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Registro Completo |
Biblioteca(s): |
Biblioteca Rui Tendinha. |
Data corrente: |
22/02/2016 |
Data da última atualização: |
31/03/2016 |
Autoria: |
CANDAL NETO, J. F.; PACOVA, B. E. V.; DAN, E.; VENTURA, J. A. |
Afiliação: |
João Francisco Candal Neto, EMCAPA; Braz Eduardo Vieira Pacova, EMCAPA; Edvino Dan, EMCAPA; Jose Aires Ventura, EMCAPA. |
Título: |
Ocorrência de mancha de ascoquita (Ascochyta sp.) na cultura do feijão (Phaseolus vulgaris L.) no Espírito Santo. |
Ano de publicação: |
1981 |
Fonte/Imprenta: |
COMUNICADO TÉCNICO, Cariacica, n. 1, p. 1-9, março 1981. |
Série: |
(EMCAPA. Comunicado, 1). |
Idioma: |
Português |
Palavras-Chave: |
Ascochyta; Ascochyta boltshauseri; Ascochyta phaseolorum; Ascoquita; Bean; Brasil; Brazil; Disease; Doenca; Doencas; Espirito Santo; Feijao; Feijoeiro; Fungo; Fungos; Fungus; Mancha; Mancha de ascoquita; Phaseolus vulgaris. |
Categoria do assunto: |
H Saúde e Patologia |
URL: |
http://biblioteca.incaper.es.gov.br/digital/bitstream/item/1443/1/BRT-comunicado-n01-1981-Emcapa.pdf
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Marc: |
LEADER 01032nam a2200373 a 4500 001 1009891 005 2016-03-31 008 1981 bl uuuu u00u1 u #d 100 1 $aCANDAL NETO, J. F. 245 $aOcorrência de mancha de ascoquita (Ascochyta sp.) na cultura do feijão (Phaseolus vulgaris L.) no Espírito Santo.$h[electronic resource] 260 $aCOMUNICADO TÉCNICO, Cariacica, n. 1, p. 1-9, março 1981.$c1981 490 $a(EMCAPA. Comunicado, 1). 653 $aAscochyta 653 $aAscochyta boltshauseri 653 $aAscochyta phaseolorum 653 $aAscoquita 653 $aBean 653 $aBrasil 653 $aBrazil 653 $aDisease 653 $aDoenca 653 $aDoencas 653 $aEspirito Santo 653 $aFeijao 653 $aFeijoeiro 653 $aFungo 653 $aFungos 653 $aFungus 653 $aMancha 653 $aMancha de ascoquita 653 $aPhaseolus vulgaris 700 1 $aPACOVA, B. E. V. 700 1 $aDAN, E. 700 1 $aVENTURA, J. A.
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Biblioteca Rui Tendinha (BRT) |
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Registro Completo |
Biblioteca(s): |
Biblioteca Rui Tendinha. |
Data corrente: |
23/02/2023 |
Data da última atualização: |
25/04/2023 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Autoria: |
MAURASTONI, M.; ANTUNES, T. F. S.; ABREU, E. F. M.; RIBEIRO, S. G.; MEHTA, A.; SANCHES, M. M.; FONTES, W.; KITAJIMA, E. W.; CRUZ, F. T.; SANTOS, A. M. C.; VENTURA, J. A.; GOMES, A. C. M. M.; ZERBINI, F. M.; SOSA-ACOSTA, P.; NOGUEIRA, F. C. S.; RODRIGUES, S. P.; ARAGÃO, F. J. L.; WHITFIELD, A. E.; FERNANDES, P. M. B. |
Afiliação: |
Marlonni Maurastoni, UFES; Tathiana F. Sá Antunes, UFES; Emanuel F. M. Abreu, Embrapa Recursos Genéticos e Biotecnologia; Simone G. Ribeiro, Embrapa Recursos Genéticos e Biotecnologia; Angela Mehta, Embrapa Recursos Genéticos e Biotecnologia; Marcio M. Sanches, Embrapa Recursos Genéticos e Biotecnologia; Wagner Fontes, UNB; Elliot W. Kitajima, USP; Fabiano T. Cruz, UFES; Alexandre M. C. Santos, UFES; Jose Aires Ventura, Incaper; Ana C. M. M. Gomes, Embrapa Recursos Genéticos e Biotecnologia; F. Murilo Zerbini, UFV; Patricia Sosa-Acosta, UFRJ; Fábio C. S. Nogueira, UFRJ; Silas P. Rodrigues, UFRJ; Francisco J. L. Aragão, Embrapa Recursos Genéticos e Biotecnologia; Anna E. Whitfield, North Carolina State University; Patricia M. B. Fernandes, UFES. |
Título: |
A capsid protein fragment of a Toti-like Virus Found in Carica papaya Latex interacts with the 50S ribosomal protein L17 |
Ano de publicação: |
2023 |
Fonte/Imprenta: |
Viruses, v. 15, n. 541, p. 1-20, 2023. |
DOI: |
10.3390/v15020541 |
Idioma: |
Inglês |
Conteúdo: |
