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  1 / 8725 MEDLINE  
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[PMID]:28451968
[Au] Autor:Suzuki S; Ishida T; Ohue M; Kakuta M; Akiyama Y
[Ad] Endereço:Department of Computer Science, Graduate School of Information Science and Engineering, Tokyo Institute of Technology, 2-12-1 Ookayama, Meguro-ku, 152-8550, Tokyo, Japan.
[Ti] Título:GHOSTX: A Fast Sequence Homology Search Tool for Functional Annotation of Metagenomic Data.
[So] Source:Methods Mol Biol;1611:15-25, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Metagenomic analysis based on whole genome shotgun sequencing data requires fast protein sequence homology searches for predicting the function of proteins coded on metagenome short reads. However, huge amounts of sequence data cause even general homology search analyses using BLASTX to become difficult in terms of computational cost. GHOSTX is a sequence homology search tool specifically developed for functional annotation of metagenome sequences. The tool is more than 160 times faster than BLASTX and has sufficient search sensitivity for metagenomic analysis. Using this tool, user can perform functional annotation of metagenomic data within a short time and infer metabolic pathways within an environment.
[Mh] Termos MeSH primário: Metagenômica/métodos
Ferramenta de Busca
Software
[Mh] Termos MeSH secundário: Algoritmos
Bases de Dados Genéticas
Anotação de Sequência Molecular
Homologia de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[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:170429
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-7015-5_2


  2 / 8725 MEDLINE  
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[PMID]:28749495
[Au] Autor:Pedroso MM; Selleck C; Enculescu C; Harmer JR; Mitic N; Craig WR; Helweh W; Hugenholtz P; Tyson GW; Tierney DL; Larrabee JA; Schenk G
[Ad] Endereço:School of Chemistry and Molecular Biosciences, The University of Queensland, St. Lucia, Queensland 4072, Australia. m.pedroso@uq.edu.au schenk@uq.edu.au.
[Ti] Título:Characterization of a highly efficient antibiotic-degrading metallo-ß-lactamase obtained from an uncultured member of a permafrost community.
[So] Source:Metallomics;9(8):1157-1168, 2017 Aug 16.
[Is] ISSN:1756-591X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Antibiotic resistance is a major global health problem, one that threatens to derail the benefits garnered from arguably the greatest success of modern medicine, the discovery of antibiotics. Among the most potent agents contributing to antibiotic resistance are metallo-ß-lactamases (MBLs). The discovery of MBL-like enzymes in microorganisms that are not in contact with the human population is of particular concern as these proteins already have the in-built capacity to inactivate antibiotics, even though they may not need MBL activity for their survival. Here, we demonstrate that a microbiome from a remote and frozen environment in Alaska harbours at least one highly efficient MBL, LRA-8. LRA-8 is homologous to the B3 subgroup of MBLs and has a substrate profile and catalytic properties similar to well-known members of this enzyme family, which are expressed by major human pathogens. LRA-8 is predominantly a penicillinase, but is also active towards carbapenems, but not cephalosporins. Spectroscopic studies indicate that LRA-8 has an active site structure similar to that of other MBLs (in particular B3 subgroup representative AIM-1), and a combination of steady-state and pre-steady-state kinetic data demonstrate that the enzyme is likely to employ a metal ion-bridging hydroxide to initiate catalysis. The rate-limiting step is the decay of a chromophoric, tetrahedral intermediate, as is observed in various other MBLs. Thus, studying the properties of such "pristine" MBL-like proteins may provide insight into the structural plasticity of this family of enzymes that may facilitate functional promiscuity, while important insight into the evolution of MBLs may also be gained.
[Mh] Termos MeSH primário: Antibacterianos/metabolismo
Proteínas de Bactérias/metabolismo
Pergelissolo/microbiologia
beta-Lactamases/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Catálise
Seres Humanos
Metagenoma
Metais/metabolismo
Modelos Moleculares
Fenótipo
Homologia de Sequência
Especificidade por Substrato
beta-Lactamases/química
beta-Lactamases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (Metals); EC 3.5.2.6 (beta-Lactamases)
[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:170728
[St] Status:MEDLINE
[do] DOI:10.1039/c7mt00195a


  3 / 8725 MEDLINE  
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[PMID]:28743721
[Au] Autor:Taviti AC; Beuria TK
[Ad] Endereço:Institute of Life Sciences, Nalco Square, Bhubaneswar, Odisha 751023, India.
