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  1 / 1032 MEDLINE  
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[PMID]:28458037
[Au] Autor:Okesli A; Khosla C; Bassik MC
[Ad] Endereço:Departments of Chemistry, Genetics, and Chemical Engineering, and Stanford ChEM-H, Stanford University, Stanford, CA 94305, United States.
[Ti] Título:Human pyrimidine nucleotide biosynthesis as a target for antiviral chemotherapy.
[So] Source:Curr Opin Biotechnol;48:127-134, 2017 Dec.
[Is] ISSN:1879-0429
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The development of broad-spectrum, host-acting antiviral therapies remains an important but elusive goal in anti-infective drug discovery. To replicate efficiently, viruses not only depend on their hosts for an adequate supply of pyrimidine nucleotides, but also up-regulate pyrimidine nucleotide biosynthesis in infected cells. In this review, we outline our understanding of mammalian de novo and salvage metabolic pathways for pyrimidine nucleotide biosynthesis. The available spectrum of experimental and FDA-approved drugs that modulate individual steps in these metabolic pathways is also summarized. The logic of a host-acting combination antiviral therapy comprised of inhibitors of dihydroorotate dehydrogenase and uridine/cytidine kinase is discussed.
[Mh] Termos MeSH primário: Antivirais/uso terapêutico
Inibidores Enzimáticos/uso terapêutico
Oxirredutases atuantes sobre Doadores de Grupo CH-CH/antagonistas & inibidores
Nucleotídeos de Pirimidina/biossíntese
Vírus/efeitos dos fármacos
[Mh] Termos MeSH secundário: Seres Humanos
Vírus/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (Enzyme Inhibitors); 0 (Pyrimidine Nucleotides); EC 1.3.- (Oxidoreductases Acting on CH-CH Group Donors); EC 1.3.5.2 (dihydroorotate dehydrogenase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE


  2 / 1032 MEDLINE  
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[PMID]:28180308
[Au] Autor:Robert-Paganin J; Halladjian M; Blaud M; Lebaron S; Delbos L; Chardon F; Capeyrou R; Humbert O; Henry Y; Henras AK; Réty S; Leulliot N
[Ad] Endereço:Laboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Sorbonne Paris Cité, Faculté de Pharmacie, Paris, France.
[Ti] Título:Functional link between DEAH/RHA helicase Prp43 activation and ATP base binding.
[So] Source:Nucleic Acids Res;45(3):1539-1552, 2017 02 17.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The DEAH box helicase Prp43 is a bifunctional enzyme from the DEAH/RHA helicase family required both for the maturation of ribosomes and for lariat intron release during splicing. It interacts with G-patch domain containing proteins which activate the enzymatic activity of Prp43 in vitro by an unknown mechanism. In this work, we show that the activation by G-patch domains is linked to the unique nucleotide binding mode of this helicase family. The base of the ATP molecule is stacked between two residues, R159 of the RecA1 domain (R-motif) and F357 of the RecA2 domain (F-motif). Using Prp43 F357A mutants or pyrimidine nucleotides, we show that the lack of stacking of the nucleotide base to the F-motif decouples the NTPase and helicase activities of Prp43. In contrast the R159A mutant (R-motif) showed reduced ATPase and helicase activities. We show that the Prp43 R-motif mutant induces the same phenotype as the absence of the G-patch protein Gno1, strongly suggesting that the processing defects observed in the absence of Gno1 result from a failure to activate the Prp43 helicase. Overall we propose that the stacking between the R- and F-motifs and the nucleotide base is important for the activity and regulation of this helicase family.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/metabolismo
RNA Helicases DEAD-box/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/química
Substituição de Aminoácidos
Domínio Catalítico/genética
Cristalografia por Raios X
RNA Helicases DEAD-box/química
RNA Helicases DEAD-box/genética
Ativação Enzimática
Cinética
Modelos Moleculares
Mutagênese Sítio-Dirigida
Domínios e Motivos de Interação entre Proteínas
Nucleotídeos de Pirimidina/química
Nucleotídeos de Pirimidina/metabolismo
Proteínas de Ligação a RNA/química
Proteínas de Ligação a RNA/genética
Proteínas de Ligação a RNA/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gno1 protein, S cerevisiae); 0 (PFA1 protein, S cerevisiae); 0 (Pyrimidine Nucleotides); 0 (RNA-Binding Proteins); 0 (Recombinant Proteins); 0 (Saccharomyces cerevisiae Proteins); 8L70Q75FXE (Adenosine Triphosphate); EC 3.6.1.- (PRP43 protein, S cerevisiae); EC 3.6.4.13 (DEAD-box RNA Helicases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170210
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkw1233


  3 / 1032 MEDLINE  
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[PMID]:27906631
[Au] Autor:Wang L
[Ad] Endereço:a Department of Anatomy, Physiology and Biochemistry , Swedish University of Agricultural Sciences , Uppsala , Sweden.
