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  1 / 1866 MEDLINE  
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[PMID]:27776974
[Au] Autor:Shears SB; Baughman BM; Gu C; Nair VS; Wang H
[Ad] Endereço:Laboratory of Signal Transduction, National Institute of Environmental Health Sciences, National Institutes of Health, 101 T.W. Alexander Drive, Research Triangle Park, NC, 27709, USA. Electronic address: shears@niehs.nih.gov.
[Ti] Título:The significance of the 1-kinase/1-phosphatase activities of the PPIP5K family.
[So] Source:Adv Biol Regul;63:98-106, 2017 Jan.
[Is] ISSN:2212-4934
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The inositol pyrophosphates (diphosphoinositol polyphosphates), which include 1-InsP , 5-InsP , and InsP , are highly 'energetic' signaling molecules that play important roles in many cellular processes, particularly with regards to phosphate and bioenergetic homeostasis. Two classes of kinases synthesize the PP-InsPs: IP6Ks and PPIP5Ks. The significance of the IP6Ks - and their 5-InsP product - has been widely reported. However, relatively little is known about the biological significance of the PPIP5Ks. The purpose of this review is to provide an update on developments in our understanding of key features of the PPIP5Ks, which we believe strengthens the hypothesis that their catalytic activities serve important cellular functions. Central to this discussion is the recent discovery that the PPIP5K is a rare example of a single protein that catalyzes a kinase/phosphatase futile cycle.
[Mh] Termos MeSH primário: Hidrolases Anidrido Ácido/metabolismo
Fosfatos de Inositol/metabolismo
Fosfotransferases (Aceptor do Grupo Fosfato)/metabolismo
Ácido Fítico/metabolismo
[Mh] Termos MeSH secundário: Hidrolases Anidrido Ácido/genética
Motivos de Aminoácidos
Metabolismo Energético/genética
Regulação da Expressão Gênica
Seres Humanos
Fosfotransferases (Aceptor do Grupo Fosfato)/química
Fosfotransferases (Aceptor do Grupo Fosfato)/genética
Domínios Proteicos
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Inositol Phosphates); 0 (inositol heptakisphosphate); 7IGF0S7R8I (Phytic Acid); EC 2.7.4.- (Phosphotransferases (Phosphate Group Acceptor)); EC 2.7.4.21 (PPIP5K1 protein, human); EC 3.6.- (Acid Anhydride Hydrolases); EC 3.6.1.- (diphosphoinositol polyphosphate phosphohydrolase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE


  2 / 1866 MEDLINE  
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[PMID]:27773744
[Au] Autor:Schrock MS; Karras JR; Guggenbiller MJ; Druck T; Batar B; Huebner K
[Ad] Endereço:Department of Cancer Biology and Genetics, The Ohio State University Wexner Medical Center, Columbus, OH, USA.
[Ti] Título:Fhit and Wwox loss-associated genome instability: A genome caretaker one-two punch.
[So] Source:Adv Biol Regul;63:167-176, 2017 Jan.
[Is] ISSN:2212-4934
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Expression of Fhit and Wwox protein is frequently lost or reduced in many human cancers. In this report, we provide data that further characterizes the molecular consequences of Fhit loss in the initiation of DNA double-strand breaks (DSBs), and of Wwox loss in altered repair of DSBs. We show that loss of Fhit initiates mild genome instability in early passage mouse kidney cells, confirming that DNA damage associated with Fhit-deficiency is not limited to cancer cells. We also demonstrate that the cause of Fhit-deficient DSBs: thymidine deficiency-induced replication stress, can be resolved with thymidine supplementation in early passage mouse kidney cells before extensive genome instability occurs. As for consequences of Wwox loss in cancer, we show in a small panel of breast cancer cells and mouse embryonic fibroblasts that Wwox expression predicts response to radiation and mitomycin C, all agents that cause DSBs. In addition, loss of Wwox significantly reduced progression free survival in a cohort of ovarian cancer patients treated with platin-based chemotherapies. Finally, stratification of a cohort of squamous lung cancers by Fhit expression reveals that Wwox expression is significantly reduced in the low Fhit-expressing group, suggesting that loss of Fhit is quickly succeeded by loss of Wwox. We propose that Fhit and Wwox loss work synergistically in cancer progression and that DNA damage caused by Fhit could be targeted early in cancer initiation for prevention, while DNA damage caused by Wwox loss could be targeted later in cancer progression, particularly in cancers that develop resistance to genotoxic therapies.
