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  1 / 5043 MEDLINE  
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[PMID]:29215959
[Au] Autor:Garcia-Peña EI; Niño-Navarro C; Chairez I; Torres-Bustillos L; Ramírez-Muñoz J; Salgado-Manjarrez E
[Ad] Endereço:a Department of Bioprocesses , Unidad Profesional Interdisciplinaria de Biotecnología, Instituto Politécnico Nacional , Mexico City , Mexico.
[Ti] Título:Performance intensification of a stirred bioreactor for fermentative biohydrogen production.
[So] Source:Prep Biochem Biotechnol;48(1):64-74, 2018 Jan 02.
[Is] ISSN:1532-2297
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In this study, the biohydrogen (bioH ) production of a microbial consortium was optimized by adjusting the type and configuration of two impellers, the mixing regimen and the mass transfer process (K a coefficients). A continuous stirred-tank reactor (CSTR) system, with a nonstandard geometry, was characterized. Two different mixing configurations with either predominant axial (PB4 impeller) or radial pumping (Rushton impeller) were assessed and four different impeller configurations to produce bioH . The best configuration for an adequate mixing time was determined by an ANOVA analysis. A response surface methodology was also used to fully elucidate the optimal configuration. When the PB4 impellers were placed in best configuration, c/Dt = 0.5, s/Di = 1, the maximum bioH productivity obtained was 440 mL L hr , with a bioH molar yield of 1.8. The second best configuration obtained with the PB4 impellers presented a bioH productivity of 407.94 mL L hr . The configurations based on Rushton impellers showed a lower bioH productivity and bioH molar yield of 177.065 mL L hr and 0.71, respectively. The experiments with axial impellers (PB4) showed the lowest K a coefficient and the highest bioH production, suggesting that mixing is more important than K a for the enhanced production of bioH
[Mh] Termos MeSH primário: Reatores Biológicos
Hidrogênio/metabolismo
Microbiologia Industrial/instrumentação
[Mh] Termos MeSH secundário: Análise de Variância
Reatores Biológicos/microbiologia
Desenho de Equipamento
Fermentação
Hidrodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
7YNJ3PO35Z (Hydrogen)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171208
[St] Status:MEDLINE
[do] DOI:10.1080/10826068.2017.1405269


  2 / 5043 MEDLINE  
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[PMID]:29194020
[Au] Autor:Zhang J; Yuan J; Zhang WX; Tu F; Jiang Y; Sun CZ
[Ad] Endereço:a Department of Life Science and Food Engineering/Key Laboratory of Fermentation Resource and Application in Sichuan/Department of Library , Yibin University , Yibin , Sichuan , China.
[Ti] Título:Anaerobic detoxification fermentation by Rhodospirillum rubrum for rice straw as feed with moderate pretreatment.
[So] Source:Prep Biochem Biotechnol;48(1):75-83, 2018 Jan 02.
[Is] ISSN:1532-2297
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A novel and effective process was put forward for converting rice straw into feed by combining diluted acid hydrolysis and ammonization with Rhodospirillum rubrum fermentation. After pretreatment with dilute sulfuric or phosphoric acid (1%, w/w) at 100°C, materials were subjected to fermentation under several gases (N , CO , and air) and different light intensities in a 2-L fermentor. The key indexes of feed for fermented materials were estimated and several toxic substances were investigated during the fermentation. Following sulfuric acid treatment, the true protein of rice straw increased from 29 to 143 g kg and the crude fiber decreased from 359 to 136 g kg after fermentation at 0.3 L min L of N flow and a light intensity of 3400 lux; and following phosphoric acid treatment, the true protein increased by 286% and the crude fiber decreased by 52% after fermentation at 0.4 L min L of N flow and a light intensity of 3000 lux. Other key contents were also improved for use as feed, and some toxic substances (i.e., furfural, hydroxymethylfurfural, acetic acid, phenol, cresol) produced by the pretreatments could be removed at low levels during the fermentations.
[Mh] Termos MeSH primário: Ração Animal/análise
Oryza/metabolismo
Rhodospirillum rubrum/metabolismo
[Mh] Termos MeSH secundário: Ração Animal/toxicidade
Fermentação
Hidrólise
Microbiologia Industrial
Luz
Ácidos Fosfóricos/metabolismo
Ácidos Sulfúricos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phosphoric Acids); 0 (Sulfuric Acids); E4GA8884NN (phosphoric acid); O40UQP6WCF (sulfuric acid)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171202
[St] Status:MEDLINE
[do] DOI:10.1080/10826068.2017.1405023


