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  1 / 166611 MEDLINE  
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[PMID]:29408396
[Au] Autor:Wang W; Zhang H; Wei X; Yang L; Yang B; Zhang L; Li J; Jiang YQ
[Ad] Endereço:State Key Laboratory of Crop Stress Biology for Arid Areas, College of Life Sciences, Northwest A & F University, Yangling, Shaanxi 712100, China.
[Ti] Título:Functional characterization of calcium-dependent protein kinase (CPK) 2 gene from oilseed rape (Brassica napus L.) in regulating reactive oxygen species signaling and cell death control.
[So] Source:Gene;651:49-56, 2018 Apr 20.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Calcium-dependent protein kinases (CPKs), being Ser/Thr protein kinases found only in plants and some protozoans are calcium sensors that regulate diverse biological processes. However, the function and mode of CPKs in oilseed rape (Brassica napus) remain elusive. In this study, we identified CPK2 from oilseed rape as a novel regulator of reactive oxygen species (ROS) and cell death. BnaCPK2 was identified to be located at the endoplasmic reticulum membrane. Expression of BnaCPK2 was induced during Bax-induced cell death. Overexpression of the constitutively active form of BnaCPK2 led to significantly more accumulation of ROS and cell death than the full-length CPK2, which is supported by various measurements of physiological data. In addition, a quantitative RT-PCR survey revealed that the expression levels of a few marker genes are significantly changed as a result of CPK2 expression. Mating-based split ubiquitin system (mbSUS) and bimolecular fluorescence complementation (BiFC) were used to screen and confirm the BnaCPK2 interacting proteins. We identified and confirmed that CPK2 interacted with NADPH oxidase-like respiratory burst oxidase homolog D (RbohD), but not with RbohF. Based on its function and interacting partners, we propose that BnaCPK2 plays an important role in ROS and cell death control through interacting with RbohD.
[Mh] Termos MeSH primário: Brassica napus/genética
Morte Celular/genética
Proteínas de Plantas/genética
Proteínas Quinases/genética
Espécies Reativas de Oxigênio/metabolismo
[Mh] Termos MeSH secundário: Brassica napus/enzimologia
Clonagem Molecular
DNA de Plantas
Proteínas de Plantas/metabolismo
Proteínas Quinases/metabolismo
Análise de Sequência de DNA
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Plant); 0 (Plant Proteins); 0 (Reactive Oxygen Species); EC 2.7.- (Protein Kinases); EC 2.7.1.- (calcium-dependent protein kinase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180207
[St] Status:MEDLINE


  2 / 166611 MEDLINE  
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[PMID]:29382572
[Au] Autor:Lv C; Mo C; Liu H; Wu C; Li Z; Li J; Wang Y
[Ad] Endereço:Key Laboratory of Bio-resources and Eco-environment of Ministry of Education, College of Life Sciences, Sichuan University, Chengdu 610065, PR China.
[Ti] Título:Dopamine D2-like receptors (DRD2 and DRD4) in chickens: Tissue distribution, functional analysis, and their involvement in dopamine inhibition of pituitary prolactin expression.
[So] Source:Gene;651:33-43, 2018 Apr 20.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Dopamine (DA) D2-like (and D1-like) receptors are suggested to mediate the dopamine actions in the anterior pituitary and/or CNS of birds. However, the information regarding the structure, functionality, and expression of avian D2-like receptors have not been fully characterized. In this study, we cloned two D2-like receptors (cDRD2, cDRD4) from chicken brain using RACE PCR. The cloned cDRD4 is a 378-amino acid receptor, which shows 57% amino acid (a.a.) identity with mouse DRD4. As in mammals, two cDRD2 isoforms, cDRD2L (long isoform, 437 a.a.) and cDRD2S (short isoform, 408 a.a.), which differ in their third intracellular loop, were identified in chickens. Using cell-based luciferase reporter assays or Western blot, we demonstrated that cDRD4, cDRD2L and cDRD2S could be activated by dopamine and quinpirole (a D2-like receptor agonist) dose-dependently, and their activation inhibits cAMP signaling pathway and stimulates MAPK/ERK signaling cascade, indicating that they are functional receptors capable of mediating dopamine actions. Quantitative real-time PCR revealed that cDRD2 and cDRD4 are widely expressed in chicken tissues with abundant expression noted in anterior pituitary, and their expressions are likely controlled by their promoters near exon 1, as demonstrated by dual-luciferase reporter assays in DF-1 cells. In accordance with cDRD2/cDRD4 expression in the pituitary, DA or quinpirole could partially inhibit vasoactive intestinal peptide-induced prolactin expression in cultured chick pituitary cells. Together, our data proves the functionality of DRD2 and DRD4 in birds and aids to uncover the conserved roles of DA/D2-like receptor system in vertebrates, such as its action on the pituitary.
