Base de dados : MEDLINE
Pesquisa : D12.776.037 [Categoria DeCS]
Referências encontradas : 1601 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 161 ir para página                         

  1 / 1601 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29023570
[Au] Autor:Sato N; Kamimura R; Kaneta K; Yoshikawa M; Tsuzuki M
[Ad] Endereço:School of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo, Japan.
[Ti] Título:Species-specific roles of sulfolipid metabolism in acclimation of photosynthetic microbes to sulfur-starvation stress.
[So] Source:PLoS One;12(10):e0186154, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Photosynthetic organisms utilize sulfate for the synthesis of sulfur-compounds including proteins and a sulfolipid, sulfoquinovosyl diacylglycerol. Upon ambient deficiency in sulfate, cells of a green alga, Chlamydomonas reinhardtii, degrade the chloroplast membrane sulfolipid to ensure an intracellular-sulfur source for necessary protein synthesis. Here, the effects of sulfate-starvation on the sulfolipid stability were investigated in another green alga, Chlorella kessleri, and two cyanobacteria, Synechocystis sp. PCC 6803 and Synechococcus elongatus PCC 7942. The results showed that sulfolipid degradation was induced only in C. kessleri, raising the possibility that this degradation ability was obtained not by cyanobacteria, but by eukaryotic algae during the evolution of photosynthetic organisms. Meanwhile, Synechococcus disruptants concerning sqdB and sqdX genes, which are involved in successive reactions in the sulfolipid synthesis pathway, were respectively characterized in cellular response to sulfate-starvation. Phycobilisome degradation intrinsic to Synechococcus, but not to Synechocystis, and cell growth under sulfate-starved conditions were repressed in the sqdB and sqdX disruptants, respectively, relative to in the wild type. Their distinct phenotypes, despite the common loss of the sulfolipid, inferred specific roles of sqdB and sqdX. This study demonstrated that sulfolipid metabolism might have been developed to enable species- or cyanobacterial-strain dependent processes for acclimation to sulfate-starvation.
[Mh] Termos MeSH primário: Chlorella/crescimento & desenvolvimento
Glicolipídeos/metabolismo
Enxofre/metabolismo
Synechococcus/crescimento & desenvolvimento
Synechocystis/crescimento & desenvolvimento
[Mh] Termos MeSH secundário: Aclimatação
Proteínas de Algas/genética
Proteínas de Bactérias/genética
Chlorella/genética
Chlorella/metabolismo
Evolução Molecular
Fotossíntese
Especificidade da Espécie
Estresse Fisiológico
Synechococcus/genética
Synechococcus/metabolismo
Synechocystis/genética
Synechocystis/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Algal Proteins); 0 (Bacterial Proteins); 0 (Glycolipids); 0 (sulfoquinovosyl diglyceride); 70FD1KFU70 (Sulfur)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171013
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186154


  2 / 1601 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28938114
[Au] Autor:Freeman Rosenzweig ES; Xu B; Kuhn Cuellar L; Martinez-Sanchez A; Schaffer M; Strauss M; Cartwright HN; Ronceray P; Plitzko JM; Förster F; Wingreen NS; Engel BD; Mackinder LCM; Jonikas MC
[Ad] Endereço:Department of Biology, Stanford University, Stanford, CA 94305, USA; Department of Plant Biology, Carnegie Institution for Science, Stanford, CA 94305, USA.
[Ti] Título:The Eukaryotic CO -Concentrating Organelle Is Liquid-like and Exhibits Dynamic Reorganization.
[So] Source:Cell;171(1):148-162.e19, 2017 Sep 21.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Approximately 30%-40% of global CO fixation occurs inside a non-membrane-bound organelle called the pyrenoid, which is found within the chloroplasts of most eukaryotic algae. The pyrenoid matrix is densely packed with the CO -fixing enzyme Rubisco and is thought to be a crystalline or amorphous solid. Here, we show that the pyrenoid matrix of the unicellular alga Chlamydomonas reinhardtii is not crystalline but behaves as a liquid that dissolves and condenses during cell division. Furthermore, we show that new pyrenoids are formed both by fission and de novo assembly. Our modeling predicts the existence of a "magic number" effect associated with special, highly stable heterocomplexes that influences phase separation in liquid-like organelles. This view of the pyrenoid matrix as a phase-separated compartment provides a paradigm for understanding its structure, biogenesis, and regulation. More broadly, our findings expand our understanding of the principles that govern the architecture and inheritance of liquid-like organelles.
[Mh] Termos MeSH primário: Chlamydomonas reinhardtii/citologia
Cloroplastos/ultraestrutura
[Mh] Termos MeSH secundário: Proteínas de Algas/metabolismo
Dióxido de Carbono/metabolismo
Chlamydomonas reinhardtii/química
Chlamydomonas reinhardtii/metabolismo
Cloroplastos/química
Cloroplastos/metabolismo
Microscopia Crioeletrônica
Biogênese de Organelas
Ribulose-Bifosfato Carboxilase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Algal Proteins); 142M471B3J (Carbon Dioxide); EC 4.1.1.39 (Ribulose-Bisphosphate Carboxylase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170923
[St] Status:MEDLINE


