Base de dados : MEDLINE
Pesquisa : D13.444.600.723.480 [Categoria DeCS]
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[PMID]:28542524
[Au] Autor:Piatek MJ; Henderson V; Fearn A; Chaudhry B; Werner A
[Ad] Endereço:RNA Interest Group, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, United Kingdom.
[Ti] Título:Ectopically expressed Slc34a2a sense-antisense transcripts cause a cerebellar phenotype in zebrafish embryos depending on RNA complementarity and Dicer.
[So] Source:PLoS One;12(5):e0178219, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Natural antisense transcripts (NATs) are complementary to protein coding genes and potentially regulate their expression. Despite widespread occurrence of NATs in the genomes of higher eukaryotes, their biological role and mechanism of action is poorly understood. Zebrafish embryos offer a unique model system to study sense-antisense transcript interplay at whole organism level. Here, we investigate putative antisense transcript-mediated mechanisms by ectopically co-expressing the complementary transcripts during early zebrafish development. In zebrafish the gene Slc34a2a (Na-phosphate transporter) is bi-directionally transcribed, the NAT predominantly during early development up to 48 hours after fertilization. Declining levels of the NAT, Slc34a2a(as), coincide with an increase of the sense transcript. At that time, sense and antisense transcripts co-localize in the endoderm at near equal amounts. Ectopic expression of the sense transcript during embryogenesis leads to specific failure to develop a cerebellum. The defect is RNA-mediated and dependent on sense-antisense complementarity. Overexpression of a Slc34a2a paralogue (Slc34a2b) or the NAT itself had no phenotypic consequences. Knockdown of Dicer rescued the brain defect suggesting that RNA interference is required to mediate the phenotype. Our results corroborate previous reports of Slc34a2a-related endo-siRNAs in two days old zebrafish embryos and emphasize the importance of coordinated expression of sense-antisense transcripts. Our findings suggest that RNAi is involved in gene regulation by certain natural antisense RNAs.
[Mh] Termos MeSH primário: RNA Helicases DEAD-box/genética
RNA Complementar/metabolismo
Proteínas Cotransportadoras de Sódio-Fosfato Tipo IIb/genética
Proteínas de Peixe-Zebra/metabolismo
Peixe-Zebra/metabolismo
[Mh] Termos MeSH secundário: Animais
Cerebelo/crescimento & desenvolvimento
Cerebelo/metabolismo
RNA Helicases DEAD-box/antagonistas & inibidores
RNA Helicases DEAD-box/metabolismo
Embrião não Mamífero/metabolismo
Desenvolvimento Embrionário/genética
Regulação da Expressão Gênica no Desenvolvimento
Hibridização In Situ
Morfolinos/metabolismo
Interferência de RNA
RNA Interferente Pequeno/metabolismo
Proteínas Cotransportadoras de Sódio-Fosfato Tipo IIb/antagonistas & inibidores
Proteínas Cotransportadoras de Sódio-Fosfato Tipo IIb/metabolismo
Peixe-Zebra/genética
Proteínas de Peixe-Zebra/antagonistas & inibidores
Proteínas de Peixe-Zebra/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Morpholinos); 0 (RNA, Complementary); 0 (RNA, Small Interfering); 0 (Sodium-Phosphate Cotransporter Proteins, Type IIb); 0 (Zebrafish Proteins); 0 (slc34a2a protein, zebrafish); EC 3.6.4.13 (DEAD-box RNA Helicases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170526
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0178219


  2 / 1465 MEDLINE  
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[PMID]:28530165
[Au] Autor:Hara K; Kashiwagi T; Hamada N; Watanabe H
[Ad] Endereço:Department of Infection Control and Prevention, Kurume University School of Medicine, Fukuoka 830-0011, Japan.
[Ti] Título:Basic amino acids in the N-terminal half of the PB2 subunit of influenza virus RNA polymerase are involved in both transcription and replication.
[So] Source:J Gen Virol;98(5):900-905, 2017 May.
