Base de dados : MEDLINE
Pesquisa : D12.776.775 [Categoria DeCS]
Referências encontradas : 433 [refinar]
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  1 / 433 MEDLINE  
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[PMID]:29218572
[Au] Autor:Peng X; Pan H; Muhammad A; An H; Fang S; Li W; Zhang S
[Ad] Endereço:Engineering Research Centre of Ecology and Agricultural Use of Wetland, Ministry of Education, Hubei Collaborative Innovation Center for Grain Industry, Yangtze University, Jingzhou, 434025, Hubei, China.
[Ti] Título:Complete genome sequence of a new strain of Lagenaria siceraria endornavirus from China.
[So] Source:Arch Virol;163(3):805-808, 2018 Mar.
[Is] ISSN:1432-8798
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:An RNA virus tentatively named Lagenaria siceraria endornavirus-Hubei (LsEV-HuB) was isolated from Lagenaria siceraria var. hispida in Hubei, China. The LsEV-HuB genome consists of 15,098 bp and contains a single open reading frame (ORF) encoding a large protein with several conserved domains, including one helicase domain, one glycosyltransferase domain, two capsular polysaccharide synthesis protein (CPS) domains, and one RNA-dependent RNA polymerase (RdRp) domain. LsEV-HuB has nucleotide and amino acid sequence identities of 72.96% and 77.95%, respectively, to Lagenaria siceraria endornavirus-California (LsEV-CA), the closest relative of LsEV-HuB.
[Mh] Termos MeSH primário: Cucurbitaceae/virologia
DNA Viral/genética
Genoma Viral
Filogenia
Poliproteínas/genética
Vírus de RNA/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
China
Tamanho do Genoma
Fases de Leitura Aberta
Doenças das Plantas/virologia
Vírus de RNA/classificação
Vírus de RNA/isolamento & purificação
Recombinação Genética
Análise de Sequência de DNA
Homologia de Sequência de Aminoácidos
Sequenciamento Completo do Genoma
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Viral); 0 (Polyproteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171209
[St] Status:MEDLINE
[do] DOI:10.1007/s00705-017-3664-y


  2 / 433 MEDLINE  
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[PMID]:29188364
[Au] Autor:Lan P; Zhao J; Zhou Y; Li Y; Shen D; Liao Q; Li R; Li F
[Ad] Endereço:State Key Laboratory for Conservation and Utilization of Bio-Resources in Yunnan, Yunnan Agricultural University, Kunming, 650201, China.
[Ti] Título:Complete genome sequence of Paris mosaic necrosis virus, a distinct member of the genus Potyvirus.
[So] Source:Arch Virol;163(3):787-790, 2018 Mar.
[Is] ISSN:1432-8798
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:The complete genomic sequence of a novel potyvirus was determined from Paris polyphylla var. yunnanensis. Its genomic RNA consists of 9,660 nucleotides (nt) excluding the 3'-terminal poly (A) tail, containing the typical open reading frame (ORF) of potyviruses and encoding a putative large polyprotein of 3030 amino acids. The virus shares 53.9-70.1% nt sequence identity and 43.9-73.2% amino acid sequence identity with other viruses classified within the genus Potyvirus. Proteolytic cleavage sites and conserved motifs of the potyviruses were identified in the polyprotein and within individual proteins. Phylogenetic analysis indicated that the virus is most closely related to members of the BCMV subgroup. The results suggest that the virus should be classified as a novel species within the genus Potyvirus, which we tentatively name "Paris mosaic necrosis virus".
[Mh] Termos MeSH primário: Genoma Viral
Melanthiaceae/virologia
Filogenia
Potyvirus/genética
RNA Viral/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Tamanho do Genoma
Sequenciamento de Nucleotídeos em Larga Escala
Fases de Leitura Aberta
Doenças das Plantas/virologia
Poliproteínas
Potyvirus/classificação
Potyvirus/isolamento & purificação
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Polyproteins); 0 (RNA, Viral)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE
[do] DOI:10.1007/s00705-017-3649-x