[Mh] Termos MeSH primário: Galinhas/metabolismo
Dopamina/metabolismo
Hipófise/metabolismo
Prolactina/biossíntese
Receptores de Dopamina D2/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Galinhas/genética
Clonagem Molecular
DNA Complementar
Feminino
Regulação da Expressão Gênica
Células HEK293
Seres Humanos
Masculino
Prolactina/antagonistas & inibidores
Regiões Promotoras Genéticas
Receptores de Dopamina D2/genética
Receptores de Dopamina D2/fisiologia
Transdução de Sinais
Distribuição Tecidual
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Complementary); 0 (Receptors, Dopamine D2); 9002-62-4 (Prolactin); VTD58H1Z2X (Dopamine)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180201
[St] Status:MEDLINE


  3 / 166611 MEDLINE  
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[PMID]:29346450
[Au] Autor:Sridharan J; Haremaki T; Weinstein DC
[Ad] Endereço:Biology Department, Queens College of the City University of New York, Flushing, New York, United States of America.
[Ti] Título:Cloning and spatiotemporal expression of Xenopus laevis Apolipoprotein CI.
[So] Source:PLoS One;13(1):e0191470, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Apolipoprotein CI (ApoCI) belongs to the Apolipoprotein superfamily, members of which are involved in lipid transport, uptake and homeostasis. Excessive ApoCI has been implicated in atherosclerosis and Alzheimer's disease in humans. In this study we report the isolation of Xenopus laevis apoCI and describe the expression pattern of this gene during early development, using reverse transcription polymerase chain reaction and whole mount in situ hybridization. Xenopus apoCI is enriched in the dorsal ectoderm during gastrulation, and is subsequently expressed in sensory placodes, neural tube and cranial neural crest. These data suggest as yet uncharacterized roles for ApoCI during early vertebrate embryogenesis.
[Mh] Termos MeSH primário: Apolipoproteína C-I/genética
[Mh] Termos MeSH secundário: Animais
Clonagem Molecular
Gastrulação
Hibridização In Situ
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Xenopus laevis/embriologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Apolipoprotein C-I)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180119
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191470


  4 / 166611 MEDLINE  
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[PMID]:28465230
[Au] Autor:Zhu F; Xiao S; Zhang Y; Shao Y; Tang F; Chen S; Bai X
[Ad] Endereço:Institute of Sericulture and Apiculture, Yunnan Academy of Agricultural Sciences, Mengzi 661101, Yunnan, China. Electronic address: 18287322700@163.com.
[Ti] Título:Molecular characterization and expression analysis of Turtle protein in silkworm that is associated with Nosema bombycis infection.
[So] Source:Infect Genet Evol;52:67-74, 2017 Aug.
[Is] ISSN:1567-7257
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:In this report, we describe the cloning and characterization of a member of the immunoglobulin superfamily (IgSF); i.e., Turtle. The cDNA of Turtle was cloned from the silkworm Bombyx mori using the rapid amplification of cDNA ends (RACE) technique. Three isoforms of Bombyx Turtle were obtained, including Bmtutl-464, Bmtutl-519, and Bmtutl-810. The three isoforms had identical 27-amino acid signal peptides and four extracellular immunoglobulin (Ig) domains (IgI-IgIV). Sequence similarity and phylogenic analysis indicated that Bmtutl-810 belongs to the group of insect Turtle isoforms and shares 76.2% identity with Drosophila Turtle. Quantitative real-time PCR analysis revealed that the Bombyx Turtle isoforms were expressed throughout the entire development period, the highest levels of expression of Bmtutl-464 and Bmtutl-519 were observed at the second instar larvae stage, whereas that of Bmtutl-810 peaked at the embryonic stage. The ubiquitous expression of Bmtutl-464, Bmtutl-519, and Bmtutl-810 were observed in all studied tissues, except for Bmtutl-519 in the silk gland. The expression level of Bmtutl-464 was highest in the ovary, whereas that of Bmtutl-519 and Bmtutl-810 was highest in the hemolymph. Bmtutl-519 was upregulated in BmN cells infected by Nosema bombycis, We speculated that Bombyx Turtle was not only involved in neural development in silkworm, as well as Drosophila Turtle, but was also involved in the regulation of other biological functions. For example, Bmtutl-519 might be involved in N. bombycis infection and may play an important role in the immune response of silkworms to N. bombycis infection.
