Base de dados : MEDLINE
Pesquisa : B05.256 [Categoria DeCS]
Referências encontradas : 28 [refinar]
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  1 / 28 MEDLINE  
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[PMID]:27771364
[Au] Autor:Loder AJ; Han Y; Hawkins AB; Lian H; Lipscomb GL; Schut GJ; Keller MW; Adams MWW; Kelly RM
[Ad] Endereço:Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, NC 27695-7905, United States.
[Ti] Título:Reaction kinetic analysis of the 3-hydroxypropionate/4-hydroxybutyrate CO fixation cycle in extremely thermoacidophilic archaea.
[So] Source:Metab Eng;38:446-463, 2016 11.
[Is] ISSN:1096-7184
[Cp] País de publicação:Belgium
[La] Idioma:eng
[Ab] Resumo:The 3-hydroxypropionate/4-hydroxybutyrate (3HP/4HB) cycle fixes CO in extremely thermoacidophilic archaea and holds promise for metabolic engineering because of its thermostability and potentially rapid pathway kinetics. A reaction kinetics model was developed to examine the biological and biotechnological attributes of the 3HP/4HB cycle as it operates in Metallosphaera sedula, based on previous information as well as on kinetic parameters determined here for recombinant versions of five of the cycle enzymes (malonyl-CoA/succinyl-CoA reductase, 3-hydroxypropionyl-CoA synthetase, 3-hydroxypropionyl-CoA dehydratase, acryloyl-CoA reductase, and succinic semialdehyde reductase). The model correctly predicted previously observed features of the cycle: the 35-65% split of carbon flux through the acetyl-CoA and succinate branches, the high abundance and relative ratio of acetyl-CoA/propionyl-CoA carboxylase (ACC) and MCR, and the significance of ACC and hydroxybutyryl-CoA synthetase (HBCS) as regulated control points for the cycle. The model was then used to assess metabolic engineering strategies for incorporating CO into chemical intermediates and products of biotechnological importance: acetyl-CoA, succinate, and 3-hydroxypropionate.
[Mh] Termos MeSH primário: Dióxido de Carbono/metabolismo
Hidroxibutiratos/metabolismo
Ácido Láctico/análogos & derivados
Análise do Fluxo Metabólico/métodos
Redes e Vias Metabólicas/fisiologia
Modelos Biológicos
Sulfolobaceae/metabolismo
[Mh] Termos MeSH secundário: Archaea/metabolismo
Extremófilos/metabolismo
Cinética
Ácido Láctico/metabolismo
Taxa de Depuração Metabólica
Transdução de Sinais/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Hydroxybutyrates); 142M471B3J (Carbon Dioxide); 30IW36W5B2 (4-hydroxybutyric acid); 33X04XA5AT (Lactic Acid); C4ZF6XLD2X (hydracrylic acid)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


  2 / 28 MEDLINE  
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[PMID]:29176819
[Au] Autor:White RSA; McHugh PA; Glover CN; McIntosh AR
[Ad] Endereço:School of Biological Sciences, University of Canterbury, Christchurch, New Zealand.
[Ti] Título:Metabolism drives distribution and abundance in extremophile fish.
[So] Source:PLoS One;12(11):e0187597, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Differences in population density between species of varying size are frequently attributed to metabolic rates which are assumed to scale with body size with a slope of 0.75. This assumption is often criticised on the grounds that 0.75 scaling of metabolic rate with body size is not universal and can vary significantly depending on species and life-history. However, few studies have investigated how interspecific variation in metabolic scaling relationships affects population density in different sized species. Here we predict inter-specific differences in metabolism from niche requirements, thereby allowing metabolic predictions of species distribution and abundance at fine spatial scales. Due to the differences in energetic efficiency required along harsh-benign gradients, an extremophile fish (brown mudfish, Neochanna apoda) living in harsh environments had slower metabolism, and thus higher population densities, compared to a fish species (banded kokopu, Galaxias fasciatus) in physiologically more benign habitats. Interspecific differences in the intercepts for the relationship between body and density disappeared when species mass-specific metabolic rates, rather than body sizes, were used to predict density, implying population energy use was equivalent between mudfish and kokopu. Nevertheless, despite significant interspecific differences in the slope of the metabolic scaling relationships, mudfish and kokopu had a common slope for the relationship between body size and population density. These results support underlying logic of energetic equivalence between different size species implicit in metabolic theory. However, the precise slope of metabolic scaling relationships, which is the subject of much debate, may not be a reliable indicator of population density as expected under metabolic theory.
