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[PMID]:29244187
[Au] Autor:Salinas-Giegé T; Cavaiuolo M; Cognat V; Ubrig E; Remacle C; Duchêne AM; Vallon O; Maréchal-Drouard L
[Ad] Endereço:Institut de biologie moléculaire des plantes, CNRS, Université de Strasbourg, 67084 Strasbourg, France.
[Ti] Título:Polycytidylation of mitochondrial mRNAs in Chlamydomonas reinhardtii.
[So] Source:Nucleic Acids Res;45(22):12963-12973, 2017 Dec 15.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The unicellular photosynthetic organism, Chlamydomonas reinhardtii, represents a powerful model to study mitochondrial gene expression. Here, we show that the 5'- and 3'-extremities of the eight Chlamydomonas mitochondrial mRNAs present two unusual characteristics. First, all mRNAs start primarily at the AUG initiation codon of the coding sequence which is often marked by a cluster of small RNAs. Second, unusual tails are added post-transcriptionally at the 3'-extremity of all mRNAs. The nucleotide composition of the tails is distinct from that described in any other systems and can be partitioned between A/U-rich tails, predominantly composed of Adenosine and Uridine, and C-rich tails composed mostly of Cytidine. Based on 3' RACE experiments, 22% of mRNAs present C-rich tails, some of them composed of up to 20 consecutive Cs. Polycytidylation is specific to mitochondria and occurs primarily on mRNAs. This unprecedented post-transcriptional modification seems to be a specific feature of the Chlorophyceae class of green algae and points out the existence of novel strategies in mitochondrial gene expression.
[Mh] Termos MeSH primário: Chlamydomonas reinhardtii/genética
Mitocôndrias/genética
RNA Mensageiro/genética
Transcrição Genética
[Mh] Termos MeSH secundário: Sequência de Bases
Chlamydomonas reinhardtii/metabolismo
Clorófitas/classificação
Clorófitas/genética
Genoma Mitocondrial/genética
Mitocôndrias/metabolismo
Filogenia
Poli C/metabolismo
RNA Mensageiro/metabolismo
Homologia de Sequência do Ácido Nucleico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Messenger); 0 (mitochondrial messenger RNA); 30811-80-4 (Poly C)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180115
[Lr] Data última revisão:
180115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171216
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx903


  2 / 771 MEDLINE  
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[PMID]:28137374
[Au] Autor:Careaga M; Murai T; Bauman MD
[Ad] Endereço:UC Davis MIND Institute, University of California, Davis, California; Department of Psychiatry and Behavioral Sciences, University of California, Davis, California.
[Ti] Título:Maternal Immune Activation and Autism Spectrum Disorder: From Rodents to Nonhuman and Human Primates.
[So] Source:Biol Psychiatry;81(5):391-401, 2017 Mar 01.
[Is] ISSN:1873-2402
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A subset of women who are exposed to infection during pregnancy have an increased risk of giving birth to a child who will later be diagnosed with a neurodevelopmental or neuropsychiatric disorder. Although epidemiology studies have primarily focused on the association between maternal infection and an increased risk of offspring schizophrenia, mounting evidence indicates that maternal infection may also increase the risk of autism spectrum disorder. A number of factors, including genetic susceptibility, the intensity and timing of the infection, and exposure to additional aversive postnatal events, may influence the extent to which maternal infection alters fetal brain development and which disease phenotype (autism spectrum disorder, schizophrenia, other neurodevelopmental disorders) is expressed. Preclinical animal models provide a test bed to systematically evaluate the effects of maternal infection on fetal brain development, determine the relevance to human central nervous system disorders, and to evaluate novel preventive and therapeutic strategies. Maternal immune activation models in mice, rats, and nonhuman primates suggest that the maternal immune response is the critical link between exposure to infection during pregnancy and subsequent changes in brain and behavioral development of offspring. However, differences in the type, severity, and timing of prenatal immune challenge paired with inconsistencies in behavioral phenotyping approaches have hindered the translation of preclinical results to human studies. Here we highlight the promises and limitations of the maternal immune activation model as a preclinical tool to study prenatal risk factors for autism spectrum disorder, and suggest specific changes to improve reproducibility and maximize translational potential.