[Ti] Título:MinD directly interacting with FtsZ at the H10 helix suggests a model for robust activation of MinC to destabilize FtsZ polymers.
[So] Source:Biochem J;474(18):3189-3205, 2017 09 07.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cell division in bacteria is a highly controlled and regulated process. FtsZ, a bacterial cytoskeletal protein, forms a ring-like structure known as the Z-ring and recruits more than a dozen other cell division proteins. The Min system oscillates between the poles and inhibits the Z-ring formation at the poles by perturbing FtsZ assembly. This leads to an increase in the FtsZ concentration at the mid-cell and helps in Z-ring positioning. MinC, the effector protein, interferes with Z-ring formation through two different mechanisms mediated by its two domains with the help of MinD. However, the mechanism by which MinD triggers MinC activity is not yet known. We showed that MinD directly interacts with FtsZ with an affinity stronger than the reported MinC-FtsZ interaction. We determined the MinD-binding site of FtsZ using computational, mutational and biochemical analyses. Our study showed that MinD binds to the H10 helix of FtsZ. Single-point mutations at the charged residues in the H10 helix resulted in a decrease in the FtsZ affinity towards MinD. Based on our findings, we propose a novel model for MinCD-FtsZ interaction, where MinD through its direct interaction with FtsZ would trigger MinC activity to inhibit FtsZ functions.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/metabolismo
Proteínas de Bactérias/metabolismo
Proteínas do Citoesqueleto/metabolismo
Proteínas de Escherichia coli/metabolismo
Escherichia coli/metabolismo
Proteínas de Membrana/metabolismo
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/antagonistas & inibidores
Adenosina Trifosfatases/química
Sequência de Aminoácidos
Proteínas de Bactérias/química
Sítios de Ligação
Proteínas do Citoesqueleto/química
Escherichia coli/crescimento & desenvolvimento
Proteínas de Escherichia coli/química
Proteínas de Membrana/química
Multimerização Proteica
Homologia de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cytoskeletal Proteins); 0 (Escherichia coli Proteins); 0 (FtsZ protein, Bacteria); 0 (Membrane Proteins); 0 (MinC protein, E coli); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.1.- (MinD protein, E coli)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171217
[Lr] Data última revisão:
171217
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20170357


  4 / 8725 MEDLINE  
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[PMID]:29030254
[Au] Autor:Chen N; Sha LN; Dong ZZ; Tang C; Wang Y; Kang HY; Zhang HQ; Yan XB; Zhou YH; Fan X
[Ad] Endereço:Triticeae Research Institute, Sichuan Agricultural University, Chengdu, Sichuan 611130, China; Key Laboratory of Crop Genetic Resources and Improvement, Ministry of Education, Sichuan Agricultural University, Yaan 625014, Sichuan, China.
[Ti] Título:Complete structure and variation of the chloroplast genome of Agropyron cristatum (L.) Gaertn.
[So] Source:Gene;640:86-96, 2018 Jan 15.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Agropyron cristatum (L.) Gaertner, a perennial grass in the tribe Triticeae (Poaceae), is a wild relative of cereal crops that is suitable for genetic improvement. In this study, we first sequenced the complete chloroplast (cp) genome of Ag. cristatum using Hiseq4000 PE150. The Ag. cristatum chloroplast genome is 135,554bp in length, has a typical quadripartite structure and contains 76 protein-coding genes, 29 tRNA genes and four rRNA genes. The cp genome of Ag. cristatum was used for comparison with other seven Triticeae species. One large variable region (800bp), which primarily contained the rpl23 (non-reciprocally translocated from IRs) and accD genes, was detected between rbcL gene and psaI gene within LSC region. The deletion of the accD and translocated rpl23 genes in Ag. cristatum indicated an independent gene-loss events or an additional divergence in Triticeae. Analyses of the dn/ds ratio and K2-P's genetic distance for 76 protein-coding genes showed that genes with evolutionary divergence might suffer from the effect of sequence regional constraints or gene functional constraints in Triticeae species. Our research will generally contribute to the knowledge of plastid genome evolution in Triticeae.
