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Referências encontradas : 702 [refinar]
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  1 / 702 MEDLINE  
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[PMID]:28314126
[Au] Autor:Spannaus R; Miller C; Lindemann D; Bodem J
[Ad] Endereço:Institut für Virologie und Immunbiologie, Julius-Maximilians-Universität Würzburg, Germany.
[Ti] Título:Purification of foamy viral particles.
[So] Source:Virology;506:28-33, 2017 Jun.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Foamy viruses are non-pathogenic retroviruses and represent a tool for vector development. For gene therapy applications and for analyses of viral protein composition infectious particles need to be purified, which has been difficult for foamy viruses in the past. Here, we describe a novel, simple, and fast purification method for prototype foamy viruses with high purity using size exclusion and affinity chromatography. More than 99,9% of the contaminating proteins were removed. The purified viruses were used to determine the amount of the incorporated Pol protein relative to Gag. The determined Gag to Pol PR-RT ratio of 30:1 confirmed previous studies suggesting FV virions encapsidate fewer number of Pol molecules than orthoretroviruses.
[Mh] Termos MeSH primário: Cromatografia de Afinidade/métodos
Cromatografia em Gel/métodos
Spumavirus/crescimento & desenvolvimento
Vírion/crescimento & desenvolvimento
[Mh] Termos MeSH secundário: Regulação Viral da Expressão Gênica
Produtos do Gene pol/genética
Produtos do Gene pol/metabolismo
Seres Humanos
Infecções por Retroviridae/virologia
Spumavirus/genética
Spumavirus/isolamento & purificação
Spumavirus/fisiologia
Vírion/genética
Vírion/isolamento & purificação
Vírion/fisiologia
Montagem de Vírus
Cultura de Vírus
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gene Products, pol)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170705
[Lr] Data última revisão:
170705
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170318
[St] Status:MEDLINE


  2 / 702 MEDLINE  
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[PMID]:28270144
[Au] Autor:Yuan P; Dong L; Cheng Q; Wang S; Li Z; Sun Y; Han S; Yin J; Peng B; He X; Liu W
[Ad] Endereço:Hubei Province Key Laboratory of Allergy and Immunology, School of Basic Medical Sciences, Wuhan University, No. 185, Donghu Road, Wuchang District, Wuhan, 430071, China.
[Ti] Título:Prototype foamy virus elicits complete autophagy involving the ER stress-related UPR pathway.
[So] Source:Retrovirology;14(1):16, 2017 Mar 07.
[Is] ISSN:1742-4690
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Prototype foamy virus (PFV) is a member of the Spumaretrovirinae subfamily of retroviruses, which maintains lifelong latent infection while being nonpathogenic to their natural hosts. Autophagy is a cell-programmed mechanism that plays a pivotal role in controlling homeostasis and defense against exotic pathogens. However, whether autophagy is the mechanism for host defense in PFV infection has not been investigated. FINDINGS: Our results revealed that PFV infection induced the accumulation of autophagosomes and triggered complete autophagic flux in BHK-21 cells. PFV infection also altered endoplasmic reticulum (ER) homeostasis. The PERK, IRE1 and ATF6 pathways, all of which are components of the ER stress-related unfolded protein response (UPR), were activated in PFV-infected cells. In addition, accelerating autophagy suppressed PFV replication, and inhibition of autophagy promoted viral replication. CONCLUSIONS: Our data indicate that PFV infection can induce complete autophagy through activating the ER stress-related UPR pathway in BHK-21 cells. In turn, autophagy negatively regulates PFV replication.
[Mh] Termos MeSH primário: Autofagia
Estresse do Retículo Endoplasmático
Interações Hospedeiro-Patógeno
Spumavirus/imunologia
Spumavirus/fisiologia
Resposta a Proteínas não Dobradas
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Cricetinae
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170510
[Lr] Data última revisão:
170510
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170309
[St] Status:MEDLINE
[do] DOI:10.1186/s12977-017-0341-x