[Mh] Termos MeSH primário: Transtorno do Espectro Autista/imunologia
Encéfalo/imunologia
Modelos Animais de Doenças
Complicações Infecciosas na Gravidez/imunologia
Efeitos Tardios da Exposição Pré-Natal/imunologia
[Mh] Termos MeSH secundário: Animais
Transtorno do Espectro Autista/etiologia
Encéfalo/crescimento & desenvolvimento
Feminino
Seres Humanos
Macaca mulatta
Troca Materno-Fetal
Camundongos
Poli C
Gravidez
Ratos
Fatores de Risco
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
30811-80-4 (Poly C)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170810
[Lr] Data última revisão:
170810
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170201
[St] Status:MEDLINE


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[PMID]:27002920
[Au] Autor:Huang Q; Yu W; Hu T
[Ad] Endereço:National Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences , Beijing 100190, China.
[Ti] Título:Potent Antigen-Adjuvant Delivery System by Conjugation of Mycobacterium tuberculosis Ag85B-HspX Fusion Protein with Arabinogalactan-Poly(I:C) Conjugate.
[So] Source:Bioconjug Chem;27(4):1165-74, 2016 Apr 20.
[Is] ISSN:1520-4812
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Protein-based vaccine is promising to improve or replace Mycobacterium bovis BCG vaccine for its specificity, safety, and easy production. However, protein-based vaccine calls for potent adjuvants and improved delivery systems to protect against Mycobacterium tuberculosis. Poly(I:C) is one of the most potent pathogen-associated molecular patterns that signals primarily via TLR3. Arabinogalactan (AG) is a biocompatible polysaccharide that can increase splenocyte proliferation and stimulate macrophages. The AG-poly(I:C) conjugate (AG-P) showed an adjuvant potency through a synergistic interaction of AG and poly(I:C). Ag85B and HspX are two important virulent protein antigens of Mycobacterium tuberculosis and Ag85B-HspX fusion protein (AH) was prepared. An antigen-adjuvant delivery system (AH-AG-P) was developed by conjugation of AH with AG-P to ensure that both AH and AG-P reach the APCs simultaneously. AH-AG-P elicited high AH-specific IgG titers and stimulated lymphocyte proliferation. AH-AG-P provoked the secretion of Th1-type cytokines (TNF-α, IFN-γ, and IL-2) and Th2-type cytokines (IL-4 and IL-10). Pharmacokinetics revealed that conjugation with AG-P could prolong the serum exposure of AH to the immune system. Pharmacodynamics suggested that conjugation with AG-P led to a rapid and intense production of AH-specific IgG. Accordingly, conjugation with AG-P could promote a robust cellular and humoral immune response to AH. Thus, conjugation of AH with a potent adjuvant AG-P is an effective strategy to develop an efficacious protein-based vaccine against Mycobacterium tuberculosis.
[Mh] Termos MeSH primário: Adjuvantes Imunológicos/administração & dosagem
Antígenos de Bactérias/administração & dosagem
Proteínas de Bactérias/administração & dosagem
Galactanos/química
Mycobacterium tuberculosis/imunologia
Poli C/química
Tuberculose/tratamento farmacológico
[Mh] Termos MeSH secundário: Antígenos de Bactérias/química
Proteínas de Bactérias/química
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adjuvants, Immunologic); 0 (Antigens, Bacterial); 0 (Bacterial Proteins); 0 (Galactans); 0 (HspX protein, Mycobacterium tuberculosis); 30811-80-4 (Poly C); SL4SX1O487 (arabinogalactan)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170117
[Lr] Data última revisão:
170117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160323
[St] Status:MEDLINE
[do] DOI:10.1021/acs.bioconjchem.6b00116


  4 / 771 MEDLINE  
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[PMID]:26759450
[Au] Autor:Majerfeld I; Puthenvedu D; Yarus M
[Ad] Endereço:Department of Molecular, Cellular and Developmental Biology, University of Colorado, Boulder, Colorado 80309-0347, USA.
