Base de dados : MEDLINE
Pesquisa : B01.050.150.900.090.180.610.500.562 [Categoria DeCS]
Referências encontradas : 24072 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 2408 ir para página                         

  1 / 24072 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[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


  2 / 24072 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28462392
[Au] Autor:Li WC; Zhu XY; Ritson E
[Ad] Endereço:University of St Andrews, St Andrews, Fife KY16 9JP, Scotland.
[Ti] Título:Mechanosensory Stimulation Evokes Acute Concussion-Like Behavior by Activating GIRKs Coupled to Muscarinic Receptors in a Simple Vertebrate.
[So] Source:eNeuro;4(2), 2017 Mar-Apr.
[Is] ISSN:2373-2822
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Most vertebrates show concussion responses when their heads are hit suddenly by heavy objects. Previous studies have focused on the direct physical injuries to the neural tissue caused by the concussive blow. We study a similar behavior in a simple vertebrate, the tadpole. We find that concussion-like behavior can be reliably induced by the mechanosensory stimulation of the head skin without direct physical impacts on the brain. Head skin stimulation activates a cholinergic pathway which then opens G protein-coupled inward-rectifying potassium channels (GIRKs) via postsynaptic M muscarinic receptors to inhibit brainstem neurons critical for the initiation and maintenance of swimming for up to minutes and can explain many features commonly observed immediately after concussion. We propose that some acute symptoms of concussion in vertebrates can be explained by the opening of GIRKs following mechanosensory stimulation to the head.
[Mh] Termos MeSH primário: Acetilcolina/metabolismo
Canais de Potássio Corretores do Fluxo de Internalização Acoplados a Proteínas G/metabolismo
Neurônios/metabolismo
Receptores Muscarínicos/metabolismo
[Mh] Termos MeSH secundário: Animais
Concussão Encefálica/metabolismo
Tronco Encefálico/metabolismo
Seres Humanos
Oócitos/metabolismo
Vertebrados/metabolismo
Xenopus laevis/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (G Protein-Coupled Inwardly-Rectifying Potassium Channels); 0 (Receptors, Muscarinic); N9YNS0M02X (Acetylcholine)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE


  3 / 24072 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29223398
[Au] Autor:Sun J; Wang X; Shi Y; Li J; Li C; Shi Z; Chen Y; Mao B
[Ad] Endereço:State Key Laboratory of Genetic Resources and Evolution, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, China.
[Ti] Título:EphA7 regulates claudin6 and pronephros development in Xenopus.
[So] Source:Biochem Biophys Res Commun;495(2):1580-1587, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Eph/ephrin molecules are widely expressed during embryonic development, and function in a variety of developmental processes. Here we studied the roles of the Eph receptor EphA7 and its soluble form in Xenopus pronephros development. EphA7 is specifically expressed in pronephric tubules at tadpole stages and knockdown of EphA7 by a translation blocking morpholino led to defects in tubule cell differentiation and morphogenesis. A soluble form of EphA7 (sEphA7) was also identified. Interestingly, the membrane level of claudin6 (CLDN6), a tetraspan transmembrane tight junction protein, was dramatically reduced in the translation blocking morpholino injected embryos, but not when a splicing morpholino was used, which blocks only the full length EphA7. In cultured cells, EphA7 binds and phosphorylates CLDN6, and reduces its distribution at the cell surface. Our work suggests a role of EphA7 in the regulation of cell adhesion during pronephros development, whereas sEphA7 works as an antagonist.
[Mh] Termos MeSH primário: Claudinas/metabolismo
Pronefro/embriologia
Receptor EphA7/metabolismo
Proteínas de Xenopus/metabolismo
Xenopus laevis/embriologia
Xenopus laevis/metabolismo
[Mh] Termos MeSH secundário: Animais
Membrana Celular/metabolismo
Regulação da Expressão Gênica no Desenvolvimento
Técnicas de Silenciamento de Genes
Oligodesoxirribonucleotídeos Antissenso/genética
Pronefro/metabolismo
Receptor EphA7/antagonistas & inibidores
Receptor EphA7/genética
Solubilidade
Proteínas de Xenopus/antagonistas & inibidores
Proteínas de Xenopus/genética
Xenopus laevis/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Claudins); 0 (Oligodeoxyribonucleotides, Antisense); 0 (Xenopus Proteins); 0 (claudin 6); EC 2.7.10.1 (Receptor, EphA7)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171211
[St] Status:MEDLINE


