Base de dados : MEDLINE
Pesquisa : E05.601 [Categoria DeCS]
Referências encontradas : 3371 [refinar]
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  1 / 3371 MEDLINE  
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[PMID]:29378185
[Au] Autor:Cook A; Hari-Gupta Y; Toseland CP
[Ad] Endereço:School of Biosciences, University of Kent, Canterbury, CT2 7NJ, UK.
[Ti] Título:Application of the SSB biosensor to study in vitro transcription.
[So] Source:Biochem Biophys Res Commun;496(3):820-825, 2018 02 12.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Gene expression, catalysed by RNA polymerases (RNAP), is one of the most fundamental processes in living cells. The majority of methods to quantify mRNA are based upon purification of the nucleic acid which leads to experimental inaccuracies and loss of product, or use of high cost dyes and sensitive spectrophotometers. Here, we describe the use of a fluorescent biosensor based upon the single stranded binding (SSB) protein. In this study, the SSB biosensor showed similar binding properties to mRNA, to that of its native substrate, single-stranded DNA (ssDNA). We found the biosensor to be reproducible with no associated loss of product through purification, or the requirement for expensive dyes. Therefore, we propose that the SSB biosensor is a useful tool for comparative measurement of mRNA yield following in vitro transcription.
[Mh] Termos MeSH primário: Técnicas Biossensoriais/métodos
Proteínas de Ligação a DNA/metabolismo
Corantes Fluorescentes/metabolismo
Técnicas de Sonda Molecular
RNA Mensageiro/metabolismo
Espectrometria de Fluorescência/métodos
Transcrição Genética/fisiologia
[Mh] Termos MeSH secundário: Escherichia coli/metabolismo
Sondas Moleculares/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (Fluorescent Dyes); 0 (Molecular Probes); 0 (RNA, Messenger)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180130
[St] Status:MEDLINE


  2 / 3371 MEDLINE  
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[PMID]:29366791
[Au] Autor:Ganareal TACS; Balbin MM; Monserate JJ; Salazar JR; Mingala CN
[Ad] Endereço:Department of Chemistry, College of Arts and Sciences, Central Luzon State University, Science City of Muñoz 3120, Nueva Ecija, Philippines.
[Ti] Título:Gold nanoparticle-based probes for the colorimetric detection of Mycobacterium avium subspecies paratuberculosis DNA.
[So] Source:Biochem Biophys Res Commun;496(3):988-997, 2018 02 12.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Gold nanoparticle (AuNP) is considered to be the most stable metal nanoparticle having the ability to be functionalized with biomolecules. Recently, AuNP-based DNA detection methods captured the interest of researchers worldwide. Paratuberculosis or Johne's disease, a chronic gastroenteritis in ruminants caused by Mycobacterium avium subsp. paratuberculosis (MAP), was found to have negative effect in the livestock industry. In this study, AuNP-based probes were evaluated for the specific and sensitive detection of MAP DNA. AuNP-based probe was produced by functionalization of AuNPs with thiol-modified oligonucleotide and was confirmed by Fourier-Transform Infrared (FTIR) spectroscopy. UV-Vis spectroscopy and Scanning Electron Microscopy (SEM) were used to characterize AuNPs. DNA detection was done by hybridization of 10 µL of DNA with 5 µL of probe at 63 °C for 10 min and addition of 3 µL salt solution. The method was specific to MAP with detection limit of 103 ng. UV-Vis and SEM showed dispersion and aggregation of the AuNPs for the positive and negative results, respectively, with no observed particle growth. This study therefore reports an AuNP-based probes which can be used for the specific and sensitive detection of MAP DNA.