[Is] ISSN:1465-2099
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The PB2 subunit of influenza virus RNA polymerase is known to be involved in the initiation of transcription of the virus genome via cap binding. However, other specific roles of PB2 for viral RNA synthesis are not well understood. Here, we demonstrate that basic residues, 124R, 142R, 143R, 268R and 331K/332R, in the N-terminal half of PB2 are important for the polymerase activity. Notably, R124A mutation remarkably reduced the synthesis of mRNA, cRNA and vRNA in vivo, which was in good agreement with the data obtained in vitro. Cross-linking studies suggested that a reduction of the polymerase activity in the R124A mutant was due to a significant decrease in binding to the viral RNA promoter. In the three-dimensional structure of the polymerase, 124R is visible through the NTP tunnel and is located close to the polymerase active site. We propose that 124R plays a key role in promoter binding during RNA synthesis.
[Mh] Termos MeSH primário: Aminoácidos Básicos/metabolismo
Orthomyxoviridae/fisiologia
Transcrição Genética
Proteínas Virais/metabolismo
Replicação Viral
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Aminoácidos Básicos/genética
Domínio Catalítico
Análise Mutacional de DNA
Modelos Moleculares
Conformação Proteica
RNA Complementar/biossíntese
RNA Mensageiro/biossíntese
RNA Viral/biossíntese
Proteínas Virais/química
Proteínas Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids, Basic); 0 (PB2 protein, influenza virus); 0 (RNA, Complementary); 0 (RNA, Messenger); 0 (RNA, Viral); 0 (Viral Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170523
[St] Status:MEDLINE
[do] DOI:10.1099/jgv.0.000750


  3 / 1465 MEDLINE  
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[PMID]:28333931
[Au] Autor:Yang C; Hu G; Li Z; Wang Q; Wang X; Yuan C; Wang Z; Hong W; Lu W; Cao L; Chen J; Wang Y; Yu S; Zhou Y; Yi Z; Fang Y
[Ad] Endereço:Division of Mood Disorders, Shanghai Mental Health Center, Shanghai Jiao Tong University School of Medicine, Shanghai, China.
[Ti] Título:Differential gene expression in patients with subsyndromal symptomatic depression and major depressive disorder.
[So] Source:PLoS One;12(3):e0172692, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Subsyndromal symptomatic depression (SSD) is a subtype of subthreshold depressive and can lead to significant psychosocial functional impairment. Although the pathogenesis of major depressive disorder (MDD) and SSD still remains poorly understood, a set of studies have found that many same genetic factors play important roles in the etiology of these two disorders. Nowadays, the differential gene expression between MDD and SSD is still unknown. In our previous study, we compared the expression profile and made the classification with the leukocytes by using whole-genome cRNA microarrays among drug-free first-episode subjects with SSD, MDD and matched healthy controls (8 subjects in each group), and finally determined 48 gene expression signatures. Based on these findings, we further clarify whether these genes mRNA was different expressed in peripheral blood in patients with SSD, MDD and healthy controls (60 subjects respectively). METHOD: With the help of the quantitative real-time reverse transcription-polymerase chain reaction (RT-qPCR), we gained gene relative expression levels among the three groups. RESULTS: We found that there are three of the forty eight co-regulated genes had differential expression in peripheral blood among the three groups, which are CD84, STRN, CTNS gene (F = 3.528, p = 0.034; F = 3.382, p = 0.039; F = 3.801, p = 0.026, respectively) while there were no significant differences for other genes. CONCLUSION: CD84, STRN, CTNS gene may have significant value for performing diagnostic functions and classifying SSD, MDD and healthy controls.
[Mh] Termos MeSH primário: Depressão/genética
Transtorno Depressivo Maior/genética
Expressão Gênica/genética
[Mh] Termos MeSH secundário: Adulto
Estudos de Casos e Controles
Feminino
Seres Humanos
Leucócitos/metabolismo
Masculino
RNA Complementar/genética
RNA Mensageiro/genética
Índice de Gravidade de Doença
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Complementary); 0 (RNA, Messenger)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170823
[Lr] Data última revisão:
170823
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170324
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0172692


  4 / 1465 MEDLINE  
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[PMID]:28332825
[Au] Autor:Lou C; Samuelsen SV; Christensen NJ; Vester B; Wengel J
[Ti] Título:Oligonucleotides Containing Aminated 2'-Amino-LNA Nucleotides: Synthesis and Strong Binding to Complementary DNA and RNA.