  3 / 5043 MEDLINE  
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[PMID]:29194017
[Au] Autor:Abdul Manan FM; Attan N; Widodo N; Aboul-Enein HY; Wahab RA
[Ad] Endereço:a Department of Chemistry, Faculty of Science , Universiti Teknologi Malaysia , Skudai , Malaysia.
[Ti] Título:Rhizomucor miehei lipase immobilized on reinforced chitosan-chitin nanowhiskers support for synthesis of eugenyl benzoate.
[So] Source:Prep Biochem Biotechnol;48(1):92-102, 2018 Jan 02.
[Is] ISSN:1532-2297
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:An alternative environmentally benign support was prepared from chitosan-chitin nanowhiskers (CS/CNWs) for covalent immobilization of Rhizomucor miehei lipase (RML) to increase the operational stability and recyclability of RML in synthesizing eugenyl benzoate. The CS/CNWs support and RML-CS/CNWs were characterized using X-ray diffraction, fluorescent microscopy, and Fourier transform infrared spectroscopy. Efficiency of the RML-CS/CNWs was compared to the free RML to synthesize eugenyl benzoate for parameters: reaction temperature, stirring rate, reusability, and thermal stability. Under optimal experimental conditions (50°C, 250 rpm, catalyst loading 3 mg/mL), a twofold increase in yield of eugenyl benzoate was observed for RML-CS/CNWs as compared to free RML, with the former achieving maximum yield of the ester at 62.1% after 5 hr. Results demonstrated that the strategy adopted to prepare RML-CS/CNWs was useful, producing an improved and prospectively greener biocatalyst that supported a sustainable process to prepare eugenyl benzoate. Moreover, RML-CS/CNWs are biodegradable and perform esterification reactions under ambient conditions as compared to the less eco-friendly conventional acid catalyst. This research provides a facile and promising approach for improving activity of RML in which the resultant RML-CS/CNWs demonstrated good operational stability for up to eight successive esterification cycles to synthesize eugenyl benzoate.
[Mh] Termos MeSH primário: Benzoatos/metabolismo
Quitina/química
Quitosana/química
Enzimas Imobilizadas/metabolismo
Eugenol/análogos & derivados
Lipase/metabolismo
Rhizomucor/enzimologia
[Mh] Termos MeSH secundário: Benzoatos/química
Estabilidade Enzimática
Enzimas Imobilizadas/química
Esterificação
Eugenol/metabolismo
Microbiologia Industrial
Lipase/química
Nanoestruturas/química
Rhizomucor/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzoates); 0 (Enzymes, Immobilized); 1398-61-4 (Chitin); 3T8H1794QW (Eugenol); 9012-76-4 (Chitosan); EC 3.1.1.3 (Lipase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171202
[St] Status:MEDLINE
[do] DOI:10.1080/10826068.2017.1405021


  4 / 5043 MEDLINE  
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[PMID]:28468279
[Au] Autor:Terfrüchte M; Reindl M; Jankowski S; Sarkari P; Feldbrügge M; Schipper K
[Ad] Endereço:Institute for Microbiology, Cluster for Excellence on Plant Sciences, Heinrich Heine University Düsseldorf, 40204 Düsseldorf, Germany. marius.terfruechte@hhu.de.
[Ti] Título:Applying Unconventional Secretion in Ustilago maydis for the Export of Functional Nanobodies.
[So] Source:Int J Mol Sci;18(5), 2017 Apr 29.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Exploiting secretory pathways for production of heterologous proteins is highly advantageous with respect to efficient downstream processing. In eukaryotic systems the vast majority of heterologous proteins for biotechnological application is exported via the canonical endoplasmic reticulum-Golgi pathway. In the endomembrane system target proteins are often glycosylated and may thus be modified with foreign glycan patterns. This can be destructive for their activity or cause immune reactions against therapeutic proteins. Hence, using unconventional secretion for protein expression is an attractive alternative. In the fungal model , chitinase Cts1 is secreted via an unconventional pathway connected to cell separation which can be used to co-export heterologous proteins. Here, we apply this mechanism for the production of nanobodies. First, we achieved expression and unconventional secretion of a functional nanobody directed against green fluorescent protein (Gfp). Second, we found that Cts1 binds to chitin and that this feature can be applied to generate a Gfp-trap. Thus, we demonstrated the dual use of Cts1 serving both as export vehicle and as purification tag. Finally, we established and optimized the production of a nanobody against botulinum toxin A and hence describe the first pharmaceutically relevant target exported by Cts1-mediated unconventional secretion.
[Mh] Termos MeSH primário: Quitinases/metabolismo
Proteínas Fúngicas/metabolismo
Anticorpos de Domínio Único/metabolismo
Ustilago/metabolismo
[Mh] Termos MeSH secundário: Toxinas Botulínicas Tipo A/imunologia
Quitina/metabolismo
Clonagem Molecular
Proteínas de Fluorescência Verde/imunologia
Microbiologia Industrial
Transporte Proteico
Proteínas Recombinantes/genética
Proteínas Recombinantes/imunologia
Proteínas Recombinantes/metabolismo
Anticorpos de Domínio Único/genética
Anticorpos de Domínio Único/imunologia
Ustilago/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (Recombinant Proteins); 0 (Single-Domain Antibodies); 1398-61-4 (Chitin); 147336-22-9 (Green Fluorescent Proteins); EC 3.2.1.14 (Chitinases); EC 3.4.24.69 (Botulinum Toxins, Type A)
[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:170505
[St] Status:MEDLINE