[Ti] Título:Cross-backbone templating; ribodinucleotides made on poly(C).
[So] Source:RNA;22(3):397-407, 2016 Mar.
[Is] ISSN:1469-9001
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:G(5')pp(5')G synthesis from pG and chemically activated 2MeImpG is accelerated by the addition of complementary poly(C), but affected only slightly by poly(G) and not at all by poly(U) and poly(A). This suggests that 3'-5' poly(C) is a template for uncatalyzed synthesis of 5'-5' GppG, as was poly(U) for AppA synthesis, previously. The reaction occurs at 50 mM mono- and divalent ion concentrations, at moderate temperatures, and near pH 7. The reactive complex at the site of enhanced synthesis of 5'-5' GppG seems to contain a single pG, a single phosphate-activated nucleotide 2 MeImpG, and a single strand of poly(C). Most likely this structure is base-paired, as the poly(C)-enhanced reaction is completely disrupted between 30 and 37 °C, whereas slower, untemplated synthesis of GppG accelerates. More specifically, the reactive center acts as would be expected for short, isolated G nucleotide stacks expanded and ordered by added poly(C). For example, poly(C)-mediated GppG production is very nonlinear in overall nucleotide concentration. Uncatalyzed NppN synthesis is now known for two polymers and their complementary free nucleotides. These data suggest that varied, simple, primordial 3'-5' RNA sequences could express a specific chemical phenotype by encoding synthesis of complementary, reactive, coenzyme-like 5'-5' ribodinucleotides.
[Mh] Termos MeSH primário: Poli C/química
Ribonucleotídeos/síntese química
[Mh] Termos MeSH secundário: Cromatografia em Camada Delgada
Ribonucleotídeos/química
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ribonucleotides); 30811-80-4 (Poly C)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:160301
[Lr] Data última revisão:
160301
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160114
[St] Status:MEDLINE
[do] DOI:10.1261/rna.054866.115


  5 / 771 MEDLINE  
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[PMID]:26742581
[Au] Autor:Raveendran D; Raghavan SC
[Ad] Endereço:Department of Biochemistry, Indian Institute of Science, Bangalore, 560 012, India.
[Ti] Título:Biochemical Characterization of Nonamer Binding Domain of RAG1 Reveals its Thymine Preference with Respect to Length and Position.
[So] Source:Sci Rep;6:19091, 2016 Jan 08.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:RAG complex consisting of RAG1 and RAG2 is a site-specific endonuclease responsible for the generation of antigen receptor diversity. It cleaves recombination signal sequence (RSS), comprising of conserved heptamer and nonamer. Nonamer binding domain (NBD) of RAG1 plays a central role in the recognition of RSS. To investigate the DNA binding properties of the domain, NBD of murine RAG1 was cloned, expressed and purified. Electrophoretic mobility shift assays showed that NBD binds with high affinity to nonamer in the context of 12/23 RSS or heteroduplex DNA. NBD binding was specific to thymines when single stranded DNA containing poly A, C, G or T were used. Biolayer interferometry studies showed that poly T binding to NBD was robust and comparable to that of 12RSS. More than 23 nt was essential for NBD binding at homothymidine stretches. On a double-stranded DNA, NBD could bind to A:T stretches, but not G:C or random sequences. Although NBD is indispensable for sequence specific activity of RAGs, external supplementation of purified nonamer binding domain to NBD deleted cRAG1/cRAG2 did not restore its activity, suggesting that the overall domain architecture of RAG1 is important. Therefore, we define the sequence requirements of NBD binding to DNA.