[So] Source:Bioconjug Chem;28(4):1214-1220, 2017 Apr 19.
[Is] ISSN:1520-4812
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mono- and diaminated 2'-amino-LNA monomers were synthesized and introduced into oligonucleotides. Each modification imparts significant stabilization of nucleic acid duplexes and triplexes, excellent sequence selectivity, and significant nuclease resistance. Molecular modeling suggested that structural stabilization occurs via intrastrand electrostatic attraction between the protonated amino groups of the aminated 2'-amino-LNA monomers and the host oligonucleotide backbone.
[Mh] Termos MeSH primário: Oligonucleotídeos/química
[Mh] Termos MeSH secundário: DNA Complementar/metabolismo
Desoxirribonucleases
Resistência a Medicamentos
Estabilidade de Medicamentos
Modelos Moleculares
Oligonucleotídeos/síntese química
Oligonucleotídeos/metabolismo
RNA Complementar/metabolismo
Eletricidade Estática
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Complementary); 0 (Oligonucleotides); 0 (RNA, Complementary); 0 (amino-LNA); EC 3.1.- (Deoxyribonucleases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170606
[Lr] Data última revisão:
170606
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170324
[St] Status:MEDLINE
[do] DOI:10.1021/acs.bioconjchem.7b00061


  5 / 1465 MEDLINE  
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[PMID]:28270562
[Au] Autor:Nomikos M; Stamatiadis P; Sanders JR; Beck K; Calver BL; Buntwal L; Lofty M; Sideratou Z; Swann K; Lai FA
[Ad] Endereço:College of Medicine, Qatar University, PO Box 2713, Doha, Qatar mixosn@yahoo.com lait@cf.ac.uk.
[Ti] Título:Male infertility-linked point mutation reveals a vital binding role for the C2 domain of sperm PLCζ.
[So] Source:Biochem J;474(6):1003-1016, 2017 Mar 07.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Sperm-specific phospholipase C zeta (PLCζ) is widely considered to be the physiological stimulus that evokes intracellular calcium (Ca ) oscillations that are essential for the initiation of egg activation during mammalian fertilisation. A recent genetic study reported a male infertility case that was directly associated with a point mutation in the PLCζ C2 domain, where an isoleucine residue had been substituted with a phenylalanine (I489F). Here, we have analysed the effect of this mutation on the Ca oscillation-inducing activity and the biochemical properties of human PLCζ. Microinjection of cRNA or recombinant protein corresponding to PLCζ mutant at physiological concentrations completely failed to cause Ca oscillations and trigger development. However, this infertile phenotype could be effectively rescued by microinjection of relatively high (non-physiological) amounts of recombinant mutant PLCζ protein, leading to Ca oscillations and egg activation. Our biochemical analysis suggested that the PLCζ mutant displayed similar enzymatic properties, but dramatically reduced binding to PI(3)P and PI(5)P-containing liposomes compared with wild-type PLCζ. Our findings highlight the importance of PLCζ at fertilisation and the vital role of the C2 domain in PLCζ function, possibly due to its novel binding characteristics.
