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| 121. |  | ARAÚJO, V. F.; CORBELINI, D. D.; FETTER, M. da R.; MARTINS, D.; SCHWENGBER, J. E.; VIZZOTTO, M. Comportamento de diferentes cultivares de morangueiro em sistema de produção de base ecológica com relação à capacidade antioxidante, teores de fenóis e antocianinas. In: SEMINÁRIO INTERNACIONAL DE EDUCAÇÃO E PESQUISA EM ECOLOGIA, 2., 2010, Pelotas, RS. Anais... Pelotas: Universidade Católica de Pelotas, 2010. p. 36-39. Coordenação de José Antonio Weykamp Cruz. p. 36-39| Biblioteca(s): Embrapa Clima Temperado. |
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| 122. | | BARBOSA, F. J. V.; DINIZ, F. M.; COSTA, A. P. R.; BRITTO, F. B.; CLEMENTINO, C. S.; MARTINS, D. M. Caracterização morfo-genética e desempenho de grupos de galinhas naturalizadas no nordeste brasileiro. In: ENCONTRO DE AVALIAÇÃO DO PROGRAMA REDE NORDESTE DE BIOTECNOLOGIA - RENORBIO, 1., 2008, São Paulo. Resumos... São Paulo: RENORBIO, 2008. p.50-51| Biblioteca(s): Embrapa Meio-Norte. |
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| 125. | | JARDINE, J. G.; NESHICH, G.; MAZONI, I.; MARTINS, D.; MARANGONI, S.; NOVELLO, J. C.; GATTAZ, W. F.; DIAS-NETO, E. Molecular modeling and structural analysis of the Myelin basic protein-Q65ZS4. In: INTERNATIONAL CONFERENCE OF THE BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 3., 2007, São Paulo. Proceedings... Campinas: Embrapa Informática Agropecuária, 2007. p. 138. X-meeting 2007.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 127. | | MARTINS, D de S.; WATTHIER, M.; SCHWENGBER, J. E.; SILVA, D. R da; SCHUBERT, R. N.; PEIL, R. M. N. Planting density and number of stems for ecological crop determinate growth tomato. African Journal of Agricultural Research, v. 13, n. 12, p. 544-550, Mar. 2018.| Biblioteca(s): Embrapa Clima Temperado. |
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| 129. | | TEODORO, K. B. R.; MIGLIORINI, F. L.; FACURE, M. H. M.; SANFELICE, R. C.; MARTINS, D.; CORREA, D. S. Novel chemical sensors based on green composite materials for environmental analysis. In: KUMAR, V.; GULERIA, P.; RANJAN, S.; DASGUPTA. N.; LICHTFOUSE, E. (ed.). Nanosensors for Environment, Food and Agriculture, v. 1, 2021. 109 - 138| Biblioteca(s): Embrapa Instrumentação. |
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| 132. | | SOARES, S. F.; De MUNER, L. H.; FORNAZIER, M. J.; MARTINS, D. S.; SILVA, A. E. S.; SALGADO, J. S. Difusão e transferência de tecnologia para a cultura do cafeeiro no Estado do Espírito Santo: manejo da broca-do-café. In: SIMPÓSIO DE PESQUISA DOS CAFÉS DO BRASIL, 2., 2001, Vitória. Anais... Brasília, DF: Embrapa Café, 2002.| Biblioteca(s): Embrapa Café. |
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| 133. | | SIMÃO, E. de P.; RESENDE, A. V. de; GONTIJO NETO, M. M.; BORGHI, E.; MARTINS, D. C.; VANIN, A. Demanda de nutrientes pelo milho safrinha em função da época de semeadura e adubação. Revista Brasileira de Milho e Sorgo, Sete Lagoas, v. 16, n. 3, p. 481-494, 2017.| Biblioteca(s): Embrapa Milho e Sorgo. |
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| 134. | | LIMA, V. P. de; MARTINS, D. S.; ALVES, R. E. de A.; MARTINS, M. R.; SCHULTZ, N.; URQUIAGA, S. Potencial produtivo de cana-de-açúcar cultivada em solo de baixa fertilidade natural, em tanque de concreto em estudo de longo prazo In: CONGRESSO BRASILEIRO DE CIÊNCIA DO SOLO, 35., 2015, Natal. O solo e suas múltiplas funções: anais. Natal: Sociedade Brasileira de Ciência do Solo, 2015.| Biblioteca(s): Embrapa Agrobiologia. |
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| 135. | | LIMA, V. P. de; MARTINS, D. S.; ALVES, R. E. de A.; MARTINS, M. R.; SCHULTZ, N.; URQUIAGA, S. Potencial produtivo de cana-de-açúcar em solo de baixa fertilidade sem adubação nitrogenada em estudo de longo prazo In: CONGRESSO BRASILEIRO DE CIÊNCIA DO SOLO, 35., 2015, Natal. O solo e suas múltiplas funções: anais. Natal: Sociedade Brasileira de Ciência do Solo, 2015.| Biblioteca(s): Embrapa Agrobiologia. |