  3 / 702 MEDLINE  
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[PMID]:28185138
[Au] Autor:Chen D; Song J; Sun Y; Li Z; Wen D; Liu Q; Liu W; He X
[Ad] Endereço:College of Life Sciences, Shaanxi Normal University, No. 620 West Chang'an Avenue, Chang'an District, Xi'an, 710119, Shaanxi, People's Republic of China.
[Ti] Título:The fourth central polypurine tract guides the synthesis of prototype foamy virus plus-strand DNA.
[So] Source:Virus Genes;53(2):259-265, 2017 Apr.
[Is] ISSN:1572-994X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Foamy virus (FV) is a nonpathogenic retrovirus that has the potential to serve as a gene therapy vector. In retroviral replication, the central polypurine tract (cPPT) is used as a primer to synthesize plus-strand DNA. The cPPT is subsequently degraded to produce a single-stranded gap in the double-stranded viral DNA molecule. In the prototype foamy virus (PFV), four cPPT-like motifs have been previously identified, in which there is a gap with uncertain terminals. In this study, we determined the length of the PFV gap varying from 144 to 731 bp. The 3' terminus of the cleavage sites is located between 6272 bp and 6274 bp from the first base of PFV genome, while the 5' terminus is located within a 465 bp range. The start and terminal nucleotides of the gap are located on either side of the fourth cPPT element. Deletion, mutation, and replacement of the fourth cPPT with the Human immunodeficiency virus 1 (HIV-1) cPPT resulted in a significant reduction in modified PFV virions, indicating that the fourth cPPT ought to be the primer that guides the synthesis of PFV plus-strand DNA. These results improve the theoretical basis for understanding FVs replication and will help construct new FV vectors with simple genome sequences containing only the necessary cis elements.
[Mh] Termos MeSH primário: Replicação do DNA/genética
DNA Viral/genética
Spumavirus/genética
Replicação Viral/genética
[Mh] Termos MeSH secundário: Sequência de Bases
DNA Viral/biossíntese
Vetores Genéticos
Seres Humanos
Purinas/metabolismo
Spumavirus/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Viral); 0 (Purines); W60KTZ3IZY (purine)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170211
[St] Status:MEDLINE
[do] DOI:10.1007/s11262-016-1425-8


  4 / 702 MEDLINE  
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[PMID]:28040837
[Au] Autor:Wagner TC; Bodem J
[Ad] Endereço:Institut für Virologie und Immubiologie, Julius-Maximilians-Universität, Würzburg, Germany.
[Ti] Título:Sequence errors in foamy virus sequences in the GenBank database: resequencing of the prototypic foamy virus proviral plasmids.
[So] Source:Arch Virol;162(4):1141-1144, 2017 Apr.
[Is] ISSN:1432-8798
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:Nucleotide sequences are the fundamental basis for work on molecular mechanisms and for phylogenetic analysis. Recently, we identified sequence errors in all of the LTR sequences of the prototypic foamy virus stored in the GenBank database. Here, we report the resequencing of the proviral plasmids pHSRV13 and pHSRV2. Sequence comparisons revealed an error rate for the foamy virus sequences stored in the database of up to 10 errors per 1000 bp. Even the newest sequences of the codon-optimized foamy virus synthetic Gag, Pol, and Env amino acid sequences showed exchanges compared to the new proviral pHSRV13n sequence. Our results provide evidence that some prototypic foamy virus sequences contain errors and should be revised.
[Mh] Termos MeSH primário: Bases de Dados de Ácidos Nucleicos/normas
Plasmídeos/genética
Análise de Sequência de DNA/normas
Spumavirus/genética
[Mh] Termos MeSH secundário: Sequência de Bases
Dados de Sequência Molecular
Filogenia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170315
[Lr] Data última revisão:
170315
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170102
[St] Status:MEDLINE
[do] DOI:10.1007/s00705-016-3206-z