[Ti] Título:Mitochondrial purine and pyrimidine metabolism and beyond.
[So] Source:Nucleosides Nucleotides Nucleic Acids;35(10-12):578-594, 2016 Dec.
[Is] ISSN:1532-2335
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Carefully balanced deoxynucleoside triphosphate (dNTP) pools are essential for both nuclear and mitochondrial genome replication and repair. Two synthetic pathways operate in cells to produce dNTPs, e.g., the de novo and the salvage pathways. The key regulatory enzymes for de novo synthesis are ribonucleotide reductase (RNR) and thymidylate synthase (TS), and this process is considered to be cytosolic. The salvage pathway operates both in the cytosol (TK1 and dCK) and the mitochondria (TK2 and dGK). Mitochondrial dNTP pools are separated from the cytosolic ones owing to the double membrane structure of the mitochondria, and are formed by the salvage enzymes TK2 and dGK together with NMPKs and NDPK in postmitotic tissues, while in proliferating cells the mitochondrial dNTPs are mainly imported from the cytosol produced by the cytosolic pathways. Imbalanced mitochondrial dNTP pools lead to mtDNA depletion and/or deletions resulting in serious mitochondrial diseases. The mtDNA depletion syndrome is caused by deficiencies not only in enzymes in dNTP synthesis (TK2, dGK, p53R2, and TP) and mtDNA replication (mtDNA polymerase and twinkle helicase), but also in enzymes in other metabolic pathways such as SUCLA2 and SUCLG1, ABAT and MPV17. Basic questions are why defects in these enzymes affect dNTP synthesis and how important is mitochondrial nucleotide synthesis in the whole cell/organism perspective? This review will focus on recent studies on purine and pyrimidine metabolism, which have revealed several important links that connect mitochondrial nucleotide metabolism with amino acids, glucose, and fatty acid metabolism.
[Mh] Termos MeSH primário: Nucleotídeos de Purina/biossíntese
Erros Inatos do Metabolismo da Purina-Pirimidina/metabolismo
Nucleotídeos de Pirimidina/biossíntese
[Mh] Termos MeSH secundário: Animais
Vias Biossintéticas
Replicação do DNA
DNA Mitocondrial/biossíntese
DNA Mitocondrial/genética
Seres Humanos
Mitocôndrias/metabolismo
Estresse Oxidativo
Erros Inatos do Metabolismo da Purina-Pirimidina/tratamento farmacológico
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (DNA, Mitochondrial); 0 (Purine Nucleotides); 0 (Pyrimidine Nucleotides)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170317
[Lr] Data última revisão:
170317
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161202
[St] Status:MEDLINE


  4 / 1032 MEDLINE  
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[PMID]:26921316
[Au] Autor:Patel D; Menon D; Bernfeld E; Mroz V; Kalan S; Loayza D; Foster DA
[Ad] Endereço:From the Department of Biological Sciences, Hunter College of the City University of New York, New York, New York 10065, Biochemistry Program and.
[Ti] Título:Aspartate Rescues S-phase Arrest Caused by Suppression of Glutamine Utilization in KRas-driven Cancer Cells.
