Base de dados : MEDLINE
Pesquisa : B01.175 [Categoria DeCS]
Referências encontradas : 103 [refinar]
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  1 / 103 MEDLINE  
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[PMID]:29257953
[Au] Autor:Sigg MA; Menchen T; Lee C; Johnson J; Jungnickel MK; Choksi SP; Garcia G; Busengdal H; Dougherty GW; Pennekamp P; Werner C; Rentzsch F; Florman HM; Krogan N; Wallingford JB; Omran H; Reiter JF
[Ad] Endereço:Department of Biochemistry and Biophysics, Cardiovascular Research Institute, University of California, San Francisco, CA 94158, USA.
[Ti] Título:Evolutionary Proteomics Uncovers Ancient Associations of Cilia with Signaling Pathways.
[So] Source:Dev Cell;43(6):744-762.e11, 2017 12 18.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cilia are organelles specialized for movement and signaling. To infer when during evolution signaling pathways became associated with cilia, we characterized the proteomes of cilia from sea urchins, sea anemones, and choanoflagellates. We identified 437 high-confidence ciliary candidate proteins conserved in mammals and discovered that Hedgehog and G-protein-coupled receptor pathways were linked to cilia before the origin of bilateria and transient receptor potential (TRP) channels before the origin of animals. We demonstrated that candidates not previously implicated in ciliary biology localized to cilia and further investigated ENKUR, a TRP channel-interacting protein identified in the cilia of all three organisms. ENKUR localizes to motile cilia and is required for patterning the left-right axis in vertebrates. Moreover, mutation of ENKUR causes situs inversus in humans. Thus, proteomic profiling of cilia from diverse eukaryotes defines a conserved ciliary proteome, reveals ancient connections to signaling, and uncovers a ciliary protein that underlies development and human disease.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Proteínas de Ligação a Calmodulina/metabolismo
Cílios/genética
Cílios/metabolismo
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/genética
Animais
Proteínas de Ligação a Calmodulina/genética
Técnicas de Cultura de Células
Coanoflagelados/metabolismo
Proteínas Hedgehog/metabolismo
Seres Humanos
Camundongos
Mutação
Organelas/metabolismo
Filogenia
Proteômica/métodos
Receptores Acoplados a Proteínas-G/metabolismo
Anêmonas-do-Mar/metabolismo
Ouriços-do-Mar/metabolismo
Transdução de Sinais/genética
Transdução de Sinais/fisiologia
Canais de Receptores Transientes de Potencial/metabolismo
Xenopus laevis/metabolismo
Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Calmodulin-Binding Proteins); 0 (ENKUR protein, human); 0 (Hedgehog Proteins); 0 (Receptors, G-Protein-Coupled); 0 (Transient Receptor Potential Channels)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180210
[Lr] Data última revisão:
180210
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171220
[St] Status:MEDLINE


  2 / 103 MEDLINE  
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[PMID]:28976747
[Au] Autor:Lamarche LB; Kumar RP; Trieu MM; Devine EL; Cohen-Abeles LE; Theobald DL; Oprian DD
[Ad] Endereço:Department of Biochemistry, Brandeis University , Waltham, Massachusetts 02454, United States.
[Ti] Título:Purification and Characterization of RhoPDE, a Retinylidene/Phosphodiesterase Fusion Protein and Potential Optogenetic Tool from the Choanoflagellate Salpingoeca rosetta.
[So] Source:Biochemistry;56(43):5812-5822, 2017 Oct 31.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:RhoPDE is a type I rhodopsin/phosphodiesterase gene fusion product from the choanoflagellate Salpingoeca rosetta. The gene was discovered around the time that a similar type I rhodopsin/guanylyl cyclase fusion protein, RhoGC, was shown to control phototaxis of an aquatic fungus through a cGMP signaling pathway. RhoPDE has potential as an optogenetic tool catalyzing the hydrolysis of cyclic nucleotides. Here we provide an expression and purification system for RhoPDE, as well as a crystal structure of the C-terminal phosphodiesterase catalytic domain. We show that RhoPDE contains an even number of transmembrane segments, with N- and C-termini both located on the cytoplasmic surface of the cell membrane. The purified protein exhibits an absorption maximum at 490 nm in the dark state, which shifts to 380 nm upon exposure to light. The protein acts as a cGMP-selective phosphodiesterase. However, the activity does not appear to be modulated by light. The protein is also active with cAMP as a substrate, but with a roughly 5-7-fold lower k . A truncation consisting solely of the phosphodiesterase domain is also active with a k for cGMP roughly 6-9-fold lower than that of the full-length protein. The isolated PDE domain was crystallized, and the X-ray structure showed the protein to be a dimer similar to human PDE9. We anticipate that the purification system introduced here will enable further structural and biochemical experiments to improve our understanding of the function and mechanism of this unique fusion protein.
[Mh] Termos MeSH primário: Coanoflagelados/enzimologia
Diester Fosfórico Hidrolases
Proteínas de Protozoários
[Mh] Termos MeSH secundário: Coanoflagelados/genética
Cristalografia por Raios X
Expressão Gênica
Seres Humanos
Diester Fosfórico Hidrolases/biossíntese
Diester Fosfórico Hidrolases/química
Diester Fosfórico Hidrolases/genética
Diester Fosfórico Hidrolases/isolamento & purificação
Domínios Proteicos
Proteínas de Protozoários/biossíntese
Proteínas de Protozoários/química
Proteínas de Protozoários/genética
Proteínas de Protozoários/isolamento & purificação
Proteínas Recombinantes de Fusão/biossíntese
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protozoan Proteins); 0 (Recombinant Fusion Proteins); EC 3.1.4.- (Phosphoric Diester Hydrolases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171005
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00519


