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Pesquisa : D08.811.074.249.750 [Categoria DeCS]
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  1 / 173 MEDLINE  
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[PMID]:28973458
[Au] Autor:Garcia-Gomez A; Li T; Kerick M; Català-Moll F; Comet NR; Rodríguez-Ubreva J; de la Rica L; Branco MR; Martín J; Ballestar E
[Ad] Endereço:Chromatin and Disease Group, Cancer Epigenetics and Biology Programme (PEBC), Bellvitge Biomedical Research Institute (IDIBELL), 08908 L'Hospitalet de Llobregat, Barcelona, Spain.
[Ti] Título:TET2- and TDG-mediated changes are required for the acquisition of distinct histone modifications in divergent terminal differentiation of myeloid cells.
[So] Source:Nucleic Acids Res;45(17):10002-10017, 2017 Sep 29.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The plasticity of myeloid cells is illustrated by a diversity of functions including their role as effectors of innate immunity as macrophages (MACs) and bone remodelling as osteoclasts (OCs). TET2, a methylcytosine dioxygenase highly expressed in these cells and frequently mutated in myeloid leukemias, may be a key contributor to this plasticity. Through transcriptomic and epigenomic analyses, we investigated 5-methylcytosine (5mC), 5-hydroxymethylcytosine (5hmC) and gene expression changes in two divergent terminal myeloid differentiation processes, namely MAC and OC differentiation. MACs and OCs undergo highly similar 5hmC and 5mC changes, despite their wide differences in gene expression. Many TET2- and thymine-DNA glycosylase (TDG)-dependent 5mC and 5hmC changes directly activate the common terminal myeloid differentiation programme. However, the acquisition of differential features between MACs and OCs also depends on TET2/TDG. In fact, 5mC oxidation precedes differential histone modification changes between MACs and OCs. TET2 and TDG downregulation impairs the acquisition of such differential histone modification and expression patterns at MAC-/OC-specific genes. We prove that the histone H3K4 methyltransferase SETD1A is differentially recruited between MACs and OCs in a TET2-dependent manner. We demonstrate a novel role of these enzymes in the establishment of specific elements of identity and function in terminal myeloid differentiation.
[Mh] Termos MeSH primário: Diferenciação Celular/genética
Proteínas de Ligação a DNA/genética
Epigênese Genética
Macrófagos/metabolismo
Osteoclastos/metabolismo
Proteínas Proto-Oncogênicas/genética
Timina DNA Glicosilase/genética
[Mh] Termos MeSH secundário: 5-Metilcitosina/análogos & derivados
5-Metilcitosina/metabolismo
Linhagem da Célula/genética
Proteínas de Ligação a DNA/metabolismo
Perfilação da Expressão Gênica
Histona-Lisina N-Metiltransferase/genética
Histona-Lisina N-Metiltransferase/metabolismo
Histonas/genética
Histonas/metabolismo
Seres Humanos
Fator Estimulador de Colônias de Macrófagos/farmacologia
Macrófagos/citologia
Macrófagos/efeitos dos fármacos
Osteoclastos/citologia
Osteoclastos/efeitos dos fármacos
Cultura Primária de Células
Proteínas Proto-Oncogênicas/metabolismo
Ligante RANK/farmacologia
Timina DNA Glicosilase/metabolismo
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (Histones); 0 (Proto-Oncogene Proteins); 0 (RANK Ligand); 0 (TET2 protein, human); 0 (TNFSF11 protein, human); 1123-95-1 (5-hydroxymethylcytosine); 6R795CQT4H (5-Methylcytosine); 81627-83-0 (Macrophage Colony-Stimulating Factor); EC 2.1.1.43 (Histone-Lysine N-Methyltransferase); EC 2.1.1.43 (Setd1A protein, human); EC 3.2.2.- (Thymine DNA Glycosylase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171004
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx666


  2 / 173 MEDLINE  
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[PMID]:28512237
[Au] Autor:Ho JJ; Cattoglio C; McSwiggen DT; Tjian R; Fong YW
[Ad] Endereço:Department of Molecular and Cell Biology, Li Ka Shing Center for Biomedical and Health Sciences, California Institute for Regenerative Medicine Center of Excellence, University of California at Berkeley, Berkeley, California 94720, USA.