[So] Source:J Biol Chem;291(17):9322-9, 2016 Apr 22.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:During G1-phase of the cell cycle, normal cells respond first to growth factors that indicate that it is appropriate to divide and then later in G1 to the presence of nutrients that indicate sufficient raw material to generate two daughter cells. Dividing cells rely on the "conditionally essential" amino acid glutamine (Q) as an anaplerotic carbon source for TCA cycle intermediates and as a nitrogen source for nucleotide biosynthesis. We previously reported that while non-transformed cells arrest in the latter portion of G1 upon Q deprivation, mutant KRas-driven cancer cells bypass the G1 checkpoint, and instead, arrest in S-phase. In this study, we report that the arrest of KRas-driven cancer cells in S-phase upon Q deprivation is due to the lack of deoxynucleotides needed for DNA synthesis. The lack of deoxynucleotides causes replicative stress leading to activation of the ataxia telangiectasia and Rad3-related protein (ATR)-mediated DNA damage pathway, which arrests cells in S-phase. The key metabolite generated from Q utilization was aspartate, which is generated from a transaminase reaction whereby Q-derived glutamate is converted to α-ketoglutarate with the concomitant conversion of oxaloacetate to aspartate. Aspartate is a critical metabolite for both purine and pyrimidine nucleotide biosynthesis. This study identifies the molecular basis for the S-phase arrest caused by Q deprivation in KRas-driven cancer cells that arrest in S-phase in response to Q deprivation. Given that arresting cells in S-phase sensitizes cells to apoptotic insult, this study suggests novel therapeutic approaches to KRas-driven cancers.
[Mh] Termos MeSH primário: Ácido Aspártico/metabolismo
Ciclo do Ácido Cítrico
Ácido Glutâmico/metabolismo
Proteínas Proto-Oncogênicas p21(ras)/metabolismo
Pontos de Checagem da Fase S do Ciclo Celular
[Mh] Termos MeSH secundário: Ácido Aspártico/genética
Proteínas Mutadas de Ataxia Telangiectasia/genética
Proteínas Mutadas de Ataxia Telangiectasia/metabolismo
Pontos de Checagem da Fase G1 do Ciclo Celular/genética
Ácido Glutâmico/genética
Seres Humanos
Células MCF-7
Proteínas Proto-Oncogênicas p21(ras)/genética
Nucleotídeos de Purina/biossíntese
Nucleotídeos de Purina/genética
Nucleotídeos de Pirimidina/biossíntese
Nucleotídeos de Pirimidina/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (KRAS protein, human); 0 (Purine Nucleotides); 0 (Pyrimidine Nucleotides); 30KYC7MIAI (Aspartic Acid); 3KX376GY7L (Glutamic Acid); EC 2.7.11.1 (ATR protein, human); EC 2.7.11.1 (Ataxia Telangiectasia Mutated Proteins); EC 3.6.5.2 (Proto-Oncogene Proteins p21(ras))
[Em] Mês de entrada:1611
[Cu] Atualização por classe:170422
[Lr] Data última revisão:
170422
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160228
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.710145


  5 / 1032 MEDLINE  
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[PMID]:26911685
[Au] Autor:Hockley JR; Tranter MM; McGuire C; Boundouki G; Cibert-Goton V; Thaha MA; Blackshaw LA; Michael GJ; Baker MD; Knowles CH; Winchester WJ; Bulmer DC
[Ad] Endereço:Wingate Institute of Neurogastroenterology, Blizard Institute, Barts and the London School of Medicine and Dentistry, Queen Mary University of London, London E1 2AJ, United Kingdom, National Centre for Bowel Research and Surgical Innovation, and.
[Ti] Título:P2Y Receptors Sensitize Mouse and Human Colonic Nociceptors.
[So] Source:J Neurosci;36(8):2364-76, 2016 Feb 24.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Activation of visceral nociceptors by inflammatory mediators contributes to visceral hypersensitivity and abdominal pain associated with many gastrointestinal disorders. Purine and pyrimidine nucleotides (e.g., ATP and UTP) are strongly implicated in this process following their release from epithelial cells during mechanical stimulation of the gut, and from immune cells during inflammation. Actions of ATP are mediated through both ionotropic P2X receptors and metabotropic P2Y receptors. P2X receptor activation causes excitation of visceral afferents; however, the impact of P2Y receptor activation on visceral afferents innervating the gut is unclear. Here we investigate the effects of stimulating P2Y receptors in isolated mouse colonic sensory neurons, and visceral nociceptor fibers in mouse and human nerve-gut preparations. Additionally, we investigate the role of Nav1.9 in mediating murine responses. The application of UTP (P2Y2 and P2Y4 agonist) sensitized colonic sensory neurons by increasing action potential firing to current injection and depolarizing the membrane potential. The application of ADP (P2Y1, P2Y12, and P2Y13 agonist) also increased action potential firing, an effect blocked by the selective P2Y1 receptor antagonist MRS2500. UTP or ADP stimulated afferents, including mouse and human visceral nociceptors, in nerve-gut preparations. P2Y1 and P2Y2 transcripts were detected in 80% and 56% of retrogradely labeled colonic neurons, respectively. Nav1.9 transcripts colocalized in 86% of P2Y1-positive and 100% of P2Y2-positive colonic neurons, consistent with reduced afferent fiber responses to UTP and ADP in Na(v)1.9(-/-) mice. These data demonstrate that P2Y receptor activation stimulates mouse and human visceral nociceptors, highlighting P2Y-dependent mechanisms in the generation of visceral pain during gastrointestinal disease.