  5 / 5043 MEDLINE  
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[PMID]:28467833
[Au] Autor:Bian X; Tang B; Yu Y; Tu Q; Gross F; Wang H; Li A; Fu J; Shen Y; Li YZ; Stewart AF; Zhao G; Ding X; Müller R; Zhang Y
[Ad] Endereço:Shandong University-Helmholtz Institute of Biotechnology, State Key Laboratory of Microbial Technology, School of Life Science, Shandong University , Qingdao 266235, China.
[Ti] Título:Heterologous Production and Yield Improvement of Epothilones in Burkholderiales Strain DSM 7029.
[So] Source:ACS Chem Biol;12(7):1805-1812, 2017 Jul 21.
[Is] ISSN:1554-8937
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The cloning of microbial natural product biosynthetic gene clusters and their heterologous expression in a suitable host have proven to be a feasible approach to improve the yield of valuable natural products and to begin mining cryptic natural products in microorganisms. Myxobacteria are a prolific source of novel bioactive natural products with only limited choices of heterologous hosts that have been exploited. Here, we describe the use of Burkholderiales strain DSM 7029 as a potential heterologous host for the functional expression of myxobacterial secondary metabolites. Using a newly established electroporation procedure, the 56 kb epothilone biosynthetic gene cluster from the myxobacterium Sorangium cellulosum was introduced into the chromosome of strain DSM 7029 by transposition. Production of epothilones A, B, C, and D was detected despite their yields being low. Optimization of the medium, introduction of the exogenous methylmalonyl-CoA biosynthetic pathway, and overexpression of rare tRNA genes resulted in an approximately 75-fold increase in the total yields of epothilones to 307 µg L . These results show that strain DSM 7029 has the potential to produce epothilones with reasonable titers and might be a broadly applicable host for the heterologous expression of other myxobacterial polyketide synthases and nonribosomal peptide synthetases, expediting the process of genome mining.
[Mh] Termos MeSH primário: Produtos Biológicos/metabolismo
Epotilonas/biossíntese
Microbiologia Industrial/métodos
Myxococcales/metabolismo
[Mh] Termos MeSH secundário: Cromatografia Líquida de Alta Pressão
Eletroporação
Epotilonas/química
Epotilonas/genética
Estrutura Molecular
Myxococcales/genética
RNA de Transferência/genética
RNA de Transferência/metabolismo
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biological Products); 0 (Epothilones); 9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180207
[Lr] Data última revisão:
180207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1021/acschembio.7b00097