[Mh] Termos MeSH primário: Colorimetria/métodos
DNA/genética
DNA/isolamento & purificação
Ouro/química
Nanopartículas Metálicas/química
Mycobacterium avium/genética
Mycobacterium avium/isolamento & purificação
[Mh] Termos MeSH secundário: Técnicas Biossensoriais/métodos
Hibridização In Situ/métodos
Técnicas de Sonda Molecular
Sondas Moleculares/química
Reprodutibilidade dos Testes
Sensibilidade e Especificidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Molecular Probes); 7440-57-5 (Gold); 9007-49-2 (DNA)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180126
[St] Status:MEDLINE


  3 / 3371 MEDLINE  
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[PMID]:29305261
[Au] Autor:Magni C; Sessa F; Capraro J; Duranti M; Maffioli E; Scarafoni A
[Ad] Endereço:Department of Food, Environmental and Nutritional Sciences (DeFENS), Università degli Studi di Milano, Via G. Celoria, 2, 20133, Milan, Italy.
[Ti] Título:Structural and functional insights into the basic globulin 7S of soybean seeds by using trypsin as a molecular probe.
[So] Source:Biochem Biophys Res Commun;496(1):89-94, 2018 01 29.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The basic 7S globulin (Bg7S) is one of the major globulins of soybean seeds. Despite its dual subunit composition and oligomeric assembly, Bg7S has a compact 3D structure (PDB: 3AUP) which is stabilized by a network of inter- and intra-chain disulphide bridges. Bg7S shares several structural elements with a number of homologous proteins from other seeds, whose function is still uncertain. In this work, Bg7S native conformation was probed by using the proteolytic enzyme trypsin. In spite of the presence of many arginine and lysine residues, the protein resulted extremely recalcitrant to in vitro enzymatic cleavage. Indeed, only two scissile bonds located near the C- and N-termini of the large and small subunits, respectively, were cleaved. The partially cleaved products were stable even at prolonged incubation times. Although the generated small peptide fragments were not covalently bound to the remnant of the main chains, they were held in place, as assessed by denaturing and non-denaturing chromatographic approaches. Moreover, both the already observed pH-dependent association/dissociation behaviour of the protein and its insulin binding capacity were preserved both at neutral and acidic pH values. These results are in line with the growing view that the degradation of seed proteins, either storage and non-storage, may be a controlled process related to specific functionalities.
[Mh] Termos MeSH primário: Globulinas/química
Técnicas de Sonda Molecular
Sementes/química
Proteínas de Soja/química
Feijão de Soja/química
Tripsina/química
[Mh] Termos MeSH secundário: Sítios de Ligação
Modelos Químicos
Modelos Moleculares
Sondas Moleculares/química
Ligação Proteica
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Globulins); 0 (Molecular Probes); 0 (Soybean Proteins); EC 3.4.21.4 (Trypsin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180107
[St] Status:MEDLINE


  4 / 3371 MEDLINE  
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[PMID]:29198700
[Au] Autor:Citak F; Ghai I; Rosenkötter F; Benier L; Winterhalter M; Wagner R
[Ad] Endereço:Department of Life Sciences and Chemistry, key, 28719 Bremen, Germany.
[Ti] Título:Probing transport of fosfomycin through substrate specific OprO and OprP from Pseudomonas aeruginosa.