  3 / 1601 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28938113
[Au] Autor:Mackinder LCM; Chen C; Leib RD; Patena W; Blum SR; Rodman M; Ramundo S; Adams CM; Jonikas MC
[Ad] Endereço:Department of Plant Biology, Carnegie Institution for Science, Stanford, CA 94305, USA.
[Ti] Título:A Spatial Interactome Reveals the Protein Organization of the Algal CO -Concentrating Mechanism.
[So] Source:Cell;171(1):133-147.e14, 2017 Sep 21.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Approximately one-third of global CO fixation is performed by eukaryotic algae. Nearly all algae enhance their carbon assimilation by operating a CO -concentrating mechanism (CCM) built around an organelle called the pyrenoid, whose protein composition is largely unknown. Here, we developed tools in the model alga Chlamydomonas reinhardtii to determine the localizations of 135 candidate CCM proteins and physical interactors of 38 of these proteins. Our data reveal the identity of 89 pyrenoid proteins, including Rubisco-interacting proteins, photosystem I assembly factor candidates, and inorganic carbon flux components. We identify three previously undescribed protein layers of the pyrenoid: a plate-like layer, a mesh layer, and a punctate layer. We find that the carbonic anhydrase CAH6 is in the flagella, not in the stroma that surrounds the pyrenoid as in current models. These results provide an overview of proteins operating in the eukaryotic algal CCM, a key process that drives global carbon fixation.
[Mh] Termos MeSH primário: Proteínas de Algas/metabolismo
Ciclo do Carbono
Chlamydomonas reinhardtii/citologia
Chlamydomonas reinhardtii/metabolismo
Cloroplastos/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Algas/química
Dióxido de Carbono/metabolismo
Anidrases Carbônicas/metabolismo
Chlamydomonas reinhardtii/química
Cloroplastos/química
Proteínas Luminescentes/análise
Microscopia Confocal
Fotossíntese
Proteínas de Plantas/metabolismo
Ribulose-Bifosfato Carboxilase/química
Ribulose-Bifosfato Carboxilase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Algal Proteins); 0 (Luminescent Proteins); 0 (Plant Proteins); 142M471B3J (Carbon Dioxide); EC 4.1.1.39 (Ribulose-Bisphosphate Carboxylase); EC 4.2.1.1 (Cah6 protein, Chlamydomonas reinhardtii); EC 4.2.1.1 (Carbonic Anhydrases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170923
[St] Status:MEDLINE