[Mh] Termos MeSH primário: Hidrolases Anidrido Ácido/genética
Neoplasias da Mama/genética
Regulação Neoplásica da Expressão Gênica
Instabilidade Genômica
Neoplasias Pulmonares/genética
Proteínas de Neoplasias/genética
Neoplasias Ovarianas/genética
Proteínas Supressoras de Tumor/genética
Oxidorredutase com Domínios WW/genética
[Mh] Termos MeSH secundário: Hidrolases Anidrido Ácido/deficiência
Animais
Antineoplásicos/uso terapêutico
Neoplasias da Mama/tratamento farmacológico
Neoplasias da Mama/mortalidade
Neoplasias da Mama/patologia
Quebras de DNA de Cadeia Dupla
Reparo do DNA
DNA de Neoplasias/genética
DNA de Neoplasias/metabolismo
Feminino
Seres Humanos
Neoplasias Pulmonares/tratamento farmacológico
Neoplasias Pulmonares/mortalidade
Neoplasias Pulmonares/patologia
Camundongos
Proteínas de Neoplasias/deficiência
Neoplasias Ovarianas/tratamento farmacológico
Neoplasias Ovarianas/mortalidade
Neoplasias Ovarianas/patologia
Transdução de Sinais
Análise de Sobrevida
Proteínas Supressoras de Tumor/deficiência
Oxidorredutase com Domínios WW/deficiência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (DNA, Neoplasm); 0 (Neoplasm Proteins); 0 (Tumor Suppressor Proteins); 0 (fragile histidine triad protein); EC 1.1.1.- (WW Domain-Containing Oxidoreductase); EC 1.1.1.- (WWOX protein, human); EC 3.6.- (Acid Anhydride Hydrolases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


  3 / 1866 MEDLINE  
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[PMID]:29095316
[Au] Autor:Suh Y; Lee C
[Ad] Endereço:Department of Bioinformatics and Life Science, Soongsil University, Seoul, Korea.
[Ti] Título:Genome-wide association study for genetic variants related with maximal voluntary ventilation reveals two novel genomic signals associated with lung function.
[So] Source:Medicine (Baltimore);96(44):e8530, 2017 Nov.
[Is] ISSN:1536-5964
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Genome-wide association studies (GWAS) for spirometry parameters have been limited to forced vital capacity (FVC), forced expiratory volume in 1 second (FEV1), and their ratio. This study examined to identify genetic variants associated with maximal voluntary ventilation (MVV), an important spirometry parameter presenting inspiratory muscle strength.A total of 8842 Korean subjects participated in the Korean Association REsource Consortium were used to identify nucleotide variants associated with MVV and other spirometry parameters through a GWAS. Genetic associations were determined by employing a mixed model that can control background polygenic effects.The analysis revealed 3 nucleotide variants associated with MVV (P < 5 × 10). One (rs1496255) was also associated with FVC and FEV1. The other 2 variants were identified only for MVV and located in the genes of LOC102724340 (rs41434646) and FHIT (rs9833533). In particular, FHIT represses transcriptional activity of ß-catenin, a critical protein for growth of skeletal muscle, and thus might have influenced the level of MVV.The current study revealed 2 novel nucleotide variants as genetic association signals for MVV. The association signals were suggested specific for neuromuscular diseases with a restrictive ventilatory impairment. Further studies are required to understand underlying mechanisms for their influence to restrictive lung diseases.