[Mh] Termos MeSH primário: Agropyron/genética
DNA de Cloroplastos/genética
Genes de Cloroplastos
Marcadores Genéticos
Variação Genética
Genoma de Cloroplastos
[Mh] Termos MeSH secundário: Agropyron/crescimento & desenvolvimento
Sequência de Bases
Evolução Molecular
Filogenia
Sequências Repetitivas de Ácido Nucleico
Análise de Sequência de DNA/métodos
Homologia de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Chloroplast); 0 (Genetic Markers)
[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:171015
[St] Status:MEDLINE


  5 / 8725 MEDLINE  
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[PMID]:29017964
[Au] Autor:Ishinishi R; Matsuura H; Tanaka S; Nozawa S; Tanada K; Kawashita N; Fujiyama K; Miyasaka H; Hirata K
[Ad] Endereço:Applied Environmental Biology Laboratory, Graduate School of Pharmaceutical Sciences, Osaka University, 1-6 Yamadaoka, Suita, Osaka 565-0871, Japan.
[Ti] Título:Isolation and characterization of a stress-responsive gene encoding a CHRD domain-containing protein from a halotolerant green alga.
[So] Source:Gene;640:14-20, 2018 Jan 15.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The genetic basis of stress resistance in extremophilic microalgae is not well studied. In this study, a gene of unknown function, the cluster58 or CL58 gene, was identified from the halotolerant green alga Chlamydomonas W80 and characterized. The CL58 gene encodes a protein containing a domain of unknown function, the CHRD domain, and a putative secretory signaling sequence at its N-terminus. The levels of CL58 mRNA increased in response to high copper levels and low temperatures. When the CL58 gene was heterologously expressed as a fusion gene with the NanoLuc luciferase gene in Chlamydomonas reinhardtii, a majority of the NanoLuc activity was detected in the culture medium compared with that in the intracellular fraction. A mutagenic analysis revealed that the putative secretory signaling sequence was sufficient for the secretion of the CL58-NanoLuc fusion protein. In addition, we expressed the protein encoded by the CL58 gene in Escherichia coli; the recombinant, soluble protein was then purified. In summary, we identified a novel gene from C. W80 that appears to encode a stress-responsive, CHRD domain-containing secreted protein.
[Mh] Termos MeSH primário: Chlamydomonas reinhardtii/genética
DNA de Algas/genética
Glicoproteínas/química
Peptídeos e Proteínas de Sinalização Intercelular/química
Proteínas de Plantas/genética
Estresse Fisiológico/genética
Transgenes/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sequência de Bases
Chlamydomonas reinhardtii/crescimento & desenvolvimento
Chlamydomonas reinhardtii/metabolismo
Temperatura Baixa
Cobre/toxicidade
Proteínas de Plantas/metabolismo
Domínios Proteicos
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Homologia de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Algal); 0 (Glycoproteins); 0 (Intercellular Signaling Peptides and Proteins); 0 (Plant Proteins); 0 (Recombinant Proteins); 789U1901C5 (Copper); 93586-27-7 (chordin)
[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:171012
[St] Status:MEDLINE


  6 / 8725 MEDLINE  
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[PMID]:29073136
[Au] Autor:Harms A; Liesch M; Körner J; Québatte M; Engel P; Dehio C
[Ad] Endereço:Focal Area Infection Biology, Biozentrum, University of Basel, Basel, Switzerland.
[Ti] Título:A bacterial toxin-antitoxin module is the origin of inter-bacterial and inter-kingdom effectors of Bartonella.