[Ti] Título:Regulation of DNA demethylation by the XPC DNA repair complex in somatic and pluripotent stem cells.
[So] Source:Genes Dev;31(8):830-844, 2017 Apr 15.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Faithful resetting of the epigenetic memory of a somatic cell to a pluripotent state during cellular reprogramming requires DNA methylation to silence somatic gene expression and dynamic DNA demethylation to activate pluripotency gene transcription. The removal of methylated cytosines requires the base excision repair enzyme TDG, but the mechanism by which TDG-dependent DNA demethylation occurs in a rapid and site-specific manner remains unclear. Here we show that the XPC DNA repair complex is a potent accelerator of global and locus-specific DNA demethylation in somatic and pluripotent stem cells. XPC cooperates with TDG genome-wide to stimulate the turnover of essential intermediates by overcoming slow TDG-abasic product dissociation during active DNA demethylation. We further establish that DNA demethylation induced by XPC expression in somatic cells overcomes an early epigenetic barrier in cellular reprogramming and facilitates the generation of more robust induced pluripotent stem cells, characterized by enhanced pluripotency-associated gene expression and self-renewal capacity. Taken together with our previous studies establishing the XPC complex as a transcriptional coactivator, our findings underscore two distinct but complementary mechanisms by which XPC influences gene regulation by coordinating efficient TDG-mediated DNA demethylation along with active transcription during somatic cell reprogramming.
[Mh] Termos MeSH primário: Reprogramação Celular/genética
Metilação de DNA/genética
Proteínas de Ligação a DNA/metabolismo
Células-Tronco Pluripotentes/fisiologia
[Mh] Termos MeSH secundário: Animais
Células-Tronco Embrionárias
Epigênese Genética/genética
Fibroblastos/fisiologia
Regulação da Expressão Gênica
Estudo de Associação Genômica Ampla
Células HEK293
Seres Humanos
Camundongos
Timina DNA Glicosilase/genética
Timina DNA Glicosilase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 156533-34-5 (XPC protein, human); EC 3.2.2.- (Thymine DNA Glycosylase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171110
[Lr] Data última revisão:
171110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170518
[St] Status:MEDLINE
[do] DOI:10.1101/gad.295741.116


  3 / 173 MEDLINE  
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[PMID]:28318075
[Au] Autor:Nakamura T; Murakami K; Tada H; Uehara Y; Nogami J; Maehara K; Ohkawa Y; Saitoh H; Nishitani H; Ono T; Nishi R; Yokoi M; Sakai W; Sugasawa K
[Ad] Endereço:Biosignal Research Center, Kobe University, Kobe, 657-8501, Japan.
[Ti] Título:Thymine DNA glycosylase modulates DNA damage response and gene expression by base excision repair-dependent and independent mechanisms.
[So] Source:Genes Cells;22(4):392-405, 2017 Apr.
[Is] ISSN:1365-2443
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Thymine DNA glycosylase (TDG) is a base excision repair (BER) enzyme, which is implicated in correction of deamination-induced DNA mismatches, the DNA demethylation process and regulation of gene expression. Because of these pivotal roles associated, it is crucial to elucidate how the TDG functions are appropriately regulated in vivo. Here, we present evidence that the TDG protein undergoes degradation upon various types of DNA damage, including ultraviolet light (UV). The UV-induced degradation of TDG was dependent on proficiency in nucleotide excision repair and on CRL4 -mediated ubiquitination that requires a physical interaction between TDG and DNA polymerase clamp PCNA. Using the Tdg-deficient mouse embryonic fibroblasts, we found that ectopic expression of TDG compromised cellular survival after UV irradiation and repair of UV-induced DNA lesions. These negative effects on cellular UV responses were alleviated by introducing mutations in TDG that impaired its BER function. The expression of TDG induced a large-scale alteration in the gene expression profile independently of its DNA glycosylase activity, whereas a subset of genes was affected by the catalytic activity of TDG. Our results indicate the presence of BER-dependent and BER-independent functions of TDG, which are involved in regulation of cellular DNA damage responses and gene expression patterns.