  4 / 24072 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29305262
[Au] Autor:Ågren R; Sahlholm K; Nilsson J; Århem P
[Ad] Endereço:Department of Neuroscience, Retzius väg 8, Karolinska Institutet, SE-171 77, Stockholm, Sweden. Electronic address: richard.agren@stud.ki.se.
[Ti] Título:Point mutation of a conserved aspartate, D69, in the muscarinic M receptor does not modify voltage-sensitive agonist potency.
[So] Source:Biochem Biophys Res Commun;496(1):101-104, 2018 01 29.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The muscarinic M receptor (M R) has been shown to display voltage-sensitive agonist binding, based on G protein-activated inward rectifier potassium channel (GIRK) opening and radioligand binding at different membrane voltages. A conserved aspartate in transmembrane segment (TM) II of M R, D69, has been proposed as the voltage sensor. While a recent paper instead presented evidence of tyrosines in TMs III, VI, and VII acting as voltage sensors, these authors were not able to record GIRK channel activation by a D69N mutant M R. In the present study, we succeeded in recording ACh-induced GIRK channel activation by this mutant at -80 and 0 mV. The acetylcholine EC was about 2.5-fold higher at 0 mV, a potency shift very similar to that observed at wild-type M R, indicating that voltage sensitivity persists at the D69N mutant. Thus, our present observations corroborate the notion that D69 is not responsible for voltage sensitivity of the M R.
[Mh] Termos MeSH primário: Acetilcolina/administração & dosagem
Canais de Potássio Corretores do Fluxo de Internalização Acoplados a Proteínas G/metabolismo
Potenciais da Membrana/efeitos dos fármacos
Potenciais da Membrana/fisiologia
Receptor Muscarínico M2/genética
Receptor Muscarínico M2/metabolismo
[Mh] Termos MeSH secundário: Animais
Ácido Aspártico/genética
Células Cultivadas
Sequência Conservada
Relação Dose-Resposta a Droga
Mutagênese Sítio-Dirigida
Oócitos
Mutação Puntual/genética
Receptor Muscarínico M2/efeitos dos fármacos
Relação Estrutura-Atividade
Xenopus laevis
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (G Protein-Coupled Inwardly-Rectifying Potassium Channels); 0 (Receptor, Muscarinic M2); 30KYC7MIAI (Aspartic Acid); N9YNS0M02X (Acetylcholine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180107
[St] Status:MEDLINE


  5 / 24072 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29190819
[Au] Autor:Mathavan K; Khedgikar V; Bartolo V; Alfandari D
[Ad] Endereço:Department of Veterinary and Animal Sciences, University of Massachusetts Amherst, Amherst, Massachusetts, United States of America.
[Ti] Título:The ectodomain of cadherin-11 binds to erbB2 and stimulates Akt phosphorylation to promote cranial neural crest cell migration.
[So] Source:PLoS One;12(11):e0188963, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:During development, a multi-potent group of cells known as the cranial neural crest (CNC) migrate to form craniofacial structures. Proper migration of these cells requires proteolysis of cell adhesion molecules, such as cadherins. In Xenopus laevis, preventing extracellular cleavage of cadherin-11 impairs CNC migration. However, overexpression of the soluble cleavage product (EC1-3) is capable of rescuing this phenotype. The mechanism by which EC1-3 promotes CNC migration has not been investigated until now. Here we show that EC1-3 stimulates phosphorylation of Akt, a target of PI3K, in X.laevis CNC. Through immunoprecipitation experiments, we determined that EC1-3 interacts with all ErbB receptors, PDGFRα, and FGFR1. Of these receptors, only ErbB2 was able to produce an increase in Akt phosphorylation upon treatment with a recombinant EC1-3. This increase was abrogated by mubritinib, an inhibitor of ErbB2. We were able to recapitulate this decrease in Akt phosphorylation in vivo by knocking down ErbB2 in CNC cells. Knockdown of the receptor also significantly reduced CNC migration in vivo. We confirmed the importance of ErbB2 and ErbB receptor signaling in CNC migration using mubritinib and canertinib, respectively. Mubritinib and the PI3K inhibitor LY294002 significantly decreased cell migration while canertinib nearly prevented it altogether. These data show that ErbB2 and Akt are important for CNC migration and implicate other ErbB receptors and Akt-independent signaling pathways. Our findings provide the first example of a functional interaction between the extracellular domain of a type II classical cadherin and growth factor receptors.
[Mh] Termos MeSH primário: Encéfalo/citologia
Caderinas/metabolismo
Movimento Celular
Crista Neural/citologia
Proteínas Proto-Oncogênicas c-akt/metabolismo
Receptor ErbB-2/metabolismo
[Mh] Termos MeSH secundário: Animais
Encéfalo/metabolismo
Caderinas/química
Células HEK293
Seres Humanos
Fosforilação
Ligação Proteica
Xenopus laevis/embriologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cadherins); 156621-71-5 (osteoblast cadherin); EC 2.7.10.1 (ERBB2 protein, human); EC 2.7.10.1 (Receptor, ErbB-2); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188963


