Base de dados : MEDLINE
Pesquisa : G05.360.600.300 [Categoria DeCS]
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  1 / 1013 MEDLINE  
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[PMID]:27777078
[Au] Autor:Chandler JC; Pérez-Méndez A; Paar J; Doolittle MM; Bisha B; Goodridge LD
[Ad] Endereço:National Wildlife Research Center, Wildlife Services, Animal and Plant Health Inspection Service, United States Department of Agriculture, Fort Collins, CO, USA.
[Ti] Título:Field-based evaluation of a male-specific (F+) RNA coliphage concentration method.
[So] Source:J Virol Methods;239:9-16, 2017 01.
[Is] ISSN:1879-0984
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Fecal contamination of water poses a significant risk to public health due to the potential presence of pathogens, including enteric viruses. Therefore, sensitive, reliable and easy to use methods for the concentration, detection and quantification of microorganisms associated with the safety and quality of water are needed. In this study, we performed a field evaluation of an anion exchange resin-based method to concentrate male-specific (F+) RNA coliphages (FRNA), fecal indicator organisms, from diverse environmental waters that were suspected to be contaminated with feces. In this system, FRNA coliphages are adsorbed to anion exchange resin and direct nucleic acid isolation is performed, yielding a sample amenable to real-time reverse transcriptase (RT)-PCR detection. Matrix-dependent inhibition of this method was evaluated using known quantities of spiked FRNA coliphages belonging to four genogroups (GI, GII, GII and GIV). RT-PCR-based detection was successful in 97%, 72%, 85% and 98% of the samples spiked (10 pfu/l) with GI, GII, GIII and GIV, respectively. Differential FRNA coliphage genogroup detection was linked to inhibitors that altered RT-PCR assay efficiency. No association between inhibition and the physicochemical properties of the water samples was apparent. Additionally, the anion exchange resin method facilitated detection of naturally present FRNA coliphages in 40 of 65 environmental water samples (61.5%), demonstrating the viability of this system to concentrate FRNA coliphages from water.
[Mh] Termos MeSH primário: Resinas de Troca de Ânions
Colífagos/isolamento & purificação
Leviviridae/isolamento & purificação
Microbiologia da Água
Poluição da Água
[Mh] Termos MeSH secundário: Adsorção
Resinas de Troca de Ânions/economia
Colífagos/química
Colífagos/genética
Colífagos/fisiologia
Monitoramento Ambiental/métodos
Fator F
Fezes/virologia
Seres Humanos
Leviviridae/química
Leviviridae/genética
Leviviridae/fisiologia
RNA Viral/genética
Reação em Cadeia da Polimerase em Tempo Real
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Poluição da Água/análise
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Anion Exchange Resins); 0 (RNA, Viral)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171222
[Lr] Data última revisão:
171222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161107
[St] Status:MEDLINE


  2 / 1013 MEDLINE  
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[PMID]:28370625
[Au] Autor:Olejniczak M; Storz G
[Ad] Endereço:Institute of Molecular Biology and Biotechnology, Faculty of Biology, Adam Mickiewicz University, Umultowska 89, Poznan, 61-614, Poland.
[Ti] Título:ProQ/FinO-domain proteins: another ubiquitous family of RNA matchmakers?