  4 / 1601 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28892495
[Au] Autor:Yamamoto R; Obbineni JM; Alford LM; Ide T; Owa M; Hwang J; Kon T; Inaba K; James N; King SM; Ishikawa T; Sale WS; Dutcher SK
[Ad] Endereço:Department of Biological Sciences, Graduate School of Science, Osaka University, Osaka, Japan.
[Ti] Título:Chlamydomonas DYX1C1/PF23 is essential for axonemal assembly and proper morphology of inner dynein arms.
[So] Source:PLoS Genet;13(9):e1006996, 2017 Sep.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cytoplasmic assembly of ciliary dyneins, a process known as preassembly, requires numerous non-dynein proteins, but the identities and functions of these proteins are not fully elucidated. Here, we show that the classical Chlamydomonas motility mutant pf23 is defective in the Chlamydomonas homolog of DYX1C1. The pf23 mutant has a 494 bp deletion in the DYX1C1 gene and expresses a shorter DYX1C1 protein in the cytoplasm. Structural analyses, using cryo-ET, reveal that pf23 axonemes lack most of the inner dynein arms. Spectral counting confirms that DYX1C1 is essential for the assembly of the majority of ciliary inner dynein arms (IDA) as well as a fraction of the outer dynein arms (ODA). A C-terminal truncation of DYX1C1 shows a reduction in a subset of these ciliary IDAs. Sucrose gradients of cytoplasmic extracts show that preassembled ciliary dyneins are reduced compared to wild-type, which suggests an important role in dynein complex stability. The role of PF23/DYX1C1 remains unknown, but we suggest that DYX1C1 could provide a scaffold for macromolecular assembly.
[Mh] Termos MeSH primário: Proteínas de Algas/genética
Axonema/genética
Chlamydomonas reinhardtii/genética
Proteínas do Tecido Nervoso/genética
Proteínas Nucleares/genética
[Mh] Termos MeSH secundário: Animais
Axonema/química
Cílios/química
Cílios/genética
Citoplasma/genética
Citoplasma/metabolismo
Dineínas/química
Dineínas/genética
Flagelos/genética
Seres Humanos
Mutação
Proteínas do Tecido Nervoso/química
Proteínas Nucleares/química
Domínios Proteicos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Algal Proteins); 0 (DYX1C1 protein, human); 0 (Nerve Tissue Proteins); 0 (Nuclear Proteins); EC 3.6.4.2 (Dyneins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170912
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006996


  5 / 1601 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28659342
[Au] Autor:Kaufmann JCD; Krause BS; Grimm C; Ritter E; Hegemann P; Bartl FJ
[Ad] Endereço:From the Institut für medizinische Physik und Biophysik, Charité-Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany, joel.kaufmann@charite.de.
[Ti] Título:Proton transfer reactions in the red light-activatable channelrhodopsin variant ReaChR and their relevance for its function.
[So] Source:J Biol Chem;292(34):14205-14216, 2017 Aug 25.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Channelrhodopsins (ChRs) are light-gated ion channels widely used for activating selected cells in large cellular networks. ChR variants with a red-shifted absorption maximum, such as the modified ChR1 red-activatable channelrhodopsin ("ReaChR," λ = 527 nm), are of particular interest because longer wavelengths allow optical excitation of cells in deeper layers of organic tissue. In all ChRs investigated so far, proton transfer reactions and hydrogen bond changes are crucial for the formation of the ion-conducting pore and the selectivity for protons cations, such as Na , K , and Ca (1). By using a combination of electrophysiological measurements and UV-visible and FTIR spectroscopy, we characterized the proton transfer events in the photocycle of ReaChR and describe their relevance for its function. 1) The central gate residue Glu (Glu in ( ) ChR2) (i) undergoes a hydrogen bond change in D → K transition and (ii) deprotonates in K → M transition. Its negative charge in the open state is decisive for proton selectivity. 2) The counter-ion Asp (Asp in ChR2) receives the retinal Schiff base proton during M-state formation. Starting from M, a photocycle branching occurs involving (i) a direct M → D transition and (ii) formation of late photointermediates N and O. 3) The DC pair residue Asp (Asp in ChR2) deprotonates in N → O transition. Interestingly, the D196N mutation increases 15- -retinal at the expense of 15- , which is the predominant isomer in the wild type, and abolishes the peak current in electrophysiological measurements. This suggests that the peak current is formed by 15- species, whereas 15- species contribute only to the stationary current.
[Mh] Termos MeSH primário: Proteínas de Algas/metabolismo
Chlamydomonas reinhardtii/metabolismo
Clorófitas/metabolismo
Modelos Moleculares
Proteínas de Plantas/metabolismo
Rodopsina/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Algas/química
Proteínas de Algas/genética
Substituição de Aminoácidos
Domínio Catalítico/efeitos da radiação
Chlamydomonas reinhardtii/efeitos da radiação
Clorófitas/efeitos da radiação
Fenômenos Eletrofisiológicos
Células HEK293
Seres Humanos
Ligações de Hidrogênio/efeitos da radiação
Luz
Simulação de Dinâmica Molecular
Mutagênese Sítio-Dirigida
Mutação
Proteínas de Plantas/química
Proteínas de Plantas/genética
Conformação Proteica/efeitos da radiação
Isoformas de Proteínas/química
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
Estabilidade Proteica
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Rodopsina/química
Rodopsina/genética
Espectroscopia de Infravermelho com Transformada de Fourier
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Algal Proteins); 0 (Plant Proteins); 0 (Protein Isoforms); 0 (Recombinant Fusion Proteins); 0 (Recombinant Proteins); 9009-81-8 (Rhodopsin)
[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:170630
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.779629


