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[PMID]:28453848
[Au] Autor:Kakiuchi S; Tsuji M; Nishimura H; Yoshikawa T; Wang L; Takayama-Ito M; Kinoshita H; Lim CK; Fujii H; Yamada S; Harada S; Oka A; Mizuguchi M; Taniguchi S; Saijo M
[Ad] Endereço:Department of Virology 1, National Institute of Infectious Diseases, Tokyo, Japan.
[Ti] Título:Association of the Emergence of Acyclovir-Resistant Herpes Simplex Virus Type 1 With Prognosis in Hematopoietic Stem Cell Transplantation Patients.
[So] Source:J Infect Dis;215(6):865-873, 2017 03 15.
[Is] ISSN:1537-6613
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Background: Antiviral-resistant herpes simplex virus type 1 (HSV-1) has been recognized as an emerging clinical problem among patients undergoing hematopoietic stem cell transplantation (HSCT). Methods: A prospective observational study was conducted at a hematological center over a 2-year period. Oropharyngeal swab samples were serially collected each week from 1 week before and up to 100 days after HSCT and were tested for virus isolation. The HSV-1 isolates were tested for sensitivity to acyclovir (ACV). The prognosis of patients with ACV-resistant (ACVr) HSV-1 and the genetic background of the ACVr HSV-1 isolates were assessed. Results: Herpes simplex virus type 1 was isolated in 39 of 268 (15%) HSCT patients within 100 days after transplantation. Acyclovir-resistant HSV-1 emerged in 11 of these 39 patients (28%). The 100-day death rates of HSCT patients without HSV-1 shedding, those with only ACV-sensitive HSV-1 shedding, and those with ACVr HSV-1 shedding were 31%, 39%, and 64%, respectively. Patients with HSV-1, including ACVr HSV-1, shedding showed a significantly higher mortality rate. Relapsed malignancies were a significant risk factor for the emergence of ACVr HSV-1. Acyclovir resistance was attributable to viral thymidine kinase and DNA polymerase mutations in 6 and 5 patients, respectively. Conclusions: Herpes simplex virus type 1, including ACVr HSV-1, shedding was associated with poorer outcome in HSCT patients, even if HSV disease did not always occur. Patients with relapsed malignancies were at especially high risk for the emergence of ACVr HSV-1.
[Mh] Termos MeSH primário: Aciclovir/uso terapêutico
Antivirais/uso terapêutico
Farmacorresistência Viral
Transplante de Células-Tronco Hematopoéticas/mortalidade
Herpes Simples/tratamento farmacológico
Herpesvirus Humano 1/efeitos dos fármacos
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
DNA Polimerase Dirigida por DNA/genética
Feminino
Transplante de Células-Tronco Hematopoéticas/efeitos adversos
Herpes Simples/virologia
Herpesvirus Humano 1/isolamento & purificação
Seres Humanos
Japão
Masculino
Testes de Sensibilidade Microbiana
Meia-Idade
Análise Multivariada
Complicações Pós-Operatórias/virologia
Prognóstico
Modelos de Riscos Proporcionais
Estudos Prospectivos
Recidiva
Taxa de Sobrevida
Timidina Quinase/genética
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; OBSERVATIONAL STUDY
[Nm] Nome de substância:
0 (Antiviral Agents); EC 2.7.1.21 (Thymidine Kinase); EC 2.7.7.7 (DNA-Directed DNA Polymerase); X4HES1O11F (Acyclovir)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1093/infdis/jix042


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[PMID]:29307819
[Au] Autor:Kong L; Murata MM; Digman MA
[Ad] Endereço:Laboratory for Fluorescence Dynamics, Department of Biomedical Engineering, University of California, Irvine, CA 92697, USA; University High School, Irvine, CA 92612, USA.
[Ti] Título:Absence of REV3L promotes p53-regulated cancer cell metabolism in cisplatin-treated lung carcinoma cells.