[Mh] Termos MeSH primário: Hidrolases Anidrido Ácido/genética
Grupo com Ancestrais do Continente Asiático/genética
Variação Genética
Pneumopatias/genética
Ventilação Voluntária Máxima/genética
Proteínas de Neoplasias/genética
[Mh] Termos MeSH secundário: Proteínas de Transporte/genética
Feminino
Volume Expiratório Forçado/genética
Estudo de Associação Genômica Ampla
Seres Humanos
Pulmão/fisiologia
Masculino
Glicoproteínas de Membrana/genética
República da Coreia
Espirometria/métodos
Capacidade Vital/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (HHIP protein, human); 0 (Membrane Glycoproteins); 0 (Neoplasm Proteins); 0 (fragile histidine triad protein); EC 3.6.- (Acid Anhydride Hydrolases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:171103
[St] Status:MEDLINE
[do] DOI:10.1097/MD.0000000000008530


  4 / 1866 MEDLINE  
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[PMID]:28808133
[Au] Autor:Bowden KE; Wiese NS; Perwez T; Mohanty BK; Kushner SR
[Ad] Endereço:Department of Genetics, University of Georgia, Athens, Georgia, USA.
[Ti] Título:The -Encoded Truncated RNase PH Protein Inhibits RNase P Maturation of Pre-tRNAs with Short Leader Sequences in the Absence of RppH.
[So] Source:J Bacteriol;199(22), 2017 Nov 15.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:RNase PH, encoded by the gene, is a 3'→5' exoribonuclease that in participates primarily in the 3' maturation of pre-tRNAs and the degradation of rRNA in stationary-phase cells. Interestingly, the routinely used laboratory strains of MG1655 and W3110 have naturally acquired the allele, encoding a truncated catalytically inactive RNase PH protein which is widely assumed to be benign. Contrary to this assumption, we show that the -encoded Rph-1 protein inhibits RNase P-mediated 5'-end maturation of primary pre-tRNAs with leaders of <5 nucleotides in the absence of RppH, an RNA pyrophosphohydrolase. In contrast, RppH is not required for 5'-end maturation of endonucleolytically generated pre-tRNAs in the strain and for any tRNAs in Δ mutant or strains. We propose that the Rph-1 protein bound to the 3' end of the substrate creates a steric hindrance that in the presence of a triphosphate at the 5' end reduces the ability of RNase P to bind to the pre-tRNA. In this paper, we demonstrate that the mutation found in commonly used strains leads to the synthesis of a truncated functionally inactive RNase PH protein that interferes with the 5'-end maturation of specific tRNAs with short 5' leaders by RNase P in the absence of RppH, an RNA pyrophosphohydrolase that converts primary 5' triphosphates into 5' monophosphates. The data presented indicate that the presence of the triphosphate interferes with RNase P binding to the pre-tRNA.
[Mh] Termos MeSH primário: Hidrolases Anidrido Ácido/genética
Hidrolases Anidrido Ácido/metabolismo
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Exorribonucleases/genética
RNA de Transferência/metabolismo
Ribonuclease P/metabolismo
[Mh] Termos MeSH secundário: Endorribonucleases/genética
Endorribonucleases/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Exorribonucleases/metabolismo
Mutação
Sinais Direcionadores de Proteínas
Precursores de RNA/química
Precursores de RNA/genética
Precursores de RNA/metabolismo
Processamento Pós-Transcricional do RNA
RNA Bacteriano/genética
RNA Bacteriano/metabolismo
RNA de Transferência/química
RNA de Transferência/genética
Ribonuclease P/genética
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Protein Sorting Signals); 0 (RNA Precursors); 0 (RNA, Bacterial); 9014-25-9 (RNA, Transfer); EC 2.7.7.56 (ribonuclease PH); EC 3.1.- (Endoribonucleases); EC 3.1.- (Exoribonucleases); EC 3.1.26.5 (Ribonuclease P); EC 3.1.4.- (ribonuclease E); EC 3.6.- (Acid Anhydride Hydrolases); EC 3.6.1.- (RppH protein, E coli)
[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:170816
[St] Status:MEDLINE


  5 / 1866 MEDLINE  
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[PMID]:28673541
[Au] Autor:Luciano DJ; Vasilyev N; Richards J; Serganov A; Belasco JG
[Ad] Endereço:Kimmel Center for Biology and Medicine at the Skirball Institute, New York University School of Medicine, 540 First Avenue, New York, NY 10016, USA; Department of Microbiology, New York University School of Medicine, 540 First Avenue, New York, NY 10016, USA.