[So] Source:Mol Microbiol;104(6):905-915, 2017 Jun.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Small RNAs (sRNAs), particularly those that act by limited base pairing with mRNAs, are part of most regulatory networks in bacteria. In many cases, the base-pairing interaction is facilitated by the RNA chaperone Hfq. However, not all bacteria encode Hfq and some base-pairing sRNAs do not require Hfq raising the possibility of other RNA chaperones. Candidates are proteins with homology to FinO, a factor that promotes base pairing between the FinP antisense sRNA and the traJ mRNA to control F plasmid transfer. Recent papers have shown that the Salmonella enterica FinO-domain protein ProQ binds a large suite of sRNAs, including the RaiZ sRNA, which represses translation of the hupA mRNA, and the Legionella pneumophila protein RocC binds the RocR sRNA, which blocks expression of competence genes. Here we discuss what is known about FinO-domain structures, including the recently solved Escherichia coli ProQ structure, as well as the RNA binding properties of this family of proteins and evidence they act as chaperones. We compare these properties with those of Hfq. We further summarize what is known about the physiological roles of FinO-domain proteins and enumerate outstanding questions whose answers will establish whether they constitute a second major class of RNA chaperones.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/metabolismo
Proteínas de Escherichia coli/fisiologia
Proteínas de Ligação a RNA/metabolismo
Proteínas de Ligação a RNA/fisiologia
Proteínas Repressoras/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas da Membrana Bacteriana Externa/metabolismo
Proteínas de Bactérias/metabolismo
Sequência Conservada
Escherichia coli/genética
Escherichia coli/metabolismo
Fator F
Chaperonas Moleculares/metabolismo
Conformação de Ácido Nucleico
Domínios Proteicos
RNA Antissenso/metabolismo
RNA Bacteriano/metabolismo
RNA Mensageiro/metabolismo
Proteínas Repressoras/fisiologia
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Bacterial Outer Membrane Proteins); 0 (Bacterial Proteins); 0 (Escherichia coli Proteins); 0 (Molecular Chaperones); 0 (ProQ protein, E coli); 0 (RNA, Antisense); 0 (RNA, Bacterial); 0 (RNA, Messenger); 0 (RNA-Binding Proteins); 0 (Repressor Proteins); 146889-94-3 (FinO protein, E coli)
[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:170404
[St] Status:MEDLINE
[do] DOI:10.1111/mmi.13679


  3 / 1013 MEDLINE  
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[PMID]:28356461
[Au] Autor:Wolters FJ; van der Lee SJ; Koudstaal PJ; van Duijn CM; Hofman A; Ikram MK; Vernooij MW; Ikram MA
[Ad] Endereço:Departments of Epidemiology (F.J.W., S.J.v.d.L., C.M.v.D., A.H., M.K.I., M.W.V., M.A.I.), Neurology (F.J.W., P.J.K., M.K.I., M.A.I.), and Radiology and Nuclear Medicine (M.W.V., M.A.I.), Erasmus Medical Centre, Rotterdam, the Netherlands; and Department of Epidemiology (F.J.W., A.H.), Harvard T.H. C
[Ti] Título:Parental family history of dementia in relation to subclinical brain disease and dementia risk.
[So] Source:Neurology;88(17):1642-1649, 2017 Apr 25.
[Is] ISSN:1526-632X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To determine the association of parental family history with risk of dementia by age at onset and sex of affected parent in a population-based cohort. METHODS: From 2000 to 2002, we assessed parental history of dementia in participants without dementia of the Rotterdam Study. We investigated associations of parental history with risk of dementia until 2015, adjusting for demographics, cardiovascular risk factors, and known genetic risk variants. Furthermore, we determined the association between parental history and markers of neurodegeneration and vascular disease on MRI. RESULTS: Of 2,087 participants (mean age 64 years, 55% female), 407 (19.6%) reported a history of dementia in either parent (mean age at diagnosis 79 years). During a mean follow-up of 12.2 years, 142 participants developed dementia. Parental history was associated with risk of dementia independently of known genetic risk factors (hazard ratio [HR] 1.67, 95% confidence interval [CI] 1.12-2.48), in particular when parents were diagnosed at younger age (<80 years: HR 2.58, 95% CI 1.61-4.15; ≥80 years: HR 1.01, 95% CI 0.58-1.77). Accordingly, age at diagnosis in probands was highly correlated with age at diagnosis in their parents <80 years ( = 0.57, = 0.001) but not thereafter ( = 0.17, = 0.55). Among 1,161 participants without dementia with brain MRI, parental history was related to lower cerebral perfusion and higher burden of white matter lesions and microbleeds. Dementia risk and MRI markers were similar for paternal and maternal history. CONCLUSIONS: Parental history of dementia increases risk of dementia, primarily when age at parental diagnosis is <80 years. Unexplained heredity may be attributed in part to cerebral hypoperfusion and small vessel disease. We found no evidence of preferential maternal compared to paternal transmission.
