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Pesquisa : D08.811.277.352.365 [Categoria DeCS]
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  1 / 2071 MEDLINE  
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[PMID]:29321179
[Au] Autor:Reginato G; Cannavo E; Cejka P
[Ad] Endereço:Institute for Research in Biomedicine, Università della Svizzera italiana, Bellinzona 6500, Switzerland.
[Ti] Título:Physiological protein blocks direct the Mre11-Rad50-Xrs2 and Sae2 nuclease complex to initiate DNA end resection.
[So] Source:Genes Dev;31(23-24):2325-2330, 2017 12 01.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:DNA double-strand break repair by homologous recombination is initiated by DNA end resection, which is commenced by the Mre11-Rad50-Xrs2 complex and Sae2 in yeast. Here we report that the nonhomologous end joining factor Ku limits the exonuclease activity of Mre11 and promotes its endonuclease to cleave 5'-terminated DNA strands at break sites. Following initial endonucleolytic cleavage past the obstacle, Exo1 specifically extends the resection track, leading to the generation of long 3' overhangs that are required for homologous recombination. These experiments provide mechanistic insights into how short-range and long-range DNA end resection enzymes overcome obstacles near broken DNA ends to initiate recombination.
[Mh] Termos MeSH primário: Reparo do DNA por Junção de Extremidades
Endonucleases/metabolismo
Exonucleases/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/fisiologia
[Mh] Termos MeSH secundário: Animais
Clivagem do DNA
Proteínas de Ligação a DNA/metabolismo
Endodesoxirribonucleases/metabolismo
Ativação Enzimática/genética
Exodesoxirribonucleases/metabolismo
Complexos Multiproteicos/metabolismo
Saccharomyces cerevisiae/enzimologia
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Células Sf9
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (Multiprotein Complexes); 0 (RAD50 protein, S cerevisiae); 0 (SAE2 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (XRS2 protein, S cerevisiae); 0 (high affinity DNA-binding factor, S cerevisiae); EC 3.1.- (Endodeoxyribonucleases); EC 3.1.- (Endonucleases); EC 3.1.- (Exodeoxyribonucleases); EC 3.1.- (Exonucleases); EC 3.1.- (MRE11 protein, S cerevisiae); EC 3.1.11.1 (exodeoxyribonuclease I)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE
[do] DOI:10.1101/gad.308254.117


  2 / 2071 MEDLINE  
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[PMID]:29321177
[Au] Autor:Wang W; Daley JM; Kwon Y; Krasner DS; Sung P
[Ad] Endereço:Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
[Ti] Título:Plasticity of the Mre11-Rad50-Xrs2-Sae2 nuclease ensemble in the processing of DNA-bound obstacles.
[So] Source:Genes Dev;31(23-24):2331-2336, 2017 12 01.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The budding yeast Mre11-Rad50-Xrs2 (MRX) complex and Sae2 function together in DNA end resection during homologous recombination. Here we show that the Ku complex shields DNA ends from exonucleolytic digestion but facilitates endonucleolytic scission by MRX with a dependence on ATP and Sae2. The incision site is enlarged into a DNA gap via the exonuclease activity of MRX, which is stimulated by Sae2 without ATP being present. RPA renders a partially resected or palindromic DNA structure susceptible to MRX-Sae2, and internal protein blocks also trigger DNA cleavage. We present models for how MRX-Sae2 creates entry sites for the long-range resection machinery.