  6 / 24072 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[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


  7 / 24072 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29179200
[Au] Autor:Rinné S; Kiper AK; Schmidt C; Ortiz-Bonnin B; Zwiener S; Seebohm G; Decher N
[Ad] Endereço:Institute of Physiology and Pathophysiology, Vegetative Physiology, University of Marburg, Marburg, Germany.
[Ti] Título:Stress-Kinase Regulation of TASK-1 and TASK-3.
[So] Source:Cell Physiol Biochem;44(3):1024-1037, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIMS: TASK channels belong to the two-pore-domain potassium (K2P) channel family. TASK-1 is discussed to contribute to chronic atrial fibrillation (AFib) and has been together with uncoupling protein 1 found as a marker protein of brown adipose tissue (BAT) fat. In addition, TASK-1 was linked in a genome-wide association study to an increased body mass index. A recent study showed that TASK-1 inhibition is causing obesity in mice by a BAT whitening and that these effects are linked to the mineralocorticoid receptor pathway, albeit the mechanism remained elusive. Therefore, we aimed to probe whether K2P channels are regulated by serum- and glucocorticoid-inducible kinases (SGKs) which are known to modify many cellular functions by modulating ion channels. METHODS: To this end we used functional co-expression studies and chemiluminescence-assays in Xenopus oocytes, together with fluorescence imaging and quantitative PCR experiments. RESULTS: SGKs and proteinkinase B (PKB) induced a strong, dose- and time-dependent current reduction of TASK-1 and TASK-3. SGK co-expression reduced the surface expression of TASK-1/3, leading to a predominant localization of the channels into late endosomes. The down regulation of TASK-3 channels was abrogated by the dynamin inhibitor dynasore, confirming a role of SGKs in TASK-1/3 channel endocytosis. CONCLUSION: Stress-mediated changes in SGK expression pattern or activation is likely to alter TASK-1/3 expression at the surface membrane. The observed TASK-1 regulation might contribute to the pathogenesis of chronic AFib and provide a mechanistic link between increased mineralocorticoid levels and TASK-1 reduction, both linked to BAT whitening.
[Mh] Termos MeSH primário: Proteínas do Tecido Nervoso/metabolismo
Canais de Potássio de Domínios Poros em Tandem/metabolismo
[Mh] Termos MeSH secundário: Proteínas Quinases Dependentes de 3-Fosfoinositídeo/metabolismo
Animais
Células COS
Cercopithecus aethiops
Clatrina/metabolismo
Endocitose
Endossomos/metabolismo
Células HeLa
Seres Humanos
Hidrazonas/farmacologia
Proteínas Imediatamente Precoces/genética
Proteínas Imediatamente Precoces/metabolismo
Medições Luminescentes
Microscopia de Fluorescência
Proteínas do Tecido Nervoso/genética
Oócitos/química
Oócitos/fisiologia
Técnicas de Patch-Clamp
Plasmídeos/genética
Plasmídeos/metabolismo
Canais de Potássio de Domínios Poros em Tandem/genética
Proteínas Serina-Treonina Quinases/genética
Proteínas Serina-Treonina Quinases/metabolismo
Proteínas Proto-Oncogênicas c-akt/metabolismo
Imagem com Lapso de Tempo
Xenopus laevis/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Clathrin); 0 (Hydrazones); 0 (Immediate-Early Proteins); 0 (KCNK9 protein, human); 0 (N'-(3,4-dihydroxybenzylidene)-3-hydroxy-2-naphthahydrazide); 0 (Nerve Tissue Proteins); 0 (Potassium Channels, Tandem Pore Domain); 0 (potassium channel subfamily K member 3); EC 2.7.11.1 (3-Phosphoinositide-Dependent Protein Kinases); EC 2.7.11.1 (PDPK1 protein, human); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 2.7.11.1 (serum-glucocorticoid regulated kinase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180118
[Lr] Data última revisão:
180118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1159/000485402