[Mh] Termos MeSH primário: Demência/epidemiologia
Predisposição Genética para Doença
[Mh] Termos MeSH secundário: Idade de Início
Idoso
Apolipoproteínas E/genética
Encéfalo/diagnóstico por imagem
Doenças Cardiovasculares/epidemiologia
Estudos de Coortes
Demência/diagnóstico por imagem
Demência/genética
Fator F
Feminino
Seguimentos
Técnicas de Genotipagem
Seres Humanos
Imagem por Ressonância Magnética
Masculino
Meia-Idade
Pais
Fatores de Risco
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apolipoproteins E)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170331
[St] Status:MEDLINE
[do] DOI:10.1212/WNL.0000000000003871


  4 / 1013 MEDLINE  
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[PMID]:28302951
[Au] Autor:Tashiro Y; Eida H; Ishii S; Futamata H; Okabe S
[Ad] Endereço:Division of Environmental Engineering, Faculty of Engineering, Hokkaido University.
[Ti] Título:Generation of Small Colony Variants in Biofilms by Escherichia coli Harboring a Conjugative F Plasmid.
[So] Source:Microbes Environ;32(1):40-46, 2017 Mar 31.
[Is] ISSN:1347-4405
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:A conjugative F plasmid induces mature biofilm formation by Escherichia coli by promoting F-pili-mediated cell-cell interactions and increasing the expression of biofilm-related genes. We herein demonstrated another function for the F plasmid in E. coli biofilms; it contributes to the emergence of genetic and phenotypic variations by spontaneous mutations. Small colony variants (SCVs) were more frequently generated in a continuous flow-cell biofilm than in the planktonic state of E. coli harboring the F plasmid. E. coli SCVs represented typical phenotypic changes such as slower growth, less biofilm formation, and greater resistance to aminoglycoside antibiotics than the parent strain. Genomic and complementation analyses indicated that the small colony phenotype was caused by the insertion of Tn1000, which was originally localized in the F plasmid, into the hemB gene. Furthermore, the Tn1000 insertion was removed from hemB in the revertant, which showed a normal colony phenotype. This study revealed that the F plasmid has the potential to increase genetic variations not only by horizontal gene transfer via F pili, but also by site-specific recombination within a single cell.
[Mh] Termos MeSH primário: Biofilmes/crescimento & desenvolvimento
Escherichia coli/crescimento & desenvolvimento
Fator F
Fenótipo
[Mh] Termos MeSH secundário: Aminoglicosídeos/metabolismo
Antibacterianos/metabolismo
Biofilmes/efeitos dos fármacos
Elementos de DNA Transponíveis
Escherichia coli/efeitos dos fármacos
Escherichia coli/genética
Proteínas de Escherichia coli/genética
Teste de Complementação Genética
Variação Genética
Genoma Bacteriano
Mutagênese Insercional
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aminoglycosides); 0 (Anti-Bacterial Agents); 0 (DNA Transposable Elements); 0 (Escherichia coli Proteins)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170414
[Lr] Data última revisão:
170414
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170318
[St] Status:MEDLINE
[do] DOI:10.1264/jsme2.ME16121


  5 / 1013 MEDLINE  
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[PMID]:27907029
[Au] Autor:Yeom SJ; Lee DH; Kim YJ; Lee J; Kwon KK; Han GH; Kim H; Kim HS; Lee SG
[Ad] Endereço:Synthetic Biology & Bioengineering Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, Republic of Korea.
[Ti] Título:Long-Term Stable and Tightly Controlled Expression of Recombinant Proteins in Antibiotics-Free Conditions.
[So] Source:PLoS One;11(12):e0166890, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Plasmid-based gene expression is a fundamental tool in the field of biotechnology. However, overexpression of genes of interest with multi-copy plasmids often causes detrimental effects on host cells. To overcome this problem, chromosomal integration of target genes has been used for decades; however, insufficient protein expression occurred with this method. In this study, we developed a novel cloning and expression system named the chromosomal vector (ChroV) system, that has features of stable and high expression of target genes on the F' plasmid in the Escherichia coli JM109(DE3) strain. We used an RMT cluster (KCTC 11994BP) containing a silent cat gene from a previous study to clone a gene into the F' plasmid. The ChroV system was applied to clone two model targets, GFPuv and carotenoids gene clusters (4 kb), and successfully used to prove the inducible tightly regulated protein expression in the F' plasmid. In addition, we verified that the expression of heterologous genes in ChroV system maintained stably in the absence of antibiotics for 1 week, indicating ChroV system is applicable to antibiotics-free production of valuable proteins. This protocol can be widely applied to recombinant protein expression for antibiotics-free, stable, and genome-based expression, providing a new platform for recombinant protein synthesis in E. coli. Overall, our approach can be widely used for the economical and industrial production of proteins in E. coli.