[Mh] Termos MeSH primário: Reparo do DNA por Junção de Extremidades
Reparo do DNA/fisiologia
Endonucleases/metabolismo
Exonucleases/metabolismo
Complexos Multienzimáticos/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/fisiologia
[Mh] Termos MeSH secundário: Clivagem do DNA
Proteínas de Ligação a DNA/metabolismo
Endodesoxirribonucleases/metabolismo
Ativação Enzimática/genética
Exodesoxirribonucleases/metabolismo
Complexos Multiproteicos/metabolismo
Saccharomyces cerevisiae/enzimologia
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (Multienzyme Complexes); 0 (Multiprotein Complexes); 0 (RAD50 protein, S cerevisiae); 0 (SAE2 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (XRS2 protein, S cerevisiae); 0 (high affinity DNA-binding factor, S cerevisiae); EC 3.1.- (Endodeoxyribonucleases); EC 3.1.- (Endonucleases); EC 3.1.- (Exodeoxyribonucleases); EC 3.1.- (Exonucleases); EC 3.1.- (MRE11 protein, S cerevisiae); EC 3.1.11.1 (exodeoxyribonuclease I)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE
[do] DOI:10.1101/gad.307900.117


  3 / 2071 MEDLINE  
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[PMID]:28467681
[Au] Autor:Ma DL; Dong ZZ; Vellaisamy K; Cheung KM; Yang G; Leung CH
[Ad] Endereço:Department of Chemistry, Hong Kong Baptist University, Kowloon Tong, Hong Kong.
[Ti] Título:Luminescent Strategies for Label-Free G-Quadruplex-Based Enzyme Activity Sensing.
[So] Source:Chem Rec;17(11):1135-1145, 2017 11.
[Is] ISSN:1528-0691
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:By catalyzing highly specific and tightly controlled chemical reactions, enzymes are essential to maintaining normal cellular physiology. However, aberrant enzymatic activity can be linked to the pathogenesis of various diseases. Therefore, the unusual activity of particular enzymes can represent testable biomarkers for the diagnosis or screening of certain diseases. In recent years, G-quadruplex-based platforms have attracted wide attention for the monitoring of enzymatic activities. In this Personal Account, we discuss our group's works on the development of G-quadruplex-based sensing system for enzyme activities by using mainly iridium(III) complexes as luminescent label-free probes. These studies showcase the versatility of the G-quadruplex for developing assays for a variety of different enzymes.
[Mh] Termos MeSH primário: Complexos de Coordenação/química
Ensaios Enzimáticos/métodos
Quadruplex G
Irídio/química
Substâncias Luminescentes/química
Medições Luminescentes/métodos
[Mh] Termos MeSH secundário: Animais
Técnicas Biossensoriais/métodos
Enzimas Reparadoras do DNA/análise
Enzimas Reparadoras do DNA/metabolismo
DNA Polimerase Dirigida por DNA/análise
DNA Polimerase Dirigida por DNA/metabolismo
Endonucleases/análise
Endonucleases/metabolismo
Exonucleases/análise
Exonucleases/metabolismo
Seres Humanos
Peptídeo Hidrolases/análise
Peptídeo Hidrolases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Coordination Complexes); 0 (Luminescent Agents); 44448S9773 (Iridium); EC 2.7.7.7 (DNA-Directed DNA Polymerase); EC 3.1.- (Endonucleases); EC 3.1.- (Exonucleases); EC 3.4.- (Peptide Hydrolases); EC 6.5.1.- (DNA Repair Enzymes)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171211
[Lr] Data última revisão:
171211
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1002/tcr.201700014


  4 / 2071 MEDLINE  
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[PMID]:28899942
[Au] Autor:Ma M; Li de la Sierra-Gallay I; Lazar N; Pellegrini O; Lepault J; Condon C; Durand D; van Tilbeurgh H
[Ad] Endereço:Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS UMR 9198, Univ. Paris-Sud, Université Paris-Saclay, 91198 Gif sur Yvette Cedex, France.
[Ti] Título:Trz1, the long form RNase Z from yeast, forms a stable heterohexamer with endonuclease Nuc1 and mutarotase.
[So] Source:Biochem J;474(21):3599-3613, 2017 Oct 18.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Proteomic studies have established that Trz1, Nuc1 and mutarotase form a complex in yeast. Trz1 is a ß-lactamase-type RNase composed of two ß-lactamase-type domains connected by a long linker that is responsible for the endonucleolytic cleavage at the 3'-end of tRNAs during the maturation process (RNase Z activity); Nuc1 is a dimeric mitochondrial nuclease involved in apoptosis, while mutarotase (encoded by YMR099C) catalyzes the conversion between the α- and ß-configuration of glucose-6-phosphate. Using gel filtration, small angle X-ray scattering and electron microscopy, we demonstrated that Trz1, Nuc1 and mutarotase form a very stable heterohexamer, composed of two copies of each of the three subunits. A Nuc1 homodimer is at the center of the complex, creating a two-fold symmetry and interacting with both Trz1 and mutarotase. Enzymatic characterization of the ternary complex revealed that the activities of Trz1 and mutarotase are not affected by complex formation, but that the Nuc1 activity is completely inhibited by mutarotase and partially by Trz1. This suggests that mutarotase and Trz1 might be regulators of the Nuc1 apoptotic nuclease activity.