  6 / 1601 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28647463
[Au] Autor:Engelbrecht V; Rodríguez-Maciá P; Esselborn J; Sawyer A; Hemschemeier A; Rüdiger O; Lubitz W; Winkler M; Happe T
[Ad] Endereço:AG Photobiotechnologie, Fakultät für Biologie und Biotechnologie, Ruhr-Universität Bochum, Universitätsstraße 150, 44801 Bochum, Germany.
[Ti] Título:The structurally unique photosynthetic Chlorella variabilis NC64A hydrogenase does not interact with plant-type ferredoxins.
[So] Source:Biochim Biophys Acta;1858(9):771-778, 2017 09.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Hydrogenases from green algae are linked to the photosynthetic electron transfer chain via the plant-type ferredoxin PetF. In this work the [FeFe]-hydrogenase from the Trebouxiophycean alga Chlorella variabilis NC64A (CvHydA1), which in contrast to other green algal hydrogenases contains additional FeS-cluster binding domains, was purified and specific enzyme activities for both hydrogen (H ) production and H oxidation were determined. Interestingly, although C. variabilis NC64A, like many Chlorophycean algal strains, exhibited light-dependent H production activity upon sulfur deprivation, CvHydA1 did not interact in vitro with several plant-type [2Fe-2S]-ferredoxins, but only with a bacterial2[4Fe4S]-ferredoxin. In an electrochemical characterization, the enzyme exhibited features typical of bacterial [FeFe]-hydrogenases (e.g. minor anaerobic oxidative inactivation), as well as of algal enzymes (very high oxygen sensitivity).
[Mh] Termos MeSH primário: Proteínas de Algas/metabolismo
Chlorella/enzimologia
Ferredoxinas/metabolismo
Hidrogenase/metabolismo
Proteínas com Ferro-Enxofre/metabolismo
Proteínas de Plantas/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Algas/química
Proteínas de Algas/isolamento & purificação
Sequência de Aminoácidos
Monóxido de Carbono/farmacologia
Chlamydomonas reinhardtii/química
Chlorella/efeitos da radiação
Técnicas Eletroquímicas
Transporte de Elétrons
Hidrogênio/metabolismo
Hidrogenase/antagonistas & inibidores
Hidrogenase/química
Hidrogenase/isolamento & purificação
Proteínas com Ferro-Enxofre/antagonistas & inibidores
Proteínas com Ferro-Enxofre/química
Proteínas com Ferro-Enxofre/isolamento & purificação
Luz
Modelos Moleculares
Oxirredução
Oxigênio/farmacologia
Fotossíntese
Conformação Proteica
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Enxofre/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Algal Proteins); 0 (Ferredoxins); 0 (Iron-Sulfur Proteins); 0 (Plant Proteins); 0 (Recombinant Proteins); 70FD1KFU70 (Sulfur); 7U1EE4V452 (Carbon Monoxide); 7YNJ3PO35Z (Hydrogen); EC 1.12.- (iron hydrogenase); EC 1.12.7.2 (Hydrogenase); S88TT14065 (Oxygen)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171025
[Lr] Data última revisão:
171025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170626
[St] Status:MEDLINE


