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 | Acesso ao texto completo restrito à biblioteca da Embrapa Milho e Sorgo. Para informações adicionais entre em contato com cnpms.biblioteca@embrapa.br. |
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Registro Completo |
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Biblioteca(s): |
Embrapa Milho e Sorgo. |
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Data corrente: |
13/02/2015 |
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Data da última atualização: |
27/09/2017 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
OLIVEIRA, E. de; TERNES, S.; VILAMIU, R.; LANDAU, E. C.; OLIVEIRA, C. M. de. |
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Afiliação: |
ELIZABETH DE OLIVEIRA SABATO, CNPMS; ELENA CHARLOTTE LANDAU, CNPMS; CHARLES MARTINS DE OLIVEIRA, CPAC. |
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Título: |
Abundance of the insect vector of two different Mollicutes plant pathogens in the vegetative maize cycle. |
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Ano de publicação: |
2015 |
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Fonte/Imprenta: |
Phytopathogenic Mollicutes, New Delhi, v. 5, S117-S118, 2015. |
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DOI: |
1O.5958/2249-4677.2015.00050.X |
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Idioma: |
Inglês |
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Conteúdo: |
The abundance of Dalbulus maidis leafhopper was evaluated in intervals of 20 days in the vegetative cycle of maize and popcom hybrids simultaneously cultivated in three areas at four different sowing dates. The amount of leafhoppers increased Irom the first until the third sampling, araund the flowering, and decreased after that. The híghest amount of leafhoppers detected in the late sowings was attributed to effect of their concentration derived fram oldest maize crops. |
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Palavras-Chave: |
Fitoplasma. |
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Thesagro: |
Zea mays. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 01115naa a2200205 a 4500
001 2008694
005 2017-09-27
008 2015 bl uuuu u00u1 u #d
024 7 $a1O.5958/2249-4677.2015.00050.X$2DOI
100 1 $aOLIVEIRA, E. de
245 $aAbundance of the insect vector of two different Mollicutes plant pathogens in the vegetative maize cycle.$h[electronic resource]
260 $c2015
520 $aThe abundance of Dalbulus maidis leafhopper was evaluated in intervals of 20 days in the vegetative cycle of maize and popcom hybrids simultaneously cultivated in three areas at four different sowing dates. The amount of leafhoppers increased Irom the first until the third sampling, araund the flowering, and decreased after that. The híghest amount of leafhoppers detected in the late sowings was attributed to effect of their concentration derived fram oldest maize crops.
650 $aZea mays
653 $aFitoplasma
700 1 $aTERNES, S.
700 1 $aVILAMIU, R.
700 1 $aLANDAU, E. C.
700 1 $aOLIVEIRA, C. M. de
773 $tPhytopathogenic Mollicutes, New Delhi$gv. 5, S117-S118, 2015.
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Embrapa Milho e Sorgo (CNPMS) |
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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. |
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Data corrente: |
15/04/2004 |
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Data da última atualização: |
17/01/2020 |
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Autoria: |
FERNANDEZ, J. H.; HAYASHI, M. A. F.; CAMARGO, A. C. M.; NESHICH, G. |
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Afiliação: |
JORGE H. FERNANDEZ, Instituto Butantan; MIRIAN A. F. HAYASHI, Instituto Butantan; ANTONIO C. M. CAMARGO, Instituto Butantan; GORAN NESHICH, CNPTIA. |
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Título: |
Structural basis of the lisinopril-binding specificity in N- and C-domains of human somatic ACE. |
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Ano de publicação: |
2003 |
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Fonte/Imprenta: |
Biochemichal and Biophysical Research Communications, New York, v. 308, n. 2, p. 219-226, Aug. 2003. |
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DOI: |
10.1016/S0006-291X(03)01363-9 |
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Idioma: |
Inglês |
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Conteúdo: |
Angiotensin I-converting enzyme (ACE) is a dipeptidylcarboxypeptidase which converts angiotensin I into the vasopressor peptide angiotensin II and also inactivates the hypotensive peptide bradykinin, playing an important role in blood pressure regulation. The present work describes the molecular modeling of the N-terminal human somatic ACE in complex with the inhibitor lisinopril, identifying the residues involved in the inhibitor-binding pocket. The obtained results identify differences in the lisinopril lysine moiety-binding residues for N- and C-terminals of sACE domains and an important carboxy-terminal proline hydrophobic accommodations mediated by the aromatic ring of Tyr532 and Tyr1128 residues, respectively. The present model will be useful for the development of a new inhibitor family based on the natural BPP peptides and derivatives, or even to improve the binding capacities and the domain specificity of the already known inhibitors. |
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Palavras-Chave: |
Angiotensin I-converting enzyme; Bk-potentiating peptides; Homology modeling; Lisinopril; Modelagem molecular; Molecular modeling; Somatic ACE. |
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Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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Marc: |
LEADER 01799naa a2200253 a 4500
001 1008856
005 2020-01-17
008 2003 bl uuuu u00u1 u #d
024 7 $a10.1016/S0006-291X(03)01363-9$2DOI
100 1 $aFERNANDEZ, J. H.
245 $aStructural basis of the lisinopril-binding specificity in N- and C-domains of human somatic ACE.$h[electronic resource]
260 $c2003
520 $aAngiotensin I-converting enzyme (ACE) is a dipeptidylcarboxypeptidase which converts angiotensin I into the vasopressor peptide angiotensin II and also inactivates the hypotensive peptide bradykinin, playing an important role in blood pressure regulation. The present work describes the molecular modeling of the N-terminal human somatic ACE in complex with the inhibitor lisinopril, identifying the residues involved in the inhibitor-binding pocket. The obtained results identify differences in the lisinopril lysine moiety-binding residues for N- and C-terminals of sACE domains and an important carboxy-terminal proline hydrophobic accommodations mediated by the aromatic ring of Tyr532 and Tyr1128 residues, respectively. The present model will be useful for the development of a new inhibitor family based on the natural BPP peptides and derivatives, or even to improve the binding capacities and the domain specificity of the already known inhibitors.
653 $aAngiotensin I-converting enzyme
653 $aBk-potentiating peptides
653 $aHomology modeling
653 $aLisinopril
653 $aModelagem molecular
653 $aMolecular modeling
653 $aSomatic ACE
700 1 $aHAYASHI, M. A. F.
700 1 $aCAMARGO, A. C. M.
700 1 $aNESHICH, G.
773 $tBiochemichal and Biophysical Research Communications, New York$gv. 308, n. 2, p. 219-226, Aug. 2003.
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