[Mh] Termos MeSH primário: Colo/metabolismo
Nociceptores/metabolismo
Receptores Purinérgicos P2Y/biossíntese
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
Idoso de 80 Anos ou mais
Animais
Células Cultivadas
Colo/efeitos dos fármacos
Feminino
Gânglios Espinais/efeitos dos fármacos
Gânglios Espinais/metabolismo
Seres Humanos
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Meia-Idade
Canal de Sódio Disparado por Voltagem NAV1.9/fisiologia
Nucleotídeos de Purina/farmacologia
Nucleotídeos de Pirimidina/farmacologia
Especificidade da Espécie
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (NAV1.9 Voltage-Gated Sodium Channel); 0 (Purine Nucleotides); 0 (Pyrimidine Nucleotides); 0 (Receptors, Purinergic P2Y); 0 (Scn11a protein, mouse)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160226
[St] Status:MEDLINE
[do] DOI:10.1523/JNEUROSCI.3369-15.2016


  6 / 1032 MEDLINE  
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[PMID]:26700143
[Au] Autor:Xue Q; Zhong M; Liu B; Tang Y; Wei Z; Guengerich FP; Zhang H
[Ad] Endereço:Institute of Toxicology, College of Preventive Medicine, Third Military Medical University, Chongqing, PR China.
[Ti] Título:Kinetic analysis of bypass of 7,8-dihydro-8-oxo-2'-deoxyguanosine by the catalytic core of yeast DNA polymerase η.
[So] Source:Biochimie;121:161-9, 2016 Feb.
[Is] ISSN:1638-6183
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Reactive oxygen species damage DNA bases to produce 7,8-dihydro-8-oxo-2'-deoxyguanosine (8-oxoG), which results in G:C to T:A transversions. To better understand mechanisms of dNTP incorporation opposite 8-oxoG, we performed pre-steady-state kinetic analysis of nucleotide incorporation using the catalytic core of yeast DNA polymerase η (Pol ηcore, residues 1-513) instead of full-length Pol η, eliminating potential effects of the C-terminal C2H2 sequence motif on dNTP incorporation. Kinetic analysis showed that Pol ηcore preferred to incorporate dCTP opposite 8-oxoG. A lack of a pre-steady-state kinetic burst for Pol ηcore suggested that dCTP incorporation is slower than the dissociation of the polymerase from DNA. The extension products beyond the 8-oxoG were determined by LC-MS/MS and showed that 57% of the products corresponded to the correct incorporation (C) and 43% corresponded to dATP misincorporation. More dATP was incorporated opposite 8-oxoG with a mixture of dNTPs than predicted using only a single dNTP. The kinetic analysis of 8-oxoG bypass by yeast DNA Pol ηcore provides further understanding of the mechanism of mutation at this oxidation lesion with yeast DNA polymerase η.
[Mh] Termos MeSH primário: DNA Polimerase Dirigida por DNA/metabolismo
Desoxiguanosina/análogos & derivados
[Mh] Termos MeSH secundário: Domínio Catalítico
Desoxiguanosina/química
Desoxiguanosina/metabolismo
Cinética
Nucleotídeos de Pirimidina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Pyrimidine Nucleotides); 88847-89-6 (8-oxo-7-hydrodeoxyguanosine); EC 2.7.7.7 (DNA-Directed DNA Polymerase); G9481N71RO (Deoxyguanosine)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170224
[Lr] Data última revisão:
170224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151225
[St] Status:MEDLINE


  7 / 1032 MEDLINE  
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[PMID]:26679556
[Au] Autor:Samanta B; Seikowski J; Höbartner C
[Ad] Endereço:Institute for Organic and Biomolecular Chemistry, Georg-August-University Göttingen, Tammannstr. 2, 37077, Göttingen, Germany.