[Mh] Termos MeSH primário: Extremófilos/metabolismo
Peixes/metabolismo
[Mh] Termos MeSH secundário: Aerobiose
Animais
Metabolismo Basal
Peso Corporal
Modelos Biológicos
Densidade Demográfica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[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:171128
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0187597


  3 / 28 MEDLINE  
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[PMID]:28846925
[Au] Autor:Wu L; Uldahl KB; Chen F; Benasutti H; Logvinski D; Vu V; Banda NK; Peng X; Simberg D; Moghimi SM
[Ad] Endereço:Guangzhou Institute of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou 510530, People's Republic of China.
[Ti] Título:Interaction of extremophilic archaeal viruses with human and mouse complement system and viral biodistribution in mice.
[So] Source:Mol Immunol;90:273-279, 2017 Oct.
[Is] ISSN:1872-9142
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Archaeal viruses offer exceptional biophysical properties for modification and exploration of their potential in bionanotechnology, bioengineering and nanotherapeutic developments. However, the interaction of archaeal viruses with elements of the innate immune system has not been explored, which is a necessary prerequisite if their potential for biomedical applications to be realized. Here we show complement activation through lectin (via direct binding of MBL/MASPs) and alternative pathways by two extremophilic archaeal viruses (Sulfolobus monocaudavirus 1 and Sulfolobus spindle-shaped virus 2) in human serum. We further show some differences in initiation of complement activation pathways between these viruses. Since, Sulfolobus monocaudavirus 1 was capable of directly triggering the alternative pathway, we also demonstrate that the complement regulator factor H has no affinity for the viral surface, but factor H deposition is purely C3-dependent. This suggests that unlike some virulent pathogens Sulfolobus monocaudavirus 1 does not acquire factor H for protection. Complement activation with Sulfolobus monocaudavirus 1 also proceeds in murine sera through MBL-A/C as well as factor D-dependent manner, but C3 deficiency has no overall effect on viral clearance by organs of the reticuloendothelial system on intravenous injection. However, splenic deposition was significantly higher in C3 knockout animals compared with the corresponding wild type mice. We discuss the potential application of these viruses in biomedicine in relation to their complement activating properties.
[Mh] Termos MeSH primário: Vírus de Archaea/imunologia
Ativação do Complemento/imunologia
Via Alternativa do Complemento/imunologia
Imunidade Inata/imunologia
[Mh] Termos MeSH secundário: Adulto
Animais
Complemento C3/genética
Complemento C3/imunologia
Fator H do Complemento/imunologia
Extremófilos/imunologia
Feminino
Seres Humanos
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Microscopia Eletrônica de Transmissão
Sulfolobus/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Complement C3); 80295-65-4 (Complement Factor H)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170829
[St] Status:MEDLINE


  4 / 28 MEDLINE  
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[PMID]:28749982
[Au] Autor:Yoshida Y; Koutsovoulos G; Laetsch DR; Stevens L; Kumar S; Horikawa DD; Ishino K; Komine S; Kunieda T; Tomita M; Blaxter M; Arakawa K
[Ad] Endereço:Institute for Advanced Biosciences, Keio University, Tsuruoka, Yamagata, Japan.
[Ti] Título:Comparative genomics of the tardigrades Hypsibius dujardini and Ramazzottius varieornatus.
[So] Source:PLoS Biol;15(7):e2002266, 2017 Jul.
[Is] ISSN:1545-7885
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tardigrada, a phylum of meiofaunal organisms, have been at the center of discussions of the evolution of Metazoa, the biology of survival in extreme environments, and the role of horizontal gene transfer in animal evolution. Tardigrada are placed as sisters to Arthropoda and Onychophora (velvet worms) in the superphylum Panarthropoda by morphological analyses, but many molecular phylogenies fail to recover this relationship. This tension between molecular and morphological understanding may be very revealing of the mode and patterns of evolution of major groups. Limnoterrestrial tardigrades display extreme cryptobiotic abilities, including anhydrobiosis and cryobiosis, as do bdelloid rotifers, nematodes, and other animals of the water film. These extremophile behaviors challenge understanding of normal, aqueous physiology: how does a multicellular organism avoid lethal cellular collapse in the absence of liquid water? Meiofaunal species have been reported to have elevated levels of horizontal gene transfer (HGT) events, but how important this is in evolution, and particularly in the evolution of extremophile physiology, is unclear. To address these questions, we resequenced and reassembled the genome of H. dujardini, a limnoterrestrial tardigrade that can undergo anhydrobiosis only after extensive pre-exposure to drying conditions, and compared it to the genome of R. varieornatus, a related species with tolerance to rapid desiccation. The 2 species had contrasting gene expression responses to anhydrobiosis, with major transcriptional change in H. dujardini but limited regulation in R. varieornatus. We identified few horizontally transferred genes, but some of these were shown to be involved in entry into anhydrobiosis. Whole-genome molecular phylogenies supported a Tardigrada+Nematoda relationship over Tardigrada+Arthropoda, but rare genomic changes tended to support Tardigrada+Arthropoda.