  6 / 5043 MEDLINE  
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[PMID]:29220176
[Au] Autor:Wang S; Wang H; Lv J; Deng Z; Cheng H
[Ad] Endereço:State Key Laboratory of Microbial Metabolism, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University , Shanghai 200240, China.
[Ti] Título:Highly Efficient Erythritol Recovery from Waste Erythritol Mother Liquor by a Yeast-Mediated Biorefinery Process.
[So] Source:J Agric Food Chem;65(50):11020-11028, 2017 Dec 20.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Erythritol, a natural sugar alcohol, is produced industrially by fermentation and crystallization, but this process leaves a large amount of waste erythritol mother liquor (WEML) which contains more than 200 g/L erythritol as well as other polyol byproducts. These impurities make it very difficult to crystallize more erythritol. In our study, an efficient process for the recovery of erythritol from the WEML is described. The polyol impurities were first identified by high-performance liquid chromatography and gas chromatography-mass spectrometry, and a yeast strain Candida maltosa CGMCC 7323 was then isolated to metabolize those impurities to purify erythritol. Our results demonstrated that the process could remarkably improve the purity of erythritol and thus make the subsequent crystallization easier. This newly developed strategy is expected to have advantages in WEML treatment and provide helpful information with regard to green cell factories and zero-waste processing.
[Mh] Termos MeSH primário: Candida/metabolismo
Eritritol/metabolismo
Resíduos/análise
Yarrowia/metabolismo
[Mh] Termos MeSH secundário: Reatores Biológicos/microbiologia
Candida/genética
Candida/isolamento & purificação
Eritritol/química
Fermentação
Microbiologia Industrial
Polímeros/química
Polímeros/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Polymers); 0 (Waste Products); 0 (polyol); RA96B954X6 (Erythritol)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180110
[Lr] Data última revisão:
180110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171209
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b04112


  7 / 5043 MEDLINE  
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[PMID]:29247264
[Au] Autor:Kong M; Wang F; Tian L; Tang H; Zhang L
[Ad] Endereço:Engineering Laboratory of Microbial Breeding and Preservation of Hebei Province; Key Laboratory of Microbial Diversity Research and Application of Hebei Province; College of Life Sciences, Hebei University, Baoding, 071002, China.
[Ti] Título:Functional identification of glutamate cysteine ligase and glutathione synthetase in the marine yeast Rhodosporidium diobovatum.
[So] Source:Naturwissenschaften;105(1-2):4, 2017 Dec 15.
[Is] ISSN:1432-1904
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Glutathione (GSH) fulfills a variety of metabolic functions, participates in oxidative stress response, and defends against toxic actions of heavy metals and xenobiotics. In this study, GSH was detected in Rhodosporidium diobovatum by high-performance liquid chromatography (HPLC). Then, two novel enzymes from R. diobovatum were characterized that convert glutamate, cysteine, and glycine into GSH. Based on reverse transcription PCR, we obtained the glutathione synthetase gene (GSH2), 1866 bp, coding for a 56.6-kDa protein, and the glutamate cysteine ligase gene (GSH1), 2469 bp, coding for a 90.5-kDa protein. The role of GSH1 and GSH2 for the biosynthesis of GSH in the marine yeast R. diobovatum was determined by deletions using the CRISPR-Cas9 nuclease system and enzymatic activity. These results also showed that GSH1 and GSH2 were involved in the production of GSH and are thus being potentially useful to engineer GSH pathways. Alternatively, pET-GSH constructed using vitro recombination could be used to detect the function of genes related to GSH biosynthesis. Finally, the fermentation parameters determined in the present study provide a reference for industrial GSH production in R. diobovatum.
[Mh] Termos MeSH primário: Organismos Aquáticos/enzimologia
Glutamato-Cisteína Ligase/metabolismo
Glutationa Sintase/metabolismo
Rhodotorula/enzimologia
[Mh] Termos MeSH secundário: Organismos Aquáticos/genética
Glutamato-Cisteína Ligase/genética
Glutationa/biossíntese
Glutationa Sintase/genética
Microbiologia Industrial
Rhodotorula/genética
Deleção de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 6.3.2.2 (Glutamate-Cysteine Ligase); EC 6.3.2.3 (Glutathione Synthase); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171228
[Lr] Data última revisão:
171228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171217
[St] Status:MEDLINE
[do] DOI:10.1007/s00114-017-1520-2