[So] Source:Biochem Biophys Res Commun;495(1):1454-1460, 2018 01 01.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Increasing antimicrobial drug resistance is a global threat especially with respect to Gram-negative bacteria. The low permeability of the bacterial outer cell wall has been identified as an important bottleneck that prevents a sufficient antibacterial effect to be achieved at low doses of the antibiotics. In particular, the outer membrane permeability for negatively charged molecules of the clinical important ESKAPE bacterium Pseudomonas aeruginosa is determined by the low conductance porins OprO and OprP Here we show that the alternative phosphonic-acid antibiotic fosfomycin is highly permeable through the OprO and OprP channels. For this, we applied an electrophysiological zero-current assay using concentration gradients of fosfomycin under tri-ionic conditions to quantify flux of fosfomycin through OprO and OprP. Our analyzes show that OprO, and to a lesser degree OprP, have unexpected very high permeability to fosfomycin, so the antibiotic should be a potentially excellent alternative choice for the control of Pseudomonas aeruginosa infections.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Permeabilidade da Membrana Celular/fisiologia
Fosfomicina/farmacocinética
Porinas/metabolismo
Pseudomonas aeruginosa/metabolismo
[Mh] Termos MeSH secundário: Análise do Fluxo Metabólico/métodos
Técnicas de Sonda Molecular
Especificidade por Substrato/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (OprO protein, Pseudomonas aeruginosa); 0 (Porins); 0 (oprP protein, Pseudomonas aeruginosa); 2N81MY12TE (Fosfomycin)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180105
[Lr] Data última revisão:
180105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE


  5 / 3371 MEDLINE  
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[PMID]:29180013
[Au] Autor:Kwon KK; Yeom SJ; Lee DH; Jeong KJ; Lee SG
[Ad] Endereço:Synthetic Biology and Bioengineering Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon 34141, Republic of Korea; Department of Chemical and Biomolecular Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, 34141, Republic of Korea
[Ti] Título:Development of a novel cellulase biosensor that detects crystalline cellulose hydrolysis using a transcriptional regulator.
[So] Source:Biochem Biophys Res Commun;495(1):1328-1334, 2018 01 01.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Successful utilization of cellulose as renewable biomass depends on the development of economically feasible technologies, which can aid in enzymatic hydrolysis. In this study, we developed a whole-cell biosensor for detecting cellulolytic activity that relies on the recognition of cellobiose using the transcriptional factor CelR from Thermobifida fusca and transcriptional activation of its downstream gfp reporter gene. The fluorescence intensity of whole-cell biosensor, which was named as cellobiose-detectible genetic enzyme screening system (CBGESS), was directly proportional to the concentration of cellobiose. The strong fluorescence intensity of CBGESS demonstrated the ability to detect cellulolytic activity with two cellulosic substrates, carboxymethyl cellulose and p-nitrophenyl ß-D-cellobioside in cellulase-expressing Escherichia coli. In addition, CBGESS easily sensed crystalline cellulolytic activity when commercial Celluclast 1.5L was dropped on an Avicel plate. Therefore, CBGESS is a powerful tool for detecting cellulolytic activity with high sensitivity in the presence of soluble or insoluble cellulosic substrates. CBGESS may be further applied to excavate novel cellulases or microbes from both genetic libraries and various environments.
[Mh] Termos MeSH primário: Bioensaio/métodos
Técnicas Biossensoriais/métodos
Celulase/metabolismo
Celulose/metabolismo
Escherichia coli/metabolismo
Espectrometria de Fluorescência/métodos
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Celulose/análise
Cristalização
Hidrólise
Técnicas de Sonda Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Transcription Factors); 9004-34-6 (Cellulose); EC 3.2.1.4 (Cellulase)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180105
[Lr] Data última revisão:
180105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171129
[St] Status:MEDLINE


  6 / 3371 MEDLINE  
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[PMID]:28842412
[Au] Autor:Bayguinov PO; Ma Y; Gao Y; Zhao X; Jackson MB
[Ad] Endereço:Department of Neuroscience.
[Ti] Título:Imaging Voltage in Genetically Defined Neuronal Subpopulations with a Cre Recombinase-Targeted Hybrid Voltage Sensor.