[Ti] Título:A Novel RNA Phosphorylation State Enables 5' End-Dependent Degradation in Escherichia coli.
[So] Source:Mol Cell;67(1):44-54.e6, 2017 07 06.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:RNA modifications that once escaped detection are now thought to be pivotal for governing RNA lifetimes in both prokaryotes and eukaryotes. For example, converting the 5'-terminal triphosphate of bacterial transcripts to a monophosphate triggers 5' end-dependent degradation by RNase E. However, the existence of diphosphorylated RNA in bacteria has never been reported, and no biological role for such a modification has ever been proposed. By using a novel assay, we show here for representative Escherichia coli mRNAs that ~35%-50% of each transcript is diphosphorylated. The remainder is primarily monophosphorylated, with surprisingly little triphosphorylated RNA evident. Furthermore, diphosphorylated RNA is the preferred substrate of the RNA pyrophosphohydrolase RppH, whose biological function was previously assumed to be pyrophosphate removal from triphosphorylated transcripts. We conclude that triphosphate-to-monophosphate conversion to induce 5' end-dependent RNA degradation is a two-step process in E. coli involving γ-phosphate removal by an unidentified enzyme to enable subsequent ß-phosphate removal by RppH.
[Mh] Termos MeSH primário: Hidrolases Anidrido Ácido/metabolismo
Proteínas de Escherichia coli/metabolismo
Escherichia coli/enzimologia
Processamento Pós-Transcricional do RNA
Estabilidade de RNA
RNA Bacteriano/metabolismo
RNA Mensageiro/metabolismo
[Mh] Termos MeSH secundário: Hidrolases Anidrido Ácido/genética
Difosfato de Adenosina/metabolismo
Trifosfato de Adenosina/metabolismo
Endorribonucleases/metabolismo
Escherichia coli/genética
Proteínas de Escherichia coli/genética
Fosforilação
RNA Bacteriano/genética
RNA Mensageiro/genética
Especificidade por Substrato
Fatores de Tempo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (RNA, Bacterial); 0 (RNA, Messenger); 61D2G4IYVH (Adenosine Diphosphate); 8L70Q75FXE (Adenosine Triphosphate); EC 3.1.- (Endoribonucleases); EC 3.1.4.- (ribonuclease E); EC 3.6.- (Acid Anhydride Hydrolases); EC 3.6.1.- (RppH protein, E coli)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170705
[St] Status:MEDLINE


  6 / 1866 MEDLINE  
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[PMID]:28643453
[Au] Autor:Lange S; Hacker SM; Schmid P; Scheffner M; Marx A
[Ad] Endereço:Department of Chemistry, Konstanz Research School-Chemical Biology, University of Konstanz, Universitätsstrasse 10, 78457, Konstanz, Germany.
[Ti] Título:Small-Molecule Inhibitors of the Tumor Suppressor Fhit.
[So] Source:Chembiochem;18(17):1707-1711, 2017 Sep 05.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The tumor suppressor Fhit and its substrate diadenosine triphosphate (Ap A) are important factors in cancer development and progression. Fhit has Ap A hydrolase activity and cleaves Ap A into adenosine monophosphate (AMP) and adenosine diphosphate (ADP); this is believed to terminate Fhit-mediated signaling. How the catalytic activity of Fhit is regulated and how the Fhitâ‹…Ap A complex might exert its growth-suppressive function remain to be discovered. Small-molecule inhibitors of the enzymatic activity of Fhit would provide valuable tools for the elucidation of its tumor-suppressive functions. Here we describe the development of a high-throughput screen for the identification of such small-molecule inhibitors of Fhit. Two clusters of inhibitors that decreased the activity of Fhit by at least 90 % were identified. Several derivatives were synthesized and exhibited in vitro IC values in the nanomolar range.