[So] Source:Biochem Biophys Res Commun;496(1):199-204, 2018 01 29.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lung cancer is one of the deadliest cancers in the world because of chemo-resistance to the commonly used cisplatin-based treatments. The use of low fidelity DNA polymerases in the translesional synthesis (TLS) DNA damage response pathway that repairs lesions caused by cisplatin also presents a mutational carcinogenic burden on cells that needs to be regulated by the tumor suppressor protein p53. However, there is much debate over the roles of the reversionless 3-like (REV3L) protein responsible for TLS and p53 in regulating cancer cell metabolism. In this study, the fluorescence lifetime of the metabolic coenzyme NADH reveals that the absence of REV3L can promote the p53-mediated upregulation of oxidative phosphorylation in cisplatin-treated H1299 lung carcinoma cells and increases cancer cell sensitivity to this platinum-based chemotherapy. These results demonstrate a previously unrecognized relationship between p53 and REV3L in cancer cell metabolism and may lead to improvements in chemotherapy treatment plans that reduce cisplatin resistance in lung cancer.
[Mh] Termos MeSH primário: Cisplatino/administração & dosagem
Proteínas de Ligação a DNA/metabolismo
DNA Polimerase Dirigida por DNA/metabolismo
Neoplasias Pulmonares/tratamento farmacológico
Neoplasias Pulmonares/metabolismo
Proteína Supressora de Tumor p53/metabolismo
[Mh] Termos MeSH secundário: Antineoplásicos/administração & dosagem
Apoptose/efeitos dos fármacos
Linhagem Celular Tumoral
Sobrevivência Celular/efeitos dos fármacos
Proteínas de Ligação a DNA/genética
DNA Polimerase Dirigida por DNA/genética
Relação Dose-Resposta a Droga
Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
Inativação Gênica
Seres Humanos
Neoplasias Pulmonares/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (DNA-Binding Proteins); 0 (TP53 protein, human); 0 (Tumor Suppressor Protein p53); EC 2.7.7.7 (DNA-Directed DNA Polymerase); EC 2.7.7.7 (REV3L protein, human); Q20Q21Q62J (Cisplatin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180303
[Lr] Data última revisão:
180303
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180109
[St] Status:MEDLINE


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[PMID]:29281621
[Au] Autor:Tellier-Lebegue C; Dizet E; Ma E; Veaute X; Coïc E; Charbonnier JB; Maloisel L
[Ad] Endereço:I2BC, CEA, CNRS, Univ. Paris-Sud, Univ. Paris-Saclay, Gif-sur-Yvette, France.
[Ti] Título:The translesion DNA polymerases Pol ζ and Rev1 are activated independently of PCNA ubiquitination upon UV radiation in mutants of DNA polymerase δ.
[So] Source:PLoS Genet;13(12):e1007119, 2017 12.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Replicative DNA polymerases cannot insert efficiently nucleotides at sites of base lesions. This function is taken over by specialized translesion DNA synthesis (TLS) polymerases to allow DNA replication completion in the presence of DNA damage. In eukaryotes, Rad6- and Rad18-mediated PCNA ubiquitination at lysine 164 promotes recruitment of TLS polymerases, allowing cells to efficiently cope with DNA damage. However, several studies showed that TLS polymerases can be recruited also in the absence of PCNA ubiquitination. We hypothesized that the stability of the interactions between DNA polymerase δ (Pol δ) subunits and/or between Pol δ and PCNA at the primer/template junction is a crucial factor to determine the requirement of PCNA ubiquitination. To test this hypothesis, we used a structural mutant of Pol δ in which the interaction between Pol3 and Pol31 is inhibited. We found that in yeast, rad18Δ-associated UV hypersensitivity is suppressed by pol3-ct, a mutant allele of the POL3 gene that encodes the catalytic subunit of replicative Pol δ. pol3-ct suppressor effect was specifically dependent on the Rev1 and Pol ζ TLS polymerases. This result strongly suggests that TLS polymerases could rely much less on PCNA ubiquitination when Pol δ interaction with PCNA is partially compromised by mutations. In agreement with this model, we found that the pol3-FI allele suppressed rad18Δ-associated UV sensitivity as observed for pol3-ct. This POL3 allele carries mutations within a putative PCNA Interacting Peptide (PIP) motif. We then provided molecular and genetic evidence that this motif could contribute to Pol δ-PCNA interaction indirectly, although it is not a bona fide PIP. Overall, our results suggest that the primary role of PCNA ubiquitination is to allow TLS polymerases to outcompete Pol δ for PCNA access upon DNA damage.