  3 / 433 MEDLINE  
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[PMID]:29037477
[Au] Autor:Bhatt M; Mohapatra JK; Pandey LK; Mohanty NN; Das B; Prusty BR; Pattnaik B
[Ad] Endereço:ICAR-Directorate of Foot and Mouth Disease, Mukteswar 263 138, Uttarakhand, India.
[Ti] Título:Mutational analysis of foot and mouth disease virus nonstructural polyprotein 3AB-coding region to design a negative marker virus.
[So] Source:Virus Res;243:36-43, 2018 01 02.
[Is] ISSN:1872-7492
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Inactivated purified whole virus vaccines are used for control of foot and mouth disease (FMD). ELISAs detecting antibodies to the nonstructural proteins (NSP), a marker of infection, are primarily used to differentiate FMD virus (FMDV) infected from vaccinated animals (DIVA). However, such DIVA assays have a limitation to their specificity since residual NSPs present in the relatively impure vaccines are suspected to induce an NSP-antibody response in the repeatedly vaccinated animals. Epitope-deleted negative marker vaccine strategy seems to have an advantage over the conventional vaccines in identifying the infected animals with accuracy. NSP 3AB contains an abundance of immunodominant B-cell epitopes of diagnostic importance. This study addresses the feasibility of producing 3AB-truncated FMDV mutant as a potential negative marker vaccine candidate. An infectious cDNA clone of FMDV serotype Asia 1 strain was used to engineer an array of deletion mutations in the established antigenic domain of 3AB. The maximum length of deletion tolerated by the virus was found to be restricted to amino acid residues 87-144 in the C-terminal half of 3A protein along with deletion of the first two copies of 3B peptide. The 3AB-truncated marker virus (Asia 1 IND 491/1997Δ3A 3B +FLAG) demonstrated infectivity titres comparable to that of the parental virus in BHK-21 (log 7.42 TCID /ml) and LFBK-α ß (log 8.30 TCID /ml) cell monolayer culture. The protein fragment corresponding to the viable deletion in the 3AB region was expressed in a prokaryotic system to standardize a companion assay (3A 3B I-ELISA) for the negative marker virus which showed reasonably high diagnostic sensitivity (96.9%) and specificity (100% for naïve and 97.1% for uninfected vaccinated samples). The marker virus and its companion ELISA designed in this study provide a basis to devise a marker vaccine strategy for FMD control.
[Mh] Termos MeSH primário: Vírus da Febre Aftosa/genética
Febre Aftosa/virologia
Poliproteínas/genética
Proteínas não Estruturais Virais/genética
Proteínas Virais/imunologia
[Mh] Termos MeSH secundário: Animais
Anticorpos Antivirais/imunologia
Análise Mutacional de DNA
Epitopos de Linfócito B/genética
Epitopos de Linfócito B/imunologia
Febre Aftosa/imunologia
Febre Aftosa/prevenção & controle
Vírus da Febre Aftosa/imunologia
Poliproteínas/imunologia
Proteínas não Estruturais Virais/imunologia
Proteínas Virais/genética
Vacinas Virais/genética
Vacinas Virais/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Viral); 0 (Epitopes, B-Lymphocyte); 0 (Polyproteins); 0 (Viral Nonstructural Proteins); 0 (Viral Proteins); 0 (Viral Vaccines)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171018
[St] Status:MEDLINE


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[PMID]:28918473
[Au] Autor:Charles J; Tangudu CS; Firth AE; Blitvich BJ
[Ad] Endereço:Department of Veterinary Microbiology and Preventive Medicine, College of Veterinary Medicine, Iowa State University, Ames, IA, USA.
[Ti] Título:Complete genome sequences of two insect-specific flaviviruses.
[So] Source:Arch Virol;162(12):3913-3917, 2017 Dec.
[Is] ISSN:1432-8798
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:We determined the complete genomic sequences of two previously discovered insect-specific flaviviruses, Marisma mosquito virus (MMV) and Nanay virus (NANV), using a combination of high-throughput sequencing, reverse transcription-polymerase chain reaction, 5' and 3' rapid amplification of cDNA ends and Sanger sequencing. Complete polyprotein amino acid sequence alignments revealed that the closest known relatives of MMV and NANV are Donggang virus (89% identity, 95% similarity) and Nounané virus (53% identity, 70% similarity), respectively. Phylogenetic inference is in agreement with these findings. Potential programmed -1 ribosomal frameshifting sites were bioinformatically identified in the genomes of both viruses.
[Mh] Termos MeSH primário: Flavivirus/classificação
Flavivirus/isolamento & purificação
Genoma Viral
Insetos/virologia
Análise de Sequência de DNA
[Mh] Termos MeSH secundário: Animais
Flavivirus/genética
Mudança da Fase de Leitura do Gene Ribossômico
Sequenciamento de Nucleotídeos em Larga Escala
Filogenia
Poliproteínas/genética
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Homologia de Sequência de Aminoácidos
Proteínas Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Polyproteins); 0 (Viral Proteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171119
[Lr] Data última revisão:
171119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170918
[St] Status:MEDLINE
[do] DOI:10.1007/s00705-017-3552-5