[Mh] Termos MeSH primário: Hidrolases Anidrido Ácido/metabolismo
Proteínas de Neoplasias/metabolismo
Bibliotecas de Moléculas Pequenas/metabolismo
[Mh] Termos MeSH secundário: Hidrolases Anidrido Ácido/antagonistas & inibidores
Linhagem Celular Tumoral
Sobrevivência Celular/efeitos dos fármacos
Transferência Ressonante de Energia de Fluorescência
Células HEK293
Seres Humanos
Concentração Inibidora 50
Proteínas de Neoplasias/antagonistas & inibidores
Ligação Proteica
Quinolonas/química
Quinolonas/metabolismo
Quinolonas/toxicidade
Bibliotecas de Moléculas Pequenas/química
Bibliotecas de Moléculas Pequenas/toxicidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Neoplasm Proteins); 0 (Quinolones); 0 (Small Molecule Libraries); 0 (fragile histidine triad protein); EC 3.6.- (Acid Anhydride Hydrolases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170624
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700226


  7 / 1866 MEDLINE  
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[PMID]:28639889
[Au] Autor:Shu R; He J; Wu C; Gao J
[Ad] Endereço:Department of Gynaecology and Obstetrics, The Third Affiliated Hospital of Nanchang University, Nanchang, China.
[Ti] Título:The association between RARß and FHIT promoter methylation and the carcinogenesis of patients with cervical carcinoma: A meta-analysis.
[So] Source:Tumour Biol;39(6):1010428317709126, 2017 Jun.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The RARß and FHIT promoter methylation are observed in some cervical carcinoma. However, the association between RARß and FHIT promoter methylation and cervical carcinogenesis remains unclear. This study was carried out to evaluate the correlation between RARß or FHIT promoter methylation and cervical carcinogenesis. Eligible publications were searched via online databases. The combined odds ratios and corresponding 95% confidence intervals were calculated and summarized. In all, 17 eligible articles on RARß and FHIT promoter methylation were identified in the study. RARß promoter methylation was significantly higher in cervical cancer than in cervical intraepithelial neoplasia lesions and normal cervical tissues (odds ratio = 3.90, p = 0.018; odds ratio = 12.98, p < 0.001, respectively). There was more FHIT promoter methylation in cervical cancer than in cervical intraepithelial neoplasia lesions and normal controls (odds ratio = 8.0, p = 0.055; odds ratio = 10.75, p < 0.001, respectively). In addition, FHIT promoter methylation was correlated with clinical stage (advanced stage vs early stage: odds ratio = 2.69, p = 0.056) and tumor grade (high grade vs low grade: odds ratio = 4.11, p < 0.001). RARß and FHIT promoter methylation may be associated with the carcinogenesis of cervical cancer. FHIT promoter methylation may play a crucial role in cervical cancer progression. Additional studies with large sample sizes are essential to confirm our findings.
[Mh] Termos MeSH primário: Hidrolases Anidrido Ácido/genética
Metilação de DNA/genética
Proteínas de Neoplasias/genética
Receptores do Ácido Retinoico/genética
Neoplasias do Colo do Útero/genética
[Mh] Termos MeSH secundário: Carcinogênese/genética
Neoplasia Intraepitelial Cervical
Progressão da Doença
Feminino
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Regiões Promotoras Genéticas
Neoplasias do Colo do Útero/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; META-ANALYSIS
[Nm] Nome de substância:
0 (Neoplasm Proteins); 0 (Receptors, Retinoic Acid); 0 (fragile histidine triad protein); 0 (retinoic acid receptor beta); EC 3.6.- (Acid Anhydride Hydrolases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170623
[St] Status:MEDLINE
[do] DOI:10.1177/1010428317709126


  8 / 1866 MEDLINE  
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[PMID]:28636911
[Au] Autor:Elia F; Cantini F; Chiti F; Dobson CM; Bemporad F
[Ad] Endereço:Department of Experimental and Clinical Biomedical Sciences "Mario Serio," University of Florence, Firenze, Italy.
[Ti] Título:Direct Conversion of an Enzyme from Native-like to Amyloid-like Aggregates within Inclusion Bodies.