  5 / 702 MEDLINE  
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[PMID]:28024082
[Au] Autor:Browning DL; Everson EM; Leap DJ; Hocum JD; Wang H; Stamatoyannopoulos G; Trobridge GD
[Ad] Endereço:School of Molecular Biosciences, Washington State University, Pullman, WA, USA.
[Ti] Título:Evidence for the in vivo safety of insulated foamy viral vectors.
[So] Source:Gene Ther;24(3):187-198, 2017 Mar.
[Is] ISSN:1476-5462
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Retroviral vector-mediated stem cell gene therapy is a promising approach for the treatment of hematopoietic disorders. However, genotoxic side effects from integrated vector proviruses are a significant concern for the use of retroviral vectors in the clinic. Insulated foamy viral (FV) vectors are potentially safer retroviral vectors for hematopoietic stem cell gene therapy. We evaluated two newly identified human insulators, A1 and A2, for use in FV vectors. These insulators had moderate insulating capacity and higher titers than previously developed insulated FV vectors. The A1-insulated FV vector was chosen for comparison with the previously described 650cHS4-insulated FV vector in human cord blood CD34 repopulating cells in an immunodeficient mouse model. To maximize the effects of the insulators on the safety of FV vectors, FV vectors containing a highly genotoxic spleen focus forming virus promoter were used to elicit differences in genotoxicity. In vivo, the A1-insulated FV vector showed an approximate 50% reduction in clonal dominance compared with either the 650cHS4-insulated or control FV vectors, although the transduction efficiency of the A1-insulated vector was higher. This data suggests that the A1-insulated FV vector is promising for future preclinical and clinical studies.
[Mh] Termos MeSH primário: Terapia Genética/efeitos adversos
Vetores Genéticos/genética
Elementos Isolantes
Spumavirus/genética
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Células Cultivadas
Dano ao DNA
Terapia Genética/métodos
Vetores Genéticos/efeitos adversos
Células HEK293
Transplante de Células-Tronco Hematopoéticas
Células-Tronco Hematopoéticas/metabolismo
Seres Humanos
Masculino
Camundongos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170815
[Lr] Data última revisão:
170815
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161227
[St] Status:MEDLINE
[do] DOI:10.1038/gt.2016.88


  6 / 702 MEDLINE  
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[PMID]:27840397
[Au] Autor:Hamid FB; Kim J; Shin CG
[Ad] Endereço:Department of Systems Biotechnology, Chung-Ang University, Ansung 17546, Republic of Korea.
[Ti] Título:Characterization of Prototype Foamy Virus Infectivity in Transportin 3 Knockdown Human 293t Cell Line.
[So] Source:J Microbiol Biotechnol;27(2):380-387, 2017 Feb 28.
[Is] ISSN:1738-8872
[Cp] País de publicação:Korea (South)
[La] Idioma:eng
[Ab] Resumo:The foamy viruses are currently considered essential for development as vectors for gene delivery. Previous studies demonstrated that prototype foamy virus (PFV) can infect and replicate prevalently in a variety of cell types for its exclusive replication strategy. However, the virus-host interaction, especially PFV-transportin3 (TNPO3), is still poorly understood. In our investigation of the role of TNPO3 in PFV infection, we found lower virus production in TNPO3 knockdown (KD) cells compared with wild-type 293T cells. PCR analysis revealed that viral DNAs were mostly altered to circular forms: both 1-long terminal repeat (1-LTR) and 2-LTR in TNPO3 KD cells. We therefore suggest that TNPO3 is required for successful PFV replication, at least at/after the nuclear entry step of viral DNA. These findings highlight the obscure mysteries of PFV-host interaction and the requirement of TNPO3 for productive infection of PFV in 293T cells.
[Mh] Termos MeSH primário: Spumavirus/fisiologia
Replicação Viral
beta Carioferinas/fisiologia
[Mh] Termos MeSH secundário: DNA Viral
Técnicas de Silenciamento de Genes
Células HEK293
Interações Hospedeiro-Patógeno
Seres Humanos
Spumavirus/genética
Sequências Repetidas Terminais
Transfecção
beta Carioferinas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Viral); 0 (TNPO3 protein, human); 0 (beta Karyopherins)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170328
[Lr] Data última revisão:
170328
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161115
[St] Status:MEDLINE
[do] DOI:10.4014/jmb.1606.06011