  5 / 433 MEDLINE  
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[PMID]:28358924
[Au] Autor:Sun H; Zhou N; Wang H; Huang D; Lang Z
[Ad] Endereço:Biotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing, China.
[Ti] Título:Processing and targeting of proteins derived from polyprotein with 2A and LP4/2A as peptide linkers in a maize expression system.
[So] Source:PLoS One;12(3):e0174804, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In the transformation of multiple genes, gene fusion is an attractive alternative to other methods, including sexual crossing, re-transformation, and co-transformation, among others. The 2A peptide from the foot-and-mouth disease virus (FMDV) causes the co-translational "cleavage" of polyprotein and operates in a wide variety of eukaryotic cells. LP4, a linker peptide that originates from a natural polyprotein occurring in the seed of Impatiens balsamina, can be split between the first and second amino acids in post-translational processing. LP4/2A is a hybrid linker peptide that contains the first nine amino acids of LP4 and 20 amino acids of 2A. The three linkers have been used as a suitable technique to link the expression of genes in some transgenic plants, but to date the cleavage efficiency of three linkers have not been comprehensively demonstrated in the same transformation system, especially in the staple crop. To verify the functions of 2A, LP4, and LP4/2A linker peptides in transgenic maize, six fusion protein vectors that each encoded a single open reading frame (ORF) incorporating two report genes, Green Fluorescent Protein (GFP) and ß-glucuronidase (GUS), separated by 2A (or modified 2A), LP4 or LP4/2A were assembled to compare the cleavage efficiency of the three linkers in a maize transient expression system. The results demonstrated the more protein production and higher cleavage splicing efficiency with the polyprotein construct linked by the LP4/2A peptide than those of the polyprotein constructs linked by 2A or LP4 alone. Seven other fusion proteins that each encoded a single ORF incorporating two different genes GFP and Red Fluorecent Protein (RFP) with different signal peptides were assembled to study the subcellular localization of genes linked by LP4/2A. The subcellular localization experiments suggested that both types of signal peptide, co-translational and post-translational, could lead their proteins to the target localization in maize protoplast transformed by LP4/2A polyprotein construct and it implied the LP4/2A linker peptide could alleviate the inhibition of 2A processing by the carboxy-terminal region of upstream protein of 2A when translocated into the ER.
[Mh] Termos MeSH primário: Peptídeos/metabolismo
Plantas Geneticamente Modificadas/metabolismo
Proteínas Virais/metabolismo
Zea mays/metabolismo
[Mh] Termos MeSH secundário: Vírus da Febre Aftosa/genética
Vírus da Febre Aftosa/metabolismo
Glucuronidase/genética
Glucuronidase/metabolismo
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Fases de Leitura Aberta/genética
Peptídeos/genética
Plantas Geneticamente Modificadas/genética
Poliproteínas/genética
Poliproteínas/metabolismo
Processamento de Proteína Pós-Traducional
Proteínas Virais/genética
Zea mays/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptides); 0 (Polyproteins); 0 (Viral Proteins); 147336-22-9 (Green Fluorescent Proteins); EC 3.2.1.31 (Glucuronidase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170828
[Lr] Data última revisão:
170828
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170331
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0174804


  6 / 433 MEDLINE  
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[PMID]:28247096
[Au] Autor:Elbeaino T; Belghacem I; Mascia T; Gallitelli D; Digiaro M
[Ad] Endereço:Istituto Agronomico Mediterraneo di Bari, Via Ceglie 9, Valenzano, 70010, Bari, Italy. elbeaino@iamb.it.
[Ti] Título:Next generation sequencing and molecular analysis of artichoke Italian latent virus.
[So] Source:Arch Virol;162(6):1805-1809, 2017 Jun.
[Is] ISSN:1432-8798
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:Next-generation sequencing (NGS) allowed the assembly of the complete RNA-1 and RNA-2 sequences of a grapevine isolate of artichoke Italian latent virus (AILV). RNA-1 and RNA-2 are 7,338 and 4,630 nucleotides in length excluding the 3' terminal poly(A) tail, and encode two putative polyproteins of 255.8 kDa (p1) and 149.6 kDa (p2), respectively. All conserved motifs and predicted cleavage sites, typical for nepovirus polyproteins, were found in p1 and p2. AILV p1 and p2 share high amino acid identity with their homologues in beet ringspot virus (p1, 81% and p2, 71%), tomato black ring virus (p1, 79% and p2, 63%), grapevine Anatolian ringspot virus (p1, 65% and p2, 63%), and grapevine chrome mosaic virus (p1, 60% and p2, 54%), and to a lesser extent with other grapevine nepoviruses of subgroup A and C. Phylogenetic and sequence analyses, all confirmed the strict relationship of AILV with members classified in subgroup B of genus Nepovirus.
[Mh] Termos MeSH primário: Nepovirus/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Cynara scolymus/virologia
Sequenciamento de Nucleotídeos em Larga Escala
Itália
Nepovirus/classificação
Nepovirus/isolamento & purificação
Filogenia
Doenças das Plantas/virologia
Poliproteínas/genética
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Polyproteins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170630
[Lr] Data última revisão:
170630
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170302
[St] Status:MEDLINE
[do] DOI:10.1007/s00705-017-3290-8