[Mh] Termos MeSH primário: DNA Polimerase III/metabolismo
[Mh] Termos MeSH secundário: Domínio Catalítico
DNA/genética
DNA/metabolismo
Dano ao DNA
DNA Polimerase III/genética
Reparo do DNA
Replicação do DNA
DNA Polimerase Dirigida por DNA/genética
DNA Polimerase Dirigida por DNA/metabolismo
Modelos Genéticos
Mutação
Nucleotidiltransferases/genética
Nucleotidiltransferases/metabolismo
Antígeno Nuclear de Célula em Proliferação/genética
Antígeno Nuclear de Célula em Proliferação/metabolismo
Ligação Proteica
Saccharomyces cerevisiae
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Ubiquitinação
Raios Ultravioleta
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Proliferating Cell Nuclear Antigen); 0 (Saccharomyces cerevisiae Proteins); 9007-49-2 (DNA); EC 2.7.7.- (DNA Polymerase III); EC 2.7.7.- (DNA polymerase zeta); EC 2.7.7.- (Nucleotidyltransferases); EC 2.7.7.- (REV1 protein, S cerevisiae); EC 2.7.7.7 (DNA-Directed DNA Polymerase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171228
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007119


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[PMID]:29181624
[Au] Autor:Kitchin D; Bouwer G
[Ad] Endereço:School of Molecular and Cell Biology, University of the Witwatersrand, Private Bag 3, Wits, Johannesburg, 2050, South Africa.
[Ti] Título:Significant differences in the intra-host genetic diversity of Helicoverpa armigera nucleopolyhedrovirus dnapol after serial in vivo passages in the same insect population.
[So] Source:Arch Virol;163(3):713-718, 2018 Mar.
[Is] ISSN:1432-8798
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:A denaturing gradient gel electrophoresis assay was used to assess the genetic diversity within a region of the DNA polymerase gene (dnapol) in Helicoverpa armigera nucleopolyhedrovirus (HearNPV) populations over serial in vivo passages. There was no evidence of movement towards a consensus dnapol variant composition in the different host larvae after multiple per os passages. The study showed that the HearNPV variant structure after in vivo passages in the same host population is not necessarily convergent, and that it may be reasonable to expect significant differences in intra-host HearNPV genetic diversity after inoculation of larvae with a genotypically-diverse HearNPV inoculum.
[Mh] Termos MeSH primário: DNA Viral/genética
DNA Polimerase Dirigida por DNA/genética
Mariposas/virologia
Nucleopolyhedrovirus/genética
Proteínas Virais/genética
[Mh] Termos MeSH secundário: Animais
DNA Viral/metabolismo
DNA Polimerase Dirigida por DNA/metabolismo
Eletroforese em Gel de Gradiente Desnaturante
Variação Genética
Larva/virologia
Nucleopolyhedrovirus/classificação
Nucleopolyhedrovirus/enzimologia
Nucleopolyhedrovirus/isolamento & purificação
Filogenia
Inoculações Seriadas
Proteínas Virais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Viral); 0 (Viral Proteins); EC 2.7.7.7 (DNA-Directed DNA Polymerase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171129
[St] Status:MEDLINE
[do] DOI:10.1007/s00705-017-3621-9


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[PMID]:29372656
[Au] Autor:Mikalkenas A; Ravoityte B; Tauraite D; Serviene E; Meskys R; Serva S
[Ad] Endereço:a Department of Biochemistry and Molecular Biology, Institute of Biosciences, Life Sciences Center , Vilnius University , Vilnius , Lithuania.
[Ti] Título:Conjugation of phosphonoacetic acid to nucleobase promotes a mechanism-based inhibition.