[Mh] Termos MeSH primário: Bombyx/crescimento & desenvolvimento
Clonagem Molecular/métodos
Expressão Gênica
Imunoglobulinas/genética
Imunoglobulinas/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Bombyx/genética
Bombyx/metabolismo
Linhagem Celular
Regulação da Expressão Gênica no Desenvolvimento
Imunoglobulinas/química
Proteínas de Insetos/química
Proteínas de Insetos/genética
Proteínas de Insetos/metabolismo
Filogenia
Domínios Proteicos
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Immunoglobulins); 0 (Insect Proteins); 0 (Protein Isoforms)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE


  5 / 166611 MEDLINE  
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[PMID]:29410408
[Au] Autor:Kuncha SK; Mazeed M; Singh R; Kattula B; Routh SB; Sankaranarayanan R
[Ad] Endereço:CSIR-Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad, 500007, India.
[Ti] Título:A chiral selectivity relaxed paralog of DTD for proofreading tRNA mischarging in Animalia.
[So] Source:Nat Commun;9(1):511, 2018 02 06.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:D-aminoacyl-tRNA deacylase (DTD), a bacterial/eukaryotic trans-editing factor, removes D-amino acids mischarged on tRNAs and achiral glycine mischarged on tRNA . An invariant cross-subunit Gly-cisPro motif forms the mechanistic basis of L-amino acid rejection from the catalytic site. Here, we present the identification of a DTD variant, named ATD (Animalia-specific tRNA deacylase), that harbors a Gly-transPro motif. The cis-to-trans switch causes a "gain of function" through L-chiral selectivity in ATD resulting in the clearing of L-alanine mischarged on tRNA (G4•U69) by eukaryotic AlaRS. The proofreading activity of ATD is conserved across diverse classes of phylum Chordata. Animalia genomes enriched in tRNA (G4•U69) genes are in strict association with the presence of ATD, underlining the mandatory requirement of a dedicated factor to proofread tRNA misaminoacylation. The study highlights the emergence of ATD during genome expansion as a key event associated with the evolution of Animalia.
[Mh] Termos MeSH primário: Alanina/química
Aminoaciltransferases/química
Aminoacil-RNA de Transferência/química
Treonina/química
Aminoacilação de RNA de Transferência/genética
[Mh] Termos MeSH secundário: Alanina/genética
Alanina/metabolismo
Sequência de Aminoácidos
Aminoaciltransferases/genética
Aminoaciltransferases/metabolismo
Animais
Apicomplexa/genética
Apicomplexa/metabolismo
Bactérias/genética
Bactérias/metabolismo
Sítios de Ligação
Evolução Biológica
Clonagem Molecular
Cristalografia por Raios X
Expressão Gênica
Seres Humanos
Modelos Moleculares
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Aminoacil-RNA de Transferência/genética
Aminoacil-RNA de Transferência/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
Treonina/genética
Treonina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA, Transfer, Amino Acyl); 0 (Recombinant Proteins); 2ZD004190S (Threonine); EC 2.3.2.- (Aminoacyltransferases); OF5P57N2ZX (Alanine)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180208
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02204-w


  6 / 166611 MEDLINE  
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[PMID]:29318299
[Au] Autor:Jutersek M; Klemencic M; Dolinar M
[Ti] Título:Discrimination Between Synechocystis Members (Cyanobacteria) Based on Heterogeneity of Their 16S rRNA and ITS Regions.
[So] Source:Acta Chim Slov;64(4):804-817, 2017 Dec.