[So] Source:PLoS Genet;13(10):e1007077, 2017 Oct.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Host-targeting type IV secretion systems (T4SS) evolved from conjugative T4SS machineries that mediate interbacterial plasmid transfer. However, the origins of effectors secreted by these virulence devices have remained largely elusive. Previous work showed that some effectors exhibit homology to toxins of bacterial toxin-antitoxin modules, but the evolutionary trajectories underlying these ties had not been resolved. We previously reported that FicT toxins of FicTA toxin-antitoxin modules disrupt cellular DNA topology via their enzymatic FIC (filamentation induced by cAMP) domain. Intriguingly, the FIC domain of the FicT toxin VbhT of Bartonella schoenbuchensis is fused to a type IV secretion signal-the BID (Bep intracellular delivery) domain-similar to the Bartonella effector proteins (Beps) that are secreted into eukaryotic host cells via the host-targeting VirB T4SS. In this study, we show that the VbhT toxin is an interbacterial effector protein secreted via the conjugative Vbh T4SS that is closely related to the VirB T4SS and encoded by plasmid pVbh of B. schoenbuchensis. We therefore propose that the Vbh T4SS together with its effector VbhT represent an evolutionary missing link on a path that leads from a regular conjugation system and FicTA toxin-antitoxin modules to the VirB T4SS and the Beps. Intriguingly, phylogenetic analyses revealed that the fusion of FIC and BID domains has probably occurred independently in VbhT and the common ancestor of the Beps, suggesting parallel evolutionary paths. Moreover, several other examples of TA module toxins that are bona fide substrates of conjugative T4SS indicate that their recruitment as interbacterial effectors is prevalent and serves yet unknown biological functions in the context of bacterial conjugation. We propose that the adaptation for interbacterial transfer favors the exaptation of FicT and other TA module toxins as inter-kingdom effectors and may thus constitute an important stepping stone in the evolution of host-targeted effector proteins.
[Mh] Termos MeSH primário: Antitoxinas/metabolismo
Sistemas de Secreção Bacterianos/genética
Sistemas de Secreção Bacterianos/metabolismo
Toxinas Bacterianas/metabolismo
Bartonella/genética
Bartonella/patogenicidade
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Antitoxinas/genética
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Toxinas Bacterianas/genética
Infecções por Bartonella/microbiologia
Conjugação Genética
Regulação Bacteriana da Expressão Gênica
Interações Hospedeiro-Patógeno
Plasmídeos
Homologia de Sequência
Virulência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antitoxins); 0 (Bacterial Proteins); 0 (Bacterial Secretion Systems); 0 (Bacterial Toxins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171119
[Lr] Data última revisão:
171119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171027
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007077


  7 / 8725 MEDLINE  
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[PMID]:29069084
[Au] Autor:Dahal BK; Kadyrova LY; Delfino KR; Rogozin IB; Gujar V; Lobachev KS; Kadyrov FA
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, IL, United States of America.
[Ti] Título:Involvement of DNA mismatch repair in the maintenance of heterochromatic DNA stability in Saccharomyces cerevisiae.
[So] Source:PLoS Genet;13(10):e1007074, 2017 Oct.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Heterochromatin contains a significant part of nuclear DNA. Little is known about the mechanisms that govern heterochromatic DNA stability. We show here that in the yeast Saccharomyces cerevisiae (i) DNA mismatch repair (MMR) is required for the maintenance of heterochromatic DNA stability, (ii) MutLα (Mlh1-Pms1 heterodimer), MutSα (Msh2-Msh6 heterodimer), MutSß (Msh2-Msh3 heterodimer), and Exo1 are involved in MMR at heterochromatin, (iii) Exo1-independent MMR at heterochromatin frequently leads to the formation of Pol ζ-dependent mutations, (iv) MMR cooperates with the proofreading activity of Pol ε and the histone acetyltransferase Rtt109 in the maintenance of heterochromatic DNA stability, (v) repair of base-base mismatches at heterochromatin is less efficient than repair of base-base mismatches at euchromatin, and (vi) the efficiency of repair of 1-nt insertion/deletion loops at heterochromatin is similar to the efficiency of repair of 1-nt insertion/deletion loops at euchromatin.