[Mh] Termos MeSH primário: Reparo do DNA
Timina DNA Glicosilase/metabolismo
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Linhagem Celular
Dano ao DNA
Seres Humanos
Mutação
Timina DNA Glicosilase/química
Ubiquitina-Proteína Ligases/metabolismo
Raios Ultravioleta
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 3.2.2.- (Thymine DNA Glycosylase); EC 6.3.2.- (CRL4 protein, human)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170417
[Lr] Data última revisão:
170417
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170321
[St] Status:MEDLINE
[do] DOI:10.1111/gtc.12481


  4 / 173 MEDLINE  
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[PMID]:27951654
[Au] Autor:Henry RA; Mancuso P; Kuo YM; Tricarico R; Tini M; Cole PA; Bellacosa A; Andrews AJ
[Ad] Endereço:Cancer Epigenetics and Cancer Biology Programs, Fox Chase Cancer Center , 333 Cottman Avenue, Philadelphia, Pennsylvania 19111, United States.
[Ti] Título:Interaction with the DNA Repair Protein Thymine DNA Glycosylase Regulates Histone Acetylation by p300.
[So] Source:Biochemistry;55(49):6766-6775, 2016 Dec 13.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:How protein-protein interactions regulate and alter histone modifications is a major unanswered question in epigenetics. The histone acetyltransferase p300 binds thymine DNA glycosylase (TDG); utilizing mass spectrometry to measure site-specific changes in histone acetylation, we found that the absence of TDG in mouse embryonic fibroblasts leads to a reduction in the rate of histone acetylation. We demonstrate that TDG interacts with the CH3 domain of p300 to allosterically promote p300 activity to specific lysines on histone H3 (K18 and K23). However, when TDG concentrations approach those of histones, TDG acts as a competitive inhibitor of p300 histone acetylation. These results suggest a mechanism for how histone acetylation is fine-tuned via interaction with other proteins, while also highlighting a connection between regulators of two important biological processes: histone acetylation and DNA repair/demethylation.
[Mh] Termos MeSH primário: Reparo do DNA
Proteína p300 Associada a E1A/metabolismo
Histonas/metabolismo
Timina DNA Glicosilase/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Animais
Linhagem Celular
Células Cultivadas
Camundongos
Camundongos Knockout
Timina DNA Glicosilase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histones); EC 2.3.1.48 (E1A-Associated p300 Protein); EC 2.3.1.48 (EP300 protein, human); EC 3.2.2.- (Thymine DNA Glycosylase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170510
[Lr] Data última revisão:
170510
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161214
[St] Status:MEDLINE


  5 / 173 MEDLINE  
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[PMID]:27854545
[Au] Autor:Yang Y; Pan Q; Sun B; Yang R; Fang X; Liu X; Yu X; Zhao Z
[Ad] Endereço:1 College of Animal Science, Jilin University , Changchun, People's Republic of China .
[Ti] Título:miR-29b Targets LPL and TDG Genes and Regulates Apoptosis and Triglyceride Production in MECs.
[So] Source:DNA Cell Biol;35(12):758-765, 2016 Dec.
[Is] ISSN:1557-7430
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:microRNAs are involved in various biological processes by regulating the degradation or repressing the translation of target genes. In this study, the target genes of miR-29b were analyzed and predicted by bioinformatics. And lipoprotein lipase (LPL) and thymine DNA glycosylase (TDG) were selected for further validation by dual luciferase reporter assay. In addition, we investigated the effects of miR-29b on triglyceride synthesis and mammary epithelial cell (MEC) apoptosis. The result showed that luciferase activity was significantly lower in cells that miR-29b cotransfected with LPL and TDG gene reporter vectors (pmiR-RB-REPORT-LPL-WT, pmiR-RB-REPORT-TDG-WT) than in cells of miR-29b cotransfected with gene reporter vectors (pmiR-RB-REPORT-LPL-mut and pmiR-RB-REPORT-LPL-si; pmiR-RB-REPORT-TDG-mut and pmiR-RB-REPORT-TDG-si) (p < 0.05), indicating that target sites existed in 3'UTR of LPL and TDG. Furthermore, the expressions of miR-29b were negatively correlated with levels of mRNA and protein of LPL and TDG gene using quantitative real-time polymerase chain reaction and western blot analysis, suggesting that miR-29b might play an important role in regulation of LPL and TDG gene expression. Finally, miR-29b promoted triglyceride production and suppressed apoptosis in MECs, which might be attributed to the expressions of target genes LPL and TDG.