[Mh] Termos MeSH primário: Domínios C2
Cálcio/metabolismo
Infertilidade Masculina/genética
Fosfoinositídeo Fosfolipase C/química
Mutação Puntual
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Animais
Sinalização do Cálcio
Bovinos
Feminino
Fertilização
Expressão Gênica
Seres Humanos
Isoleucina/química
Isoleucina/metabolismo
Lipossomos/química
Lipossomos/metabolismo
Masculino
Camundongos
Microinjeções
Oócitos/citologia
Oócitos/metabolismo
Fenilalanina/química
Fenilalanina/metabolismo
Fosfatos de Fosfatidilinositol/química
Fosfatos de Fosfatidilinositol/metabolismo
Fosfoinositídeo Fosfolipase C/genética
Fosfoinositídeo Fosfolipase C/metabolismo
Ligação Proteica
RNA Complementar/administração & dosagem
RNA Complementar/genética
RNA Complementar/metabolismo
Proteínas Recombinantes/administração & dosagem
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Espermatozoides/metabolismo
Espermatozoides/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Liposomes); 0 (Phosphatidylinositol Phosphates); 0 (RNA, Complementary); 0 (Recombinant Proteins); 04Y7590D77 (Isoleucine); 47E5O17Y3R (Phenylalanine); EC 3.1.4.11 (PLCZ1 protein, human); EC 3.1.4.11 (Phosphoinositide Phospholipase C); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170615
[Lr] Data última revisão:
170615
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170309
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20161057


  6 / 1465 MEDLINE  
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[PMID]:28122973
[Au] Autor:Nilsson BE; Te Velthuis AJ; Fodor E
[Ad] Endereço:Sir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom.
[Ti] Título:Role of the PB2 627 Domain in Influenza A Virus Polymerase Function.
[So] Source:J Virol;91(7), 2017 Apr 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The RNA genome of influenza A viruses is transcribed and replicated by the viral RNA-dependent RNA polymerase, composed of the subunits PA, PB1, and PB2. High-resolution structural data revealed that the polymerase assembles into a central polymerase core and several auxiliary highly flexible, protruding domains. The auxiliary PB2 cap-binding and the PA endonuclease domains are both involved in cap snatching, but the role of the auxiliary PB2 627 domain, implicated in host range restriction of influenza A viruses, is still poorly understood. In this study, we used structure-guided truncations of the PB2 subunit to show that a PB2 subunit lacking the 627 domain accumulates in the cell nucleus and assembles into a heterotrimeric polymerase with PB1 and PA. Furthermore, we showed that a recombinant viral polymerase lacking the PB2 627 domain is able to carry out cap snatching, cap-dependent transcription initiation, and cap-independent ApG dinucleotide extension , indicating that the PB2 627 domain of the influenza virus RNA polymerase is not involved in core catalytic functions of the polymerase. However, in a cellular context, the 627 domain is essential for both transcription and replication. In particular, we showed that the PB2 627 domain is essential for the accumulation of the cRNA replicative intermediate in infected cells. Together, these results further our understanding of the role of the PB2 627 domain in transcription and replication of the influenza virus RNA genome. Influenza A viruses are a major global health threat, not only causing disease in both humans and birds but also placing significant strains on economies worldwide. Avian influenza A virus polymerases typically do not function efficiently in mammalian hosts and require adaptive mutations to restore polymerase activity. These adaptations include mutations in the 627 domain of the PB2 subunit of the viral polymerase, but it still remains to be established how these mutations enable host adaptation on a molecular level. In this report, we characterize the role of the 627 domain in polymerase function and offer insights into the replication mechanism of influenza A viruses.
[Mh] Termos MeSH primário: Vírus da Influenza A Subtipo H1N1/enzimologia
RNA Replicase/metabolismo
Proteínas Virais/metabolismo
[Mh] Termos MeSH secundário: Animais
Núcleo Celular/enzimologia
Núcleo Celular/virologia
Embrião de Galinha
Células HEK293
Seres Humanos
Domínios Proteicos
Multimerização Proteica
Transporte Proteico
RNA Replicase/química
RNA Complementar/metabolismo
RNA Viral/biossíntese
Proteínas Virais/química
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (PB2 protein, Influenzavirus A); 0 (RNA, Complementary); 0 (RNA, Viral); 0 (Viral Proteins); EC 2.7.7.48 (RNA Replicase)
[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:170127
[St] Status:MEDLINE


  7 / 1465 MEDLINE  
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[PMID]:27936689
[Au] Autor:Mitsuoka Y; Yamamoto T; Kugimiya A; Waki R; Wada F; Tahara S; Sawamura M; Noda M; Fujimura Y; Kato Y; Hari Y; Obika S
[Ad] Endereço:Graduate School of Pharmaceutical Sciences, Osaka University , 1-6 Yamadaoka, Suita Osaka 565-0871, Japan.