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[PMID]:28867285
[Au] Autor:Woznica A; Gerdt JP; Hulett RE; Clardy J; King N
[Ad] Endereço:Howard Hughes Medical Institute, and Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, USA.
[Ti] Título:Mating in the Closest Living Relatives of Animals Is Induced by a Bacterial Chondroitinase.
[So] Source:Cell;170(6):1175-1183.e11, 2017 Sep 07.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We serendipitously discovered that the marine bacterium Vibrio fischeri induces sexual reproduction in one of the closest living relatives of animals, the choanoflagellate Salpingoeca rosetta. Although bacteria influence everything from nutrition and metabolism to cell biology and development in eukaryotes, bacterial regulation of eukaryotic mating was unexpected. Here, we show that a single V. fischeri protein, the previously uncharacterized EroS, fully recapitulates the aphrodisiac-like activity of live V. fischeri. EroS is a chondroitin lyase; although its substrate, chondroitin sulfate, was previously thought to be an animal synapomorphy, we demonstrate that S. rosetta produces chondroitin sulfate and thus extend the ancestry of this important glycosaminoglycan to the premetazoan era. Finally, we show that V. fischeri, purified EroS, and other bacterial chondroitin lyases induce S. rosetta mating at environmentally relevant concentrations, suggesting that bacteria likely regulate choanoflagellate mating in nature.
[Mh] Termos MeSH primário: Aliivibrio fischeri/enzimologia
Coanoflagelados/microbiologia
Coanoflagelados/fisiologia
Condroitinases e Condroitim Liases/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/química
Coanoflagelados/citologia
Sulfatos de Condroitina/metabolismo
Meiose
Reprodução
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 9007-28-7 (Chondroitin Sulfates); EC 4.2.2.- (Chondroitinases and Chondroitin Lyases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170905
[St] Status:MEDLINE


  4 / 103 MEDLINE  
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[PMID]:28302718
[Au] Autor:Yoshida K; Tsunoda SP; Brown LS; Kandori H
[Ad] Endereço:From the Department of Life Science and Applied Chemistry and.
[Ti] Título:A unique choanoflagellate enzyme rhodopsin exhibits light-dependent cyclic nucleotide phosphodiesterase activity.
[So] Source:J Biol Chem;292(18):7531-7541, 2017 May 05.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Photoactivated adenylyl cyclase (PAC) and guanylyl cyclase rhodopsin increase the concentrations of intracellular cyclic nucleotides upon illumination, serving as promising second-generation tools in optogenetics. To broaden the arsenal of such tools, it is desirable to have light-activatable enzymes that can decrease cyclic nucleotide concentrations in cells. Here, we report on an unusual microbial rhodopsin that may be able to meet the demand. It is found in the choanoflagellate and contains a C-terminal cyclic nucleotide phosphodiesterase (PDE) domain. We examined the enzymatic activity of the protein (named Rh-PDE) both in HEK293 membranes and whole cells. Although Rh-PDE was constitutively active in the dark, illumination increased its hydrolytic activity 1.4-fold toward cGMP and 1.6-fold toward cAMP, as measured in isolated crude membranes. Purified full-length Rh-PDE displayed maximal light absorption at 492 nm and formed the M intermediate with the deprotonated Schiff base upon illumination. The M state decayed to the parent spectral state in 7 s, producing long-lasting activation of the enzyme domain with increased activity. We discuss a possible mechanism of the Rh-PDE activation by light. Furthermore, Rh-PDE decreased cAMP concentration in HEK293 cells in a light-dependent manner and could do so repeatedly without losing activity. Thus, Rh-PDE may hold promise as a potential optogenetic tool for light control of intracellular cyclic nucleotides ( to study cyclic nucleotide-associated signal transduction cascades).
[Mh] Termos MeSH primário: 3´,5´-AMP Cíclico Fosfodiesterases/metabolismo
Coanoflagelados/enzimologia
Luz
Proteínas de Protozoários/metabolismo
Rodopsina/metabolismo
[Mh] Termos MeSH secundário: 3',5'-AMP Cíclico Fosfodiesterases/genética
Coanoflagelados/genética
Células HEK293
Seres Humanos
Domínios Proteicos
Proteínas de Protozoários/genética
Rodopsina/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protozoan Proteins); 9009-81-8 (Rhodopsin); EC 3.1.4.17 (3',5'-Cyclic-AMP Phosphodiesterases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170607
[Lr] Data última revisão:
170607
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170318
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.775569