[Mh] Termos MeSH primário: DNA de Cadeia Simples/química
Proteínas de Ligação a DNA/química
Proteínas de Homeodomínio/química
Poli T/química
Receptores de Antígenos/química
[Mh] Termos MeSH secundário: Animais
Linfócitos B/citologia
Linfócitos B/imunologia
Linfócitos B/metabolismo
Sequência de Bases
Sítios de Ligação
Clonagem Molecular
DNA de Cadeia Simples/genética
Proteínas de Ligação a DNA/genética
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Proteínas de Homeodomínio/genética
Camundongos
Poli A/química
Poli C/química
Poli G/química
Ligação Proteica
Domínios Proteicos
Sinais Direcionadores de Proteínas
Receptores de Antígenos/genética
Receptores de Antígenos/imunologia
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Linfócitos T/citologia
Linfócitos T/imunologia
Linfócitos T/metabolismo
Recombinação V(D)J
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Single-Stranded); 0 (DNA-Binding Proteins); 0 (Homeodomain Proteins); 0 (Protein Sorting Signals); 0 (Rag2 protein, mouse); 0 (Receptors, Antigen); 0 (Recombinant Proteins); 128559-51-3 (RAG-1 protein); 24937-83-5 (Poly A); 25086-81-1 (Poly T); 25191-14-4 (Poly G); 30811-80-4 (Poly C)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160109
[St] Status:MEDLINE
[do] DOI:10.1038/srep19091


  6 / 771 MEDLINE  
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[PMID]:26739349
[Au] Autor:Heijink IH; Jonker MR; de Vries M; van Oosterhout AJ; Telenga E; Ten Hacken NH; Postma DS; van den Berge M
[Ad] Endereço:Department of Pathology & Medical Biology, Experimental Pulmonology and Inflammation Research, University of Groningen, University Medical Center Groningen,, Hanzeplein 1, NL-9713 GZ, Groningen, The Netherlands. h.i.heijink@umcg.nl.
[Ti] Título:Budesonide and fluticasone propionate differentially affect the airway epithelial barrier.
[So] Source:Respir Res;17:2, 2016 Jan 06.
[Is] ISSN:1465-993X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: COPD patients have a higher risk of pneumonia when treated with fluticasone propionate (FP) than with placebo, and a lower risk with budesonide (BUD). We hypothesized that BUD and FP differentially affect the mucosal barrier in response to viral infection and/or cigarette smoke. METHODS: We assessed protective effects of equivalent concentrations of BUD and FP on cytokine production and barrier function (electrical resistance) in human bronchial epithelial 16HBE cells and primary bronchial epithelial cells (PBECs) upon exposure to viral mimetic poly-(I:C) and/or cigarette smoke extract (CSE) or epidermal growth factor (EGF). RESULTS: BUD and FP were equally effective in suppressing poly-(I:C)- and/or CSE-induced IL-8 secretion in 16HBE and PBECs. Poly-(I:C) substantially decreased electrical resistance in 16HBE cells and both BUD and FP fully counteracted this effect. However, FP hardly affected 16HBE barrier dysfunction induced by CSE with/without poly-(I:C), whereas BUD (16 nM) provided full protection, an effect likely mediated by affecting EGFR-downstream target GSK-3ß. Similarly, BUD, but not FP, significantly improved CSE-induced barrier dysfunction in PBECs. Finally, BUD, but not FP, exerted a modest but significant protective effect against Streptococcus Pneumoniae-induced barrier dysfunction, and BUD, but not FP, prevented cellular adhesion and/or internalization of these bacteria induced by poly-(I:C) in 16HBE. CONCLUSIONS: Collectively, both BUD and FP efficiently control epithelial pro-inflammatory responses and barrier function upon mimicry of viral infection. Of potential clinical relevance, BUD more effectively counteracted CSE-induced barrier dysfunction, reinforcing the epithelial barrier and potentially limiting access of pathogens upon smoking in vivo.