  7 / 1601 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28628130
[Au] Autor:Ajjawi I; Verruto J; Aqui M; Soriaga LB; Coppersmith J; Kwok K; Peach L; Orchard E; Kalb R; Xu W; Carlson TJ; Francis K; Konigsfeld K; Bartalis J; Schultz A; Lambert W; Schwartz AS; Brown R; Moellering ER
[Ad] Endereço:Synthetic Genomics Inc., La Jolla, California, USA.
[Ti] Título:Lipid production in Nannochloropsis gaditana is doubled by decreasing expression of a single transcriptional regulator.
[So] Source:Nat Biotechnol;35(7):647-652, 2017 Jul.
[Is] ISSN:1546-1696
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lipid production in the industrial microalga Nannochloropsis gaditana exceeds that of model algal species and can be maximized by nutrient starvation in batch culture. However, starvation halts growth, thereby decreasing productivity. Efforts to engineer N. gaditana strains that can accumulate biomass and overproduce lipids have previously met with little success. We identified 20 transcription factors as putative negative regulators of lipid production by using RNA-seq analysis of N. gaditana during nitrogen deprivation. Application of a CRISPR-Cas9 reverse-genetics pipeline enabled insertional mutagenesis of 18 of these 20 transcription factors. Knocking out a homolog of fungal Zn(II) Cys -encoding genes improved partitioning of total carbon to lipids from 20% (wild type) to 40-55% (mutant) in nutrient-replete conditions. Knockout mutants grew poorly, but attenuation of Zn(II) Cys expression yielded strains producing twice as much lipid (∼5.0 g m d ) as that in the wild type (∼2.5 g m d ) under semicontinuous growth conditions and had little effect on growth.
[Mh] Termos MeSH primário: Melhoramento Genético/métodos
Metabolismo dos Lipídeos/genética
Lipídeos/biossíntese
Elementos Reguladores de Transcrição/genética
Estramenópilas/genética
Fatores de Transcrição/genética
[Mh] Termos MeSH secundário: Proteínas de Algas/genética
Regulação para Baixo/genética
Técnicas de Inativação de Genes
Lipídeos/genética
Estramenópilas/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Algal Proteins); 0 (Lipids); 0 (Transcription Factors)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170818
[Lr] Data última revisão:
170818
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170620
[St] Status:MEDLINE
[do] DOI:10.1038/nbt.3865


  8 / 1601 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28587627
[Au] Autor:Siegler H; Valerius O; Ischebeck T; Popko J; Tourasse NJ; Vallon O; Khozin-Goldberg I; Braus GH; Feussner I
[Ad] Endereço:University of Goettingen, Albrecht-von-Haller-Institute for Plant Sciences, Department of Plant Biochemistry, Goettingen, Germany.
[Ti] Título:Analysis of the lipid body proteome of the oleaginous alga Lobosphaera incisa.
[So] Source:BMC Plant Biol;17(1):98, 2017 Jun 06.
[Is] ISSN:1471-2229
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Lobosphaera incisa (L. incisa) is an oleaginous microalga that stores triacylglycerol (TAG) rich in arachidonic acid in lipid bodies (LBs). This organelle is gaining attention in algal research, since evidence is accumulating that proteins attached to its surface fulfill important functions in TAG storage and metabolism. RESULTS: Here, the composition of the LB proteome in L incisa was investigated by comparing different cell fractions in a semiquantitative proteomics approach. After applying stringent filters to the proteomics data in order to remove contaminating proteins from the list of possible LB proteins (LBPs), heterologous expression of candidate proteins in tobacco pollen tubes, allowed us to confirm 3 true LBPs: A member of the algal Major Lipid Droplet Protein family, a small protein of unknown function and a putative lipase. In addition, a TAG lipase that belongs to the SUGAR DEPENDENT 1 family of TAG lipases known from oilseed plants was identified. Its activity was verified by functional complementation of an Arabidopsis thaliana mutant lacking the major seed TAG lipases. CONCLUSIONS: Here we describe 3 LBPs as well as a TAG lipase from the oleaginous microalga L. incisa and discuss their possible involvement in LB metabolism. This study highlights the importance of filtering LB proteome datasets and verifying the subcellular localization one by one, so that contaminating proteins can be recognized as such. Our dataset can serve as a valuable resource in the identification of additional LBPs, shedding more light on the intriguing roles of LBs in microalgae.
[Mh] Termos MeSH primário: Proteínas de Algas/metabolismo
Clorófitas/metabolismo
Gotículas Lipídicas/metabolismo
Proteoma/metabolismo
[Mh] Termos MeSH secundário: Clorófitas/enzimologia
Lipase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Algal Proteins); 0 (Proteome); EC 3.1.1.3 (Lipase)
[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:170608
[St] Status:MEDLINE
[do] DOI:10.1186/s12870-017-1042-2