  5 / 103 MEDLINE  
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[PMID]:28092805
[Au] Autor:Thomsen HA; Østergaard JB
[Ad] Endereço:National Institute of Aquatic Resources, Technical University of Denmark, Charlottenlund, Denmark. Electronic address: hat@aqua.dtu.dk.
[Ti] Título:Circumstantial evidence of life history events in loricate choanoflagellates.
[So] Source:Eur J Protistol;58:26-34, 2017 Apr.
[Is] ISSN:1618-0429
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Sex is found in all major eukaryotic groups of organisms. It has been known for some time that the choanoflagellates also possess the genes involved in meiosis and a full sexual cycle was also recently accounted for in Salpingoeca rosetta. With reference to the loricate choanoflagellates the current status is that only circumstantial evidence, from wild material of Bicosta spinifera, exists in favour of documenting division patterns that go beyond plain asexual division, and that has the potential to represent stages in a sexual life cycle. Here we present further evidence from wild material documenting possible morphotype changes that might similarly indicate the existence of complex life cycles. In this particular case, it revolves around the existence of so-called 'combination loricas' (i.e. two loricas that occur physically united), representing consistent species combinations from the genera Acanthocorbis and Stephanoeca.
[Mh] Termos MeSH primário: Coanoflagelados/crescimento & desenvolvimento
Estágios do Ciclo de Vida
[Mh] Termos MeSH secundário: Reprodução/fisiologia
Especificidade da Espécie
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170413
[Lr] Data última revisão:
170413
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170117
[St] Status:MEDLINE


  6 / 103 MEDLINE  
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[PMID]:28011296
[Au] Autor:Frank N; Helge Abuldhauge T; Daniel J R
[Ad] Endereço:Zoological Institute, General Ecology, University of Cologne, Zülpicher Str. 47b, 50674 Cologne, Germany. Electronic address: FNitsche@uni-koeln.de.
[Ti] Título:Bridging the gap between morphological species and molecular barcodes - Exemplified by loricate choanoflagellates.
[So] Source:Eur J Protistol;57:26-37, 2017 Feb.
[Is] ISSN:1618-0429
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Translating the vast amounts of molecular barcodes from global surveys of microbial eukaryotes into ecological insight depends critically on a well-curated reference database with adequate taxonomic coverage. In this respect, the choanoflagellates resemble other eukaryotic lineages: reasonable coverage at higher taxonomic levels, but missing diversity at the species level. The acanthoecid (loricate) choanoflagellates are well-characterized morphologically, with over 115 species described, but less than 10% with any sequence data. Because lorica shape is species-specific, the acanthoecids represent an opportunity to link morphological with molecular data within a lineage of eukaryotes. To match morphospecies to sequences, we sampled the Kattegat and the Isefjord in Denmark in September 2014 and February 2015. We identified 45 morphospecies and sequenced ribosomal DNA of nine previously unsequenced species, roughly doubling the number of acanthoecid species with sequence data, including the first data representing five genera: Bicosta, Calliacantha, Cosmoeca, Crinolina and Pleurasiga. Our phylogenetic analysis is mainly congruent with morphology-based systematics. Five of the newly sequenced species match a previously unidentified barcode from Tara Oceans, providing access to the global distribution of species isolated from Danish waters. One species, Calliacantha natans, is the second most globally abundant choanoflagellate present in Tara Oceans. Our project translating new ribosomal DNA sequences to distributions of described species on a global scale supports the approach linking morphology to molecular barcodes for microbial eukaryote ecology.
[Mh] Termos MeSH primário: Coanoflagelados/citologia
Coanoflagelados/genética
Código de Barras de DNA Taxonômico
[Mh] Termos MeSH secundário: Biodiversidade
Coanoflagelados/classificação
DNA Ribossômico/genética
Filogenia
Especificidade da Espécie
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Ribosomal)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170407
[Lr] Data última revisão:
170407
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161225
[St] Status:MEDLINE