  8 / 5043 MEDLINE  
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[PMID]:28451907
[Au] Autor:Bennett JW
[Ad] Endereço:Department of Plant Biology, Rutgers University, New Brunswick, NJ, 08901, USA. profmycogirl@yahoo.com.
[Ti] Título:On being an honorary member of Arny's army: some musings about fungal fermentations, secondary metabolism, and scientific communities.
[So] Source:J Ind Microbiol Biotechnol;44(4-5):507-516, 2017 May.
[Is] ISSN:1476-5535
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:This essay is an unabashed celebration of applied microbiology and secondary metabolism, and how one scientist-Arnold Demain-has been a spokesman for industrial microbiology and biotechnology. There are many reasons for Arny's professional success. During his long and distinguished career, Arnold Demain has expanded and enriched our understanding of the importance secondary metabolism. He has studied topics that ranged from pickles, to pectinolytic enzymes, to penicillin. His experimental versatility was conducted under the unifying theme of fermentation microbiology. In addition, one of his most positive achievements was his ability to bring scientists from different disciplines and national backgrounds together and thereby nucleate new collaborations. I am one of many people who has benefited from Arny's generous mentoring and speak from the heart when I say that industrial microbiology could not have a better representative. Arny has been the catalyst for much of that has gone right in my professional life and the lives of the many other applied microbiologists who have had the good fortune to know him.
[Mh] Termos MeSH primário: Fermentação
Fungos/metabolismo
[Mh] Termos MeSH secundário: Aflatoxinas
Microbiologia Industrial
Metabolismo Secundário
Sociedades Científicas
[Pt] Tipo de publicação:NEWS; PORTRAITS
[Nm] Nome de substância:
0 (Aflatoxins)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171228
[Lr] Data última revisão:
171228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1007/s10295-017-1923-2


  9 / 5043 MEDLINE  
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[PMID]:29185908
[Au] Autor:Prabhu AA; Venkata Dasu V
[Ad] Endereço:a Department of Biosciences and Bioengineering , Biochemical Engineering Laboratory, Indian Institute of Technology Guwahati , Guwahati , Assam , India.
[Ti] Título:Dual-substrate inhibition kinetic studies for recombinant human interferon gamma producing Pichia pastoris.
[So] Source:Prep Biochem Biotechnol;47(10):953-962, 2017 Nov 26.
[Is] ISSN:1532-2297
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Pichia pastoris is considered as one of the prominent host extensively used as a platform for heterologous protein production. In the present study, the growth inhibition kinetics of recombinant P. pastoris expressing human interferon gamma was studied under different initial substrate concentrations of gluconate (10-100 g L ) and methanol (2-50 g L ) in modified FM22 medium. The highest specific growth rate of 0.0206 and 0.019 hr was observed at 60 g L of gluconate and 10 g L of methanol, respectively. Various three- and four-parametric Monod-variant models were chosen to analyze the inhibition kinetics. The model parameters as well as goodness of fit were estimated using nonlinear regression analysis. The three-parameter Haldane model was found to be best fit for both gluconate (R = 0.95) and methanol substrate (R = 0.96). The parameter sensitivity analysis revealed that µ , K , and K are the most sensitive parameters for both methanol and gluconate. Different substrate inhibition models were fitted to the growth kinetic data and the additive form of double Webb model was found to be the best to explain the growth kinetics of recombinant P. pastoris.
[Mh] Termos MeSH primário: Gluconatos/metabolismo
Microbiologia Industrial/métodos
Interferon gama/metabolismo
Metanol/metabolismo
Pichia/crescimento & desenvolvimento
[Mh] Termos MeSH secundário: Meios de Cultura/metabolismo
Seres Humanos
Cinética
Pichia/metabolismo
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Culture Media); 0 (Gluconates); 0 (IFNG protein, human); 0 (Recombinant Proteins); 82115-62-6 (Interferon-gamma); R4R8J0Q44B (gluconic acid); Y4S76JWI15 (Methanol)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171225
[Lr] Data última revisão:
171225
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171130
[St] Status:MEDLINE
[do] DOI:10.1080/10826068.2017.1350977


  10 / 5043 MEDLINE  
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[PMID]:28450600
[Au] Autor:Bennett JW; Eveleigh D; Goodman RM
[Ad] Endereço:School of Environmental and Biological Sciences, Rutgers University, New Brunswick, NJ 08901, USA.
[Ti] Título:H. Boyd Woodruff (1917-2017).
[So] Source:Science;356(6336):381, 2017 Apr 28.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Antibacterianos/história
Indústria Farmacêutica/história
Microbiologia Industrial/história
[Mh] Termos MeSH secundário: Actinomyces/crescimento & desenvolvimento
Actinomyces/metabolismo
Dactinomicina/metabolismo
História do Século XX
História do Século XXI
Estados Unidos
[Pt] Tipo de publicação:BIOGRAPHY; HISTORICAL ARTICLE; JOURNAL ARTICLE
[Ps] Nome de pessoa como assunto:Woodruff HB
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 1CC1JFE158 (Dactinomycin)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171219
[Lr] Data última revisão:
171219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1126/science.aan3952



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