[Ti] Título:Fluorogenic Labeling of 5-Formylpyrimidine Nucleotides in DNA and RNA.
[So] Source:Angew Chem Int Ed Engl;55(5):1912-6, 2016 Jan 26.
[Is] ISSN:1521-3773
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:5-Formylcytosine (5fC) and 5-formyluracil (5fU) are natural nucleobase modifications that are generated by oxidative modification of 5-methylcytosine and thymine (or 5-methyluracil). Herein, we describe chemoselective labeling of 5-formylpyrimidine nucleotides in DNA and RNA by fluorogenic aldol-type condensation reactions with 2,3,3-trimethylindole derivatives. Mild and specific reaction conditions were developed for 5fU and 5fC to produce hemicyanine-like chromophores with distinct photophysical properties. Residue-specific detection was established by fluorescence readout as well as primer-extension assays. The reactions were optimized on DNA oligonucleotides and were equally suitable for the modification of 5fU- and 5fC-modified RNA. This direct labeling approach of 5-formylpyrimidines is expected to help in elucidating the occurrence, enzymatic transformations, and functional roles of these epigenetic/epitranscriptomic nucleobase modifications in DNA and RNA.
[Mh] Termos MeSH primário: DNA/química
Corantes Fluorescentes/química
Nucleotídeos de Pirimidina/química
RNA/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fluorescent Dyes); 0 (Pyrimidine Nucleotides); 63231-63-0 (RNA); 9007-49-2 (DNA)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151219
[St] Status:MEDLINE
[do] DOI:10.1002/anie.201508893


  8 / 1032 MEDLINE  
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[PMID]:26627581
[Au] Autor:Hoshino H; Kasahara Y; Fujita H; Kuwahara M; Morihiro K; Tsunoda SI; Obika S
[Ad] Endereço:Graduate School of Pharmaceutical Sciences, Osaka University, 1-6 Yamadaoka, Suita, Osaka 565-0871, Japan; National Institutes of Biomedical Innovation, Health and Nutrition (NIBIOHN), 7-6-8 Saito-Asagi, Ibaraki, Osaka 567-0085, Japan.
[Ti] Título:Consecutive incorporation of functionalized nucleotides with amphiphilic side chains by novel KOD polymerase mutant.
[So] Source:Bioorg Med Chem Lett;26(2):530-533, 2016 Jan 15.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Recently, 7-substituted 7-deazapurine nucleoside triphosphates and 5-substituted pyrimidine nucleoside triphosphates (dN(am)TPs) were synthesized to extend enzymatically using commercially available polymerase. However, extension was limited when we attempted to incorporate the substrates consecutively. To address this, we have produced a mutant polymerase that can efficiently accept the modified nucleotide with amphiphilic groups as substrates. Here we show that the KOD polymerase mutant, KOD exo(-)/A485L, had the ability to incorporate dN(am)TP continuously over 50nt, indicating that the mutant is sufficient for generating functional nucleic acid molecules.
[Mh] Termos MeSH primário: DNA Polimerase Dirigida por DNA/química
Oligodesoxirribonucleotídeos/química
Nucleotídeos de Purina/química
Nucleotídeos de Pirimidina/química
[Mh] Termos MeSH secundário: DNA Polimerase Dirigida por DNA/genética
Oligodesoxirribonucleotídeos/genética
Mutação Puntual
Polietilenoglicóis/química
Nucleotídeos de Purina/genética
Nucleotídeos de Pirimidina/genética
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Oligodeoxyribonucleotides); 0 (Purine Nucleotides); 0 (Pyrimidine Nucleotides); 30IQX730WE (Polyethylene Glycols); EC 2.7.7.7 (DNA-Directed DNA Polymerase)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170805
[Lr] Data última revisão:
170805
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151203
[St] Status:MEDLINE


  9 / 1032 MEDLINE  
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[PMID]:26753279
[Au] Autor:Tan T; Qiao X; Wan Y; Qiu H
[Ti] Título:[Deep eutectic solvent: a new kind of mobile phase modifier for hydrophilic interaction liquid chromatography].