[Is] ISSN:1318-0207
[Cp] País de publicação:Slovenia
[La] Idioma:eng
[Ab] Resumo:Cyanobacteria are an important group of microorganisms displaying a range of morphologies that enable phenotypic differentiation between the major lineages of cyanobacteria, often to the genus level, but rarely to species or strain level. We focused on the unicellular genus Synechocystis that includes the model cyanobacterial strain PCC 6803. For 11 Synechocystis members obtained from cell culture collections, we sequenced the variable part of the 16S rRNA-encoding region and the 16S - 23S internally transcribed spacer (ITS), both standardly used in taxonomy. In combination with microscopic examination we observed that 2 out of 11 strains from cell culture collections were clearly different from typical Synechocystis members. For the rest of the samples, we demonstrated that both sequenced genomic regions are useful for discrimination between investigated species and that the ITS region alone allows for a reliable differentiation between Synechocystis strains.
[Mh] Termos MeSH primário: RNA Ribossômico 16S/química
Synechocystis/genética
[Mh] Termos MeSH secundário: Clonagem Molecular
DNA Espaçador Ribossômico/química
Análise de Sequência de RNA
Synechocystis/classificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Ribosomal Spacer); 0 (RNA, Ribosomal, 16S)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180111
[St] Status:MEDLINE


  7 / 166611 MEDLINE  
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[PMID]:28461446
[Au] Autor:Pequegnat B; Laird RM; Ewing CP; Hill CL; Omari E; Poly F; Monteiro MA; Guerry P
[Ad] Endereço:Department of Chemistry, University of Guelph, Guelph, Ontario, Canada.
[Ti] Título:Phase-Variable Changes in the Position of -Methyl Phosphoramidate Modifications on the Polysaccharide Capsule of Campylobacter jejuni Modulate Serum Resistance.
[So] Source:J Bacteriol;199(14), 2017 07 15.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:polysaccharide capsules (CPS) are characterized by the presence of nonstoichiometric -methyl phosphoramidate (MeOPN) modifications. The lack of stoichiometry is due to phase variation at homopolymeric tracts within the MeOPN transferase genes. strain 81-176 contains two MeOPN transferase genes and has been shown previously to contain MeOPN modifications at the 2 and 6 positions of the galactose (Gal) moiety in the CPS. We demonstrate here that one of the two MeOPN transferases, encoded by CJJ81176_1435, is bifunctional and is responsible for the addition of MeOPN to both the 2 and the 6 positions of Gal. A new MeOPN at the 4 position of Gal was observed in a mutant lacking the CJJ81176_1435 transferase and this was encoded by the CJJ81176_1420 transferase. During routine growth of 81-176, the CJJ81176_1420 transferase was predominantly in an off configuration, while the CJJ81176_1435 transferase was primarily on. However, exposure to normal human serum selected for cells expressing the CJJ81176_1420 transferase. MeOPN modifications appear to block binding of naturally occurring antibodies to the 81-176 CPS. The absence of MeOPN-4-Gal resulted in enhanced sensitivity to serum killing, whereas the loss of MeOPN-2-Gal and MeOPN-6-Gal resulted in enhanced resistance to serum killing, perhaps by allowing more MeOPN to be put onto the 4 position of Gal. undergoes phase variation in genes encoding surface antigens, leading to the concept that a strain of this organism consists of multiple genotypes that are selected for fitness in various environments. Methyl phosphoramidate modifications on the capsule of block access of preexisting antibodies in normal human sera to the polysaccharide chain, thus preventing activation of the classical arm of the complement cascade. We show that the capsule of strain 81-176 contains more sites of MeOPN modifications than previously recognized and that one site, on the 4 position of galactose, is more critical to complement resistance than the others. Exposure to normal human serum selects for variants in the population expressing this MeOPN modification.
[Mh] Termos MeSH primário: Amidas
Cápsulas Bacterianas/fisiologia
Campylobacter jejuni/metabolismo
Soros Imunes/imunologia
Ácidos Fosfóricos
Polissacarídeos Bacterianos/metabolismo
[Mh] Termos MeSH secundário: Animais
Anticorpos Antibacterianos
Clonagem Molecular
Regulação Bacteriana da Expressão Gênica/fisiologia
Epitopos Imunodominantes
Mutação
Polissacarídeos Bacterianos/química
Polissacarídeos Bacterianos/imunologia
Coelhos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amides); 0 (Antibodies, Bacterial); 0 (Immune Sera); 0 (Immunodominant Epitopes); 0 (Phosphoric Acids); 0 (Polysaccharides, Bacterial); 9Q189608GB (phosphoramidic acid)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE


  8 / 166611 MEDLINE  
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[PMID]:29351555
[Au] Autor:Xue Y; Chen B; Win AN; Fu C; Lian J; Liu X; Wang R; Zhang X; Chai Y
[Ad] Endereço:College of Agronomy and Biotechnology, Southwest University, Chongqing, China.