[Mh] Termos MeSH primário: Extremófilos/genética
Regulação da Expressão Gênica
Proteoma/metabolismo
Tardígrados/genética
[Mh] Termos MeSH secundário: Animais
Sequência de Bases
Mapeamento Cromossômico/veterinária
DNA/química
DNA/metabolismo
Dessecação
Extremófilos/crescimento & desenvolvimento
Extremófilos/fisiologia
Perfilação da Expressão Gênica/veterinária
Transferência Genética Horizontal
Ligação Genética
Tamanho do Genoma
Estudo de Associação Genômica Ampla/veterinária
Biblioteca Genômica
Sequenciamento de Nucleotídeos em Larga Escala/veterinária
Família Multigênica
Filogenia
Proteoma/genética
Reprodutibilidade dos Testes
Especificidade da Espécie
Tardígrados/crescimento & desenvolvimento
Tardígrados/fisiologia
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; VALIDATION STUDIES
[Nm] Nome de substância:
0 (Proteome); 9007-49-2 (DNA)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170829
[Lr] Data última revisão:
170829
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pbio.2002266


  5 / 28 MEDLINE  
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[PMID]:28708392
[Au] Autor:Koyanagi T; Cifelli JL; Leriche G; Onofrei D; Holland GP; Yang J
[Ad] Endereço:Department of Chemistry and Biochemistry, University of California San Diego , La Jolla, California 92093, United States.
[Ti] Título:Thiol-Triggered Release of Intraliposomal Content from Liposomes Made of Extremophile-Inspired Tetraether Lipids.
[So] Source:Bioconjug Chem;28(8):2041-2045, 2017 Aug 16.
[Is] ISSN:1520-4812
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Liposomal drug-delivery systems have been used for delivery of drugs to targeted tissues while reducing unwanted side effects. DOXIL, for instance, is a liposomal formulation of the anticancer agent doxorubicin (DOX) that has been used to address problems associated with nonspecific toxicity of free DOX. However, while this liposomal formulation allows for a more-stable circulation of doxorubicin in the body compared to free drug, the efficacy for cancer therapy is reduced in comparison with systemic injections of free drug. A robust liposomal system that can be triggered to release DOX in cancer cells could mitigate problems associated with reduced drug efficacy. In this work, we present a serum-stable, cholesterol-integrated tetraether lipid comprising of a cleavable disulfide bond, {GcGT(S-S)PC-CH}, that is designed to respond to the reducing environment of the cell to trigger the release intraliposomal content upon cellular uptake by cancer cells. A cell viability assay revealed that DOX- loaded liposomes composed of pure GcGT(S-S)PC-CH lipids were ∼20 times more toxic than DOXIL, with an IC value comparable to that of free DOX. The low inherent membrane-leakage properties of GcGT(S-S)PC-CH liposomes in the presence of serum, combined with an intracellular triggered release of encapsulated cargo, represents a promising approach for developing improved drug-delivery formulations for the treatment of cancer and possibly other diseases.
[Mh] Termos MeSH primário: Liberação Controlada de Fármacos
Extremófilos
Lipossomos/química
Fosforilcolina/química
Compostos de Sulfidrila/química
[Mh] Termos MeSH secundário: Transporte Biológico
Colesterol/química
Doxorrubicina/química
Doxorrubicina/metabolismo
Células HeLa
Seres Humanos
Modelos Moleculares
Conformação Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Liposomes); 0 (Sulfhydryl Compounds); 107-73-3 (Phosphorylcholine); 80168379AG (Doxorubicin); 97C5T2UQ7J (Cholesterol)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170715
[St] Status:MEDLINE
[do] DOI:10.1021/acs.bioconjchem.7b00342


  6 / 28 MEDLINE  
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[PMID]:28630130
[Au] Autor:Mao D; Grogan DW
[Ad] Endereço:Department of Biological Sciences, University of Cincinnati, Cincinnati, Ohio, USA.