[So] Source:Se Pu;33(9):934-7, 2015 Sep.
[Is] ISSN:1000-8713
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:Deep eutectic solvents (DESs) were used as a new kind of mobile phase modifier in hydrophilic interaction liquid chromatography (HILIC). In our experiment, a SiO2 column (150 mm x 4.6 mm, 3 µm) was selected to separate several nucleobases and nucleosides by using the mixed solution of acetonitrile and DES (choline chloride-ethylene glycol (1:3, mol/mol) ) as mobile phase. Subsequently, the concentrations of DESs in acetonitrile and the column temperature on the effect of separation were investigated. According to the experimental results, better separation of nucleobases and nucleosides was obtained by using acetonitrile and DESs mixed solution as mobile phase than that using traditional water-based solution. For example, a baseline separation between cytosine and cytidine cannot be achieved by HILIC with water-based mobile phase, however, greater improvement was gained by HILIC with modified DES-acetonitrile mobile phase. Meanwhile, the retention times of nucleobases and nucleosides decreased as the proportion of DESs in acetonitrile increased, the most significant decrease of which was with cytidine. Similar retention behavior took place with the effect of column temperature. Decreased retention times of the analytes were observed as column temperature increased. The experimental results indicated that this new method may solve some separation difficulties in traditional water-based HILIC, which also successfully verify the feasibility of DESs as mobile phase modifiers.
[Mh] Termos MeSH primário: Cromatografia Líquida
Solventes/química
[Mh] Termos MeSH secundário: Interações Hidrofóbicas e Hidrofílicas
Nucleosídeos
Nucleotídeos de Purina
Nucleotídeos de Pirimidina
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nucleosides); 0 (Purine Nucleotides); 0 (Pyrimidine Nucleotides); 0 (Solvents)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:161018
[Lr] Data última revisão:
161018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160113
[St] Status:MEDLINE


  10 / 1032 MEDLINE  
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[PMID]:25956126
[Au] Autor:Shimada H; Minami H; Okuizumi N; Sakuma I; Ukai M; Fujii K; Yokoya A; Fukuda Y; Saitoh Y
[Ad] Endereço:Department of Applied Physics, Tokyo University of Agriculture and Technology, Koganei-shi, Tokyo 184-8588, Japan.
[Ti] Título:Nitrogen K-edge x-ray absorption near edge structure of pyrimidine-containing nucleotides in aqueous solution.
[So] Source:J Chem Phys;142(17):175102, 2015 May 07.
[Is] ISSN:1089-7690
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:X-ray absorption near edge structure (XANES) was measured at energies around the N K-edge of the pyrimidine-containing nucleotides, cytidine 5'-monophosphate (CMP), 2'-deoxythymidine 5'-monophosphate (dTMP), and uridine 5'-monophosphate (UMP), in aqueous solutions and in dried films under various pH conditions. The features of resonant excitations below the N K-edge in the XANES spectra for CMP, dTMP, and UMP changed depending on the pH of the solutions. The spectral change thus observed is systematically explained by the chemical shift of the core-levels of N atoms in the nucleobase moieties caused by structural changes due to protonation or deprotonation at different proton concentrations. This interpretation is supported by the results of theoretical calculations using density functional theory for the corresponding nucleobases in the neutral and protonated or deprotonated forms.
[Mh] Termos MeSH primário: Nucleotídeos de Pirimidina/química
Água/química
[Mh] Termos MeSH secundário: Elétrons
Concentração de Íons de Hidrogênio
Radical Hidroxila/química
Modelos Químicos
Estrutura Molecular
Nitrogênio
Prótons
Soluções
Espectroscopia por Absorção de Raios X
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Protons); 0 (Pyrimidine Nucleotides); 0 (Solutions); 059QF0KO0R (Water); 3352-57-6 (Hydroxyl Radical); N762921K75 (Nitrogen)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:150509
[Lr] Data última revisão:
150509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150510
[St] Status:MEDLINE
[do] DOI:10.1063/1.4919744



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