[Mh] Termos MeSH primário: Cromossomos Bacterianos/metabolismo
Clonagem Molecular/métodos
Escherichia coli/genética
Fator F/metabolismo
[Mh] Termos MeSH secundário: Antibacterianos
Carotenoides/biossíntese
Cromossomos Bacterianos/química
Escherichia coli/metabolismo
Fator F/química
Genes Reporter
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Família Multigênica
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Recombinant Proteins); 147336-22-9 (Green Fluorescent Proteins); 36-88-4 (Carotenoids)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170627
[Lr] Data última revisão:
170627
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161202
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0166890


  6 / 1013 MEDLINE  
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[PMID]:27610568
[Au] Autor:Costa TRD; Ilangovan A; Ukleja M; Redzej A; Santini JM; Smith TK; Egelman EH; Waksman G
[Ad] Endereço:Institute of Structural and Molecular Biology, University College London and Birkbeck, Malet Street, London WC1E 7HX, UK.
[Ti] Título:Structure of the Bacterial Sex F Pilus Reveals an Assembly of a Stoichiometric Protein-Phospholipid Complex.
[So] Source:Cell;166(6):1436-1444.e10, 2016 Sep 08.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Conjugative pili are widespread bacterial appendages that play important roles in horizontal gene transfer, in spread of antibiotic resistance genes, and as sites of phage attachment. Among conjugative pili, the F "sex" pilus encoded by the F plasmid is the best functionally characterized, and it is also historically the most important, as the discovery of F-plasmid-mediated conjugation ushered in the era of molecular biology and genetics. Yet, its structure is unknown. Here, we present atomic models of two F family pili, the F and pED208 pili, generated from cryoelectron microscopy reconstructions at 5.0 and 3.6 Å resolution, respectively. These structures reveal that conjugative pili are assemblies of stoichiometric protein-phospholipid units. We further demonstrate that each pilus type binds preferentially to particular phospholipids. These structures provide the molecular basis for F pilus assembly and also shed light on the remarkable properties of conjugative pili in bacterial secretion and phage infection.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/química
Escherichia coli/fisiologia
Fator F/química
Fímbrias Bacterianas/química
Modelos Moleculares
Fosfolipídeos/química
[Mh] Termos MeSH secundário: Sítios de Ligação Microbiológicos/genética
Microscopia Crioeletrônica
Proteínas de Escherichia coli/metabolismo
Fator F/genética
Fímbrias Bacterianas/genética
Fímbrias Bacterianas/metabolismo
Lipídeos/química
Mutação
Fosfolipídeos/metabolismo
Ligação Proteica
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
Sistemas de Secreção Tipo V/química
Sistemas de Secreção Tipo V/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Lipids); 0 (Phospholipids); 0 (Protein Subunits); 0 (Type V Secretion Systems)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:171105
[Lr] Data última revisão:
171105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160910
[St] Status:MEDLINE


  7 / 1013 MEDLINE  
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[PMID]:27454336
[Au] Autor:Jarnuczak AF; Lee DC; Lawless C; Holman SW; Eyers CE; Hubbard SJ
[Ad] Endereço:Faculty of Biology, Medicine and Health, University of Manchester , Michael Smith Building, Oxford Road, Manchester M13 9PT, United Kingdom.
[Ti] Título:Analysis of Intrinsic Peptide Detectability via Integrated Label-Free and SRM-Based Absolute Quantitative Proteomics.
[So] Source:J Proteome Res;15(9):2945-59, 2016 Sep 02.