  7 / 702 MEDLINE  
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[PMID]:27886074
[Au] Autor:Buseyne F; Gessain A; Soares MA; Santos AF; Materniak-Kornas M; Lesage P; Zamborlini A; Löchelt M; Qiao W; Lindemann D; Wöhrl BM; Stoye JP; Taylor IA; Khan AS
[Ad] Endereço:Unité d'Épidémiologie et Physiopathologie des Virus Oncogènes, Institut Pasteur, 75015 Paris, France. florence.buseyne@pasteur.fr.
[Ti] Título:Eleventh International Foamy Virus Conference-Meeting Report.
[So] Source:Viruses;8(11), 2016 Nov 23.
[Is] ISSN:1999-4915
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The Eleventh International Foamy Virus Conference took place on 9-10 June 2016 at the Institut Pasteur, Paris, France. The meeting reviewed progress on foamy virus (FV) research, as well as related current topics in retrovirology. FVs are complex retroviruses that are widespread in several animal species. Several research topics on these viruses are relevant to human health: cross-species transmission and viral emergence, vectors for gene therapy, development of antiretroviral drugs, retroviral evolution and its influence on the human genome. In this article, we review the conference presentations on these viruses and highlight the major questions to be answered.
[Mh] Termos MeSH primário: Infecções por Retroviridae/veterinária
Infecções por Retroviridae/virologia
Spumavirus/patogenicidade
[Mh] Termos MeSH secundário: Animais
Antivirais/isolamento & purificação
Antivirais/farmacologia
Transmissão de Doença Infecciosa
Vetores Genéticos
Seres Humanos
Paris
Infecções por Retroviridae/tratamento farmacológico
Infecções por Retroviridae/epidemiologia
Spumavirus/genética
[Pt] Tipo de publicação:CONGRESSES
[Nm] Nome de substância:
0 (Antiviral Agents)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170913
[Lr] Data última revisão:
170913
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161126
[St] Status:MEDLINE


  8 / 702 MEDLINE  
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[PMID]:27829070
[Au] Autor:Ball NJ; Nicastro G; Dutta M; Pollard DJ; Goldstone DC; Sanz-Ramos M; Ramos A; Müllers E; Stirnnagel K; Stanke N; Lindemann D; Stoye JP; Taylor WR; Rosenthal PB; Taylor IA
[Ad] Endereço:Macromolecular Structure Laboratory, The Francis Crick Institute, Mill Hill Laboratory, London, United Kingdom.
[Ti] Título:Structure of a Spumaretrovirus Gag Central Domain Reveals an Ancient Retroviral Capsid.
[So] Source:PLoS Pathog;12(11):e1005981, 2016 Nov.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Spumaretrovirinae, or foamy viruses (FVs) are complex retroviruses that infect many species of monkey and ape. Despite little sequence homology, FV and orthoretroviral Gag proteins perform equivalent functions, including genome packaging, virion assembly, trafficking and membrane targeting. However, there is a paucity of structural information for FVs and it is unclear how disparate FV and orthoretroviral Gag molecules share the same function. To probe the functional overlap of FV and orthoretroviral Gag we have determined the structure of a central region of Gag from the Prototype FV (PFV). The structure comprises two all α-helical domains NtDCEN and CtDCEN that although they have no sequence similarity, we show they share the same core fold as the N- (NtDCA) and C-terminal domains (CtDCA) of archetypal orthoretroviral capsid protein (CA). Moreover, structural comparisons with orthoretroviral CA align PFV NtDCEN and CtDCEN with NtDCA and CtDCA respectively. Further in vitro and functional virological assays reveal that residues making inter-domain NtDCEN-CtDCEN interactions are required for PFV capsid assembly and that intact capsid is required for PFV reverse transcription. These data provide the first information that relates the Gag proteins of Spuma and Orthoretrovirinae and suggests a common ancestor for both lineages containing an ancient CA fold.
[Mh] Termos MeSH primário: Proteínas do Capsídeo/genética
Produtos do Gene gag/química
Produtos do Gene gag/genética
Spumavirus/genética
Montagem de Vírus/fisiologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Western Blotting
Capsídeo
Linhagem Celular
Seres Humanos
Ressonância Magnética Nuclear Biomolecular
Conformação Proteica
Reação em Cadeia da Polimerase em Tempo Real
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Capsid Proteins); 0 (Gene Products, gag)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161110
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1005981