[Mh] Termos MeSH primário: Carboidratos Epimerases/química
Endonucleases/química
Endorribonucleases/química
Exonucleases/química
Proteínas de Saccharomyces cerevisiae/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Carboidratos Epimerases/genética
Endonucleases/genética
Endorribonucleases/genética
Exonucleases/genética
Estabilidade Proteica
Estrutura Secundária de Proteína
Proteínas de Saccharomyces cerevisiae/genética
Espalhamento a Baixo Ângulo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Saccharomyces cerevisiae Proteins); EC 3.1.- (Endonucleases); EC 3.1.- (Endoribonucleases); EC 3.1.- (Exonucleases); EC 3.1.- (Nuc1 protein, S cerevisiae); EC 3.1.- (RNase Z); EC 3.1.- (tRNase Z, S cerevisiae); EC 5.1.3.- (Carbohydrate Epimerases); EC 5.1.3.3 (aldose 1-epimerase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170914
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20170435


  5 / 2071 MEDLINE  
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[PMID]:28777079
[Au] Autor:Yekwa E; Khourieh J; Canard B; Papageorgiou N; Ferron F
[Ad] Endereço:CNRS, AFMB UMR 7257, 13288 Marseille, France.
[Ti] Título:Activity inhibition and crystal polymorphism induced by active-site metal swapping.
[So] Source:Acta Crystallogr D Struct Biol;73(Pt 8):641-649, 2017 Aug 01.
[Is] ISSN:2059-7983
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Arenaviridae family is one of the two RNA viral families that encode a 3'-5' exonuclease in their genome. An exonuclease domain is found in the Arenaviridae nucleoprotein and targets dsRNA specifically. This domain is directly involved in suppression of innate immunity in the host cell. Like most phosphate-processing enzymes, it requires a divalent metal ion such as Mg (or Mn ) as a cofactor to catalyse nucleotide-cleavage and nucleotide-transfer reactions. On the other hand, calcium (Ca ) inhibits this enzymatic activity, in spite of the fact that Mg and Ca present comparable binding affinities and biological availabilities. Here, the molecular and structural effects of the replacement of magnesium by calcium and its inhibition mechanism for phosphodiester cleavage, an essential reaction in the viral process of innate immunity suppression, are studied. Biochemical data and high-resolution structures of the Mopeia virus exonuclease domain complexed with each ion are reported for the first time. The consequences of the ion swap for the stability of the protein, the catalytic site and the functional role of a specific metal ion in enabling the catalytic cleavage of a dsRNA substrate are outlined.
[Mh] Termos MeSH primário: Arenavirus/química
Arenavirus/enzimologia
Exonucleases/química
Proteínas do Nucleocapsídeo/química
Nucleoproteínas/química
[Mh] Termos MeSH secundário: Infecções por Arenaviridae/virologia
Arenavirus/metabolismo
Sítios de Ligação
Cálcio/metabolismo
Domínio Catalítico
Cátions Bivalentes/metabolismo
Cristalização
Cristalografia por Raios X
Exonucleases/metabolismo
Magnésio/metabolismo
Manganês/metabolismo
Simulação de Acoplamento Molecular
Proteínas do Nucleocapsídeo/metabolismo
Nucleoproteínas/metabolismo
Domínios Proteicos
RNA Viral/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cations, Divalent); 0 (Nucleocapsid Proteins); 0 (Nucleoproteins); 0 (RNA, Viral); 42Z2K6ZL8P (Manganese); EC 3.1.- (Exonucleases); I38ZP9992A (Magnesium); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170805
[St] Status:MEDLINE
[do] DOI:10.1107/S205979831700866X


  6 / 2071 MEDLINE  
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[PMID]:28666868
[Au] Autor:Fukumoto Y; Nakayama Y; Yamaguchi N
[Ad] Endereço:Laboratory of Molecular Cell Biology, Graduate School of Pharmaceutical Sciences, Chiba University, Chiba 260-8675, Japan. Electronic address: fukumoto@faculty.chiba-u.jp.