[Mh] Termos MeSH primário: Brônquios/imunologia
Budesonida/administração & dosagem
Células Epiteliais/imunologia
Células Epiteliais/virologia
Fluticasona/administração & dosagem
Poli C/imunologia
[Mh] Termos MeSH secundário: Brônquios/efeitos dos fármacos
Brônquios/virologia
Broncodilatadores/administração & dosagem
Linhagem Celular
Permeabilidade da Membrana Celular/efeitos dos fármacos
Permeabilidade da Membrana Celular/imunologia
Citocinas/imunologia
Relação Dose-Resposta a Droga
Células Epiteliais/efeitos dos fármacos
Seres Humanos
Rhinovirus/efeitos dos fármacos
Rhinovirus/fisiologia
Alcatrões
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bronchodilator Agents); 0 (Cytokines); 0 (Tars); 0 (tobacco tar); 30811-80-4 (Poly C); 51333-22-3 (Budesonide); CUT2W21N7U (Fluticasone)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160108
[St] Status:MEDLINE
[do] DOI:10.1186/s12931-015-0318-z


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[PMID]:26612536
[Au] Autor:Zhao XL; Chen BC; Han JC; Wei L; Pan XB
[Ad] Endereço:Peking University People's Hospital, Peking University Hepatology Institute, Beijing Key Laboratory of Hepatitis C and Immunotherapy for Liver Diseases; Beijing 100044, P.R. China.
[Ti] Título:Delivery of cell-penetrating peptide-peptide nucleic acid conjugates by assembly on an oligonucleotide scaffold.
[So] Source:Sci Rep;5:17640, 2015 Nov 27.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Delivery to intracellular target sites is still one of the main obstacles in the development of peptide nucleic acids (PNAs) as antisense-antigene therapeutics. Here, we designed a self-assembled oligonucleotide scaffold that included a central complementary region for self-assembly and lateral regions complementing the PNAs. Assembly of cell-penetrating peptide (CPP)-PNAs on the scaffold significantly promoted endocytosis of PNAs by at least 10-fold in cell cultures, particularly for scaffolds in which the central complementary region was assembled by poly(guanine) and poly(cytosine). The antisense activity of CPP-PNAs increased by assembly on the scaffold and was further enhanced after co-assembly with endosomolytic peptide (EP)-PNA. This synergistic effect was also observed following the assembly of antigene CPP-PNAs\EP-PNAs on the scaffold. However, antigene activity was only observed by targeting episomal viral DNA or transfected plasmids, but not the chromosome in the cell cultures. In conclusion, assembly on oligonucleotide scaffolds significantly enhanced the antisense-antigene activity of PNAs by promoting endocytosis and endosomal escape. This oligonucleotide scaffold provided a simple strategy for assembly of multiple functional peptide-PNA conjugates, expanding the applications of PNAs and demonstrating the potential of PNAs as antiviral therapeutics.
[Mh] Termos MeSH primário: Antivirais/metabolismo
Peptídeos Penetradores de Células/genética
Técnicas de Transferência de Genes
Oligonucleotídeos Antissenso/genética
Ácidos Nucleicos Peptídicos/genética
[Mh] Termos MeSH secundário: Antivirais/química
Sequência de Bases
Peptídeos Penetradores de Células/síntese química
Peptídeos Penetradores de Células/metabolismo
DNA Viral/genética
DNA Viral/metabolismo
Endocitose
Endossomos/metabolismo
Células HeLa
Células Hep G2
Vírus da Hepatite B/genética
Vírus da Hepatite B/metabolismo
Seres Humanos
Dados de Sequência Molecular
Oligonucleotídeos Antissenso/síntese química
Oligonucleotídeos Antissenso/metabolismo
Ácidos Nucleicos Peptídicos/síntese química
Ácidos Nucleicos Peptídicos/metabolismo
Plasmídeos/química
Plasmídeos/metabolismo
Poli C/química
Poli C/metabolismo
Poli G/química
Poli G/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (Cell-Penetrating Peptides); 0 (DNA, Viral); 0 (Oligonucleotides, Antisense); 0 (Peptide Nucleic Acids); 25191-14-4 (Poly G); 30811-80-4 (Poly C)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151128
[St] Status:MEDLINE
[do] DOI:10.1038/srep17640


  8 / 771 MEDLINE  
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[PMID]:26538384
[Au] Autor:Eidelshtein G; Kotlyar A; Hashemi M; Gurevich L
[Ad] Endereço:Department of Biochemistry and Molecular Biology, George S Wise Faculty of Life Sciences and The Center of Nanoscience and Nanotechnology, Tel Aviv University, Ramat Aviv, Tel Aviv 69978, Israel.