[Ti] Título:How a Genetically Stable Extremophile Evolves: Modes of Genome Diversification in the Archaeon Sulfolobus acidocaldarius.
[So] Source:J Bacteriol;199(17), 2017 Sep 01.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In order to analyze in molecular terms how genomes diverge, damage-induced mutations and natural polymorphisms (PMs) were identified in laboratory constructs and wild-type isolates, respectively, of Among wild-type isolates drawn from one local population, pairwise nucleotide divergence averaged 4 × 10 , which is about 0.15% of the corresponding divergence reported for The most variable features of wild-type genomes were homopolymer (mononucleotide) tracts and longer tandem repeats, consistent with the spontaneous mutations that occur under laboratory conditions. Natural isolates, however, also revealed large insertions/deletions and inversions, which did not occur in any of the laboratory-manipulated strains. Several of the large insertions/deletions could be attributed to the integration or excision of mobile genetic elements (MGEs), and each MGE represented a distinct system of site-specific recombination. The mode of recombination associated with one MGE, a provirus related to , was also seen in certain chromosomal inversions. Artificially induced mutations, non-MGE insertions/deletions, and small PMs exhibited different distributions over the genome, suggesting that large-scale patterning of genomes begins early in the divergence process. Unlike induced mutations, natural base pair substitutions occurred in clusters, and one cluster exhibited properties expected of nonreciprocal recombination (gene conversion) between dispersed imperfect repeats. Taken together, the results identify simple replication errors, slipped-strand events promoted by tandem repeats, homologous recombination, and rearrangements promoted by MGEs as the primary sources of genetic variation for this extremely acidophilic archaeon in its geothermal environment. The optimal growth temperatures of hyperthermophilic archaea accelerate DNA decomposition, which is expected to make DNA repair especially important for their genetic stability, yet these archaea lack certain broadly conserved types of DNA repair proteins. In this study, the genome of the extreme thermoacidophile was found to be remarkably stable, accumulating few mutations in many (though not all) laboratory manipulations and in natural populations. Furthermore, all the genetic processes that were inferred to diversify these genomes also operate in mesophilic bacteria and eukaryotes. This suggests that a common set of mechanisms produces most of the genetic variation in all microorganisms, despite the fundamental differences in physiology, DNA repair systems, and genome structure represented in the three domains of life.
[Mh] Termos MeSH primário: Evolução Molecular
Extremófilos/genética
Genoma Arqueal
Polimorfismo Genético
Sulfolobus acidocaldarius/genética
[Mh] Termos MeSH secundário: Replicação do DNA
Sequências Repetitivas Dispersas
Mutação
Recombinação Genética
Sulfolobus acidocaldarius/classificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170827
[Lr] Data última revisão:
170827
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170621
[St] Status:MEDLINE


  7 / 28 MEDLINE  
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[PMID]:28500892
[Au] Autor:Shehab NA; Ortiz-Medina JF; Katuri KP; Hari AR; Amy G; Logan BE; Saikaly PE
[Ad] Endereço:Biological and Environmental Sciences and Engineering Division, Water Desalination and Reuse Research Center, King Abdullah University of Science and Technology, Thuwal 23955-6900, Saudi Arabia; Research Product Development Innovations, The Business Gate Qurtubah, Riyadh 13244, Saudi Arabia.
[Ti] Título:Enrichment of extremophilic exoelectrogens in microbial electrolysis cells using Red Sea brine pools as inocula.
[So] Source:Bioresour Technol;239:82-86, 2017 Sep.
[Is] ISSN:1873-2976
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Applying microbial electrochemical technologies for the treatment of highly saline or thermophilic solutions is challenging due to the lack of proper inocula to enrich for efficient exoelectrogens. Brine pools from three different locations (Valdivia, Atlantis II and Kebrit) in the Red Sea were investigated as potential inocula sources for enriching exoelectrogens in microbial electrolysis cells (MECs) under thermophilic (70°C) and hypersaline (25% salinity) conditions. Of these, only the Valdivia brine pool produced high and consistent current 6.8±2.1A/m -anode in MECs operated at a set anode potential of +0.2V vs. Ag/AgCl (+0.405V vs. standard hydrogen electrode). These results show that exoelectrogens are present in these extreme environments and can be used to startup MEC under thermophilic and hypersaline conditions. Bacteroides was enriched on the anode of the Valdivia MEC, but it was not detected in the open circuit voltage reactor seeded with the Valdivia brine pool.