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| 136. | | MARTINS, D. de S.; STRASSBURGER, A. S.; PEIL, R. M. N.; SCHWENGBER, J. E.; REISSER JUNIOR, C.; FURTADO, I. G. Fisiologia da produção de morangueiro. In: TIMM, L. C.; TAVARES, V. E. Q.; REISSER JUNIOR, C.; ESTRELA, C. C. (Ed.). Morangueiro irrigado: aspectos técnicos e ambientais do cultivo. Pelotas: Universidade Federal de Pelotas, 2009. p. 16-29| Biblioteca(s): Embrapa Clima Temperado. |
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| 137. | | MACIEL, R. M.; LOPES, S. T. dos A.; SANTURIO, J. M.; MARTINS, D. B.; ROSA, A. P.; EMANUELLI, M. P. Função hepática e renal de frangos de corte alimentados com dietas com aflatoxinas e clinoptilolita natural Pesquisa Agropecuária Brasileira, Brasília, DF, v. 42, n. 9, p. 1221-1225, set. 2007 Título em inglês: Hepatic and renal functions in broilers fed on diets with aflatoxins and natural clinoptilolite.| Biblioteca(s): Embrapa Unidades Centrais. |
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| 138. | | MARTINS, D. M.; CLEMENTINO, C. de S.; SOUSA, S. de A.; BARBOSA, F. J. V.; DINIZ, F. M. Fatores climáticos intervenientes na incubação artificial de ovos de galinhas caipiras (Gallus gallus domesticus). In: CONGRESSO BRASILEIRO DE ORNITOLOGIA, 16., 2008, Palmas,TO. A ornitologia no Cerrado e Ecótonos do Brasil: livro de resumos. Palmas,TO: CBO: Universidade Federal do Tocantins: Sociedade Brasileira de Ornitologia: Grupo de Pesquisa em Ecologia e Conservação de Aves, 2008. p. 48| Biblioteca(s): Embrapa Meio-Norte. |
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| 139. | | PEREIRA, M. R. R.; SILVA, J. I. C. da; RODRIGUES, A. C. P.; MARTINS, D.; KLAR, A. K. Influência de laminas de chuva no controle de plantas daninhas, semeadas em diferentes profundidades no solo, com aplicação de herbicidas pré-emergentes. Irriga, Botucatu, v. 15, n. 2, p. 184-192, abr./jun. 2010. 1 CD-ROM| Biblioteca(s): Embrapa Hortaliças. |
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| 140. | | MACHADO, L. C.; OLIVEIRA, V. C.; PARAVENTI, M. D.; CARDOSO, R. N. R.; MARTINS, D. S.; AMBRÓSIO, C. E. Maintenance of brazilian biodiversity by germplasm bank. Pesquisa Veterinária Brasileira, Rio de Janeiro, v. 36, n. 1, p. 62-66, jan. 2016.| Biblioteca(s): Embrapa Unidades Centrais. |
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| Registros recuperados : 249 | |
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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
|
Biblioteca(s): |
Embrapa Agricultura Digital. |
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Data corrente: |
26/11/2009 |
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Data da última atualização: |
15/01/2020 |
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Tipo da produção científica: |
Resumo em Anais de Congresso |
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Autoria: |
NESHICH, I. A. P.; MORAES, F. R. de; MARANGONI, S.; MARTINS, D.; SALIM, J. A.; MAZONI, I.; MANCINI, A.; NESHICH, G.; JARDINE, J. G. |
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Afiliação: |
IZABELLA AGOSTINHO PENA NESHICH, Estagiária/CNPTIA; FABIO ROGERIO DE MORAES, Bolsista/CNPTIA; S. MARANGONI, Unicamp; D. MARTINS, Unicamp; JOSÉ AUGUSTO SALIM, Estagiário/CNPTIA; IVAN MAZONI, CNPTIA; ADAUTO LUIZ MANCINI, CNPTIA; GORAN NESHICH, CNPTIA; JOSE GILBERTO JARDINE, CNPTIA. |
|
Título: |
Xylella fastidiosa hexameric pilus retraction motor PILT interfaces are maintained by non-hydrophobic contacts. |
|
Ano de publicação: |
2009 |
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Fonte/Imprenta: |
In: INTERNATIONAL CONFERENCE OF THE BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 5., 2009, Angra dos Reis. Abstracts book... Angra dos Reis: ABBCB, 2009. |
|
Páginas: |
Não paginado. |
|
Idioma: |
Inglês |
|
Notas: |
X-Meeting 2009. |
|
Conteúdo: |