  9 / 702 MEDLINE  
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[PMID]:27589786
[Au] Autor:Hamann MV; Lindemann D
[Ad] Endereço:Institute of Virology, Medical Faculty Carl Gustav Carus, Technische Universität Dresden, 01307 Dresden, Germany. martin.hamann@tu-dresden.de.
[Ti] Título:Foamy Virus Protein-Nucleic Acid Interactions during Particle Morphogenesis.
[So] Source:Viruses;8(9), 2016 Aug 30.
[Is] ISSN:1999-4915
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Compared with orthoretroviruses, our understanding of the molecular and cellular replication mechanism of foamy viruses (FVs), a subfamily of retroviruses, is less advanced. The FV replication cycle differs in several key aspects from orthoretroviruses, which leaves established retroviral models debatable for FVs. Here, we review the general aspect of the FV protein-nucleic acid interactions during virus morphogenesis. We provide a summary of the current knowledge of the FV genome structure and essential sequence motifs required for RNA encapsidation as well as Gag and Pol binding in combination with details about the Gag and Pol biosynthesis. This leads us to address open questions in FV RNA engagement, binding and packaging. Based on recent findings, we propose to shift the point of view from individual glycine-arginine-rich motifs having functions in RNA interactions towards envisioning the FV Gag C-terminus as a general RNA binding protein module. We encourage further investigating a potential new retroviral RNA packaging mechanism, which seems more complex in terms of the components that need to be gathered to form an infectious particle. Additional molecular insights into retroviral protein-nucleic acid interactions help us to develop safer, more specific and more efficient vectors in an era of booming genome engineering and gene therapy approaches.
[Mh] Termos MeSH primário: RNA Viral/metabolismo
Spumavirus/fisiologia
Proteínas Virais/metabolismo
Montagem de Vírus
[Mh] Termos MeSH secundário: Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (RNA, Viral); 0 (Viral Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160903
[St] Status:MEDLINE


  10 / 702 MEDLINE  
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[PMID]:27579920
[Au] Autor:Zurnic I; Hütter S; Rzeha U; Stanke N; Reh J; Müllers E; Hamann MV; Kern T; Gerresheim GK; Lindel F; Serrao E; Lesbats P; Engelman AN; Cherepanov P; Lindemann D
[Ad] Endereço:Institute of Virology, Medical Faculty "Carl Gustav Carus", Technische Universität Dresden, Dresden, Germany.
[Ti] Título:Interactions of Prototype Foamy Virus Capsids with Host Cell Polo-Like Kinases Are Important for Efficient Viral DNA Integration.
[So] Source:PLoS Pathog;12(8):e1005860, 2016 Aug.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Unlike for other retroviruses, only a few host cell factors that aid the replication of foamy viruses (FVs) via interaction with viral structural components are known. Using a yeast-two-hybrid (Y2H) screen with prototype FV (PFV) Gag protein as bait we identified human polo-like kinase 2 (hPLK2), a member of cell cycle regulatory kinases, as a new interactor of PFV capsids. Further Y2H studies confirmed interaction of PFV Gag with several PLKs of both human and rat origin. A consensus Ser-Thr/Ser-Pro (S-T/S-P) motif in Gag, which is conserved among primate FVs and phosphorylated in PFV virions, was essential for recognition by PLKs. In the case of rat PLK2, functional kinase and polo-box domains were required for interaction with PFV Gag. Fluorescently-tagged PFV Gag, through its chromatin tethering function, selectively relocalized ectopically expressed eGFP-tagged PLK proteins to mitotic chromosomes in a Gag STP motif-dependent manner, confirming a specific and dominant nature of the Gag-PLK interaction in mammalian cells. The functional relevance of the Gag-PLK interaction was examined in the context of replication-competent FVs and single-round PFV vectors. Although STP motif mutated viruses displayed wild type (wt) particle release, RNA packaging and intra-particle reverse transcription, their replication capacity was decreased 3-fold in single-cycle infections, and up to 20-fold in spreading infections over an extended time period. Strikingly similar defects were observed when cells infected with single-round wt Gag PFV vectors were treated with a pan PLK inhibitor. Analysis of entry kinetics of the mutant viruses indicated a post-fusion defect resulting in delayed and reduced integration, which was accompanied with an enhanced preference to integrate into heterochromatin. We conclude that interaction between PFV Gag and cellular PLK proteins is important for early replication steps of PFV within host cells.
[Mh] Termos MeSH primário: Capsídeo/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
Infecções por Retroviridae/metabolismo
Spumavirus/metabolismo
Integração Viral/fisiologia
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Animais
Produtos do Gene gag/genética
Produtos do Gene gag/metabolismo
Células HeLa
Seres Humanos
Camundongos
Fosforilação/genética
Domínios Proteicos
Proteínas Serina-Treonina Quinases/genética
Ratos
Infecções por Retroviridae/genética
Spumavirus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gene Products, gag); EC 2.7.11.- (PLK2 protein, human); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.21 (Plk2 protein, rat); EC 2.7.11.21 (serum-inducible kinase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170623
[Lr] Data última revisão:
170623
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160901
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1005860



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