[Mh] Termos MeSH primário: Fontes de Energia Bioelétrica
Sais
[Mh] Termos MeSH secundário: Bactérias
Eletrólise
Extremófilos
Oceano Índico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Salts); 0 (brine)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170514
[St] Status:MEDLINE


  8 / 28 MEDLINE  
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[PMID]:28394913
[Au] Autor:Zebardast Roodi F; Aminzadeh S; Farrokhi N; Karkhane A; Haghbeen K
[Ad] Endereço:Department of Industrial and Environmental Biotechnology, National Institute for Genetic Engineering and Biotechnology (NIGEB), Tehran, Iran.
[Ti] Título:Cohnella amylopullulanases: Biochemical characterization of two recombinant thermophilic enzymes.
[So] Source:PLoS One;12(4):e0175013, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Some industries require newer, more efficient recombinant enzymes to accelerate their ongoing biochemical reactions in harsh environments with less replenishment. Thus, the search for native enzymes from extremophiles that are suitable for use under industrial conditions is a permanent challenge for R & D departments. Here and toward such discoveries, two sequences homologous to amylopullulanases (EC 3.2.1.41, GH57) from an endogenous Cohnella sp., [Coh00831 (KP335161; 1998 bp) and Coh01133 (KP335160: 3678 bp)] were identified. The genes were heterologously expressed in E. coli to both determine their type and further characterize their properties. The isolated DNA was PCR amplified with gene specific primers and cloned in pET28a, and the recombinant proteins were expressed in E. coli BL21 (DE3). The temperatures and pH optima of purified recombinants Coh 01133 and Coh 00831 enzymes were 70°C and 8, and 60°C and 6, respectively. These enzymes are stable more than 90% in 60°C and 50°C for 90 min respectively. The major reactions released sugars which could be fractionated by HPLC analysis, from soluble starch were mainly maltose (G2), maltotriose (G3) and maltotetraose (G4). The enzymes hydrolyzed pullulan to maltotriose (G3) only. Enzyme activities for both proteins were improved in the availability of Mn2+, Ba2+, Ca2+, and Mg2+ and reduced in the presence of Fe2+, Li2+, Na2+, Triton X100 and urea. Moreover, Co2+, K+, and Cu2+ had a negative effect only on Coh 01133 enzyme.
[Mh] Termos MeSH primário: Bacillales/enzimologia
Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Extremófilos/enzimologia
Glicosídeo Hidrolases/química
Glicosídeo Hidrolases/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Cátions/química
Cátions/farmacologia
Cromatografia Líquida de Alta Pressão
Sequência Conservada
Estabilidade Enzimática
Escherichia coli/genética
Glucanos/metabolismo
Glicosídeo Hidrolases/genética
Temperatura Alta
Concentração de Íons de Hidrogênio
Metais/química
Metais/farmacologia
Filogenia
Reação em Cadeia da Polimerase
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Homologia de Sequência de Aminoácidos
Amido/química
Amido/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cations); 0 (Glucans); 0 (Metals); 0 (Recombinant Proteins); 8ZQ0AYU1TT (pullulan); 9005-25-8 (Starch); EC 3.2.1.- (Glycoside Hydrolases); EC 3.2.1.41 (amylopullulanase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170830
[Lr] Data última revisão:
170830
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170411
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0175013


  9 / 28 MEDLINE  
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[PMID]:28103321
[Au] Autor:Lomonosova AV; Ulitin AB; Kazakov AS; Mirzabekov TA; Permyakov EA; Permyakov SE
[Ad] Endereço:Institute for Biological Instrumentation of the Russian Academy of Sciences, Pushchino, Moscow region, Russia.
[Ti] Título:Derivative of Extremophilic 50S Ribosomal Protein L35Ae as an Alternative Protein Scaffold.