[Ti] Título:Triazole- and Tetrazole-Bridged Nucleic Acids: Synthesis, Duplex Stability, Nuclease Resistance, and in Vitro and in Vivo Antisense Potency.
[So] Source:J Org Chem;82(1):12-24, 2017 01 06.
[Is] ISSN:1520-6904
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Antisense oligonucleotides are attractive therapeutic agents for several types of disease. One of the most promising modifications of antisense oligonucleotides is the introduction of bridged nucleic acids. As we report here, we designed novel bridged nucleic acids, triazole-bridged nucleic acid (TrNA), and tetrazole-bridged nucleic acid (TeNA), whose sugar conformations are restricted to N-type by heteroaromatic ring-bridged structures. We then successfully synthesized TrNA and TeNA and introduced these monomers into oligonucleotides. In UV-melting experiments, TrNA-modified oligonucleotides exhibited increased binding affinity toward complementary RNA and decreased binding affinity toward complementary DNA, although TeNA-modified oligonucleotides were decomposed under the annealing conditions. Enzymatic degradation experiments demonstrated that introduction of TrNA at the 3'-terminus rendered oligonucleotides resistant to nuclease digestion. Furthermore, we tested the silencing potencies of TrNA-modified antisense oligonucleotides using in vitro and in vivo assays. These experiments revealed that TrNA-modified antisense oligonucleotides induced potent downregulation of gene expression in liver. In addition, TrNA-modified antisense oligonucleotides showed a tendency for increased liver biodistribution. Taken together, our findings indicate that TrNA is a good candidate for practical application in antisense methodology.
[Mh] Termos MeSH primário: DNA Complementar/química
Desoxirribonucleases/química
Ácidos Nucleicos/síntese química
Oligonucleotídeos Antissenso/química
RNA Complementar/química
Tetrazóis/síntese química
[Mh] Termos MeSH secundário: Desoxirribonucleases/metabolismo
Seres Humanos
Conformação de Ácido Nucleico
Ácidos Nucleicos/química
Tetrazóis/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Complementary); 0 (Nucleic Acids); 0 (Oligonucleotides, Antisense); 0 (RNA, Complementary); 0 (Tetrazoles); 288-94-8 (1H-tetrazole); EC 3.1.- (Deoxyribonucleases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161213
[St] Status:MEDLINE
[do] DOI:10.1021/acs.joc.6b02417


  8 / 1465 MEDLINE  
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[PMID]:27978824
[Au] Autor:Schaarschuch A; Redies C; Hertel N; Molecular Anatomy and Dysfunction of Mouse Development Group
[Ad] Endereço:Institute of Anatomy I, Friedrich Schiller University School of Medicine, Jena University Hospital, 07743, Jena, Germany.
[Ti] Título:Unspecific binding of cRNA probe to plaques in two mouse models for Alzheimer's disease.
[So] Source:J Negat Results Biomed;15(1):22, 2016 Dec 16.
[Is] ISSN:1477-5751
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Alzheimer's disease (AD) is characterized by the pathological deposition of amyloid-ß (Aß) protein-containing plaques. Microglia and astrocytes are commonly attracted to the plaques by an unknown mechanism that may involve cell adhesion. One cell adhesion family of proteins, the cadherins, are widely expressed in the central nervous system. Therefore, our study was designed to map the expression of cadherins in AD mouse brains. A particular focus was on plaques because diverse mRNA-species were found in plaques and their surrounding area in brains of AD patients. METHODS: In this study, we used in situ hybridization to visualize cadherin expression in brains of two mouse models for AD (APP/PS1 and APP23). RESULTS: A variable number of plaques was detected in transgenic brain sections, depending on the probe used. Our first impression was that the cadherin probes visualized specific mRNA expression in plaques and that endogenous staining was unaffected. However, control experiments revealed unspecific binding with sense probes. Further experiments with variations in probe length, probe sequence, molecular tag and experimental procedure lead us to conclude that cRNA probes bind generally and in an unspecific manner to plaques. CONCLUSIONS: We demonstrate unspecific binding of cRNA probes to plaques in two mouse models for AD. The widespread and general staining of the plaques prevented us from studying endogenous expression of cadherins in transgenic brain by in situ hybridization.