  8 / 24072 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27773672
[Au] Autor:Dankert JF; Rona G; Clijsters L; Geter P; Skaar JR; Bermudez-Hernandez K; Sassani E; Fenyö D; Ueberheide B; Schneider R; Pagano M
[Ad] Endereço:Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, 522 First Avenue, SRB 1107, New York, NY 10016, USA; Perlmutter NYU Cancer Center, New York University School of Medicine, 522 First Avenue, SRB 1107, New York, NY 10016, USA.
[Ti] Título:Cyclin F-Mediated Degradation of SLBP Limits H2A.X Accumulation and Apoptosis upon Genotoxic Stress in G2.
[So] Source:Mol Cell;64(3):507-519, 2016 Nov 03.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:SLBP (stem-loop binding protein) is a highly conserved factor necessary for the processing, translation, and degradation of H2AFX and canonical histone mRNAs. We identified the F-box protein cyclin F, a substrate recognition subunit of an SCF (Skp1-Cul1-F-box protein) complex, as the G2 ubiquitin ligase for SLBP. SLBP interacts with cyclin F via an atypical CY motif, and mutation of this motif prevents SLBP degradation in G2. Expression of an SLBP stable mutant results in increased loading of H2AFX mRNA onto polyribosomes, resulting in increased expression of H2A.X (encoded by H2AFX). Upon genotoxic stress in G2, high levels of H2A.X lead to persistent γH2A.X signaling, high levels of H2A.X phosphorylated on Tyr142, high levels of p53, and induction of apoptosis. We propose that cyclin F co-evolved with the appearance of stem-loops in vertebrate H2AFX mRNA to mediate SLBP degradation, thereby limiting H2A.X synthesis and cell death upon genotoxic stress.
[Mh] Termos MeSH primário: Ciclinas/genética
Dano ao DNA
Pontos de Checagem da Fase G2 do Ciclo Celular/genética
Histonas/genética
Proteínas Nucleares/genética
RNA Mensageiro/genética
Fatores de Poliadenilação e Clivagem de mRNA/genética
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Animais
Apoptose
Sítios de Ligação
Linhagem Celular Tumoral
Ciclinas/metabolismo
Regulação da Expressão Gênica
Células HEK293
Células HeLa
Histonas/metabolismo
Seres Humanos
Camundongos
Proteínas Nucleares/metabolismo
Fosforilação
Polirribossomos/genética
Polirribossomos/metabolismo
Ligação Proteica
Proteólise
RNA Mensageiro/metabolismo
Ratos
Transdução de Sinais
Xenopus laevis
Peixe-Zebra
Fatores de Poliadenilação e Clivagem de mRNA/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CCNF protein, human); 0 (Cyclins); 0 (H2AFX protein, human); 0 (Histones); 0 (Nuclear Proteins); 0 (RNA, Messenger); 0 (SLBP protein, human); 0 (mRNA Cleavage and Polyadenylation Factors)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:180119
[Lr] Data última revisão:
180119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161105
[St] Status:MEDLINE


  9 / 24072 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29244877
[Au] Autor:Steinmann ME; Schmidt RS; Macêdo JP; Kunz Renggli C; Bütikofer P; Rentsch D; Mäser P; Sigel E
[Ad] Endereço:Institute of Biochemistry and Molecular Medicine, University of Bern, Bern, Switzerland.
[Ti] Título:Identification and characterization of the three members of the CLC family of anion transport proteins in Trypanosoma brucei.
[So] Source:PLoS One;12(12):e0188219, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:CLC type anion transport proteins are homo-dimeric or hetero-dimeric with an integrated transport function in each subunit. We have identified and partially characterized three members of this family named TbVCL1, TbVCL2 and TbVCL3 in Trypanosoma brucei. Among the human CLC family members, the T. brucei proteins display highest similarity to CLC-6 and CLC-7. TbVCL1, but not TbVCL2 and TbVCL3 is able to complement growth of a CLC-deficient Saccharomyces cerevisiae mutant. All TbVCL-HA fusion proteins localize intracellulary in procyclic form trypanosomes. TbVCL1 localizes close to the Golgi apparatus and TbVCL2 and TbVCL3 to the endoplasmic reticulum. Upon expression in Xenopus oocytes, all three proteins induce similar outward rectifying chloride ion currents. Currents are sensitive to low concentrations of DIDS, insensitive to the pH in the range 5.4 to 8.4 and larger in nitrate than in chloride medium.
[Mh] Termos MeSH primário: Canais de Cloreto/genética
Retículo Endoplasmático/metabolismo
Estágios do Ciclo de Vida/fisiologia
Proteínas de Protozoários/genética
Saccharomyces cerevisiae/metabolismo
Trypanosoma brucei brucei/metabolismo
[Mh] Termos MeSH secundário: Ácido 4,4'-Di-Isotiocianoestilbeno-2,2'-Dissulfônico/farmacologia
Animais
Canais de Cloreto/antagonistas & inibidores
Canais de Cloreto/metabolismo
Cloretos/metabolismo
Retículo Endoplasmático/ultraestrutura
Feminino
Expressão Gênica
Teste de Complementação Genética
Complexo de Golgi/metabolismo
Complexo de Golgi/ultraestrutura
Seres Humanos
Transporte de Íons
Potenciais da Membrana/efeitos dos fármacos
Potenciais da Membrana/fisiologia
Nitratos/metabolismo
Oócitos/citologia
Oócitos/efeitos dos fármacos
Oócitos/metabolismo
Técnicas de Patch-Clamp
Multimerização Proteica
Proteínas de Protozoários/antagonistas & inibidores
Proteínas de Protozoários/metabolismo
Saccharomyces cerevisiae/genética
Trypanosoma brucei brucei/crescimento & desenvolvimento
Trypanosoma brucei brucei/ultraestrutura
Xenopus laevis
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CLCN6 protein, human); 0 (CLCN7 protein, human); 0 (Chloride Channels); 0 (Chlorides); 0 (Nitrates); 0 (Protozoan Proteins); Q1O6DSW23R (4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180108
[Lr] Data última revisão:
180108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171216
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188219