[Ti] Título:The polyanionic C-terminal tail of human Rad17 regulates interaction with the 9-1-1 complex.
[So] Source:Biochem Biophys Res Commun;490(4):1147-1153, 2017 Sep 02.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In the activation and maintenance of ATR-dependent DNA damage checkpoint, the interaction between the Rad17-RFC2-5 and 9-1-1 complexes is essential, however, the regulatory mechanism of the interaction is not known. Here we show that vertebrate Rad17 proteins contain a polyanionic 12-amino acid sequence in the C-terminal ends that is important for the 9-1-1 interaction. We demonstrate that the C-terminal tail contains a conserved sequence designated iVERGE that must be intact for the 9-1-1 interaction and contains potential posttranslational modification sites. Our data raise a possibility that the Rad17 C-terminal tail is a molecular switch that regulates the 9-1-1 interaction and the ATR pathway.
[Mh] Termos MeSH primário: Proteínas de Ciclo Celular/metabolismo
Complexos Multiproteicos/metabolismo
Polímeros/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Ciclo Celular/química
Células Cultivadas
Exonucleases/metabolismo
Seres Humanos
Complexos Multiproteicos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (HUS1B protein, human); 0 (Multiprotein Complexes); 0 (Polymers); 0 (Rad17 protein, human); 0 (polyanions); 139691-42-2 (rad9 protein); EC 3.1.- (Exonucleases); EC 3.1.11.- (Rad1 protein, human)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170702
[St] Status:MEDLINE


  7 / 2071 MEDLINE  
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[PMID]:28626879
[Au] Autor:Alexiadis A; Delidakis C; Kalantidis K
[Ad] Endereço:Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology-Hellas, Heraklion, Greece.
[Ti] Título:Snipper, an Eri1 homologue, affects histone mRNA abundance and is crucial for normal Drosophila melanogaster development.
[So] Source:FEBS Lett;591(14):2106-2120, 2017 Jul.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The conserved 3'-5' RNA exonuclease ERI1 is implicated in RNA interference inhibition, 5.8S rRNA maturation and histone mRNA maturation and turnover. The single ERI1 homologue in Drosophila melanogaster Snipper (Snp) is a 3'-5' exonuclease, but its in vivo function remains elusive. Here, we report Snp requirement for normal Drosophila development, since its perturbation leads to larval arrest and tissue-specific downregulation results in abnormal tissue development. Additionally, Snp directly interacts with histone mRNA, and its depletion results in drastic reduction in histone transcript levels. We propose that Snp protects the 3'-ends of histone mRNAs and upon its absence, histone transcripts are readily degraded. This in turn may lead to cell cycle delay or arrest, causing growth arrest and developmental perturbations.
[Mh] Termos MeSH primário: Proteínas de Drosophila/metabolismo
Drosophila melanogaster/enzimologia
Drosophila melanogaster/crescimento & desenvolvimento
Exonucleases/metabolismo
Histonas/genética
Homologia de Sequência de Aminoácidos
[Mh] Termos MeSH secundário: Animais
Sequência de Bases
Proteínas de Drosophila/química
Drosophila melanogaster/genética
Exonucleases/química
Histonas/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
RNA Ribossômico 5,8S/genética
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (Histones); 0 (RNA, Messenger); 0 (RNA, Ribosomal, 5.8S); EC 3.1.- (Exonucleases); EC 3.1.- (Snipper protein, Drosophila)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170815
[Lr] Data última revisão:
170815
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170620
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12719


  8 / 2071 MEDLINE  
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[PMID]:28575400
[Au] Autor:Dalia TN; Yoon SH; Galli E; Barre FX; Waters CM; Dalia AB
[Ad] Endereço:Department of Biology, Indiana University, Bloomington, IN 47401, USA.
