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Registro Completo |
Biblioteca(s): |
Embrapa Trigo. |
Data corrente: |
25/05/2023 |
Data da última atualização: |
05/07/2023 |
Tipo da produção científica: |
Autoria/Organização/Edição de Livros |
Autoria: |
REUNIÃO NACIONAL DE PESQUISA DE CEVADA, 33., 2022, Passo Fundo, RS. |
Título: |
Indicações técnicas para a produção de cevada cervejeira nas safras 2023 e 2024. |
Ano de publicação: |
2023 |
Fonte/Imprenta: |
Passo Fundo: Embrapa Trigo, 2023. |
Páginas: |
88 p. |
ISBN: |
978-65-89957-76-8 |
Idioma: |
Português |
Notas: |
Aloisio Alcantara Vilarinho, editor técnico. |
Conteúdo: |
Indicações Técnicas para a Produção de Cevada Cervejeira nas Safras 2023 e 2024; Planejamento da lavoura; Zoneamento Agrícola de Risco Climático (ZARC) para a Cevada Cervejeira no Brasil, Ano-Safra 2022/2023; Cultivares; Práticas Culturais; Manejo e Conservação de Solo; Adubação e Calagem; Controle de Plantas Daninhas; Controle de Insetos Pragas; Controle de Doenças; Colheita; Secagem |
Palavras-Chave: |
Cevada cervejeira; Selo ODS 12; Selo ODS 2. |
Thesagro: |
Cevada; Pesquisa; Pesquisa Agrícola. |
Categoria do assunto: |
F Plantas e Produtos de Origem Vegetal |
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/doc/1153987/1/IndicacoesTecnicasCevada-Safra2023-2024-.pdf
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Marc: |
LEADER 01088nam a2200217 a 4500 001 2153987 005 2023-07-05 008 2023 bl uuuu 00u1 u #d 020 $a978-65-89957-76-8 100 1 $aREUNIÃO NACIONAL DE PESQUISA DE CEVADA, 33., 2022, Passo Fundo, RS. 245 $aIndicações técnicas para a produção de cevada cervejeira nas safras 2023 e 2024.$h[electronic resource] 260 $aPasso Fundo: Embrapa Trigo$c2023 300 $a88 p. 500 $aAloisio Alcantara Vilarinho, editor técnico. 520 $aIndicações Técnicas para a Produção de Cevada Cervejeira nas Safras 2023 e 2024; Planejamento da lavoura; Zoneamento Agrícola de Risco Climático (ZARC) para a Cevada Cervejeira no Brasil, Ano-Safra 2022/2023; Cultivares; Práticas Culturais; Manejo e Conservação de Solo; Adubação e Calagem; Controle de Plantas Daninhas; Controle de Insetos Pragas; Controle de Doenças; Colheita; Secagem 650 $aCevada 650 $aPesquisa 650 $aPesquisa Agrícola 653 $aCevada cervejeira 653 $aSelo ODS 12 653 $aSelo ODS 2
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Registro original: |
Embrapa Trigo (CNPT) |
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Registro Completo
Biblioteca(s): |
Embrapa Mandioca e Fruticultura. |
Data corrente: |
05/11/2020 |
Data da última atualização: |
05/11/2020 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Circulação/Nível: |
A - 1 |
Autoria: |
LEASTRO, M. O.; ASTUA, J. de F.; KITAJIMA, E. W.; PALLÁS, V.; SÁNCHEZ-NAVARRO, J. Á. |
Afiliação: |
MIKHAIL OLIVEIRA LEASTRO, Instituto Biológico; JULIANA DE FREITAS ASTUA, CNPMF; ELLIOT WATANABE KITAJIMA, ESALQ; VICENTE PALLÁS, Universidad Politécnica de Valencia; JESÚS ÁNGEL SÁNCHEZ-NAVARRO, Universidad Politécnica de Valencia. |
Título: |
Dichorhaviruses Movement Protein and Nucleoprotein Form a Protein Complex That May Be Required for Virus Spread and Interacts in vivo With Viral Movement-Related Cilevirus Proteins. |
Ano de publicação: |
2020 |
Fonte/Imprenta: |
Frontiers in Microbiology, v.11, November 2020. |
Idioma: |
Inglês |
Conteúdo: |
Brevipalpus-transmitted viruses (BTVs) belong to the genera Dichorhavirus and Cilevirus and are the main causal agents of the citrus leprosis (CL) disease. In this report, we explored aspects related to the movement mechanism mediated by dichorhaviruses movement proteins (MPs) and the homologous and heterologous interactions among viral proteins related to the movement of citrus leprosis-associated viruses. The membrane-spanning property and topology analysis of the nucleocapsid (N) and MP proteins from two dichorhaviruses revealed that the MPs are proteins tightly associated with the cell membrane, exposing their N- and C-termini to the cytoplasm and the inner part of the nucleus, whereas the N proteins are not membrane-associated. Subcellular localization analysis revealed the presence of dichorhavirus MPs at the cell surface and in the nucleus, while the phosphoproteins (P) were located exclusively in the nucleus and the N proteins in both the cytoplasm and the nucleus. Co-expression analysis with the MP, P, and N proteins showed an interaction network formed between them. We highlight the MP capability to partially redistribute the previously reported N-P core complex, redirecting a portion of the N from the nucleus to the plasmodesmata at the cell periphery, which indicates not only that the MP might guide the intracellular trafficking of the viral infective complex but also that the N protein may be associated with the cell-to-cell movement mechanism of dichorhaviruses. The movement functionality of these MPs was analyzed by using three movement-defective infectious systems. Also, the MP capacity to generate tubular structures