  7 / 433 MEDLINE  
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[PMID]:28027478
[Au] Autor:Gushchin VA; Karlin DG; Makhotenko AV; Khromov AV; Erokhina TN; Solovyev AG; Morozov SY; Agranovsky AA
[Ad] Endereço:Faculty of Biology, Moscow State University, Moscow 119991, Russia; N.F. Gamaleya Federal Research Centre for Epidemiology and Microbiology, Ministry of Health of the Russian Federation, Russia.
[Ti] Título:A conserved region in the Closterovirus 1a polyprotein drives extensive remodeling of endoplasmic reticulum membranes and induces motile globules in Nicotiana benthamiana cells.
[So] Source:Virology;502:106-113, 2017 Feb.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In infected plant cells, closterovirus replicative polyproteins 1a and 1ab drive membrane remodeling and formation of multivesicular replication platforms. Polyprotein 1a contains a variable Central Region (CR) between the methyltransferase and helicase domains. In a previous study, we have found that transient expression of the Beet yellows virus CR-2 segment (aa 1305-1494) in Nicotiana benthamiana induces the formation of ~1µm mobile globules originating from the ER membranes. In the present study, sequence analysis has shown that a part of the CR named the "Zemlya region" (overlapping the CR-2), is conserved in all members of the Closterovirus genus and contains a predicted amphipathic helix (aa 1368-1385). By deletion analysis, the CR-2 region responsible for the induction of 1-µm globules has been mapped to aa 1368-1432. We suggest that the conserved membrane-modifying region of the BYV 1a may be involved in the biogenesis of closterovirus replication platforms.
[Mh] Termos MeSH primário: Closterovirus/genética
Retículo Endoplasmático/virologia
Doenças das Plantas/virologia
Poliproteínas/química
Poliproteínas/metabolismo
Tabaco/virologia
Proteínas Virais/química
Proteínas Virais/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Closterovirus/química
Closterovirus/metabolismo
Sequência Conservada
Retículo Endoplasmático/metabolismo
Dados de Sequência Molecular
Poliproteínas/genética
Alinhamento de Sequência
Proteínas Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Polyproteins); 0 (Viral Proteins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170622
[Lr] Data última revisão:
170622
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161228
[St] Status:MEDLINE


  8 / 433 MEDLINE  
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[PMID]:28006103
[Au] Autor:da Silva MA; Lenton S; Hughes M; Brockwell DJ; Dougan L
[Ad] Endereço:School of Physics and Astronomy and ‡Astbury Centre for Structural Molecular Biology, University of Leeds , Leeds LS2 9JT, United Kingdom.
[Ti] Título:Assessing the Potential of Folded Globular Polyproteins As Hydrogel Building Blocks.
[So] Source:Biomacromolecules;18(2):636-646, 2017 Feb 13.
[Is] ISSN:1526-4602
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The native states of proteins generally have stable well-defined folded structures endowing these biomolecules with specific functionality and molecular recognition abilities. Here we explore the potential of using folded globular polyproteins as building blocks for hydrogels. Photochemically cross-linked hydrogels were produced from polyproteins containing either five domains of I27 ((I27) ), protein L ((pL) ), or a 1:1 blend of these proteins. SAXS analysis showed that (I27) exists as a single rod-like structure, while (pL) shows signatures of self-aggregation in solution. SANS measurements showed that both polyprotein hydrogels have a similar nanoscopic structure, with protein L hydrogels being formed from smaller and more compact clusters. The polyprotein hydrogels showed small energy dissipation in a load/unload cycle, which significantly increased when the hydrogels were formed in the unfolded state. This study demonstrates the use of folded proteins as building blocks in hydrogels, and highlights the potential versatility that can be offered in tuning the mechanical, structural, and functional properties of polyproteins.
[Mh] Termos MeSH primário: Hidrogel de Polietilenoglicol-Dimetacrilato/química
Poliproteínas/química
Engenharia de Proteínas
[Mh] Termos MeSH secundário: Seres Humanos
Reologia
Espalhamento a Baixo Ângulo
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Polyproteins); 25852-47-5 (Hydrogel, Polyethylene Glycol Dimethacrylate)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161223
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biomac.6b01877