[Mh] Termos MeSH primário: Reparo de Erro de Pareamento de DNA
DNA Fúngico/química
Heterocromatina
Proteínas de Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: Sequência de Bases
Dano ao DNA
DNA Fúngico/genética
Exodesoxirribonucleases/genética
Genes pol
Histona Acetiltransferases/genética
Proteínas MutL/genética
Proteína MutS de Ligação de DNA com Erro de Pareamento/genética
Homologia de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Fungal); 0 (Heterochromatin); 0 (Saccharomyces cerevisiae Proteins); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (Rtt109 protein, S cerevisiae); EC 3.1.- (Exodeoxyribonucleases); EC 3.1.11.1 (exodeoxyribonuclease I); EC 3.6.1.3 (MutL Proteins); EC 3.6.1.3 (MutS DNA Mismatch-Binding Protein)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171119
[Lr] Data última revisão:
171119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171026
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007074


  8 / 8725 MEDLINE  
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[PMID]:28942965
[Au] Autor:Feichtinger RG; Oláhová M; Kishita Y; Garone C; Kremer LS; Yagi M; Uchiumi T; Jourdain AA; Thompson K; D'Souza AR; Kopajtich R; Alston CL; Koch J; Sperl W; Mastantuono E; Strom TM; Wortmann SB; Meitinger T; Pierre G; Chinnery PF; Chrzanowska-Lightowlers ZM; Lightowlers RN; DiMauro S; Calvo SE; Mootha VK; Moggio M; Sciacco M; Comi GP; Ronchi D; Murayama K; Ohtake A; Rebelo-Guiomar P; Kohda M; Kang D; Mayr JA; Taylor RW; Okazaki Y; Minczuk M; Prokisch H
[Ad] Endereço:Department of Pediatrics, University Hospital Salzburg, Paracelsus Medical University, 5020 Salzburg, Austria.
[Ti] Título:Biallelic C1QBP Mutations Cause Severe Neonatal-, Childhood-, or Later-Onset Cardiomyopathy Associated with Combined Respiratory-Chain Deficiencies.
[So] Source:Am J Hum Genet;101(4):525-538, 2017 Oct 05.
[Is] ISSN:1537-6605
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Complement component 1 Q subcomponent-binding protein (C1QBP; also known as p32) is a multi-compartmental protein whose precise function remains unknown. It is an evolutionary conserved multifunctional protein localized primarily in the mitochondrial matrix and has roles in inflammation and infection processes, mitochondrial ribosome biogenesis, and regulation of apoptosis and nuclear transcription. It has an N-terminal mitochondrial targeting peptide that is proteolytically processed after import into the mitochondrial matrix, where it forms a homotrimeric complex organized in a doughnut-shaped structure. Although C1QBP has been reported to exert pleiotropic effects on many cellular processes, we report here four individuals from unrelated families where biallelic mutations in C1QBP cause a defect in mitochondrial energy metabolism. Infants presented with cardiomyopathy accompanied by multisystemic involvement (liver, kidney, and brain), and children and adults presented with myopathy and progressive external ophthalmoplegia. Multiple mitochondrial respiratory-chain defects, associated with the accumulation of multiple deletions of mitochondrial DNA in the later-onset myopathic cases, were identified in all affected individuals. Steady-state C1QBP levels were decreased in all individuals' samples, leading to combined respiratory-chain enzyme deficiency of complexes I, III, and IV. C1qbp mouse embryonic fibroblasts (MEFs) resembled the human disease phenotype by showing multiple defects in oxidative phosphorylation (OXPHOS). Complementation with wild-type, but not mutagenized, C1qbp restored OXPHOS protein levels and mitochondrial enzyme activities in C1qbp MEFs. C1QBP deficiency represents an important mitochondrial disorder associated with a clinical spectrum ranging from infantile lactic acidosis to childhood (cardio)myopathy and late-onset progressive external ophthalmoplegia.
[Mh] Termos MeSH primário: Cardiomiopatias/genética
Proteínas de Transporte/genética
Transporte de Elétrons/fisiologia
Doenças Mitocondriais/genética
Proteínas Mitocondriais/genética
Mutação
[Mh] Termos MeSH secundário: Adulto
Idade de Início
Idoso
Alelos
Sequência de Aminoácidos
Animais
Cardiomiopatias/complicações
Cardiomiopatias/patologia
Proteínas de Transporte/química
Proteínas de Transporte/metabolismo
Células Cultivadas
Pré-Escolar
Estudos de Coortes
DNA Mitocondrial
Embrião de Mamíferos/metabolismo
Embrião de Mamíferos/patologia
Feminino
Fibroblastos/metabolismo
Fibroblastos/patologia
Seres Humanos
Recém-Nascido
Masculino
Camundongos
Meia-Idade
Doenças Mitocondriais/complicações
Doenças Mitocondriais/patologia
Proteínas Mitocondriais/química
Proteínas Mitocondriais/metabolismo
Fosforilação Oxidativa
Linhagem
Conformação Proteica
Homologia de Sequência
Índice de Gravidade de Doença
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (C1QBP protein, human); 0 (Carrier Proteins); 0 (DNA, Mitochondrial); 0 (Mitochondrial Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171122
[Lr] Data última revisão:
171122
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170926
[St] Status:MEDLINE


  9 / 8725 MEDLINE  
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[PMID]:28940019
[Au] Autor:Fehér E; Kaszab E; Forró B; Bali K; Marton S; Lengyel G; Bányai K
[Ad] Endereço:Institute for Veterinary Medical Research, Centre of Agricultural Research, Hungarian Academy of Sciences, P.O. Box 18, 1581, Budapest, Hungary.