[So] Source:J Neurosci;37(38):9305-9319, 2017 Sep 20.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Genetically encoded voltage indicators create an opportunity to monitor electrical activity in defined sets of neurons as they participate in the complex patterns of coordinated electrical activity that underlie nervous system function. Taking full advantage of genetically encoded voltage indicators requires a generalized strategy for targeting the probe to genetically defined populations of cells. To this end, we have generated a mouse line with an optimized hybrid voltage sensor (hVOS) probe within a locus designed for efficient Cre recombinase-dependent expression. Crossing this mouse with Cre drivers generated double transgenics expressing hVOS probe in GABAergic, parvalbumin, and calretinin interneurons, as well as hilar mossy cells, new adult-born neurons, and recently active neurons. In each case, imaging in brain slices from male or female animals revealed electrically evoked optical signals from multiple individual neurons in single trials. These imaging experiments revealed action potentials, dynamic aspects of dendritic integration, and trial-to-trial fluctuations in response latency. The rapid time response of hVOS imaging revealed action potentials with high temporal fidelity, and enabled accurate measurements of spike half-widths characteristic of each cell type. Simultaneous recording of rapid voltage changes in multiple neurons with a common genetic signature offers a powerful approach to the study of neural circuit function and the investigation of how neural networks encode, process, and store information. Genetically encoded voltage indicators hold great promise in the study of neural circuitry, but realizing their full potential depends on targeting the sensor to distinct cell types. Here we present a new mouse line that expresses a hybrid optical voltage sensor under the control of Cre recombinase. Crossing this line with Cre drivers generated double-transgenic mice, which express this sensor in targeted cell types. In brain slices from these animals, single-trial hybrid optical voltage sensor recordings revealed voltage changes with submillisecond resolution in multiple neurons simultaneously. This imaging tool will allow for the study of the emergent properties of neural circuits and permit experimental tests of the roles of specific types of neurons in complex circuit activity.
[Mh] Termos MeSH primário: Integrases/genética
Rede Nervosa/citologia
Neurônios/citologia
Neurônios/fisiologia
Optogenética/métodos
Imagens com Corantes Sensíveis à Voltagem/métodos
[Mh] Termos MeSH secundário: Animais
Feminino
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Técnicas de Sonda Molecular
Rede Nervosa/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.7.7.- (Cre recombinase); EC 2.7.7.- (Integrases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171008
[Lr] Data última revisão:
171008
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170827
[St] Status:MEDLINE
[do] DOI:10.1523/JNEUROSCI.1363-17.2017


  7 / 3371 MEDLINE  
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[PMID]:28832998
[Au] Autor:Noda N; Awais R; Sutton R; Awais M; Ozawa T
[Ad] Endereço:Department of Chemistry, School of Science, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
[Ti] Título:Dynamic monitoring of p53 translocation to mitochondria for the analysis of specific inhibitors using luciferase-fragment complementation.
[So] Source:Biotechnol Bioeng;114(12):2818-2827, 2017 Dec.
[Is] ISSN:1097-0290
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Intracellular protein translocation plays a pivotal role in regulating complex biological processes, including cell death. The tumor suppressor p53 is a transcription factor activated by DNA damage and oxidative stress that also translocates from the cytosol into the mitochondrial matrix to facilitate necrotic cell death. However, specific inhibitors of p53 mitochondrial translocation are largely unknown. To explore the inhibitors of p53, we developed a bioluminescent probe to monitor p53 translocation from cytosol to mitochondria using luciferase fragment complementation assays. The probe is composed of a novel pair of luciferase fragments, the N-terminus of green click beetle luciferase CBG68 (CBGN) and multiple-complement luciferase fragment (McLuc1). The combination of luciferase fragments showed significant luminescence intensity and high signal-to-background ratio. When the p53 connected with McLuc1 translocates from cytosol into mitochondrial matrix, CBGN in mitochondrial matrix enables to complement with McLuc1, resulting in the restoration of the luminescence. The luminescence intensity was significantly increased under hydrogen peroxide-induced oxidative stress following the complementation of CBGN and McLuc1. Pifithrin-µ, a selective inhibitor of p53 mitochondrial translocation, prevented the mitochondrial translocation of the p53 probe in a concentration-dependent manner. Furthermore, the high luminescence intensity made it easier to visualize the p53 translocation at a single cell level under a bioluminescence microscope. This p53 mitochondrial translocation assay is a new tool for high-throughput screening to identify novel p53 inhibitors, which could be developed as drugs to treat diseases in which necrotic cell death is a major contributor.