[So] Source:PLoS One;12(1):e0170349, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Small antibody mimetics, or alternative binding proteins (ABPs), extend and complement antibody functionality with numerous applications in research, diagnostics and therapeutics. Given the superiority of ABPs, the last two decades have witnessed development of dozens of alternative protein scaffolds (APSs) for the design of ABPs. Proteins from extremophiles with their high structural stability are especially favorable for APS design. Here, a 10X mutant of the 50S ribosomal protein L35Ae from hyperthermophilic archaea Pyrococcus horikoshii has been probed as an APS. A phage display library of L35Ae 10X was generated by randomization of its three CDR-like loop regions (repertoire size of 2×108). Two L35Ae 10X variants specific to a model target, the hen egg-white lysozyme (HEL), were isolated from the resulting library using phage display. The affinity of these variants (L4 and L7) to HEL ranges from 0.10 µM to 1.6 µM, according to surface plasmon resonance data. While L4 has 1-2 orders of magnitude lower affinity to HEL homologue, bovine α-lactalbumin (BLA), L7 is equally specific to HEL and BLA. The reference L35Ae 10X is non-specific to both HEL and BLA. L4 and L7 are more resistant to denaturation by guanidine hydrochloride compared to the reference L35Ae 10X (mid-transition concentration is higher by 0.1-0.5 M). Chemical crosslinking experiments reveal an increased propensity of L4 and L7 to multimerization. Overall, the CDR-like loop regions of L35Ae 10X represent a proper interface for generation of functional ABPs. Hence, L35Ae is shown to extend the growing family of protein scaffolds dedicated to the design of novel binding proteins.
[Mh] Termos MeSH primário: Proteínas Arqueais/química
Pyrococcus horikoshii/química
Proteínas Ribossômicas/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Proteínas Arqueais/genética
Proteínas Arqueais/metabolismo
Materiais Biomiméticos/química
Materiais Biomiméticos/metabolismo
Biotecnologia
Proteínas de Transporte/química
Proteínas de Transporte/genética
Proteínas de Transporte/metabolismo
Bovinos
Galinhas
Extremófilos/química
Extremófilos/genética
Lactalbumina/metabolismo
Modelos Moleculares
Muramidase/metabolismo
Biblioteca de Peptídeos
Engenharia de Proteínas
Estrutura Terciária de Proteína
Pyrococcus horikoshii/genética
Proteínas Ribossômicas/genética
Proteínas Ribossômicas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Carrier Proteins); 0 (Peptide Library); 0 (Ribosomal Proteins); 9013-90-5 (Lactalbumin); EC 3.2.1.- (hen egg lysozyme); EC 3.2.1.17 (Muramidase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170120
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0170349


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[PMID]:28067849
[Au] Autor:Zhang H; Fei R; Xue B; Yu S; Zhang Z; Zhong S; Gao Y; Zhou X
[Ad] Endereço:Department of Cell Biology, College of Basic Medical Sciences, Jilin University, Changchun 130021, China. zhanghuan1990@yahoo.com.
[Ti] Título:Pnserpin: A Novel Serine Protease Inhibitor from Extremophile Pyrobaculum neutrophilum.
[So] Source:Int J Mol Sci;18(1), 2017 Jan 07.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Serine protease inhibitors (serpins) are native inhibitors of serine proteases, constituting a large protein family with members spread over eukaryotes and prokaryotes. However, only very few prokaryotic serpins, especially from extremophiles, have been characterized to date. In this study, Pnserpin, a putative serine protease inhibitor from the thermophile , was overexpressed in for purification and characterization. It irreversibly inhibits chymotrypsin-, trypsin-, elastase-, and subtilisin-like proteases in a temperature range from 20 to 100 °C in a concentration-dependent manner. The stoichiometry of inhibition (SI) of Pnserpin for proteases decreases as the temperature increases, indicating that the inhibitory activity of Pnserpin increases with the temperature. SDS-PAGE (sodium dodecyl sulfate polyacrylamide gel electrophoresis) showed that Pnserpin inhibits proteases by forming a SDS-resistant covalent complex. Homology modeling and molecular dynamic simulations predicted that Pnserpin can form a stable common serpin fold. Results of the present work will help in understanding the structural and functional characteristics of thermophilic serpin and will broaden the current knowledge about serpins from extremophiles.
[Mh] Termos MeSH primário: Extremófilos/química
Pyrobaculum/química
Inibidores de Serino Proteinase/isolamento & purificação
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Eletroforese em Gel de Poliacrilamida
Concentração de Íons de Hidrogênio
Cinética
Simulação de Dinâmica Molecular
Estabilidade Proteica
Reprodutibilidade dos Testes
Alinhamento de Sequência
Análise de Sequência de Proteína
Inibidores de Serino Proteinase/química
Homologia Estrutural de Proteína
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Serine Proteinase Inhibitors)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170424
[Lr] Data última revisão:
170424
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170110
[St] Status:MEDLINE



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