[Is] ISSN:1535-3907
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Quantitative mass spectrometry-based proteomics of complex biological samples remains challenging in part due to the variability and charge competition arising during electrospray ionization (ESI) of peptides and the subsequent transfer and detection of ions. These issues preclude direct quantification from signal intensity alone in the absence of a standard. A deeper understanding of the governing principles of peptide ionization and exploitation of the inherent ionization and detection parameters of individual peptides is thus of great value. Here, using the yeast proteome as a model system, we establish the concept of peptide F-factor as a measure of detectability, closely related to ionization efficiency. F-factor is calculated by normalizing peptide precursor ion intensity by absolute abundance of the parent protein. We investigated F-factor characteristics in different shotgun proteomics experiments, including across multiple ESI-based LC-MS platforms. We show that F-factors mirror previously observed physicochemical predictors as peptide detectability but demonstrate a nonlinear relationship between hydrophobicity and peptide detectability. Similarly, we use F-factors to show how peptide ion coelution adversely affects detectability and ionization. We suggest that F-factors have great utility for understanding peptide detectability and gas-phase ion chemistry in complex peptide mixtures, selection of surrogate peptides in targeted MS studies, and for calibration of peptide ion signal in label-free workflows. Data are available via ProteomeXchange with identifier PXD003472.
[Mh] Termos MeSH primário: Proteínas Fúngicas/análise
Proteoma/análise
Proteômica/métodos
[Mh] Termos MeSH secundário: Calibragem
Fator F/normas
Interações Hidrofóbicas e Hidrofílicas
Proteômica/normas
Leveduras/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (Proteome)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160726
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jproteome.6b00048


  8 / 1013 MEDLINE  
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[PMID]:27355474
[Au] Autor:Ruhe ZC; Nguyen JY; Chen AJ; Leung NY; Hayes CS; Low DA
[Ad] Endereço:Department of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, Santa Barbara, California, United States of America.
[Ti] Título:CDI Systems Are Stably Maintained by a Cell-Contact Mediated Surveillance Mechanism.
[So] Source:PLoS Genet;12(6):e1006145, 2016 06.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Contact-dependent growth inhibition (CDI) systems are widespread amongst Gram-negative bacteria where they play important roles in inter-cellular competition and biofilm formation. CDI+ bacteria use cell-surface CdiA proteins to bind neighboring bacteria and deliver C-terminal toxin domains. CDI+ cells also express CdiI immunity proteins that specifically neutralize toxins delivered from adjacent siblings. Genomic analyses indicate that cdi loci are commonly found on plasmids and genomic islands, suggesting that these Type 5 secretion systems are spread through horizontal gene transfer. Here, we examine whether CDI toxin and immunity activities serve to stabilize mobile genetic elements using a minimal F plasmid that fails to partition properly during cell division. This F plasmid is lost from Escherichia coli populations within 50 cell generations, but is maintained in ~60% of the cells after 100 generations when the plasmid carries the cdi gene cluster from E. coli strain EC93. By contrast, the ccdAB "plasmid addiction" module normally found on F exerts only a modest stabilizing effect. cdi-dependent plasmid stabilization requires the BamA receptor for CdiA, suggesting that plasmid-free daughter cells are inhibited by siblings that retain the CDI+ plasmid. In support of this model, the CDI+ F plasmid is lost rapidly from cells that carry an additional cdiI immunity gene on a separate plasmid. These results indicate that plasmid stabilization occurs through elimination of non-immune cells arising in the population via plasmid loss. Thus, genetic stabilization reflects a strong selection for immunity to CDI. After long-term passage for more than 300 generations, CDI+ plasmids acquire mutations that increase copy number and result in 100% carriage in the population. Together, these results show that CDI stabilizes genetic elements through a toxin-mediated surveillance mechanism in which cells that lose the CDI system are detected and eliminated by their siblings.
[Mh] Termos MeSH primário: Inibição de Contato/genética
Inibição de Contato/fisiologia
Proteínas de Escherichia coli/metabolismo
Escherichia coli/metabolismo
Escherichia coli/fisiologia
Proteínas de Membrana/metabolismo
[Mh] Termos MeSH secundário: Toxinas Bacterianas/metabolismo
Biofilmes/crescimento & desenvolvimento
Fator F/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Toxins); 0 (Escherichia coli Proteins); 0 (Membrane Proteins)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170320
[Lr] Data última revisão:
170320
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160630
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006145


  9 / 1013 MEDLINE  
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[PMID]:26992840
[Au] Autor:Creuzot-Garcher C; Benzenine E; Mariet AS; de Lazzer A; Chiquet C; Bron AM; Quantin C
[Ad] Endereço:Department of Ophthalmology, University Hospital, Dijon, France; Eye and Nutrition Research Group, Bourgogne Franche-Comté University, Dijon, France. Electronic address: catherine.creuzot-garcher@chu-dijon.fr.