Xylella fastidiosa (Xf) causes CVC and Pierce?s Disease (affecting citrus and grape). Xf colonizes the xylem vessels in plants. Pathogenicity of the Xf are related to ability to move within the xylem. Avirulent strains rarely move from the inoculation point. Xf has proteins involved in type IV pili, which cause the twitching motility - a form of surface-associated movement. Satyshur and coworkers had solved four structures from PilT proteins (PDB codes: 2GSZ, 2EWV, 2EWW and 2EYU) from a hyperthermophilic organism, Aquifex aeolicus (Aa). PilT is a hexameric ATPase from a subgroup of the bacterial type II/type IV secretion systems, with two major domains: the Nterminal Domain (NTD) and the C-Terminal Domain (CTD) which contains the ATPase core. The importance of polar and charged CTDn: NTDn+1 interface interactions to retraction motion was discussed. Through site-directed mutagenesis on Pseudomonas aeruginosa PilT, they demonstrated that some residues are crucial to protein function, half of them (D29, R95 and R207) located on interface region. The Xf PilT has 68% of similarity and 49% of identical aminoacids to Aa). We modelled each Xf PilT chain. We analyzed the hexameric structure of Aa Pilt (PDB code: 2GSZ) and Xf PilT hexamer model (named here as 2HXF) using Blue Star STING platform. By analysis of Interface Forming Residues (IFR), we found that there was a significant difference among the interfaces: Xf PilT interfaces area occupied mainly by charged amino acids. This does not hold for the free surfaces (molecular surface without interfaces). In 2GSZ the interface area is occupied by hydrophobic and polar AA; In addition, the interfaces have less charged AA than free surface. The Aa PilT interfaces are more hydrophobic when compared to Xf PilT. The number and energies of contacts established between IFRs in 2HXF are higher than 2GSZ, suggesting that Xf PilT interfaces are more stable. Apparently, the most important IFRs (which establish most energetic contacts at the surface) are conserved within Proteobacteria and Aquificae PilTs (Clustalw alignment data). Thus, we suggest that the difference among amino acid composition of interfaces between Xf PilT and Aa PilT reflect their crucial importance on successful host infections across the Proteobacteria. We hypothesize here that similarities found in primary sequence alignment could be maintained at 3D level, indicating a possible higher selective pressure on these locations in Proteobacteria (as compared to the Aa PilT). We also suggest that these residues, crucially important to protein functionality, might serve as potential targets to eliminate bacteria pathogenicity. MenosXylella fastidiosa (Xf) causes CVC and Pierce?s Disease (affecting citrus and grape). Xf colonizes the xylem vessels in plants. Pathogenicity of the Xf are related to ability to move within the xylem. Avirulent strains rarely move from the inoculation point. Xf has proteins involved in type IV pili, which cause the twitching motility - a form of surface-associated movement. Satyshur and coworkers had solved four structures from PilT proteins (PDB codes: 2GSZ, 2EWV, 2EWW and 2EYU) from a hyperthermophilic organism, Aquifex aeolicus (Aa). PilT is a hexameric ATPase from a subgroup of the bacterial type II/type IV secretion systems, with two major domains: the Nterminal Domain (NTD) and the C-Terminal Domain (CTD) which contains the ATPase core. The importance of polar and charged CTDn: NTDn+1 interface interactions to retraction motion was discussed. Through site-directed mutagenesis on Pseudomonas aeruginosa PilT, they demonstrated that some residues are crucial to protein function, half of them (D29, R95 and R207) located on interface region. The Xf PilT has 68% of similarity and 49% of identical aminoacids to Aa). We modelled each Xf PilT chain. We analyzed the hexameric structure of Aa Pilt (PDB code: 2GSZ) and Xf PilT hexamer model (named here as 2HXF) using Blue Star STING platform. By analysis of Interface Forming Residues (IFR), we found that there was a significant difference among the interfaces: Xf PilT interfaces area occupied mainly by charged amino acids. This do... Mostrar Tudo |
|
Palavras-Chave: |
Aminoácidos; Bioinformática; Contatos não hidrofóbicos; Proteínas. |
|
Thesagro: |
Xylella Fastidiosa. |
|
Thesaurus NAL: |
Bioinformatics; Proteins. |
|
Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
|
Marc: |
LEADER 03706nam a2200313 a 4500
001 1576270
005 2020-01-15
008 2009 bl uuuu u00u1 u #d
100 1 $aNESHICH, I. A. P.
