPO, C.B.
773 $tIn: INTERNATIONAL CONGRESS OF ENTOMOLOGY, 21., 2000, Foz do Iguassu. Abstracts... Londrina: Embrapa Soja, 2000.
Download
Esconder MarcMostrar Marc Completo |
|
Registro original: |
Embrapa Soja (CNPSO) |
|
|
Biblioteca |
ID |
Origem |
Tipo/Formato |
Classificação |
Cutter |
Registro |
Volume |
Status |
URL |
Voltar
|
|
|
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
|
|
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.
Download
Esconder MarcMostrar Marc Completo |
|
Registro original: |
Embrapa Recursos Genéticos e Biotecnologia (CENARGEN) |
|
|
Biblioteca |
ID |
Origem |
Tipo/Formato |
Classificação |
Cutter |
Registro |
Volume |
Status |
Fechar
|
| Expressão de busca inválida. Verifique!!! |
|
|