[Mh] Termos MeSH primário: Doença de Alzheimer/metabolismo
Placa Amiloide/metabolismo
Sondas RNA/metabolismo
RNA Complementar/metabolismo
[Mh] Termos MeSH secundário: Doença de Alzheimer/genética
Animais
Caderinas/metabolismo
Modelos Animais de Doenças
Feminino
Regulação da Expressão Gênica
Hibridização In Situ
Masculino
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Placa Amiloide/genética
Coloração e Rotulagem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cadherins); 0 (RNA Probes); 0 (RNA, Complementary)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170410
[Lr] Data última revisão:
170410
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161217
[St] Status:MEDLINE


  9 / 1465 MEDLINE  
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[PMID]:27430149
[Au] Autor:Liu Z; Wang F; Yuan L; Zhang X; Ying Q; Yu L; Zhang L; Cheng L; Zhang F; Lu J; Wu X
[Ad] Endereço:Department of Microbiology, The Fourth Military Medical University, Xi'an, Shaanxi, P.R. China.
[Ti] Título:Development of a SYBR-Green â…  quantitative PCR assay for the detection and genotyping of different hantaviruses.
[So] Source:Int J Mol Med;38(3):951-60, 2016 Sep.
[Is] ISSN:1791-244X
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:Hemorrhagic fever with renal syndrome (HFRS) is a severe, viral zoonotic disease which occurs worldwide, particularly in Asia and Europe. In China, the Hantaan virus (HTNV) and the Seoul virus (SEOV) are known to be the most prevalent causative agents of HFRS. Since no protective vaccines or effective treatments are available for human use, accurate and reliable diagnostic methods are essential for disease surveillance. In the present study, the viral loads in cell culture supernatant, infected mice blood and clinical serum samples were quantified using the SYBR­Green I-based reverse transcription-quantitiative polymerase chain reaction (RT-qPCR) assay, which targeted the S gene sequence of the HTNV and SEOV genomes. The cRNA of these two viruses were synthesized as a positive control and 10-fold serially diluted from 1x105 to 1x100 copies/µl. Standard curves were generated by plotting the mean cycle threshold (Ct) values versus copy numbers. The standard curve of HTNV had a correlation coefficient (R2) of 0.994, efficiency of amplification (E) of 101.9%, and the slope of -3.278, whereas that of SEOV had an R2 of 0.993, E of 104.8%, and the slope of -3.212. The minimum detection limit of the RT-qPCR assay for HTNV and SEOV was 101 copies/µl. Two qPCR assays were successfully established for the detection of HTNV and SEOV, respectively. Taken together, these findings demonstrate that using the SYBR­Green I-based RT-qPCR assay, the HTNV and SEOV may be genotyped precisely without cross-reactivity. Furthermore, viral RNA may be detected and quantified in cells, mice and infected individuals, which may be useful in epidemiological studies as well as for early monitoring and further preventative treatment against SEOV and HTNV-induced diseases.