[Mh] Termos MeSH primário: Células Epiteliais/metabolismo
Lipase Lipoproteica/genética
MicroRNAs/genética
Timina DNA Glicosilase/genética
Triglicerídeos/biossíntese
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Animais
Apoptose/genética
Sequência de Bases
Bovinos
Células Epiteliais/citologia
Feminino
Regulação da Expressão Gênica
Genes Reporter
Metabolismo dos Lipídeos/genética
Lipase Lipoproteica/metabolismo
Luciferases/genética
Luciferases/metabolismo
Glândulas Mamárias Animais/citologia
Glândulas Mamárias Animais/metabolismo
MicroRNAs/metabolismo
Cultura Primária de Células
Ligação Proteica
Biossíntese de Proteínas
Transdução de Sinais
Timina DNA Glicosilase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (MicroRNAs); 0 (Triglycerides); EC 1.13.12.- (Luciferases); EC 3.1.1.34 (Lipoprotein Lipase); EC 3.2.2.- (Thymine DNA Glycosylase)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170125
[Lr] Data última revisão:
170125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161118
[St] Status:MEDLINE


  6 / 173 MEDLINE  
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[PMID]:27805810
[Au] Autor:Pidugu LS; Flowers JW; Coey CT; Pozharski E; Greenberg MM; Drohat AC
[Ad] Endereço:Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine , Baltimore, Maryland 21201, United States.
[Ti] Título:Structural Basis for Excision of 5-Formylcytosine by Thymine DNA Glycosylase.
[So] Source:Biochemistry;55(45):6205-6208, 2016 Nov 15.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Thymine DNA glycosylase (TDG) is a base excision repair enzyme with key functions in epigenetic regulation. Performing a critical step in a pathway for active DNA demethylation, TDG removes 5-formylcytosine and 5-carboxylcytosine, oxidized derivatives of 5-methylcytosine that are generated by TET (ten-eleven translocation) enzymes. We determined a crystal structure of TDG bound to DNA with a noncleavable (2'-fluoroarabino) analogue of 5-formyldeoxycytidine flipped into its active site, revealing how it recognizes and hydrolytically excises fC. Together with previous structural and biochemical findings, the results illustrate how TDG employs an adaptable active site to excise a broad variety of nucleobases from DNA.
[Mh] Termos MeSH primário: Citosina/análogos & derivados
DNA/metabolismo
Timina DNA Glicosilase/metabolismo
[Mh] Termos MeSH secundário: 5-Metilcitosina/química
5-Metilcitosina/metabolismo
Domínio Catalítico
Cristalografia por Raios X
Citosina/química
Citosina/metabolismo
DNA/química
DNA/genética
Metilação de DNA
Reparo do DNA
Seres Humanos
Espectroscopia de Ressonância Magnética
Modelos Moleculares
Estrutura Molecular
Conformação de Ácido Nucleico
Oligodesoxirribonucleotídeos/química
Oligodesoxirribonucleotídeos/metabolismo
Oxirredução
Ligação Proteica
Domínios Proteicos
Especificidade por Substrato
Timina DNA Glicosilase/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (5-carboxylcytosine); 0 (5-formylcytosine); 0 (Oligodeoxyribonucleotides); 6R795CQT4H (5-Methylcytosine); 8J337D1HZY (Cytosine); 9007-49-2 (DNA); EC 3.2.2.- (Thymine DNA Glycosylase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171115
[Lr] Data última revisão:
171115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161103
[St] Status:MEDLINE


  7 / 173 MEDLINE  
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[PMID]:27580719
[Au] Autor:Coey CT; Malik SS; Pidugu LS; Varney KM; Pozharski E; Drohat AC
[Ad] Endereço:Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
[Ti] Título:Structural basis of damage recognition by thymine DNA glycosylase: Key roles for N-terminal residues.