[Ti] Título:Omega-3 fatty acid desaturase gene family from two ω-3 sources, Salvia hispanica and Perilla frutescens: Cloning, characterization and expression.
[So] Source:PLoS One;13(1):e0191432, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Omega-3 fatty acid desaturase (ω-3 FAD, D15D) is a key enzyme for α-linolenic acid (ALA) biosynthesis. Both chia (Salvia hispanica) and perilla (Perilla frutescens) contain high levels of ALA in seeds. In this study, the ω-3 FAD gene family was systematically and comparatively cloned from chia and perilla. Perilla FAD3, FAD7, FAD8 and chia FAD7 are encoded by single-copy (but heterozygous) genes, while chia FAD3 is encoded by 2 distinct genes. Only 1 chia FAD8 sequence was isolated. In these genes, there are 1 to 6 transcription start sites, 1 to 8 poly(A) tailing sites, and 7 introns. The 5'UTRs of PfFAD8a/b contain 1 to 2 purine-stretches and 2 pyrimidine-stretches. An alternative splice variant of ShFAD7a/b comprises a 5'UTR intron. Their encoded proteins harbor an FA_desaturase conserved domain together with 4 trans-membrane helices and 3 histidine boxes. Phylogenetic analysis validated their identity of dicot microsomal or plastidial ω-3 FAD proteins, and revealed some important evolutionary features of plant ω-3 FAD genes such as convergent evolution across different phylums, single-copy status in algae, and duplication events in certain taxa. The qRT-PCR assay showed that the ω-3 FAD genes of two species were expressed at different levels in various organs, and they also responded to multiple stress treatments. The functionality of the ShFAD3 and PfFAD3 enzymes was confirmed by yeast expression. The systemic molecular and functional features of the ω-3 FAD gene family from chia and perilla revealed in this study will facilitate their use in future studies on genetic improvement of ALA traits in oilseed crops.
[Mh] Termos MeSH primário: Ácidos Graxos Dessaturases/genética
Genes de Plantas
Perilla frutescens/enzimologia
Perilla frutescens/genética
Proteínas de Plantas/genética
Salvia/enzimologia
Salvia/genética
[Mh] Termos MeSH secundário: Regiões 5' não Traduzidas
Processamento Alternativo
Sequência de Aminoácidos
Clonagem Molecular
Sequência Conservada
Evolução Molecular
Ácidos Graxos Dessaturases/química
Ácidos Graxos Dessaturases/metabolismo
Regulação Enzimológica da Expressão Gênica
Regulação da Expressão Gênica de Plantas
Família Multigênica
Especificidade de Órgãos
Filogenia
Proteínas de Plantas/química
Proteínas de Plantas/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
RNA de Plantas/genética
RNA de Plantas/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Homologia de Sequência de Aminoácidos
Estresse Fisiológico
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (5' Untranslated Regions); 0 (Plant Proteins); 0 (RNA, Messenger); 0 (RNA, Plant); 0 (Recombinant Proteins); EC 1.14.19.- (Fatty Acid Desaturases); EC 1.14.99.- (omega-3 fatty acid desaturase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180120
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191432


  9 / 166611 MEDLINE  
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[PMID]:28449035
[Au] Autor:Zhao JJ; Zhang Y; Fan DS; Feng JN
[Ad] Endereço:Key Laboratory of Plant Protection Resources & Pest Management of the Ministry of Education, Northwest A&F University, Yangling 712100, Shaanxi, China.
[Ti] Título:Identification and Expression Profiling of Odorant-Binding Proteins and Chemosensory Proteins of Daktulosphaira vitifoliae (Hemiptera: Phylloxeridae).
[So] Source:J Econ Entomol;110(4):1813-1820, 2017 08 01.