[Mh] Termos MeSH primário: Luciferases
Microscopia de Fluorescência/métodos
Mitocôndrias/metabolismo
Imagem Molecular/métodos
Técnicas de Sonda Molecular
Proteína Supressora de Tumor p53/metabolismo
[Mh] Termos MeSH secundário: Células HEK293
Seres Humanos
Mitocôndrias/ultraestrutura
Transporte Proteico/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (TP53 protein, human); 0 (Tumor Suppressor Protein p53); EC 1.13.12.- (Luciferases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170824
[St] Status:MEDLINE
[do] DOI:10.1002/bit.26407


  8 / 3371 MEDLINE  
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[PMID]:28737741
[Au] Autor:Rose JC; Stephany JJ; Valente WJ; Trevillian BM; Dang HV; Bielas JH; Maly DJ; Fowler DM
[Ad] Endereço:Department of Chemistry, University of Washington, Seattle, Washington, USA.
[Ti] Título:Rapidly inducible Cas9 and DSB-ddPCR to probe editing kinetics.
[So] Source:Nat Methods;14(9):891-896, 2017 Sep.
[Is] ISSN:1548-7105
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We developed a chemically inducible Cas9 (ciCas9) and a droplet digital PCR assay for double-strand breaks (DSB-ddPCR) to investigate the kinetics of Cas9-mediated generation and repair of DSBs in cells. ciCas9 is a rapidly activated, single-component Cas9 variant engineered by replacing the protein's REC2 domain with the BCL-xL protein and fusing an interacting BH3 peptide to the C terminus. ciCas9 can be tunably activated by a compound that disrupts the BCL-xL-BH3 interaction within minutes. DSB-ddPCR demonstrates time-resolved, highly quantitative, and targeted measurement of DSBs. Combining these tools facilitated an unprecedented exploration of the kinetics of Cas9-mediated DNA cleavage and repair. We find that sgRNAs targeting different sites generally induce cleavage within minutes and repair within 1 or 2 h. However, we observe distinct kinetic profiles, even for proximal sites, and this suggests that target sequence and chromatin state modulate cleavage and repair kinetics.
[Mh] Termos MeSH primário: Caspase 9/genética
Quebras de DNA de Cadeia Dupla
Sondas de DNA/genética
Edição de Genes/métodos
Técnicas de Sonda Molecular
Reação em Cadeia da Polimerase/métodos
[Mh] Termos MeSH secundário: Cinética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA Probes); EC 3.4.22.- (Caspase 9)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170725
[St] Status:MEDLINE
[do] DOI:10.1038/nmeth.4368


  9 / 3371 MEDLINE  
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[PMID]:28543037
[Au] Autor:Xiu Y; Jang S; Jones JA; Zill NA; Linhardt RJ; Yuan Q; Jung GY; Koffas MAG
[Ad] Endereço:State Key Laboratory of Chemical Resource Engineering, Beijing University of Chemical Technology, Beijing, China.
[Ti] Título:Naringenin-responsive riboswitch-based fluorescent biosensor module for Escherichia coli co-cultures.
[So] Source:Biotechnol Bioeng;114(10):2235-2244, 2017 Oct.