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[PMID]:27864009
[Au] Autor:Chen B; Shao J; Zhuang H; Wen J
[Ad] Endereço:State Key Laboratory of Genetic Resources and Evolution, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, Yunnan, China. Electronic address: chenbing@mail.kiz.ac.cn.
[Ti] Título:Evolutionary dynamics of triosephosphate isomerase gene intron location pattern in Metazoa: A new perspective on intron evolution in animals.
[So] Source:Gene;602:24-32, 2017 Feb 20.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Intron evolution, including its dynamics in the evolutionary transitions and diversification of eukaryotes, remains elusive. Inadequate taxon sampling due to data shortage, unclear phylogenetic framework, and inappropriate outgroup application might be among the causes. Besides, the integrity of all the introns within a gene was often neglected previously. Taking advantage of the ancient conserved triosephosphate isomerase gene (tim), the relatively robust phylogeny of Metazoa, and choanoflagellates as outgroup, the evolutionary dynamics of tim intron location pattern (ILP) in Metazoa was investigated. From 133 representative species of ten phyla, 30 types of ILPs were identified. A most common one, which harbors the maximum six intron positions, is deduced to be the common ancestral tim ILP of Metazoa, which almost had formed in their protozoan ancestor and was surprisingly retained and passed down till to each ancestors of metazoan phyla. In the subsequent animal diversification, it underwent different evolutionary trajectories: within Deuterostomia, it was almost completely retained only with changes in a few species with relatively recently fast-evolving histories, while within the rapidly radiating Protostomia, besides few but remarkable retention, it usually displayed extensive intron losses and a few gains. Therefore, a common ancestral exon-intron arrangement pattern of an animal gene is definitely discovered; besides the 'intron-rich view' of early animal genes being confirmed, the novel insight that high exon-intron re-arrangements of genes seem to be associated with the relatively recently rapid evolution of lineages/species/genomes but have no correlation with the ancient major evolutionary transitions in animal evolution, is revealed.
[Mh] Termos MeSH primário: Evolução Molecular
Íntrons
Triose-Fosfato Isomerase/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Coanoflagelados/enzimologia
Coanoflagelados/genética
Sequência Conservada
Seres Humanos
Filogenia
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 5.3.1.1 (Triose-Phosphate Isomerase)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170130
[Lr] Data última revisão:
170130
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161120
[St] Status:MEDLINE


  8 / 103 MEDLINE  
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[PMID]:27765632
[Au] Autor:Carr M; Richter DJ; Fozouni P; Smith TJ; Jeuck A; Leadbeater BSC; Nitsche F
[Ad] Endereço:School of Applied Sciences, University of Huddersfield, Huddersfield HD1 3DH, UK. Electronic address: M.Carr@hud.ac.uk.
[Ti] Título:A six-gene phylogeny provides new insights into choanoflagellate evolution.
[So] Source:Mol Phylogenet Evol;107:166-178, 2017 Feb.
[Is] ISSN:1095-9513
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recent studies have shown that molecular phylogenies of the choanoflagellates (Class Choanoflagellatea) are in disagreement with their traditional taxonomy, based on morphology, and that Choanoflagellatea requires considerable taxonomic revision. Furthermore, phylogenies suggest that the morphological and ecological evolution of the group is more complex than has previously been recognized. Here we address the taxonomy of the major choanoflagellate order Craspedida, by erecting four new genera. The new genera are shown to be morphologically, ecologically and phylogenetically distinct from other choanoflagellate taxa. Furthermore, we name five novel craspedid species, as well as formally describe ten species that have been shown to be either misidentified or require taxonomic revision. Our revised phylogeny, including 18 new species and sequence data for two additional genes, provides insights into the morphological and ecological evolution of the choanoflagellates. We examine the distribution within choanoflagellates of these two additional genes, EF-1A and EFL, closely related translation GTPases which are required for protein synthesis. Mapping the presence and absence of these genes onto the phylogeny highlights multiple events of gene loss within the choanoflagellates.
[Mh] Termos MeSH primário: Coanoflagelados/genética
Genes de Protozoários
Filogenia
[Mh] Termos MeSH secundário: Animais
Coanoflagelados/classificação
DNA Ribossômico/genética
Evolução Molecular
Água Doce
Funções Verossimilhança
Água do Mar
Especificidade da Espécie
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Ribosomal)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161107
[St] Status:MEDLINE