on the protoplast surface by ectopic expression was analyzed. Finally, we evaluated the in vivo protein?protein interaction networks between the dichorhavirus MP and/or N proteins with the heterologous cilevirus movement components, which suggest a broad spectrum of interactions, highlighting those among capsid proteins (CP), MPs, and Ns from citrus leprosis-associated viruses. These data may aid in understanding the mixed infection process naturally observed in the field caused by distinct BTVs. Introduction MenosBrevipalpus-transmitted viruses (BTVs) belong to the genera Dichorhavirus and Cilevirus and are the main causal agents of the citrus leprosis (CL) disease. In this report, we explored aspects related to the movement mechanism mediated by dichorhaviruses movement proteins (MPs) and the homologous and heterologous interactions among viral proteins related to the movement of citrus leprosis-associated viruses. The membrane-spanning property and topology analysis of the nucleocapsid (N) and MP proteins from two dichorhaviruses revealed that the MPs are proteins tightly associated with the cell membrane, exposing their N- and C-termini to the cytoplasm and the inner part of the nucleus, whereas the N proteins are not membrane-associated. Subcellular localization analysis revealed the presence of dichorhavirus MPs at the cell surface and in the nucleus, while the phosphoproteins (P) were located exclusively in the nucleus and the N proteins in both the cytoplasm and the nucleus. Co-expression analysis with the MP, P, and N proteins showed an interaction network formed between them. We highlight the MP capability to partially redistribute the previously reported N-P core complex, redirecting a portion of the N from the nucleus to the plasmodesmata at the cell periphery, which indicates not only that the MP might guide the intracellular trafficking of the viral infective complex but also that the N protein may be associated with the cell-to-cell movement mechanism of dichorhaviruses... Mostrar Tudo |
Thesagro: |
Vírus. |
Categoria do assunto: |
-- |
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/217521/1/2020-Leastro-fmicb-11-571807-Dichorha.pdf
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Marc: |
LEADER 02807naa a2200181 a 4500 001 2126324 005 2020-11-05 008 2020 bl uuuu u00u1 u #d 100 1 $aLEASTRO, M. O. 245 $aDichorhaviruses Movement Protein and Nucleoprotein Form a Protein Complex That May Be Required for Virus Spread and Interacts in vivo With Viral Movement-Related Cilevirus Proteins.$h[electronic resource] 260 $c2020 520 $aBrevipalpus-transmitted viruses (BTVs) belong to the genera Dichorhavirus and Cilevirus and are the main causal agents of the citrus leprosis (CL) disease. In this report, we explored aspects related to the movement mechanism mediated by dichorhaviruses movement proteins (MPs) and the homologous and heterologous interactions among viral proteins related to the movement of citrus leprosis-associated viruses. The membrane-spanning property and topology analysis of the nucleocapsid (N) and MP proteins from two dichorhaviruses revealed that the MPs are proteins tightly associated with the cell membrane, exposing their N- and C-termini to the cytoplasm and the inner part of the nucleus, whereas the N proteins are not membrane-associated. Subcellular localization analysis revealed the presence of dichorhavirus MPs at the cell surface and in the nucleus, while the phosphoproteins (P) were located exclusively in the nucleus and the N proteins in both the cytoplasm and the nucleus. Co-expression analysis with the MP, P, and N proteins showed an interaction network formed between them. We highlight the MP capability to partially redistribute the previously reported N-P core complex, redirecting a portion of the N from the nucleus to the plasmodesmata at the cell periphery, which indicates not only that the MP might guide the intracellular trafficking of the viral infective complex but also that the N protein may be associated with the cell-to-cell movement mechanism of dichorhaviruses. The movement functionality of these MPs was analyzed by using three movement-defective infectious systems. Also, the MP capacity to generate tubular structures on the protoplast surface by ectopic expression was analyzed. Finally, we evaluated the in vivo protein?protein interaction networks between the dichorhavirus MP and/or N proteins with the heterologous cilevirus movement components, which suggest a broad spectrum of interactions, highlighting those among capsid proteins (CP), MPs, and Ns from citrus leprosis-associated viruses. These data may aid in understanding the mixed infection process naturally observed in the field caused by distinct BTVs. Introduction 650 $aVírus 700 1 $aASTUA, J. de F. 700 1 $aKITAJIMA, E. W. 700 1 $aPALLÁS, V. 700 1 $aSÁNCHEZ-NAVARRO, J. Á. 773 $tFrontiers in Microbiology$gv.11, November 2020.
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