[So] Source:J Enzyme Inhib Med Chem;33(1):384-389, 2018 Dec.
[Is] ISSN:1475-6374
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Small molecule inhibitors have a powerful blocking action on viral polymerases. The bioavailability of the inhibitor, nevertheless, often raise a significant selectivity constraint and may substantially limit the efficacy of therapy. Phosphonoacetic acid has long been known to possess a restricted potential to block DNA biosynthesis. In order to achieve a better affinity, this compound has been linked with natural nucleotide at different positions. The structural context of the resulted conjugates has been found to be crucial for the acquisition by DNA polymerases. We show that nucleobase-conjugated phosphonoacetic acid is being accepted, but this alters the processivity of DNA polymerases. The data presented here not only provide a mechanistic rationale for a switch in the mode of DNA synthesis, but also highlight the nucleobase-targeted nucleotide functionalization as a route for enhancing the specificity of small molecule inhibitors.
[Mh] Termos MeSH primário: DNA Polimerase Dirigida por DNA/metabolismo
Inibidores Enzimáticos/farmacologia
Nucleotídeos/farmacologia
Ácido Fosfonoacéticos/farmacologia
[Mh] Termos MeSH secundário: Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
HIV-1/enzimologia
Estrutura Molecular
Vírus da Leucemia Murina de Moloney/enzimologia
Nucleotídeos/química
Ácido Fosfonoacéticos/síntese química
Ácido Fosfonoacéticos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Nucleotides); EC 2.7.7.7 (DNA-Directed DNA Polymerase); N919E46723 (Phosphonoacetic Acid)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180127
[St] Status:MEDLINE
[do] DOI:10.1080/14756366.2017.1417275


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[PMID]:29293599
[Au] Autor:Cai D; Behrmann O; Hufert F; Dame G; Urban G
[Ad] Endereço:Department of Microsystems Engineering (IMTEK), University of Freiburg, Freiburg, Baden-Württemberg, Germany.
[Ti] Título:Capacity of rTth polymerase to detect RNA in the presence of various inhibitors.
[So] Source:PLoS One;13(1):e0190041, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The full potential of the real-time reverse transcription polymerase chain reaction (RT-PCR) as a rapid and accurate diagnostic method is limited by DNA polymerase inhibitors as well as reverse transcriptase inhibitors which are ubiquitous in clinical samples. rTth polymerase has proven to be more resistant to DNA polymerase inhibitors present in clinical samples for DNA detection and also exhibits reverse transcriptase activity in the presence of Mn2+ ions. However, the capacity of rTth polymerase, which acts as DNA polymerase and reverse transcriptase, to detect RNA in the presence of various inhibitors has not been investigated in detail. Herein, the inhibitors originating from various clinical samples such as blood, urine, feces, bodily fluids, tissues and reagents used during nucleic acid extraction were employed to evaluate the capacity of rTth polymerase to detect RNA. The results show that the inhibitors have different inhibitory effects on the real-time RT-PCR reactions by rTth polymerase, and the inhibitory effects are concentration dependent. Additionally, the capacity of rTth polymerase to detect RNA in the presence of various inhibitors is better or at least comparable with its capacity to detect DNA in the presence of various inhibitors. As a consequence, RNA may be directly detected in the presence of co-purified inhibitors or even directly from crude clinical samples by rTth polymerase.
[Mh] Termos MeSH primário: DNA Polimerase Dirigida por DNA/metabolismo
Inibidores Enzimáticos/farmacologia
RNA/análise
[Mh] Termos MeSH secundário: DNA Polimerase Dirigida por DNA/efeitos dos fármacos
RNA/genética
Reação em Cadeia da Polimerase em Tempo Real
Reação em Cadeia da Polimerase Via Transcriptase Reversa
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 63231-63-0 (RNA); EC 2.7.7.- (DNA polymerase, Thermus thermophilus); EC 2.7.7.7 (DNA-Directed DNA Polymerase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180103
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190041


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[PMID]:29287068
[Au] Autor:Yin F; Xie Y; Fan H; Zhang J; Guo Z
[Ad] Endereço:Department of Gastroenterology and Hepatology, The Fourth Hospital of Hebei Medical University, Shijiazhuang, P.R. China.