[Mh] Termos MeSH primário: Vírus Hantaan/genética
Febre Hemorrágica com Síndrome Renal/diagnóstico
Compostos Orgânicos/química
Reação em Cadeia da Polimerase Via Transcriptase Reversa/métodos
Vírus Seoul/genética
[Mh] Termos MeSH secundário: Animais
Dosagem de Genes
Genoma Viral/genética
Genótipo
Vírus Hantaan/fisiologia
Febre Hemorrágica com Síndrome Renal/sangue
Febre Hemorrágica com Síndrome Renal/virologia
Interações Hospedeiro-Patógeno
Seres Humanos
Camundongos
RNA Complementar/sangue
RNA Complementar/química
RNA Complementar/genética
RNA Viral/sangue
RNA Viral/química
RNA Viral/genética
Reprodutibilidade dos Testes
Sensibilidade e Especificidade
Vírus Seoul/fisiologia
Especificidade da Espécie
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Organic Chemicals); 0 (RNA, Complementary); 0 (RNA, Viral); 163795-75-3 (SYBR Green I)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170321
[Lr] Data última revisão:
170321
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160720
[St] Status:MEDLINE
[do] DOI:10.3892/ijmm.2016.2678


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[PMID]:26824455
[Au] Autor:Ahmed M; Fezai M; Uzcategui NL; Hosseinzadeh Z; Lang F
[Ad] Endereço:Department of Physiology I, University of Tx00FC;bingen, Tx00FC;bingen, Germany.
[Ti] Título:SGK3 Sensitivity of Voltage Gated K+ Channel Kv1.5 (KCNA5).
[So] Source:Cell Physiol Biochem;38(1):359-67, 2016.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The serum & glucocorticoid inducible kinase isoform SGK3 is a powerful regulator of several transporters, ion channels and the Na+/K+ ATPase. Targets of SGK3 include the ubiquitin ligase Nedd4-2, which is in turn a known regulator of the voltage gated K+ channel Kv1.5 (KCNA5). The present study thus explored whether SGK3 modifies the activity of the voltage gated K+ channel KCNA5, which participates in the regulation of diverse functions including atrial cardiac action potential, activity of vascular smooth muscle cells, insulin release and tumour cell proliferation. METHODS: cRNA encoding KCNA5 was injected into Xenopus oocytes with and without additional injection of cRNA encoding wild-type SGK3, constitutively active S419DSGK3, inactive K191NSGK3 and/or wild type Nedd4-2. Voltage gated K+ channel activity was quantified utilizing dual electrode voltage clamp. RESULTS: Voltage gated current in KCNA5 expressing Xenopus oocytes was significantly enhanced by wild-type SGK3 and S419DSGK3, but not by K191NSGK3. SGK3 was effective in the presence of ouabain (1 mM) and thus did not require Na+/K+ ATPase activity. Coexpression of Nedd4-2 decreased the voltage gated current in KCNA5 expressing Xenopus oocytes, an effect largely reversed by additional coexpression of SGK3. CONCLUSION: SGK3 is a positive regulator of KCNA5, which is at least partially effective by abrogating the effect of Nedd4-2.
[Mh] Termos MeSH primário: Canal de Potássio Kv1.5/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
[Mh] Termos MeSH secundário: Potenciais de Ação/efeitos dos fármacos
Animais
Complexos Endossomais de Distribuição Requeridos para Transporte/genética
Complexos Endossomais de Distribuição Requeridos para Transporte/metabolismo
Camundongos
Mutagênese Sítio-Dirigida
Ubiquitina-Proteína Ligases Nedd4
Oócitos/metabolismo
Ouabaína/farmacologia
Técnicas de Patch-Clamp
Proteínas Serina-Treonina Quinases/genética
RNA Complementar/metabolismo
Ubiquitina-Proteína Ligases/genética
Ubiquitina-Proteína Ligases/metabolismo
Xenopus/crescimento & desenvolvimento
Xenopus/metabolismo
Proteínas de Xenopus
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Endosomal Sorting Complexes Required for Transport); 0 (Kv1.5 Potassium Channel); 0 (RNA, Complementary); 0 (Xenopus Proteins); 5ACL011P69 (Ouabain); EC 2.3.2.26 (Nedd4 Ubiquitin Protein Ligases); EC 2.3.2.26 (Nedd4 protein, Xenopus); EC 2.3.2.26 (Nedd4l protein, mouse); EC 2.3.2.26 (nedd4l protein, Xenopus); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.1 (Sgk3 protein, mouse)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160130
[St] Status:MEDLINE
[do] DOI:10.1159/000438636



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