  9 / 1601 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28521223
[Au] Autor:Sheehan JD; Savage PE
[Ad] Endereço:Department of Chemical Engineering, The Pennsylvania State University, 119 Greenberg Complex, University Park, PA 16802, USA.
[Ti] Título:Modeling the effects of microalga biochemical content on the kinetics and biocrude yields from hydrothermal liquefaction.
[So] Source:Bioresour Technol;239:144-150, 2017 Sep.
[Is] ISSN:1873-2976
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A kinetic model for the hydrothermal liquefaction (HTL) of microalgae was developed and its performance in predicting biocrude yields was tested. Kinetic interactions between algal proteins, carbohydrates, and lipids were also included for the first time. These interactions provided a better fit of the data used to determine model parameters, but the kinetics model lacking interactions provided a better prediction of published biocrude yields. This model predicted 70 published biocrude yields to within ±5wt% given the biochemical composition of the alga and the HTL temperature and time as model inputs. Forty-two other published biocrude yields were predicted to within ±10wt%. The model accurately predicts that feedstocks richer in proteins or lipids give higher biocrude yields than those abundant in carbohydrates. This updated model better predicts the combined influences of HTL reaction conditions and algae biochemical composition on HTL biocrude yields than any other model currently available.
[Mh] Termos MeSH primário: Proteínas de Algas
Lipídeos
Microalgas
[Mh] Termos MeSH secundário: Cinética
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Algal Proteins); 0 (Lipids)
[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:170519
[St] Status:MEDLINE


  10 / 1601 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28499880
[Au] Autor:Chukhutsina VU; Fristedt R; Morosinotto T; Croce R
[Ad] Endereço:Biophysics of Photosynthesis, Dep. of Physics and Astronomy, Faculty of Sciences, VU University Amsterdam, De Boelelaan 1081, 1081 HV Amsterdam, the Netherlands.
[Ti] Título:Photoprotection strategies of the alga Nannochloropsis gaditana.
[So] Source:Biochim Biophys Acta;1858(7):544-552, 2017 07.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Nannochloropsis spp. are algae with high potential for biotechnological applications due to their capacity to accumulate lipids. However, little is known about their photosynthetic apparatus and acclimation/photoprotective strategies. In this work, we studied the mechanisms of non-photochemical quenching (NPQ), the fast response to high light stress, in Nannochloropsis gaditana by "locking" the cells in six different states during quenching activation and relaxation. Combining biochemical analysis with time-resolved fluorescence spectroscopy, we correlated each NPQ state with the presence of two well-known NPQ components: de-epoxidized xanthophylls and stress-related antenna proteins (LHCXs). We demonstrated that after exposure to strong light, the rapid quenching that takes place in the antennas of both photosystems was associated with the presence of LHCXs. At later stages, quenching occurs mainly in the antennas of PSII and correlates with the amount of de-epoxidised xanthophylls. We also observed changes in the distribution of excitation energy between photosystems, which suggests redistribution of excitation between photosystems as part of the photo-protective strategy. A multistep model for NPQ induction and relaxation in N. gaditana is discussed.
[Mh] Termos MeSH primário: Estramenópilas/fisiologia
[Mh] Termos MeSH secundário: Proteínas de Algas/química
Proteínas de Algas/isolamento & purificação
Proteínas de Algas/fisiologia
Fluorescência
Luz
Complexos de Proteínas Captadores de Luz/química
Complexos de Proteínas Captadores de Luz/fisiologia
Complexo de Proteína do Fotossistema I/metabolismo
Complexo de Proteína do Fotossistema II/metabolismo
Tolerância a Radiação/fisiologia
Espectrometria de Fluorescência
Estramenópilas/química
Estramenópilas/efeitos da radiação
Xantofilas/química
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Algal Proteins); 0 (Light-Harvesting Protein Complexes); 0 (Photosystem I Protein Complex); 0 (Photosystem II Protein Complex); 0 (Xanthophylls)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170514
[St] Status:MEDLINE



página 1 de 161 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde