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[PMID]:29409851
[Au] Autor:Tan M; Li G; Qi S; Liu X; Chen X; Ma J; Zhang D; Han M
[Ad] Endereço:College of Horticulture, Northwest A & F University, Yangling, Shaanxi 712100, China.
[Ti] Título:Identification and expression analysis of the IPT and CKX gene families during axillary bud outgrowth in apple (Malus domestica Borkh.).
[So] Source:Gene;651:106-117, 2018 Apr 20.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Cytokinins (CKs) play a crucial role in promoting axillary bud outgrowth and targeting the control of CK metabolism can be used to enhance branching in plants. CK levels are maintained mainly by CK biosynthesis (isopentenyl transferase, IPT) and degradation (dehydrogenase, CKX) genes in plants. A systematic study of the IPT and CKX gene families in apple, however, has not been conducted. In the present study, 12 MdIPTs and 12 MdCKXs were identified in the apple genome. Systematic phylogenetic, structural, and synteny analyses were performed. Expression analysis of these genes in different tissues was also assessed. MdIPT and MdCKX genes exhibit distinct expression patterns in different tissues. The response of MdIPT, MdCKX, and MdPIN1 genes to various treatments (6-BA, decapitation and Lovastatin, an inhibitor of CKs synthesis) that impact branching were also investigated. Results indicated that most of the MdIPT and MdCKX, and MdPIN1 genes were upregulated by 6-BA and decapitation treatment, but inhibited by Lovastatin, a compound that effectively suppresses axillary bud outgrowth induced by decapitation. These findings suggest that cytokinin biosynthesis is required for the activation of bud break and the export of auxin from buds in apple tree with intact primary shoot apex or decapitated apple tree. MdCKX8 and MdCKX10, however, exhibited little response to decapitation, but were significantly up-regulated by 6-BA and Lovastatin, a finding that warrants further investigation in order to understand their function in bud-outgrowth.
[Mh] Termos MeSH primário: Alquil e Aril Transferases/genética
Genes de Plantas
Malus/genética
Oxirredutases/genética
[Mh] Termos MeSH secundário: Arabidopsis/genética
Compostos de Benzil/farmacologia
Mapeamento Cromossômico
Cromossomos de Plantas
Evolução Molecular
Flores/genética
Perfilação da Expressão Gênica
Regulação da Expressão Gênica de Plantas
Genoma de Planta
Lovastatina/farmacologia
Malus/enzimologia
Malus/crescimento & desenvolvimento
Família Multigênica
Filogenia
Reguladores de Crescimento de Planta
Purinas/farmacologia
Sintenia
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzyl Compounds); 0 (Plant Growth Regulators); 0 (Purines); 9LHU78OQFD (Lovastatin); EC 1.- (Oxidoreductases); EC 1.5.99.12 (cytokinin oxidase); EC 2.5.- (Alkyl and Aryl Transferases); EC 2.5.1.27 (adenylate isopentenyltransferase); KXG6A989PS (benzylaminopurine)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180208
[St] Status:MEDLINE


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[PMID]:29216817
[Au] Autor:Nivala O; Faccio G; Arvas M; Permi P; Buchert J; Kruus K; Mattinen ML
[Ad] Endereço:VTT Technical Research Centre of Finland, Ltd., P.O. Box 1000, FI-02044, Espoo, Finland. outi.nivala@helsinki.fi.
[Ti] Título:Characterization of sulfhydryl oxidase from Aspergillus tubingensis.
[So] Source:BMC Biochem;18(1):15, 2017 12 08.
[Is] ISSN:1471-2091
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Despite of the presence of sulfhydryl oxidases (SOXs) in the secretomes of industrially relevant organisms and their many potential applications, only few of these enzymes have been biochemically characterized. In addition, basic functions of most of the SOX enzymes reported so far are not fully understood. In particular, the physiological role of secreted fungal SOXs is unclear. RESULTS: The recently identified SOX from Aspergillus tubingensis (AtSOX) was produced, purified and characterized in the present work. AtSOX had a pH optimum of 6.5, and showed a good pH stability retaining more than 80% of the initial activity in a pH range 4-8.5 within 20 h. More than 70% of the initial activity was retained after incubation at 50 °C for 20 h. AtSOX contains a non-covalently bound flavin cofactor. The enzyme oxidised a sulfhydryl group of glutathione to form a disulfide bond, as verified by nuclear magnetic resonance spectroscopy. AtSOX preferred glutathione as a substrate over cysteine and dithiothreitol. The activity of the enzyme was totally inhibited by 10 mM zinc sulphate. Peptide- and protein-bound sulfhydryl groups in bikunin, gliotoxin, holomycin, insulin B chain, and ribonuclease A, were not oxidised by the enzyme. Based on the analysis of 33 fungal genomes, SOX enzyme encoding genes were found close to nonribosomal peptide synthetases (NRPS) but not with polyketide synthases (PKS). In the phylogenetic tree, constructed from 25 SOX and thioredoxin reductase sequences from IPR000103 InterPro family, AtSOX was evolutionary closely related to other Aspergillus SOXs. Oxidoreductases involved in the maturation of nonribosomal peptides of fungal and bacterial origin, namely GliT, HlmI and DepH, were also evolutionary closely related to AtSOX whereas fungal thioreductases were more distant. CONCLUSIONS: AtSOX (55 kDa) is a fungal secreted flavin-dependent enzyme with good stability to both pH and temperature. A Michaelis-Menten behaviour was observed with reduced glutathione as a substrate. Based on the location of SOX enzyme encoding genes close to NRPSs, SOXs could be involved in the secondary metabolism and act as an accessory enzyme in the production of nonribosomal peptides.
[Mh] Termos MeSH primário: Aspergillus/enzimologia
Oxirredutases/metabolismo
[Mh] Termos MeSH secundário: Dissulfetos
Estabilidade Enzimática
Glutationa/metabolismo
Concentração de Íons de Hidrogênio
Oxirredutases/química
Oxirredutases/genética
Oxirredutases/isolamento & purificação
Peptídeo Sintases
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Disulfides); EC 1.- (Oxidoreductases); EC 1.8.3.- (sulfhydryl oxidase); EC 6.3.2.- (Peptide Synthases); EC 6.3.2.- (non-ribosomal peptide synthase); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171209
[St] Status:MEDLINE
[do] DOI:10.1186/s12858-017-0090-4


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[PMID]:29311546
[Au] Autor:Yang JE; Park SJ; Kim WJ; Kim HJ; Kim BJ; Lee H; Shin J; Lee SY
[Ad] Endereço:Metabolic and Biomolecular Engineering National Research Laboratory, Department of Chemical and Biomolecular Engineering (BK21 Plus Program), Center for Systems and Synthetic Biotechnology, Institute for the BioCentury, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, 34141, Repu
[Ti] Título:One-step fermentative production of aromatic polyesters from glucose by metabolically engineered Escherichia coli strains.
[So] Source:Nat Commun;9(1):79, 2018 01 08.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Aromatic polyesters are widely used plastics currently produced from petroleum. Here we engineer Escherichia coli strains for the production of aromatic polyesters from glucose by one-step fermentation. When the Clostridium difficile isocaprenoyl-CoA:2-hydroxyisocaproate CoA-transferase (HadA) and evolved polyhydroxyalkanoate (PHA) synthase genes are overexpressed in a D-phenyllactate-producing strain, poly(52.3 mol% 3-hydroxybutyrate (3HB)-co-47.7 mol% D-phenyllactate) can be produced from glucose and sodium 3HB. Also, various poly(3HB-co-D-phenyllactate) polymers having 11.0, 15.8, 20.0, 70.8, and 84.5 mol% of D-phenyllactate are produced from glucose as a sole carbon source by additional expression of Ralstonia eutropha ß-ketothiolase (phaA) and reductase (phaB) genes. Fed-batch culture of this engineered strain produces 13.9 g l of poly(61.9 mol% 3HB-co-38.1 mol% D-phenyllactate). Furthermore, different aromatic polyesters containing D-mandelate and D-3-hydroxy-3-phenylpropionate are produced from glucose when feeding the corresponding monomers. The engineered bacterial system will be useful for one-step fermentative production of aromatic polyesters from renewable resources.
[Mh] Termos MeSH primário: Escherichia coli/metabolismo
Fermentação
Glucose/metabolismo
Engenharia Metabólica/métodos
Poliésteres/metabolismo
[Mh] Termos MeSH secundário: Ácido 3-Hidroxibutírico/metabolismo
Acetil-CoA C-Aciltransferase/genética
Acetil-CoA C-Aciltransferase/metabolismo
Aciltransferases/genética
Aciltransferases/metabolismo
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Clostridium difficile/enzimologia
Clostridium difficile/genética
Coenzima A-Transferases/genética
Coenzima A-Transferases/metabolismo
Cupriavidus necator/enzimologia
Cupriavidus necator/genética
Escherichia coli/genética
Lactatos/metabolismo
Oxirredutases/genética
Oxirredutases/metabolismo
Polietilenotereftalatos/metabolismo
Polímeros/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Lactates); 0 (Polyesters); 0 (Polyethylene Terephthalates); 0 (Polymers); 156-05-8 (3-phenyllactic acid); EC 1.- (Oxidoreductases); EC 2.3.- (Acyltransferases); EC 2.3.1.- (poly(3-hydroxyalkanoic acid) synthase); EC 2.3.1.16 (Acetyl-CoA C-Acyltransferase); EC 2.8.3.- (Coenzyme A-Transferases); IY9XDZ35W2 (Glucose); TZP1275679 (3-Hydroxybutyric Acid)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180110
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02498-w


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[PMID]:29328999
[Au] Autor:Wei H; Mao F; Ni S; Chen F; Li B; Qiu X; Hu L; Wang M; Zheng X; Zhu J; Lan L; Li J
[Ad] Endereço:Shanghai Key Laboratory of New Drug Design, School of Pharmacy, East China University of Science and Technology, 130 Mei Long Road, Shanghai 200237, China.
[Ti] Título:Discovery of novel piperonyl derivatives as diapophytoene desaturase inhibitors for the treatment of methicillin-, vancomycin- and linezolid-resistant Staphylococcus aureus infections.
[So] Source:Eur J Med Chem;145:235-251, 2018 Feb 10.
[Is] ISSN:1768-3254
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Inhibition of S. aureus diapophytoene desaturase (CrtN) could serve as an alternative approach for addressing the tricky antibiotic resistance by blocking the biosynthesis of carotenoid pigment which shields the bacterium from host oxidant killing. In this study, we designed and synthesized 44 derivatives with piperonyl scaffold targeting CrtN and the structure-activity relationships (SARs) were examined extensively to bring out the discovery of 21b with potent efficacy and better hERG safety profile compared to the first class CrtN inhibitor benzocycloalkane derivative 2. Except the excellent pigment inhibitory activity against wild-type S. aureus, 21b also showed excellent pigment inhibition against four pigmented MRSA strains. In addition, H O killing and human whole blood killing assays proved 21b could sensitize S. aureus to be killed under oxidative stress conditions. Notably, the murine study in vivo validated the efficacy of 21b against pigmented S. aureus Newman, vancomycin-intermediate S. aureus Mu50 and linezolid-resistant S. aureus NRS271.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Proteínas de Bactérias/antagonistas & inibidores
Farmacorresistência Bacteriana/efeitos dos fármacos
Oxirredutases/antagonistas & inibidores
Butóxido de Piperonila/farmacologia
Infecções Estafilocócicas/tratamento farmacológico
Staphylococcus aureus/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Antibacterianos/síntese química
Antibacterianos/química
Proteínas de Bactérias/metabolismo
Relação Dose-Resposta a Droga
Descoberta de Drogas
Seres Humanos
Linezolida/farmacologia
Meticilina/farmacologia
Camundongos
Testes de Sensibilidade Microbiana
Estrutura Molecular
Oxirredutases/metabolismo
Butóxido de Piperonila/análogos & derivados
Butóxido de Piperonila/química
Staphylococcus aureus/enzimologia
Relação Estrutura-Atividade
Vancomicina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 6Q205EH1VU (Vancomycin); EC 1.- (CrtN protein, Staphylococcus aureus); EC 1.- (Oxidoreductases); ISQ9I6J12J (Linezolid); LWK91TU9AH (Piperonyl Butoxide); Q91FH1328A (Methicillin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180113
[St] Status:MEDLINE


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[PMID]:29205772
[Au] Autor:Taher ES; Banwell MG; Buckler JN; Yan Q; Lan P
[Ad] Endereço:Research School of Chemistry, Institute of Advanced Studies, The Australian National University, Canberra, ACT 2601, Australia.
[Ti] Título:The Exploitation of Enzymatically-Derived cis-1,2-Dihydrocatechols and Related Compounds in the Synthesis of Biologically Active Natural Products.
[So] Source:Chem Rec;18(2):239-264, 2018 Feb.
[Is] ISSN:1528-0691
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The title compounds of the general form 1 can be produced at large scale and in essentially enantiomerically pure form (when X≠H) through the whole cell biotransformation of the corresponding aromatic. The "dense" and varied functionality associated with these metabolites mean that they have become increasingly useful chirons for the total synthesis of a range of natural product types. This personal account details the outcomes of a nearly three-decade long campaign within our group to exploit these compounds in the synthesis of a diverse range of small molecule natural product targets. The work is subdivided according to the key transformation(s) employed in each synthesis. The development of newer chirons that "complement" the utility of the cis-1,2-dihydrocatechols are also described.
[Mh] Termos MeSH primário: Produtos Biológicos/metabolismo
Catecóis/metabolismo
Oxirredutases/metabolismo
Oxigenases/metabolismo
[Mh] Termos MeSH secundário: Produtos Biológicos/química
Catecóis/química
Estrutura Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Biological Products); 0 (Catechols); 0 (cis-1,2-dihydrocatechol); EC 1.- (Oxidoreductases); EC 1.13.- (Oxygenases); EC 1.14.12.11 (toluene dioxygenase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171206
[St] Status:MEDLINE
[do] DOI:10.1002/tcr.201700064


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[PMID]:29317632
[Au] Autor:Fang G; Li W; Shen X; Perez-Aguilar JM; Chong Y; Gao X; Chai Z; Chen C; Ge C; Zhou R
[Ad] Endereço:School for Radiological and Interdisciplinary Sciences (RAD-X), Collaborative Innovation Center of Radiation Medicine of Jiangsu Higher Education Institutions, Soochow University, Suzhou, 215123, China.
[Ti] Título:Differential Pd-nanocrystal facets demonstrate distinct antibacterial activity against Gram-positive and Gram-negative bacteria.
[So] Source:Nat Commun;9(1):129, 2018 01 09.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Noble metal-based nanomaterials have shown promise as potential enzyme mimetics, but the facet effect and underlying molecular mechanisms are largely unknown. Herein, with a combined experimental and theoretical approach, we unveil that palladium (Pd) nanocrystals exhibit facet-dependent oxidase and peroxidase-like activities that endow them with excellent antibacterial properties via generation of reactive oxygen species. The antibacterial efficiency of Pd nanocrystals against Gram-positive bacteria is consistent with the extent of their enzyme-like activity, that is {100}-faceted Pd cubes with higher activities kill bacteria more effectively than {111}-faceted Pd octahedrons. Surprisingly, a reverse trend of antibacterial activity is observed against Gram-negative bacteria, with Pd octahedrons displaying stronger penetration into bacterial membranes than Pd nanocubes, thereby exerting higher antibacterial activity than the latter. Our findings provide a deeper understanding of facet-dependent enzyme-like activities and might advance the development of noble metal-based nanomaterials with both enhanced and targeted antibacterial activities.
[Mh] Termos MeSH primário: Antibacterianos/química
Bactérias Gram-Negativas/crescimento & desenvolvimento
Bactérias Gram-Positivas/crescimento & desenvolvimento
Nanopartículas/química
Paládio/química
[Mh] Termos MeSH secundário: Antibacterianos/metabolismo
Antibacterianos/farmacologia
Bactérias Gram-Negativas/efeitos dos fármacos
Bactérias Gram-Positivas/efeitos dos fármacos
Testes de Sensibilidade Microbiana
Microscopia Eletrônica de Transmissão
Nanopartículas/metabolismo
Nanopartículas/ultraestrutura
Oxirredutases/metabolismo
Paládio/metabolismo
Paládio/farmacologia
Peroxidase/metabolismo
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Reactive Oxygen Species); 5TWQ1V240M (Palladium); EC 1.- (Oxidoreductases); EC 1.11.1.7 (Peroxidase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180111
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02502-3


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[PMID]:28745773
[Au] Autor:Wang B; Huang W; Zhou J; Tang X; Chen Y; Peng C; Han B
[Ad] Endereço:State Key Laboratory Breeding Base of Systematic Research, Development and Utilization of Chinese Medicine Resources, Chengdu University of Traditional Chinese Medicine, Chengdu 611137, China. hanbo@cdutcm.edu.cn.
[Ti] Título:Drug design based on pentaerythritol tetranitrate reductase: synthesis and antibacterial activity of Pogostone derivatives.
[So] Source:Org Biomol Chem;15(31):6548-6556, 2017 Aug 09.
[Is] ISSN:1477-0539
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Our previous work showed that Pogostone exerts antibacterial effects by targeting pentaerythritol tetranitrate reductase (PETNR). In order to develop derivatives of Pogostone with potent antibacterial activity, we performed molecular docking studies of Pogostone with PETNR and analyzed structure-activity relationships, which guided the structure design and the subsequent facile organocatalytic synthesis of Pogostone derivatives under mild reaction conditions. Several of the synthesized compounds showed antibacterial activity in vitro, including one compound (3h) that was highly effective against methicillin-resistant Staphylococcus aureus. These results suggest that Pogostone derivatives bearing functional groups on the side chain may be good leads for antibacterial drug development.
[Mh] Termos MeSH primário: Antibacterianos/química
Antibacterianos/farmacologia
Bactérias/efeitos dos fármacos
Bactérias/enzimologia
Óleos Voláteis/química
Óleos Voláteis/farmacologia
Oxirredutases/antagonistas & inibidores
[Mh] Termos MeSH secundário: Antibacterianos/síntese química
Desenho de Drogas
Escherichia coli/efeitos dos fármacos
Escherichia coli/enzimologia
Infecções por Escherichia coli/tratamento farmacológico
Seres Humanos
Staphylococcus aureus Resistente à Meticilina/efeitos dos fármacos
Staphylococcus aureus Resistente à Meticilina/enzimologia
Testes de Sensibilidade Microbiana
Simulação de Acoplamento Molecular
Óleos Voláteis/síntese química
Oxirredutases/metabolismo
Infecções Estafilocócicas/tratamento farmacológico
Staphylococcus aureus/efeitos dos fármacos
Staphylococcus aureus/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Oils, Volatile); 0 (Pogostone); EC 1.- (Oxidoreductases); EC 1.7.99.- (pentaerythritol tetranitrate reductase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1039/c7ob01429e


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[PMID]:29293638
[Au] Autor:Campos MD; Valadas V; Campos C; Morello L; Braglia L; Breviario D; Cardoso HG
[Ad] Endereço:ICAAM-Instituto de Ciências Agrárias e Ambientais Mediterrânicas, Universidade de Évora, Pólo da Mitra, Évora, Portugal.
[Ti] Título:A TaqMan real-time PCR method based on alternative oxidase genes for detection of plant species in animal feed samples.
[So] Source:PLoS One;13(1):e0190668, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Traceability of processed food and feed products has been gaining importance due to the impact that those products can have on human/animal health and to the associated economic and legal concerns, often related to adulterations and frauds as it can be the case for meat and milk. Despite mandatory traceability requirements for the analysis of feed composition, few reliable and accurate methods are presently available to enforce the legislative frame and allow the authentication of animal feeds. In this study, nine sensitive and species-specific real-time PCR TaqMan MGB assays are described for plant species detection in animal feed samples. The method is based on selective real-time qPCR (RT-qPCR) amplification of target genes belonging to the alternative oxidase (AOX) gene family. The plant species selected for detection in feed samples were wheat, maize, barley, soybean, rice and sunflower as common components of feeds, and cotton, flax and peanut as possible undesirable contaminants. The obtained results were compared with end-point PCR methodology. The applicability of the AOX TaqMan assays was evaluated through the screening of commercial feed samples, and by the analysis of plant mixtures with known composition. The RT-qPCR methodology allowed the detection of the most abundant species in feeds but also the identification of contaminant species present in lower amounts, down to 1% w/w. AOX-based methodology provides a suitable molecular marker approach to ascertain plant species composition of animal feed samples, thus supporting feed control and enforcement of the feed sector and animal production.
[Mh] Termos MeSH primário: Ração Animal/análise
Contaminação de Alimentos/análise
Proteínas Mitocondriais/genética
Oxirredutases/genética
Proteínas de Plantas/genética
Plantas
Reação em Cadeia da Polimerase em Tempo Real/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Mitochondrial Proteins); 0 (Plant Proteins); EC 1.- (Oxidoreductases); EC 1.- (alternative oxidase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180103
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190668


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[PMID]:29264594
[Au] Autor:Hernández-Sánchez D; Villabona-Leal G; Saucedo-Orozco I; Bracamonte V; Pérez E; Bittencourt C; Quintana M
[Ad] Endereço:Instituto de Física, Universidad Autónoma de San Luis Potosí, Manuel Nava 6, Zona Universitaria, San Luis Potosí SLP 78290, Mexico. mildred@ifisica.uaslp.mx.