[So] Source:Nucleic Acids Res;44(21):10248-10258, 2016 Dec 01.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Thymine DNA Glycosylase (TDG) is a base excision repair enzyme functioning in DNA repair and epigenetic regulation. TDG removes thymine from mutagenic G·T mispairs arising from deamination of 5-methylcytosine (mC), and it processes other deamination-derived lesions including uracil (U). Essential for DNA demethylation, TDG excises 5-formylcytosine and 5-carboxylcytosine, derivatives of mC generated by Tet (ten-eleven translocation) enzymes. Here, we report structural and functional studies of TDG , a new construct containing 29 more N-terminal residues than TDG , the construct used for previous structures of DNA-bound TDG. Crystal structures and NMR experiments demonstrate that most of these N-terminal residues are disordered, for substrate- or product-bound TDG Nevertheless, G·T substrate affinity and glycosylase activity of TDG greatly exceeds that of TDG and is equivalent to full-length TDG. We report the first high-resolution structures of TDG in an enzyme-substrate complex, for G·U bound to TDG (1.54 Å) and TDG (1.71 Å), revealing new enzyme-substrate contacts, direct and water-mediated. We also report a structure of the TDG product complex (1.70 Å). TDG forms unique enzyme-DNA interactions, supporting its value for structure-function studies. The results advance understanding of how TDG recognizes and removes modified bases from DNA, particularly those resulting from deamination.
[Mh] Termos MeSH primário: Dano ao DNA
DNA/química
DNA/metabolismo
Timina DNA Glicosilase/química
Timina DNA Glicosilase/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sítios de Ligação
DNA/genética
Ativação Enzimática
Seres Humanos
Interações Hidrofóbicas e Hidrofílicas
Espectroscopia de Ressonância Magnética
Modelos Moleculares
Conformação Molecular
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes
Relação Estrutura-Atividade
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Recombinant Proteins); 9007-49-2 (DNA); EC 3.2.2.- (Thymine DNA Glycosylase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170531
[Lr] Data última revisão:
170531
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160902
[St] Status:MEDLINE


  8 / 173 MEDLINE  
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[PMID]:27513857
[Au] Autor:Zhang LJ; Liu SY; Zhu YN; Gao Y; Chen J; Yuan B; Jiang H; Dai LS; Zhang JB
[Ad] Endereço:College of Animal Science and Technology, Jilin Agricultural Science and Technology College, Jilin, China.
[Ti] Título:Thymine DNA Glycosylase Gene Knockdown Can Affect the Differentiation of Pig Preadipocytes.
[So] Source:Cell Physiol Biochem;39(3):975-84, 2016.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:AIMS: To study the effect of thymine DNA glycosylase (TDG) gene knockdown on the differentiation of pig preadipocytes. METHODS: Preadipocytes were obtained from subcutaneous adipose tissue from the neck of 1- to 7-day-old pigs. The TDG gene was knocked down using siRNA, and cell differentiation was induced. The mRNA expression level was measured using fluorescence quantitative PCR, and the protein expression level was determined using Western blot analysis. The DNA methylation levels in promoter regions of differentiation-related genes were also evaluated. RESULTS: TDG gene knockdown decreased the mRNA expression levels of the peroxisome proliferator-activated receptorγ (PPARγ) and Fatty acid binding proteins 4(FABP4 Also known as aP2) genes (P<0.01), while the mRNA expression level of the CCAAT/enhancer binding protein alpha(C/EBPα) gene did not change significantly (P>0.05). In addition, after induced differentiation, the lipid droplet production significantly decreased, and the percentages of methylation in the promoter regions of C/EBPα, PPARγ, and aP2 genes were 0.9%, 80%, and 76%, respectively. In contrast, the percentages of methylation in the negative control groups were 0.5%, 67.5%, and 58%, respectively. CONCLUSION: TDG gene knockdown could inhibit the differentiation of pig preadipocytes and affect the DNA methylation levels of some transcription factors.
[Mh] Termos MeSH primário: Adipócitos Brancos/metabolismo
Proteínas Estimuladoras de Ligação a CCAAT/genética
Epigênese Genética
Proteínas de Ligação a Ácido Graxo/genética
PPAR gama/genética
Timina DNA Glicosilase/genética
[Mh] Termos MeSH secundário: Adipócitos Brancos/citologia
Animais
Animais Recém-Nascidos
Proteínas Estimuladoras de Ligação a CCAAT/metabolismo
Diferenciação Celular
Metilação de DNA
Proteínas de Ligação a Ácido Graxo/metabolismo
Expressão Gênica
Técnicas de Silenciamento de Genes
Gotículas Lipídicas/metabolismo
Masculino
PPAR gama/metabolismo
Cultura Primária de Células
Regiões Promotoras Genéticas
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Transdução de Sinais
Gordura Subcutânea/citologia
Gordura Subcutânea/metabolismo
Suínos
Timina DNA Glicosilase/deficiência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CCAAT-Enhancer-Binding Proteins); 0 (Fatty Acid-Binding Proteins); 0 (PPAR gamma); 0 (RNA, Messenger); EC 3.2.2.- (Thymine DNA Glycosylase)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170202
[Lr] Data última revisão:
170202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160812
[St] Status:MEDLINE
[do] DOI:10.1159/000447805


  9 / 173 MEDLINE  
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[PMID]:27497170
[Au] Autor:Imhof P
[Ad] Endereço:Institute of Theoretical Physics, Free University Berlin, Berlin, Germany. Electronic address: petra.imhof@fu-berlin.de.