  9 / 103 MEDLINE  
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[PMID]:27693250
[Au] Autor:Martinez S; Yang X; Bennett B; Holz RC
[Ad] Endereço:Department of Chemistry, Marquette University, PO Box 1881, Milwaukee, WI 53201-1881, United States; Department of Chemistry and Biochemistry, Loyola University Chicago, 1068 W Sheridan Rd., Chicago, IL 60660, United States.
[Ti] Título:A cobalt-containing eukaryotic nitrile hydratase.
[So] Source:Biochim Biophys Acta;1865(1):107-112, 2017 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Nitrile hydratase (NHase), an industrially important enzyme that catalyzes the hydration of nitriles to their corresponding amides, has only been characterized from prokaryotic microbes. The putative NHase from the eukaryotic unicellular choanoflagellate organism Monosiga brevicollis (MbNHase) was heterologously expressed in Escherichia coli. The resulting enzyme expressed as a single polypeptide with fused α- and ß-subunits linked by a seventeen-histidine region. Size-exclusion chromatography indicated that MbNHase exists primarily as an (αß) homodimer in solution, analogous to the α ß homotetramer architecture observed for prokaryotic NHases. The NHase enzyme contained its full complement of Co(III) and was fully functional without the co-expression of an activator protein or E. coli GroES/EL molecular chaperones. The homology model of MbNHase was developed identifying Cys400, Cys403, and Cys405 as active site ligands. The results presented here provide the first experimental data for a mature and active eukaryotic NHase with fused subunits. Since this new member of the NHase family is expressed from a single gene without the requirement of an activator protein, it represents an alternative biocatalyst for industrial syntheses of important amide compounds.
[Mh] Termos MeSH primário: Coanoflagelados/enzimologia
Cobalto/química
Hidroliases/química
Metaloproteínas/química
Proteínas de Protozoários/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Coanoflagelados/genética
Cristalografia por Raios X
Hidroliases/genética
Metaloproteínas/genética
Modelos Moleculares
Conformação Proteica em Folha beta
Proteínas de Protozoários/genética
Espectrofotometria Ultravioleta
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Metalloproteins); 0 (Protozoan Proteins); 3G0H8C9362 (Cobalt); EC 4.2.1.- (Hydro-Lyases); EC 4.2.1.- (nitrile hydratase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161004
[St] Status:MEDLINE


  10 / 103 MEDLINE  
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[PMID]:27882869
[Au] Autor:Kirkegaard JB; Bouillant A; Marron AO; Leptos KC; Goldstein RE
[Ad] Endereço:Department of Applied Mathematics and Theoretical Physics, Centre for Mathematical Sciences, University of Cambridge, Cambridge, United Kingdom.
[Ti] Título:Aerotaxis in the closest relatives of animals.
[So] Source:Elife;5, 2016 Nov 24.
[Is] ISSN:2050-084X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:As the closest unicellular relatives of animals, choanoflagellates serve as useful model organisms for understanding the evolution of animal multicellularity. An important factor in animal evolution was the increasing ocean oxygen levels in the Precambrian, which are thought to have influenced the emergence of complex multicellular life. As a first step in addressing these conditions, we study here the response of the colony-forming choanoflagellate to oxygen gradients. Using a microfluidic device that allows spatio-temporal variations in oxygen concentrations, we report the discovery that displays positive aerotaxis. Analysis of the spatial population distributions provides evidence for logarithmic sensing of oxygen, which enhances sensing in low oxygen neighborhoods. Analysis of search strategy models on the experimental colony trajectories finds that choanoflagellate aerotaxis is consistent with stochastic navigation, the statistics of which are captured using an effective continuous version based on classical run-and-tumble chemotaxis.
[Mh] Termos MeSH primário: Quimiotaxia
Coanoflagelados/efeitos dos fármacos
Coanoflagelados/fisiologia
Oxigênio/metabolismo
[Mh] Termos MeSH secundário: Dispositivos Lab-On-A-Chip
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
S88TT14065 (Oxygen)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161125
[St] Status:MEDLINE



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