  9 / 433 MEDLINE  
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[PMID]:27722992
[Au] Autor:Hao F; Zhou Z; Wu M; Li G
[Ad] Endereço:The State Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan, 430070, Hubei, China.
[Ti] Título:Molecular characterization of a novel endornavirus from the phytopathogenic fungus Botrytis cinerea.
[So] Source:Arch Virol;162(1):313-316, 2017 Jan.
[Is] ISSN:1432-8798
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:The complete sequence of a novel endornavirus (Botrytis cinerea endornavirus 1, BcEV1) from the phytopathogenic fungus Botrytis cinerea strain HBtom-372 was determined. The BcEV1 coding strand is 11,557 nucleotides long, possessing an open reading frame (ORF) that codes for a polyprotein of 3,787 amino acid residues and lacks a site-specific nick. The polyprotein contains viral methyltransferase (MTR) domain, a cysteine-rich region (CRR), two putative viral helicase (DEXDc-like and Hel-1) domains, and an RNA-dependent RNA polymerase_2 (RdRp_2) domain. In phylogenetic analysis, BcEV1 clustered with several fungal endornaviruses, forming an independent clade, and it was detected in 4.2 % of B. cinerea strains collected from central China.
[Mh] Termos MeSH primário: Botrytis/virologia
Micovírus/genética
Micovírus/isolamento & purificação
Genoma Viral
Vírus de RNA/genética
Vírus de RNA/isolamento & purificação
Análise de Sequência de DNA
[Mh] Termos MeSH secundário: China
Análise por Conglomerados
Micovírus/classificação
Fases de Leitura Aberta
Filogenia
Poliproteínas/genética
Domínios Proteicos
Vírus de RNA/classificação
RNA Viral/genética
Homologia de Sequência
Proteínas Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Polyproteins); 0 (RNA, Viral); 0 (Viral Proteins)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170127
[Lr] Data última revisão:
170127
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161011
[St] Status:MEDLINE
[do] DOI:10.1007/s00705-016-3106-2


  10 / 433 MEDLINE  
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[PMID]:27686070
[Au] Autor:Knierim D; Menzel W; Winter S
[Ad] Endereço:Leibniz Institute DSMZ-German Collection of Microorganisms and Cell Cultures, Inhoffenstrasse 7B, 38124, Braunschweig, Germany. dennis.knierim@dsmz.de.
[Ti] Título:Analysis of the complete genome sequence of euphorbia ringspot virus, an atypical member of the genus Potyvirus.
[So] Source:Arch Virol;162(1):291-293, 2017 Jan.
[Is] ISSN:1432-8798
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:The complete genome sequence of an isolate of euphorbia ringspot virus (EuRSV) was determined by deep sequencing and rapid amplification of cDNA ends (RACE) RT-PCR. It has an RNA genome of 10,154 nucleotides in size, excluding the poly(A) tail, and encodes a polyprotein of 3265 amino acids. Phylogenetic analysis from this study supports the earlier taxonomic assignment to the genus Potyvirus; however, a gene encoding the HAM1h protein, inserted between NIb and CP of the EuRSV genome, which was previously only observed for cassava brown streak virus and Ugandan cassava brown streak virus of the genus Ipomovirus, is an unusual feature of this potyvirus, which otherwise has typical potyvirus genome features.
[Mh] Termos MeSH primário: Genoma Viral
Potyvirus/genética
Potyvirus/isolamento & purificação
RNA Viral/genética
Análise de Sequência de DNA
[Mh] Termos MeSH secundário: Análise por Conglomerados
Euphorbia/virologia
Ordem dos Genes
Sequenciamento de Nucleotídeos em Larga Escala
Filogenia
Doenças das Plantas/virologia
Poliproteínas/genética
Potyvirus/classificação
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Homologia de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Polyproteins); 0 (RNA, Viral)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170127
[Lr] Data última revisão:
170127
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161001
[St] Status:MEDLINE
[do] DOI:10.1007/s00705-016-3087-1



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