[Ti] Título:Mutations in hepatitis B virus polymerase are associated with the postoperative survival of hepatocellular carcinoma patients.
[So] Source:PLoS One;12(12):e0189730, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Proofreading deficiencies of hepatitis B virus polymerase result in frequent DNA mutations in the hepatitis B virus genome. Here, we performed sequencing analysis of the hepatitis B virus polymerase gene to assess its association with the postoperative survival in 92 patients with HBV-related hepatocellular carcinoma by using the Kaplan-Meier method. The 2525, 2733, 2738, 2768, 2946, 3063, 3066, 3109, 31, 529, 735, 939, 1078, 1137, 1383, 1461, 1485, 1544, and 1613 mutation sites were identified as being associated with HCC outcomes by the log-rank test. After adjusting for clinical characteristics by using the Cox hazard model, site 31 (relative risk, 8.929; 95% confidence interval, 3.433-23.22; P = 0.000) in the spacer domain and sites 529 (relative risk, 5.656; 95% confidence interval, 1.599-19.999; P = 0.007) and 1078 (relative risk, 3.442; 95% confidence interval, 1.070-11.068; P = 0.038) in the reverse transcriptase domain of hepatitis B virus polymerase were identified as independent predictors of postoperative survival in hepatitis B virus related hepatocellular carcinoma. The mutations at the 31 (Ser314Pro), 529 (Asp480Asn), and 1078 (Ser663Ala) sites all resulted in amino acid changes in hepatitis B virus polymerase and were associated with shortened life-span. The 31 and 529 sites were located in the overlapping region for the PreS and S genes but did not induce amino acid substitution in these two regions. Our finding of the correlation between hepatitis B virus DNA polymerase mutations and hepatocellular carcinoma survival will help identify the patients subgroup with poor prognosis, and help the clinicians to refine the therapeutic decision individualized.
[Mh] Termos MeSH primário: Carcinoma Hepatocelular/patologia
DNA Polimerase Dirigida por DNA/genética
Vírus da Hepatite B/enzimologia
Hepatite B/complicações
Neoplasias Hepáticas/patologia
Mutação
[Mh] Termos MeSH secundário: Carcinoma Hepatocelular/complicações
Carcinoma Hepatocelular/enzimologia
Carcinoma Hepatocelular/cirurgia
Feminino
Seres Humanos
Neoplasias Hepáticas/complicações
Neoplasias Hepáticas/enzimologia
Neoplasias Hepáticas/cirurgia
Masculino
Meia-Idade
Período Pós-Operatório
Reação em Cadeia da Polimerase em Tempo Real
Análise de Sobrevida
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.7.7.7 (DNA-Directed DNA Polymerase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171230
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189730


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[PMID]:27771441
[Au] Autor:Wang J; Liu H; Ma C; Wang J; Zhong L; Wu K
[Ad] Endereço:State Key Laboratory of Medical Genetics, School of Life Sciences, Central South University, Changsha 410013, China.
[Ti] Título:Label-free monitoring of DNA polymerase activity based on a thrombin-binding aptamer G-quadruplex.
[So] Source:Mol Cell Probes;32:13-17, 2017 04.
[Is] ISSN:1096-1194
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We have developed a label-free assay for the detection of DNA polymerase activity based on a thrombin-binding aptamer (TBA) G-quadruplex. In the presence of DNA polymerase, the 3'-OH termini of the hairpin substrate are immediately elongated to replace the TBA, which can be recognized quickly by the ThT dye and results in an increase of fluorescence. This method is highly sensitive with a detection limit of 0.1 U/mL. It is simple and cost-effective without any requirement of labeling with a fluorophore-quencher pair. Furthermore, the proposed method can also be applied to analyze the inhibition of DNA polymerase, which clearly indicates that the proposed method can be applied for screening of potential DNA polymerase inhibitors.