[Is] ISSN:1097-0290
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The ability to design and construct combinatorial synthetic metabolic pathways has far exceeded our capacity for efficient screening and selection of the resulting microbial strains. The need for high-throughput rapid screening techniques is of upmost importance for the future of synthetic biology and metabolic engineering. Here we describe the development of an RNA riboswitch-based biosensor module with dual fluorescent reporters, and demonstrate a high-throughput flow cytometry-based screening method for identification of naringenin over producing Escherichia coli strains in co-culture. Our efforts helped identify a number of key operating parameters that affect biosensor performance, including the selection of promoter and linker elements within the sensor-actuator domain, and the effect of host strain, fermentation time, and growth medium on sensor dynamic range. The resulting biosensor demonstrates a high correlation between specific fluorescence of the biosensor strain and naringenin titer produced by the second member of the synthetic co-culture system. This technique represents a novel application for synthetic microbial co-cultures and can be expanded from naringenin to any metabolite if a suitable riboswitch is identified. The co-culture technique presented here can be applied to a variety of target metabolites in combination with the SELEX approach for aptamer design. Due to the compartmentalization of the two genetic constructs responsible for production and detection into separate cells and application as independent modules of a synthetic microbial co-culture we have subsequently reduced the need for re-optimization of the producer module when the biosensor is replaced or removed. Biotechnol. Bioeng. 2017;114: 2235-2244. © 2017 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Técnicas Biossensoriais/métodos
Avaliação Pré-Clínica de Medicamentos/métodos
Escherichia coli/efeitos dos fármacos
Escherichia coli/genética
Flavanonas/farmacologia
Riboswitch/genética
Espectrometria de Fluorescência/métodos
[Mh] Termos MeSH secundário: Técnicas de Cocultura/métodos
Engenharia Metabólica/métodos
Técnicas de Sonda Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Flavanones); 0 (Riboswitch); HN5425SBF2 (naringenin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170526
[St] Status:MEDLINE
[do] DOI:10.1002/bit.26340


  10 / 3371 MEDLINE  
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[PMID]:28321489
[Au] Autor:Zhang LF; Jiang S; Liu MF
[Ad] Endereço:Center for RNA Research, State Key Laboratory of Molecular Biology, University of Chinese Academy of Sciences, CAS Center for Excellence in Molecular Cell Science, Shanghai, China.
[Ti] Título:MicroRNA regulation and analytical methods in cancer cell metabolism.
[So] Source:Cell Mol Life Sci;74(16):2929-2941, 2017 Aug.
[Is] ISSN:1420-9071
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The reprogramming of glucose metabolism from oxidative to glycolytic metabolism, known as the Warburg effect, is an anomalous characteristic of cancer cell metabolism. Recent studies have revealed a subset of microRNAs (miRNAs) that play critical roles in regulating the reprogramming of glucose metabolism in cancer cells. These miRNAs regulate cellular glucose metabolism by directly targeting multiple metabolic genes, including those encoding key glycolytic enzymes. In the first part of this review, we summarized the recent knowledge of miRNA regulation in the reprogramming of glucose metabolism in cancer cells and discussed the potential utilization of the key miRNA regulators as metabolic targets for developing new antitumor agents. Then, we summarized recent advances in methods and techniques for studying miRNA regulation in cancer cell metabolism.
[Mh] Termos MeSH primário: Regulação Neoplásica da Expressão Gênica
Glucose/metabolismo
MicroRNAs/metabolismo
Neoplasias/metabolismo
[Mh] Termos MeSH secundário: Animais
Glucose/genética
Proteínas Facilitadoras de Transporte de Glucose/genética
Proteínas Facilitadoras de Transporte de Glucose/metabolismo
Glicólise
Hexoquinase/genética
Hexoquinase/metabolismo
Seres Humanos
L-Lactato Desidrogenase/genética
L-Lactato Desidrogenase/metabolismo
Espectroscopia de Ressonância Magnética/métodos
Espectrometria de Massas/métodos
MicroRNAs/genética
Técnicas de Sonda Molecular
Neoplasias/genética
Proteínas Serina-Treonina Quinases/genética
Proteínas Serina-Treonina Quinases/metabolismo
Piruvato Quinase/genética
Piruvato Quinase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Glucose Transport Proteins, Facilitative); 0 (MicroRNAs); EC 1.1.1.27 (L-Lactate Dehydrogenase); EC 2.7.1.1 (Hexokinase); EC 2.7.1.40 (Pyruvate Kinase); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.2 (pyruvate dehydrogenase (acetyl-transferring) kinase); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170822
[Lr] Data última revisão:
170822
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170322
[St] Status:MEDLINE
[do] DOI:10.1007/s00018-017-2508-y



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