[Ti] Título:Enhancing multiplex genome editing by natural transformation (MuGENT) via inactivation of ssDNA exonucleases.
[So] Source:Nucleic Acids Res;45(12):7527-7537, 2017 Jul 07.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Recently, we described a method for multiplex genome editing by natural transformation (MuGENT). Mutant constructs for MuGENT require large arms of homology (>2000 bp) surrounding each genome edit, which necessitates laborious in vitro DNA splicing. In Vibrio cholerae, we uncover that this requirement is due to cytoplasmic ssDNA exonucleases, which inhibit natural transformation. In ssDNA exonuclease mutants, one arm of homology can be reduced to as little as 40 bp while still promoting integration of genome edits at rates of ∼50% without selection in cis. Consequently, editing constructs are generated in a single polymerase chain reaction where one homology arm is oligonucleotide encoded. To further enhance editing efficiencies, we also developed a strain for transient inactivation of the mismatch repair system. As a proof-of-concept, we used these advances to rapidly mutate 10 high-affinity binding sites for the nucleoid occlusion protein SlmA and generated a duodecuple mutant of 12 diguanylate cyclases in V. cholerae. Whole genome sequencing revealed little to no off-target mutations in these strains. Finally, we show that ssDNA exonucleases inhibit natural transformation in Acinetobacter baylyi. Thus, rational removal of ssDNA exonucleases may be broadly applicable for enhancing the efficacy and ease of MuGENT in diverse naturally transformable species.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Exonucleases/genética
Edição de Genes/métodos
Genoma Bacteriano
Transformação Bacteriana
[Mh] Termos MeSH secundário: Acinetobacter/genética
Acinetobacter/metabolismo
Proteínas de Bactérias/antagonistas & inibidores
Proteínas de Bactérias/metabolismo
Reparo de Erro de Pareamento de DNA
DNA Bacteriano/genética
DNA Bacteriano/metabolismo
DNA de Cadeia Simples/genética
DNA de Cadeia Simples/metabolismo
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Exonucleases/antagonistas & inibidores
Exonucleases/deficiência
Recombinação Homóloga
Reação em Cadeia da Polimerase Multiplex/métodos
Mutação
Fósforo-Oxigênio Liases/genética
Fósforo-Oxigênio Liases/metabolismo
Vibrio cholerae/genética
Vibrio cholerae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (DNA, Bacterial); 0 (DNA, Single-Stranded); 0 (Escherichia coli Proteins); EC 3.1.- (Exonucleases); EC 4.6.- (Phosphorus-Oxygen Lyases); EC 4.6.1.- (diguanylate cyclase)
[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:170603
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx496


  9 / 2071 MEDLINE  
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[PMID]:28521375
[Au] Autor:Kim S; Kleimeyer JP; Ahmed MA; Avins AL; Fredericson M; Dragoo JL; Ioannidis JPA
[Ad] Endereço:Dev. Bio., Stanford University, Stanford, United States.
[Ti] Título:A Genetic Marker Associated with Shoulder Dislocation..
[So] Source:Int J Sports Med;38(7):508-514, 2017 Jul.
[Is] ISSN:1439-3964
[Cp] País de publicação:Germany
[La] Idioma:ger
[Ab] Resumo:Shoulder dislocations are common shoulder injuries associated with athletic activity in contact sports, such as football, rugby, wrestling, and hockey. Identifying genetic loci associated with shoulder dislocation could shed light on underlying mechanisms for injury and identify predictive genetic markers. To identify DNA polymorphisms associated with shoulder dislocation, a genome-wide association screen was performed using publically available data from the Research Program in Genes, Environment and Health including 662 cases of shoulder dislocation and 82 602 controls from the European ancestry group. rs12913965 showed an association with shoulder dislocation at genome-wide significance (p=9.7×10 ; odds ratio=1.6) from the European ancestry group. Individuals carrying one copy of the risk allele (T) at rs12913965 showed a 69% increased risk for shoulder dislocation in our cohort. rs12913965 is located within an intron of the TICRR gene, which encodes TOPBP1 interacting checkpoint and replication regulator involved in the cell cycle. rs12913965 is also associated with changes in expression of the ISG20 gene, which encodes an antiviral nuclease induced by interferons. This genetic marker may one day be used to identify athletes with a higher genetic risk for shoulder dislocation. It will be important to replicate this finding in future studies.