[Is] ISSN:1938-291X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In insects, odorant-binding proteins (OBPs) and chemosensory proteins (CSPs) are primary peripheral olfactory proteins playing critical roles in odorant detection. In this study, we present the first identification of OBPs and CSPs from the transcriptome of grape phylloxera Daktulosphaira vitifoliae Fitch, an important pest that damages both roots and leaves of grapes. The OBPs contained six conserved cysteine residues and the CSPs contained four conserved cysteine residues in this insect. Phylogenetic analysis showed that most of the olfactory proteins were closely related to OBPs and CSPs from other aphids. However, DviOBP7 and DviCSP9 were different because they were classified into different independent branches, respectively. Real-time polymerase chain reaction (RT-PCR) was used to examine the tissue expression of these transcripts. DviOBP1, DviOBP6, and DviOBP7 were uniquely or primarily expressed in antennae and not in the body. DviOBP2 was more abundantly expressed in the body than in the antennae. The expression levels of OBPs and CSPs of phylloxera varied depending upon where they were expressed in different body tissues.
[Mh] Termos MeSH primário: Hemípteros/genética
Proteínas de Insetos/genética
Receptores Odorantes/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
China
Clonagem Molecular
DNA Complementar/genética
Hemípteros/metabolismo
Proteínas de Insetos/química
Proteínas de Insetos/metabolismo
Filogenia
RNA/genética
Reação em Cadeia da Polimerase em Tempo Real
Receptores Odorantes/química
Receptores Odorantes/metabolismo
Alinhamento de Sequência
Distribuição Tecidual
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Complementary); 0 (Insect Proteins); 0 (Receptors, Odorant); 0 (odorant-binding protein); 63231-63-0 (RNA)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1093/jee/tox121


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[PMID]:29360877
[Au] Autor:Verma V; Kaur C; Grover P; Gupta A; Chaudhary VK
[Ad] Endereço:Centre for Innovation in Infectious Disease Research, Education and Training (CIIDRET), University of Delhi South Campus, New Delhi, India.
[Ti] Título:Biotin-tagged proteins: Reagents for efficient ELISA-based serodiagnosis and phage display-based affinity selection.
[So] Source:PLoS One;13(1):e0191315, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The high-affinity interaction between biotin and streptavidin has opened avenues for using recombinant proteins with site-specific biotinylation to achieve efficient and directional immobilization. The site-specific biotinylation of proteins carrying a 15 amino acid long Biotin Acceptor Peptide tag (BAP; also known as AviTag) is effected on a specific lysine either by co-expressing the E. coli BirA enzyme in vivo or by using purified recombinant E. coli BirA enzyme in the presence of ATP and biotin in vitro. In this paper, we have designed a T7 promoter-lac operator-based expression vector for rapid and efficient cloning, and high-level cytosolic expression of proteins carrying a C-terminal BAP tag in E. coli with TEV protease cleavable N-terminal deca-histidine tag, useful for initial purification. Furthermore, a robust three-step purification pipeline integrated with well-optimized protocols for TEV protease-based H10 tag removal, and recombinant BirA enzyme-based site-specific in vitro biotinylation is described to obtain highly pure biotinylated proteins. Most importantly, the paper demonstrates superior sensitivities in indirect ELISA with directional and efficient immobilization of biotin-tagged proteins on streptavidin-coated surfaces in comparison to passive immobilization. The use of biotin-tagged proteins through specific immobilization also allows more efficient selection of binders from a phage-displayed naïve antibody library. In addition, for both these applications, specific immobilization requires much less amount of protein as compared to passive immobilization and can be easily multiplexed. The simplified strategy described here for the production of highly pure biotin-tagged proteins will find use in numerous applications, including those, which may require immobilization of multiple proteins simultaneously on a solid surface.
[Mh] Termos MeSH primário: Proteínas de Bactérias/isolamento & purificação
Proteínas de Bactérias/metabolismo
Biotina/metabolismo
Ensaio de Imunoadsorção Enzimática/métodos
Biblioteca de Peptídeos
Testes Sorológicos/métodos
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Biotinilação
Carbono-Nitrogênio Ligases/metabolismo
Clonagem Molecular
Citosol/metabolismo
Escherichia coli/citologia
Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Vetores Genéticos/genética
Indicadores e Reagentes/metabolismo
Mycobacterium tuberculosis/genética
Proteínas Repressoras/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Escherichia coli Proteins); 0 (Indicators and Reagents); 0 (Peptide Library); 0 (Repressor Proteins); 6SO6U10H04 (Biotin); EC 6.3.- (Carbon-Nitrogen Ligases); EC 6.3.4.15 (birA protein, E coli)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180124
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191315



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