Papaya sticky disease is caused by the association of a fusagra-like and an umbra-like virus, named papaya meleira virus (PMeV) and papaya meleira virus 2 (PMeV2), respectively. Both viral genomes are encapsidated in particles formed by the PMeV ORF1 product, which has the potential to encode a protein with 1563 amino acids (aa). However, the structural components of the viral capsid are unknown. To characterize the structural proteins of PMeV and PMeV2, virions were purified from Carica papaya latex. SDS-PAGE analysis of purified virus revealed two major proteins of ~40 kDa and ~55 kDa. Amino-terminal sequencing of the ~55 kDa protein and LC-MS/MS of purified virions indicated that this protein starts at aa 263 of the deduced ORF1 product as a result of either degradation or proteolytic processing. A yeast two-hybrid assay was used to identify Arabidopsis proteins interacting with two PMeV ORF1 product fragments (aa 321?670 and 961?1200). The 50S ribosomal protein L17 (AtRPL17) was identified as potentially associated with modulated translation-related proteins. In plant cells, AtRPL17 co-localized and interacted with the PMeV ORF1 fragments. These findings support the hypothesis that the interaction between PMeV/PMeV2 structural proteins and RPL17 is important for virus?host interactions. |
Palavras-Chave: |
Meleira. |
Thesagro: |
Carica Papaya; Mamão; Proteína; Vírus. |
Categoria do assunto: |
-- |
URL: |
https://biblioteca.incaper.es.gov.br/digital/bitstream/item/4389/1/A-Capsid-Protein-Fragment-of-a-Toti-like-Virus-2023.pdf
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Marc: |
LEADER 02456naa a2200409 a 4500 001 1024693 005 2023-04-25 008 2023 bl uuuu u00u1 u #d 024 7 $a10.3390/v15020541$2DOI 100 1 $aMAURASTONI, M. 245 $aA capsid protein fragment of a Toti-like Virus Found in Carica papaya Latex interacts with the 50S ribosomal protein L17$h[electronic resource] 260 $c2023 520 $aPapaya sticky disease is caused by the association of a fusagra-like and an umbra-like virus, named papaya meleira virus (PMeV) and papaya meleira virus 2 (PMeV2), respectively. Both viral genomes are encapsidated in particles formed by the PMeV ORF1 product, which has the potential to encode a protein with 1563 amino acids (aa). However, the structural components of the viral capsid are unknown. To characterize the structural proteins of PMeV and PMeV2, virions were purified from Carica papaya latex. SDS-PAGE analysis of purified virus revealed two major proteins of ~40 kDa and ~55 kDa. Amino-terminal sequencing of the ~55 kDa protein and LC-MS/MS of purified virions indicated that this protein starts at aa 263 of the deduced ORF1 product as a result of either degradation or proteolytic processing. A yeast two-hybrid assay was used to identify Arabidopsis proteins interacting with two PMeV ORF1 product fragments (aa 321?670 and 961?1200). The 50S ribosomal protein L17 (AtRPL17) was identified as potentially associated with modulated translation-related proteins. In plant cells, AtRPL17 co-localized and interacted with the PMeV ORF1 fragments. These findings support the hypothesis that the interaction between PMeV/PMeV2 structural proteins and RPL17 is important for virus?host interactions. 650 $aCarica Papaya 650 $aMamão 650 $aProteína 650 $aVírus 653 $aMeleira 700 1 $aANTUNES, T. F. S. 700 1 $aABREU, E. F. M. 700 1 $aRIBEIRO, S. G. 700 1 $aMEHTA, A. 700 1 $aSANCHES, M. M. 700 1 $aFONTES, W. 700 1 $aKITAJIMA, E. W. 700 1 $aCRUZ, F. T. 700 1 $aSANTOS, A. M. C. 700 1 $aVENTURA, J. A. 700 1 $aGOMES, A. C. M. M. 700 1 $aZERBINI, F. M. 700 1 $aSOSA-ACOSTA, P. 700 1 $aNOGUEIRA, F. C. S. 700 1 $aRODRIGUES, S. P. 700 1 $aARAGÃO, F. J. L. 700 1 $aWHITFIELD, A. E. 700 1 $aFERNANDES, P. M. B. 773 $tViruses$gv. 15, n. 541, p. 1-20, 2023.
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