[Mh] Termos MeSH primário: Aptâmeros de Nucleotídeos/metabolismo
DNA Polimerase Dirigida por DNA/metabolismo
Quadruplex G
Coloração e Rotulagem
[Mh] Termos MeSH secundário: Sequência de Bases
DNA Polimerase I/metabolismo
Sondas de DNA/metabolismo
Fluorescência
Tiazóis/metabolismo
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Aptamers, Nucleotide); 0 (DNA Probes); 0 (Thiazoles); 145563-68-4 (thrombin aptamer); 2390-54-7 (thioflavin T); EC 2.7.7.- (DNA Polymerase I); EC 2.7.7.7 (DNA-Directed DNA Polymerase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:180131
[Lr] Data última revisão:
180131
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE


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[PMID]:29319937
[Au] Autor:Food and Drug Administration, HHS.
[Ti] Título:Medical Devices; Clinical Chemistry and Clinical Toxicology Devices; Classification of the Reagents for Molecular Diagnostic Instrument Test Systems. Final order.
[So] Source:Fed Regist;82(247):61162-3, 2017 Dec 27.
[Is] ISSN:0097-6326
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Food and Drug Administration (FDA or we) is classifying the reagents for molecular diagnostic instrument test systems into class I (general controls). We are taking this action because we have determined that classifying the device into class I (general controls) will provide a reasonable assurance of safety and effectiveness of the device. We believe this action will also enhance patients' access to beneficial innovative devices, in part by reducing regulatory burdens.
[Mh] Termos MeSH primário: Testes de Química Clínica/classificação
Testes de Química Clínica/instrumentação
Segurança de Equipamentos/classificação
Indicadores e Reagentes/classificação
Biologia Molecular/classificação
Biologia Molecular/instrumentação
Kit de Reagentes para Diagnóstico/classificação
[Mh] Termos MeSH secundário: DNA Polimerase Dirigida por DNA/classificação
Seres Humanos
Ácidos Nucleicos/classificação
Nucleotídeos/classificação
DNA Polimerase Dirigida por RNA/classificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Indicators and Reagents); 0 (Nucleic Acids); 0 (Nucleotides); 0 (Reagent Kits, Diagnostic); EC 2.7.7.49 (RNA-Directed DNA Polymerase); EC 2.7.7.7 (DNA-Directed DNA Polymerase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180122
[Lr] Data última revisão:
180122
[Sb] Subgrupo de revista:T
[Da] Data de entrada para processamento:180111
[St] Status:MEDLINE


  10 / 11645 MEDLINE  
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[PMID]:29211756
[Au] Autor:Kropp HM; Betz K; Wirth J; Diederichs K; Marx A
[Ad] Endereço:Konstanz Research School Chemical Biology, University of Konstanz, Baden-Württemberg, Konstanz, Germany.
[Ti] Título:Crystal structures of ternary complexes of archaeal B-family DNA polymerases.
[So] Source:PLoS One;12(12):e0188005, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Archaeal B-family polymerases drive biotechnology by accepting a wide substrate range of chemically modified nucleotides. By now no structural data for archaeal B-family DNA polymerases in a closed, ternary complex are available, which would be the basis for developing next generation nucleotides. We present the ternary crystal structures of KOD and 9°N DNA polymerases complexed with DNA and the incoming dATP. The structures reveal a third metal ion in the active site, which was so far only observed for the eukaryotic B-family DNA polymerase δ and no other B-family DNA polymerase. The structures reveal a wide inner channel and numerous interactions with the template strand that provide space for modifications within the enzyme and may account for the high processivity, respectively. The crystal structures provide insights into the superiority over other DNA polymerases concerning the acceptance of modified nucleotides.
[Mh] Termos MeSH primário: Archaea/enzimologia
DNA Polimerase Dirigida por DNA/química
[Mh] Termos MeSH secundário: Domínio Catalítico
Cristalografia por Raios X
DNA Arqueal/química
Modelos Moleculares
Conformação de Ácido Nucleico
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Archaeal); EC 2.7.7.7 (DNA-Directed DNA Polymerase)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171229
[Lr] Data última revisão:
171229
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188005



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