[Ti] Título:Aligned deposition and electrical measurements on single DNA molecules.
[So] Source:Nanotechnology;26(47):475102, 2015 Nov 27.
[Is] ISSN:1361-6528
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A reliable method of deposition of aligned individual dsDNA molecules on mica, silicon, and micro/nanofabricated circuits is presented. Complexes of biotinylated double stranded poly(dG)-poly(dC) DNA with avidin were prepared and deposited on mica and silicon surfaces in the absence of Mg(2+) ions. Due to its positive charge, the avidin attached to one end of the DNA anchors the complex to negatively charged substrates. Subsequent drying with a directional gas flow yields DNA molecules perfectly aligned on the surface. In the avidin-DNA complex only the avidin moiety is strongly and irreversibly bound to the surface, while the DNA counterpart interacts with the substrates much more weakly and can be lifted from the surface and realigned in any direction. Using this technique, avidin-DNA complexes were deposited across platinum electrodes on a silicon substrate. Electrical measurements on the deposited DNA molecules revealed linear IV-characteristics and exponential dependence on relative humidity.
[Mh] Termos MeSH primário: DNA/química
Nanotecnologia/métodos
[Mh] Termos MeSH secundário: Silicatos de Alumínio/química
Avidina/química
Fenômenos Eletromagnéticos
Umidade
Microeletrodos
Microscopia de Força Atômica
Poli C/química
Poli G/química
Silício/química
Propriedades de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Aluminum Silicates); 1405-69-2 (Avidin); 25191-14-4 (Poly G); 25609-92-1 (poly(dC)); 25656-92-2 (poly(dG)); 30811-80-4 (Poly C); 9007-49-2 (DNA); V8A1AW0880 (mica); Z4152N8IUI (Silicon)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:151114
[Lr] Data última revisão:
151114
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151106
[St] Status:MEDLINE
[do] DOI:10.1088/0957-4484/26/47/475102


  9 / 771 MEDLINE  
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[PMID]:26114210
[Au] Autor:Ayub M; Stoddart D; Bayley H
[Ad] Endereço:Department of Chemistry, University of Oxford , Oxford, OX1 3TA, United Kingdom.
[Ti] Título:Nucleobase Recognition by Truncated α-Hemolysin Pores.
[So] Source:ACS Nano;9(8):7895-903, 2015 Aug 25.
[Is] ISSN:1936-086X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The α-hemolysin (αHL) protein nanopore has been investigated previously as a base detector for the strand sequencing of DNA and RNA. Recent findings have suggested that shorter pores might provide improved base discrimination. New work has also shown that truncated-barrel mutants (TBM) of αHL form functional pores in lipid bilayers. Therefore, we tested TBM pores for the ability to recognize bases in DNA strands immobilized within them. In the case of TBMΔ6, in which the barrel is shortened by ∼16 Å, one of the three recognition sites found in the wild-type pore, R1, was almost eliminated. With further mutagenesis (Met113 → Gly), R1 was completely removed, demonstrating that TBM pores can mediate sharpened recognition. Remarkably, a second mutant of TBMΔ6 (Met113 → Phe) was able to bind the positively charged ß-cyclodextrin, am7ßCD, unusually tightly, permitting the continuous recognition of individual nucleoside monophosphates, which would be required for exonuclease sequencing mediated by nanopore base identification.