[Ti] Título:A Networks Approach to Modeling Enzymatic Reactions.
[So] Source:Methods Enzymol;578:249-71, 2016.
[Is] ISSN:1557-7988
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Modeling enzymatic reactions is a demanding task due to the complexity of the system, the many degrees of freedom involved and the complex, chemical, and conformational transitions associated with the reaction. Consequently, enzymatic reactions are not determined by precisely one reaction pathway. Hence, it is beneficial to obtain a comprehensive picture of possible reaction paths and competing mechanisms. By combining individually generated intermediate states and chemical transition steps a network of such pathways can be constructed. Transition networks are a discretized representation of a potential energy landscape consisting of a multitude of reaction pathways connecting the end states of the reaction. The graph structure of the network allows an easy identification of the energetically most favorable pathways as well as a number of alternative routes.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/química
Desoxirribonucleases de Sítio Específico do Tipo II/química
Redes e Vias Metabólicas
Miosinas/química
Timina DNA Glicosilase/química
Timina/química
[Mh] Termos MeSH secundário: Biocatálise
Escherichia coli/química
Escherichia coli/enzimologia
Seres Humanos
Cinética
Simulação de Dinâmica Molecular
Conformação Proteica
Teoria Quântica
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
8L70Q75FXE (Adenosine Triphosphate); EC 3.1.21.4 (Deoxyribonucleases, Type II Site-Specific); EC 3.1.21.4 (GATATC-specific type II deoxyribonucleases); EC 3.2.2.- (Thymine DNA Glycosylase); EC 3.6.4.1 (Myosins); QR26YLT7LT (Thymine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170811
[Lr] Data última revisão:
170811
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160807
[St] Status:MEDLINE


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[PMID]:27494808
[Au] Autor:Lin S; Kang TS; Lu L; Wang W; Ma DL; Leung CH
[Ad] Endereço:Department of Chemistry, Hong Kong Baptist University, Kowloon Tong, Hong Kong, China.
[Ti] Título:A G-quadruplex-selective luminescent probe with an anchor tail for the switch-on detection of thymine DNA glycosylase activity.
[So] Source:Biosens Bioelectron;86:849-857, 2016 Dec 15.
[Is] ISSN:1873-4235
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Thymine DNA glycosylase (TDG) performs essential functions in maintaining genetic integrity and epigenetic regulation, which also plays an essential role in DNA demethylation. In this work, the novel iridium(III) complex 1 with an anchor tail was synthesized and employed to construct a G-quadruplex-based assay for detecting TDG activity in aqueous solution by using the mismatched base excising property of TDG with T4 DNA ligase and phi29 DNA polymerase, in concert with the rolling circle amplification (RCA) strategy. The assay achieved a detection limit of 0.048UmL(-)(1) (0.012ngmL(-1)), and showed high selectivity towards TDG even in the presence of other proteins and enzymes. Additionally, the assay could function in diluted cellular debris.
[Mh] Termos MeSH primário: Sondas de DNA/genética
Quadruplex G
Medições Luminescentes/instrumentação
Técnicas de Sonda Molecular/instrumentação
Timina DNA Glicosilase/análise
Timina DNA Glicosilase/genética
[Mh] Termos MeSH secundário: Desenho de Equipamento
Análise de Falha de Equipamento
Técnicas de Amplificação de Ácido Nucleico/instrumentação
Técnicas de Amplificação de Ácido Nucleico/métodos
Reprodutibilidade dos Testes
Sensibilidade e Especificidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA Probes); EC 3.2.2.- (Thymine DNA Glycosylase)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160806
[St] Status:MEDLINE



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