[Ti] Título:Genome sequence of a mallard duck origin cyclovirus, DuACyV-1.
[So] Source:Arch Virol;162(12):3925-3929, 2017 Dec.
[Is] ISSN:1432-8798
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:The genome sequence of a novel avian cyclovirus is described in this study. The genome size and orientation of predicted genes was similar to those described in other vertebrate and insect origin cycloviruses. The greatest genome sequence identity was shared with a dragonfly cyclovirus (nt, 60.6%). Phylogenetic analysis showed marginal relatedness with another avian cyclovirus, the chicken associated cyclovirus 1. In contrast, along a short fragment of the replication-associated protein coding gene (rep) (spanning nt 1240-1710) the duck origin cyclovirus was very similar to human origin and honey bee origin rep sequences (human - TN4, 98%; honey bee - hb10, 100%). Related cyclovirus strains existing amongst various animal species living in diverse ecosystems and separated by large geographic distances show the need for additional studies to better understand the ecology and epidemiology of cycloviruses.
[Mh] Termos MeSH primário: Circoviridae/classificação
Circoviridae/genética
Patos/virologia
Genoma Viral
Análise de Sequência de DNA
[Mh] Termos MeSH secundário: Animais
Circoviridae/isolamento & purificação
Ordem dos Genes
Genes Virais
Filogenia
Homologia de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170924
[St] Status:MEDLINE
[do] DOI:10.1007/s00705-017-3566-z


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[PMID]:28929273
[Au] Autor:Su J; Sun H; Liu J; Guo Z; Fan G; Gu G; Wang G
[Ad] Endereço:Key Laboratory of Mollisols Agroecology, Northeast Institute of Geography and Agroecology, Chinese Academy of Sciences, Harbin, 150081, China.
[Ti] Título:Complete genome sequence of a novel lytic bacteriophage isolated from Ralstonia solanacearum.
[So] Source:Arch Virol;162(12):3919-3923, 2017 Dec.
[Is] ISSN:1432-8798
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:A lytic podophage RSPI1 was isolated from tobacco field soil collected in Fujian Province, South China using host bacterium Ralstonia solanacearum Tb15-14. Whole genome sequencing of this phage was performed using the high-throughput Ion Torrent PGM Sequencer. The complete genome of RSPI1 was 43,211 bp in length with a mean DNA G + C content of 61.5%. A total of 48 open reading frames were identified with lengths ranging from 132 bp to 5,061 bp, of which, 11, 12 and 25 were identified as functional, structural and unknown genes, respectively. A BLAST analysis revealed that this phage genome had a query cover of 78-79% and a highest identity of 84% with four podophages that infect Burkholderia pseudomallei. Two neighbor-joining phylogenetic trees were constructed using phage DNA polymerase I and tail fiber protein sequences and showed that this phage is closely related to Burkholderia phage Bp-AMP1, and also related to several phages that infect Ralstonia solanacearum. These findings indicate that RSPI1 is a novel phage that infects the notorious plant pathogen Ralstonia solanacearum.
[Mh] Termos MeSH primário: Bacteriófagos/classificação
Bacteriófagos/isolamento & purificação
Podoviridae/classificação
Podoviridae/isolamento & purificação
Ralstonia solanacearum/virologia
[Mh] Termos MeSH secundário: Bacteriólise
Bacteriófagos/genética
Bacteriófagos/fisiologia
Composição de Bases
Burkholderia pseudomallei/virologia
China
Genoma Viral
Sequenciamento de Nucleotídeos em Larga Escala
Fases de Leitura Aberta
Filogenia
Podoviridae/genética
Podoviridae/fisiologia
Análise de Sequência de DNA
Homologia de Sequência
Microbiologia do Solo
Tabaco/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170921
[St] Status:MEDLINE
[do] DOI:10.1007/s00705-017-3555-2



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