[Ti] Título:Stable graphene oxide-gold nanoparticle platforms for biosensing applications.
[So] Source:Phys Chem Chem Phys;20(3):1685-1692, 2018 Jan 17.
[Is] ISSN:1463-9084
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Graphene oxide-gold nanoparticle (AuNPs@GO) hybrids were fabricated in water dispersions of graphene oxide (GO) and Au precursor completely free of stabilizing agents by UV-light irradiation. Gold nanoparticle (AuNP) nucleation, growth, and stabilization mechanisms at the surface of GO are discussed on the basis of UV-Vis, Raman, IR, and X-Ray photo-spectroscopy studies. The analyses of AuNPs@GO hybrids by transmission electron microscopy (TEM), thermogravimetric (TGA) and electrochemical tests show that they exhibit outstanding chemical, thermal and electrochemical stabilities. Thus, AuNPs@GO biosensing platforms were fabricated for surface enhanced Raman spectroscopy (SERS) detection of crystal violet (CV), a SERS standard molecule, and in a different set of experiments, for flavin adenine dinucleotide (FAD), a flavoprotein coenzyme that plays an important role in many oxidoreductase and reversible redox conversions in biochemical reactions. AuNPs@GO hybrids synthesized by using UV light irradiation show exceptional stability and high intensification of the Raman signals showing that they have high potential for use as biomedical probes for the detection, monitoring, and diagnosis of medical diseases.
[Mh] Termos MeSH primário: Técnicas Biossensoriais/métodos
Ouro/química
Grafite/química
Nanopartículas Metálicas/química
[Mh] Termos MeSH secundário: Técnicas Eletroquímicas
Flavina-Adenina Dinucleotídeo/química
Microscopia Eletrônica de Transmissão
Oxirredução
Óxidos/química
Oxirredutases/química
Oxirredutases/metabolismo
Espectroscopia Fotoeletrônica
Espectrofotometria
Termogravimetria
Raios Ultravioleta
Água/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Oxides); 059QF0KO0R (Water); 146-14-5 (Flavin-Adenine Dinucleotide); 7440-57-5 (Gold); 7782-42-5 (Graphite); EC 1.- (Oxidoreductases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171222
[St] Status:MEDLINE
[do] DOI:10.1039/c7cp04817c


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[PMID]:28470606
[Au] Autor:de Marco A
[Ad] Endereço:Department of Biomedical Sciences and Engineering, University of Nova Gorica, Glavni Trg 9, SI-5261, Vipava, Slovenia. ario.demarco@ung.si.
[Ti] Título:Acting on Folding Effectors to Improve Recombinant Protein Yields and Functional Quality.
[So] Source:Methods Mol Biol;1586:197-210, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Molecular and chemical chaperones /foldases can strongly contribute to improve the amounts and the structural quality of recombinant proteins. Several methodologies have been proposed to optimize their beneficial effects. This chapter presents a condensed summary of the biotechnological opportunities offered by this approach followed by a protocol describing the method we use for expressing disulfide bond-dependent recombinant antibodies in the cytoplasm of bacteria engineered to overexpress sulfhydryl oxidase and DsbC isomerase. The system is based on the possibility to trigger the foldase expression independently and before the induction of the target protein. As a consequence, the recombinant antibody synthesis starts only after enough foldases have accumulated to promote correct folding of the antibody.
[Mh] Termos MeSH primário: Anticorpos/genética
Clonagem Molecular/métodos
Escherichia coli/genética
Engenharia Genética/métodos
Dobramento de Proteína
[Mh] Termos MeSH secundário: Animais
Anticorpos/química
Anticorpos/metabolismo
Escherichia coli/metabolismo
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Seres Humanos
Oxirredutases/genética
Oxirredutases/metabolismo
Agregados Proteicos
Isomerases de Dissulfetos de Proteínas/genética
Isomerases de Dissulfetos de Proteínas/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Solubilidade
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies); 0 (Escherichia coli Proteins); 0 (Protein Aggregates); 0 (Recombinant Proteins); EC 1.- (Oxidoreductases); EC 1.8.3.- (sulfhydryl oxidase); EC 5.3.4.1 (Protein Disulfide-Isomerases); EC 5.3.4.1 (dsbC protein, E coli)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-6887-9_12



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