[So] Source:Biophys J;112(12):2540-2551, 2017 Jun 20.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The acylphosphatase from Sulfolobus solfataricus (Sso AcP) is a globular protein able to aggregate in vitro from a native-like conformational ensemble without the need for a transition across the major unfolding energy barrier. This process leads to the formation of assemblies in which the protein retains its native-like structure, which subsequently convert into amyloid-like aggregates. Here, we investigate the mechanism by which Sso AcP aggregates in vivo to form bacterial inclusion bodies after expression in E. coli. Shortly after the initiation of expression, Sso AcP is incorporated into inclusion bodies as a native-like protein, still exhibiting small but significant enzymatic activity. Additional experiments revealed that this overall process of aggregation is enhanced by the presence of the unfolded N-terminal region of the sequence and by destabilization of the globular segment of the protein. At later times, the Sso AcP molecules in the inclusion bodies lose their native-like properties and convert into ß-sheet-rich amyloid-like structures, as indicated by their ability to bind thioflavin T and Congo red. These results show that the aggregation behavior of this protein is similar in vivo to that observed in vitro, and that, at least for a predominant part of the protein population, the transition from a native to an amyloid-like structure occurs within the aggregate state.
[Mh] Termos MeSH primário: Hidrolases Anidrido Ácido/química
Proteínas Arqueais/química
Corpos de Inclusão/enzimologia
Agregados Proteicos
Sulfolobus solfataricus/enzimologia
[Mh] Termos MeSH secundário: Hidrolases Anidrido Ácido/genética
Hidrolases Anidrido Ácido/metabolismo
Amiloide/química
Amiloide/metabolismo
Proteínas Arqueais/metabolismo
Eletroforese em Gel de Poliacrilamida
Estabilidade Enzimática
Escherichia coli
Mutação
Ressonância Magnética Nuclear Biomolecular
Agregação Patológica de Proteínas
Dobramento de Proteína
Estrutura Secundária de Proteína
Espectroscopia de Infravermelho com Transformada de Fourier
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amyloid); 0 (Archaeal Proteins); 0 (Protein Aggregates); EC 3.6.- (Acid Anhydride Hydrolases); EC 3.6.1.7 (acylphosphatase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170823
[Lr] Data última revisão:
170823
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170622
[St] Status:MEDLINE


  9 / 1866 MEDLINE  
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[PMID]:28516732
[Au] Autor:Despotovic D; Brandis A; Savidor A; Levin Y; Fumagalli L; Tawfik DS
[Ad] Endereço:Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, Israel.
[Ti] Título:Diadenosine tetraphosphate (Ap4A) - an E. coli alarmone or a damage metabolite?
[So] Source:FEBS J;284(14):2194-2215, 2017 Jul.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Under stress, metabolism is changing: specific up- or down-regulation of proteins and metabolites occurs as well as side effects. Distinguishing specific stress-signaling metabolites (alarmones) from side products (damage metabolites) is not trivial. One example is diadenosine tetraphosphate (Ap4A) - a side product of aminoacyl-tRNA synthetases found in all domains of life. The earliest observations suggested that Ap4A serves as an alarmone for heat stress in Escherichia coli. However, despite 50 years of research, the signaling mechanisms associated with Ap4A remain unknown. We defined a set of criteria for distinguishing alarmones from damage metabolites to systematically classify Ap4A. In a nutshell, no indications for a signaling cascade that is triggered by Ap4A were found; rather, we found that Ap4A is efficiently removed in a constitutive, nonregulated manner. Several fold perturbations in Ap4A concentrations have no effect, yet accumulation at very high levels is toxic due to disturbance of zinc homeostasis, and also because Ap4A's structural overlap with ATP can result in spurious binding and inactivation of ATP-binding proteins. Overall, Ap4A met all criteria for a damage metabolite. While we do not exclude any role in signaling, our results indicate that the damage metabolite option should be considered as the null hypothesis when examining Ap4A and other metabolites whose levels change upon stress.