[Mh] Termos MeSH primário: Proteínas de Ciclo Celular/genética
Exonucleases/genética
Polimorfismo de Nucleotídeo Único
Luxação do Ombro/genética
[Mh] Termos MeSH secundário: Alelos
Atletas
Feminino
Frequência do Gene
Marcadores Genéticos
Estudo de Associação Genômica Ampla
Seres Humanos
Masculino
Meia-Idade
Ombro/fisiopatologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (Genetic Markers); 0 (TICRR protein, human); EC 3.1.- (Exonucleases); EC 3.1.- (ISG20 protein, human)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170519
[St] Status:MEDLINE
[do] DOI:10.1055/s-0043-106190


  10 / 2071 MEDLINE  
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[PMID]:28498284
[Au] Autor:Espinosa I; Lee CH; D'Angelo E; Palacios J; Prat J
[Ad] Endereço:*Department of Pathology, Hospital de la Santa Creu i Sant Pau, Institute of Biomedical Research (IIB Sant Pau), Autonomous University of Barcelona, Barcelona ‡Department of Pathology, Hospital Ramón y Cajal (IRYCIS), Department of Medicine, University of Alcala, Madrid, Spain †Department of Pathology, Royal Alexandra Hospital, Edmonton, AB, Canada.
[Ti] Título:Undifferentiated and Dedifferentiated Endometrial Carcinomas With POLE Exonuclease Domain Mutations Have a Favorable Prognosis.
[So] Source:Am J Surg Pathol;41(8):1121-1128, 2017 Aug.
[Is] ISSN:1532-0979
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:POLE exonuclease domain mutations have recently been described in undifferentiated endometrial carcinoma but, because of the rarity of this aggressive type of endometrial cancer, their prognostic significance is unknown. We have analyzed the immunophenotype (ARID1A, MLH1, PMS2, MSH2, MSH6, p53, ß-catenin, and SMARCB1) and mutational status (POLE, PIK3CA, and PTEN) of 21 undifferentiated carcinomas (8 undifferentiated and 13 dedifferentiated carcinomas). Loss of ARID1A expression was observed in 9 of 19 cases (47%), loss of expression of at least 1 DNA mismatch repair protein in 7 (7/21; 33%), and p53 immunoreaction was aberrant (mutated/inactivated) in 11 cases (11/21; 52%). All tumors were negative for ß-catenin. Normal nuclear SMARCB1 (INI1) staining was found in all but 1 dedifferentiated case. Two undifferentiated and 7 dedifferentiated carcinomas showed POLE exonuclease domain mutations (9/21; 42%). PIK3CA mutations occurred in six tumors (6/21; 28%) (2 undifferentiated and 4 dedifferentiated carcinomas). PTEN mutations were found in 7 of 15 cases (47%) (4 undifferentiated and 3 dedifferentiated carcinomas). POLE-mutated undifferentiated and dedifferentiated endometrial carcinomas were more frequently stage I tumors than similar carcinomas lacking exonuclease domain mutations (7/9; 78% vs. 3/12; 25%; P=0.023) and patients had significantly better outcome (disease-specific survival) than those without POLE exonuclease domain mutations (P=0.02). Determination of the POLE mutation status is important for the management of these patients.
[Mh] Termos MeSH primário: Carcinoma/genética
Carcinoma/patologia
Desdiferenciação Celular
DNA Polimerase II/genética
Neoplasias do Endométrio/genética
Neoplasias do Endométrio/patologia
Mutação
[Mh] Termos MeSH secundário: Adulto
Idoso
Exonucleases
Feminino
Seres Humanos
Meia-Idade
Proteínas de Ligação a Poli-ADP-Ribose
Prognóstico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Poly-ADP-Ribose Binding Proteins); EC 2.7.7.- (DNA Polymerase II); EC 2.7.7.7 (POLE protein, human); EC 3.1.- (Exonucleases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170513
[St] Status:MEDLINE
[do] DOI:10.1097/PAS.0000000000000873



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