[Mh] Termos MeSH primário: Adenina/análise
Técnicas Biossensoriais
Proteínas Hemolisinas/química
Poli C/análise
Porinas/química
[Mh] Termos MeSH secundário: Adenina/química
Substituição de Aminoácidos
Sequência de Bases
Proteínas Hemolisinas/genética
Bicamadas Lipídicas/química
Modelos Moleculares
Dados de Sequência Molecular
Mycobacterium smegmatis/química
Nanoporos/ultraestrutura
Mutação Puntual
Poli C/química
Porinas/genética
Estrutura Secundária de Proteína
Estrutura Terciária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Eletricidade Estática
beta-Ciclodextrinas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Hemolysin Proteins); 0 (Lipid Bilayers); 0 (Porins); 0 (Recombinant Proteins); 0 (beta-Cyclodextrins); 0 (mspA protein, Mycobacterium smegmatis); 25609-92-1 (poly(dC)); 30811-80-4 (Poly C); JAC85A2161 (Adenine); JV039JZZ3A (betadex)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150627
[St] Status:MEDLINE
[do] DOI:10.1021/nn5060317


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[PMID]:25796198
[Au] Autor:Cheng WE; Ying Chang M; Wei JY; Chen YJ; Maa MC; Leu TH
[Ad] Endereço:Graduate Institute of Clinical Science, China Medical University, Taichung, Taiwan, ROC; Division of Pulmonary and Critical Care Medicine, Department of Internal medicine, China Medical University Hospital, Taichung, Taiwan, ROC.
[Ti] Título:Berberine reduces Toll-like receptor-mediated macrophage migration by suppression of Src enhancement.
[So] Source:Eur J Pharmacol;757:1-10, 2015 Jun 15.
[Is] ISSN:1879-0712
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Berberine is an isoquinoline with anti-inflammatory activity. We previously demonstrated that there was a loop of signal amplification between nuclear factor kappa B and Src for macrophage mobility triggered by the engagement of Toll-like receptors (TLRs). The simultaneous suppression of lipopolysaccharide (LPS)-mediated upregulation of inducible nitric oxide synthase, cyclooxygenase 2, and cell mobility in berberine-treated macrophages suggested Src might be a target of berberine. Indeed, th reduced migration, greatly suppressed Src induction in both protein and RNA transcript by berberine were observed in macrophages exposed to LPS, peptidoglycan, polyinosinic-polycytidylic acid, and CpG-oligodeoxynucleotides. In addition to Src induction, berberine also inhibited LPS-mediated Src activation in Src overexpressing macrophages and S-nitroso-N-acetylpenicillamine (a nitric oxide donor) could partly restore it. Moreover, berberine suppressed Src activity in fibronectin-stimulated macrophages and in v-Src transformed cells. These results implied that by effectively reducing Src expression and activity, berberine inhibited TLR-mediated cell motility in macrophages.
[Mh] Termos MeSH primário: Anti-Inflamatórios/farmacologia
Berberina/farmacologia
Movimento Celular/efeitos dos fármacos
Macrófagos/citologia
Macrófagos/efeitos dos fármacos
Proteínas Proto-Oncogênicas pp60(c-src)/metabolismo
Receptores Toll-Like/metabolismo
[Mh] Termos MeSH secundário: Animais
Ativação Enzimática/efeitos dos fármacos
Indução Enzimática/efeitos dos fármacos
Regulação Enzimológica da Expressão Gênica/efeitos dos fármacos
Lipopolissacarídeos/farmacologia
Macrófagos/metabolismo
Camundongos
Oligodesoxirribonucleotídeos/farmacologia
Peptidoglicano/farmacologia
Poli C/farmacologia
Proteínas Proto-Oncogênicas pp60(c-src)/biossíntese
Proteínas Proto-Oncogênicas pp60(c-src)/genética
Células RAW 264.7
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents); 0 (Lipopolysaccharides); 0 (Oligodeoxyribonucleotides); 0 (Peptidoglycan); 0 (Toll-Like Receptors); 0I8Y3P32UF (Berberine); 30811-80-4 (Poly C); EC 2.7.10.2 (Proto-Oncogene Proteins pp60(c-src))
[Em] Mês de entrada:1602
[Cu] Atualização por classe:150429
[Lr] Data última revisão:
150429
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150323
[St] Status:MEDLINE



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