[Ti] Título:Incidence of Acute Postoperative Endophthalmitis after Cataract Surgery: A Nationwide Study in France from 2005 to 2014.
[So] Source:Ophthalmology;123(7):1414-20, 2016 Jul.
[Is] ISSN:1549-4713
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:PURPOSE: To report the incidence of acute postoperative endophthalmitis (POE) after cataract surgery from 2005 to 2014 in France. DESIGN: Cohort study. PARTICIPANTS: Patients undergoing operation for cataract surgery by phacoemulsification and presenting acute POE. METHODS: We identified acute POE occurring within 6 weeks after phacoemulsification cataract surgery and the use of intracameral antibiotic injection during the surgical procedure by means of billing codes from a national database. MAIN OUTCOME MEASURES: Incidence of acute POE. RESULTS: From January 2005 to December 2014, 6 371 242 eyes in 3 983 525 patients underwent phacoemulsification cataract surgery. The incidence of acute POE after phacoemulsification decreased from 0.145% to 0.053% during this 10-year period; the unadjusted incidence rate ratio (IRR) (95% confidence interval) was 0.37 (0.32-0.42; P < 0.001). In multivariate analysis, intracameral antibiotic injection was associated with a lower risk of acute POE 0.53 (0.50-0.57; P < 0.001), whereas intraoperative posterior capsule rupture, combined surgery, and gender (male) were associated with a higher risk of acute POE: 5.24 (4.11-6.68), 1.77 (1.53-2.05), and 1.48 (1.40-1.56) (P < 0.001), respectively. CONCLUSIONS: Access to a national database allowed us to observe a decrease in acute POE after phacoemulsification cataract surgery from 2005 to 2014. Within the same period, the use of intracameral antibiotics during the surgical procedures increased.
[Mh] Termos MeSH primário: Endoftalmite/epidemiologia
Infecções Oculares Bacterianas/epidemiologia
Facoemulsificação/efeitos adversos
Complicações Pós-Operatórias/epidemiologia
[Mh] Termos MeSH secundário: Doença Aguda
Adulto
Distribuição por Idade
Idoso
Idoso de 80 Anos ou mais
Antibacterianos/uso terapêutico
Cefuroxima/uso terapêutico
Endoftalmite/tratamento farmacológico
Endoftalmite/etiologia
Infecções Oculares Bacterianas/tratamento farmacológico
Infecções Oculares Bacterianas/etiologia
Fator F
Feminino
França/epidemiologia
Seres Humanos
Incidência
Masculino
Meia-Idade
Análise Multivariada
Estudos Retrospectivos
Fatores de Risco
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); O1R9FJ93ED (Cefuroxime)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170623
[Lr] Data última revisão:
170623
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160320
[St] Status:MEDLINE


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[PMID]:26034891
[Au] Autor:Chandran Darbari V; Waksman G
[Ad] Endereço:Section of Structural Biology, Department of Medicine, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom.
[Ti] Título:Structural Biology of Bacterial Type IV Secretion Systems.
[So] Source:Annu Rev Biochem;84:603-29, 2015.
[Is] ISSN:1545-4509
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Type IV secretion systems (T4SSs) are large multisubunit translocons, found in both gram-negative and gram-positive bacteria and in some archaea. These systems transport a diverse array of substrates from DNA and protein-DNA complexes to proteins, and play fundamental roles in both bacterial pathogenesis and bacterial adaptation to the cellular milieu in which bacteria live. This review describes the various biochemical and structural advances made toward understanding the biogenesis, architecture, and function of T4SSs.
[Mh] Termos MeSH primário: Bactérias/metabolismo
Sistemas de Secreção Tipo IV/química
Sistemas de Secreção Tipo IV/ultraestrutura
[Mh] Termos MeSH secundário: Bactérias/química
Bactérias/classificação
Fator F/genética
Microscopia Eletrônica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Type IV Secretion Systems)
[Em] Mês de entrada:1512
[Cu] Atualização por classe:150603
[Lr] Data última revisão:
150603
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150603
[St] Status:MEDLINE
[do] DOI:10.1146/annurev-biochem-062911-102821



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