245 $aXylella fastidiosa hexameric pilus retraction motor PILT interfaces are maintained by non-hydrophobic contacts.$h[electronic resource]
260 $aIn: INTERNATIONAL CONFERENCE OF THE BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 5., 2009, Angra dos Reis. Abstracts book... Angra dos Reis: ABBCB$c2009
300 $aNão paginado.
500 $aX-Meeting 2009.
520 $aXylella fastidiosa (Xf) causes CVC and Pierce?s Disease (affecting citrus and grape). Xf colonizes the xylem vessels in plants. Pathogenicity of the Xf are related to ability to move within the xylem. Avirulent strains rarely move from the inoculation point. Xf has proteins involved in type IV pili, which cause the twitching motility - a form of surface-associated movement. Satyshur and coworkers had solved four structures from PilT proteins (PDB codes: 2GSZ, 2EWV, 2EWW and 2EYU) from a hyperthermophilic organism, Aquifex aeolicus (Aa). PilT is a hexameric ATPase from a subgroup of the bacterial type II/type IV secretion systems, with two major domains: the Nterminal Domain (NTD) and the C-Terminal Domain (CTD) which contains the ATPase core. The importance of polar and charged CTDn: NTDn+1 interface interactions to retraction motion was discussed. Through site-directed mutagenesis on Pseudomonas aeruginosa PilT, they demonstrated that some residues are crucial to protein function, half of them (D29, R95 and R207) located on interface region. The Xf PilT has 68% of similarity and 49% of identical aminoacids to Aa). We modelled each Xf PilT chain. We analyzed the hexameric structure of Aa Pilt (PDB code: 2GSZ) and Xf PilT hexamer model (named here as 2HXF) using Blue Star STING platform. By analysis of Interface Forming Residues (IFR), we found that there was a significant difference among the interfaces: Xf PilT interfaces area occupied mainly by charged amino acids. This does not hold for the free surfaces (molecular surface without interfaces). In 2GSZ the interface area is occupied by hydrophobic and polar AA; In addition, the interfaces have less charged AA than free surface. The Aa PilT interfaces are more hydrophobic when compared to Xf PilT. The number and energies of contacts established between IFRs in 2HXF are higher than 2GSZ, suggesting that Xf PilT interfaces are more stable. Apparently, the most important IFRs (which establish most energetic contacts at the surface) are conserved within Proteobacteria and Aquificae PilTs (Clustalw alignment data). Thus, we suggest that the difference among amino acid composition of interfaces between Xf PilT and Aa PilT reflect their crucial importance on successful host infections across the Proteobacteria. We hypothesize here that similarities found in primary sequence alignment could be maintained at 3D level, indicating a possible higher selective pressure on these locations in Proteobacteria (as compared to the Aa PilT). We also suggest that these residues, crucially important to protein functionality, might serve as potential targets to eliminate bacteria pathogenicity.
650 $aBioinformatics
650 $aProteins
650 $aXylella Fastidiosa
653 $aAminoácidos
653 $aBioinformática
653 $aContatos não hidrofóbicos
653 $aProteínas
700 1 $aMORAES, F. R. de
700 1 $aMARANGONI, S.
700 1 $aMARTINS, D.
700 1 $aSALIM, J. A.
700 1 $aMAZONI, I.
700 1 $aMANCINI, A.
700 1 $aNESHICH, G.
700 1 $aJARDINE, J. G.
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