[Mh] Termos MeSH primário: Fosfatos de Dinucleosídeos/metabolismo
Escherichia coli/metabolismo
Estresse Fisiológico
[Mh] Termos MeSH secundário: Hidrolases Anidrido Ácido/genética
Hidrolases Anidrido Ácido/metabolismo
Escherichia coli/genética
Escherichia coli/crescimento & desenvolvimento
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Regulação Bacteriana da Expressão Gênica
Homeostase
Lisina-tRNA Ligase/genética
Lisina-tRNA Ligase/metabolismo
Transdução de Sinais
Zinco/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dinucleoside Phosphates); 0 (Escherichia coli Proteins); 5542-28-9 (diadenosine tetraphosphate); EC 3.6.- (Acid Anhydride Hydrolases); EC 3.6.1.- (ApaH protein, E coli); EC 6.1.1.6 (Lysine-tRNA Ligase); J41CSQ7QDS (Zinc)
[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:170519
[St] Status:MEDLINE
[do] DOI:10.1111/febs.14113


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[PMID]:28414756
[Au] Autor:Wang L; Shen H; Feng B; Zhu D; Yu L; Tian X; Ren C; Gao C; Li X; Ma D; Hu Z; Wang H
[Ad] Endereço:Key Laboratory of Cancer Invasion and Metastasis of the Ministry of Education, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, Hubei, China.
[Ti] Título:Reduction in the copy number and expression level of the recurrent human papillomavirus integration gene fragile histidine triad (FHIT) predicts the transition of cervical lesions.
[So] Source:PLoS One;12(4):e0175520, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cervical cancer is the second most common cancer and the third leading cause of cancer death in females worldwide, especially in developing countries. High risk human papillomavirus (HR-HPV) infection causes cervical cancer and precancerous cervical intraepithelial neoplasia (CIN). Integration of the HR-HPV genome into the host chromatin is an important step in cervical carcinogenesis. The detection of integrated papillomavirus sequences-PCR (DIPS-PCR) allowed us to explore HPV integration in the human genome and to determine the pattern of this integration. We performed DIPS-PCR for 4 cell lines including 3 cervical cancer cell lines and 40 tissue samples. Overall, 32 HR-HPV integration loci were detected in the clinical samples and the HeLa and SiHa cell lines. Among all the integration loci, we identified three recurrent integration loci: 3p14.2 (3 samples), 13q22.1 (2 samples and a SiHa cell line) and 8q24 (1 sample and a HeLa cell line). To further explore the effect of HR-HPV integration in the 3p14.2 locus, we used fluorescence in situ hybridization (FISH) to determine the copy number of the 3p14.2 locus and immunohistochemistry (IHC) to determine the protein expression levels of the related FHIT gene in the clinical samples. Both the 3p14.2 locus copy number and FHIT protein expression levels showed significant decreases when CIN transitioned to cervical cancer. HPV copy number was also evaluated in these clinical samples, and the copy number of HPV increased significantly between CIN and cervical cancer samples. Finally, we employed receiver operating characteristic curve (ROC curve) analysis to evaluate the potential of all these indexes in distinguishing CIN and cervical cancer, and the HPV copy number, FHIT copy number and FHIT protein expression levels have good diagnostic efficiencies.
[Mh] Termos MeSH primário: Hidrolases Anidrido Ácido/genética
Dosagem de Genes/genética
Proteínas de Neoplasias/genética
Papillomaviridae/genética
Infecções por Papillomavirus/genética
Neoplasias do Colo do Útero/genética
[Mh] Termos MeSH secundário: Adulto
Linhagem Celular Tumoral
Neoplasia Intraepitelial Cervical/genética
Neoplasia Intraepitelial Cervical/virologia
DNA Viral/genética
Feminino
Células HeLa
Seres Humanos
Imuno-Histoquímica/métodos
Hibridização in Situ Fluorescente/métodos
Meia-Idade
Infecções por Papillomavirus/virologia
Neoplasias do Colo do Útero/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Viral); 0 (Neoplasm Proteins); 0 (fragile histidine triad protein); EC 3.6.- (Acid Anhydride Hydrolases)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170505
[Lr] Data última revisão:
170505
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170418
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0175520



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