  10 / 24072 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28455449
[Au] Autor:Kaur K; Park H; Pandey N; Azuma Y; De Guzman RN
[Ad] Endereço:From the Department of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045.
[Ti] Título:Identification of a new small ubiquitin-like modifier (SUMO)-interacting motif in the E3 ligase PIASy.
[So] Source:J Biol Chem;292(24):10230-10238, 2017 06 16.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Small ubiquitin-like modifier (SUMO) conjugation is a reversible post-translational modification process implicated in the regulation of gene transcription, DNA repair, and cell cycle. SUMOylation depends on the sequential activities of E1 activating, E2 conjugating, and E3 ligating enzymes. SUMO E3 ligases enhance transfer of SUMO from the charged E2 enzyme to the substrate. We have previously identified PIASy, a member of the Siz/protein inhibitor of activated STAT (PIAS) RING family of SUMO E3 ligases, as essential for mitotic chromosomal SUMOylation in frog egg extracts and demonstrated that it can mediate effective SUMOylation. To address how PIASy catalyzes SUMOylation, we examined various truncations of PIASy for their ability to mediate SUMOylation. Using NMR chemical shift mapping and mutagenesis, we identified a new SUMO-interacting motif (SIM) in PIASy. The new SIM and the currently known SIM are both located at the C terminus of PIASy, and both are required for the full ligase activity of PIASy. Our results provide novel insights into the mechanism of PIASy-mediated SUMOylation. PIASy adds to the growing list of SUMO E3 ligases containing multiple SIMs that play important roles in the E3 ligase activity.
[Mh] Termos MeSH primário: Modelos Moleculares
Proteínas Inibidoras de STAT Ativados/metabolismo
Proteínas Repressoras/metabolismo
Proteínas Modificadoras Pequenas Relacionadas à Ubiquitina/metabolismo
Sumoilação
Ubiquitinas/metabolismo
Proteínas de Xenopus/metabolismo
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Animais
Deleção de Genes
Seres Humanos
Interações Hidrofóbicas e Hidrofílicas
Ligantes
Mutagênese Sítio-Dirigida
Mutação
Isótopos de Nitrogênio
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Proteínas Inibidoras de STAT Ativados/química
Proteínas Inibidoras de STAT Ativados/genética
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Proteínas Repressoras/química
Proteínas Repressoras/genética
Proteínas Modificadoras Pequenas Relacionadas à Ubiquitina/química
Proteínas Modificadoras Pequenas Relacionadas à Ubiquitina/genética
Ubiquitinas/química
Ubiquitinas/genética
Proteínas de Xenopus/química
Proteínas de Xenopus/genética
Xenopus laevis
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Ligands); 0 (Nitrogen Isotopes); 0 (PIASy protein, Xenopus); 0 (Peptide Fragments); 0 (Protein Inhibitors of Activated STAT); 0 (Recombinant Fusion Proteins); 0 (Recombinant Proteins); 0 (Repressor Proteins); 0 (SUMO2 protein, human); 0 (SUMO3 protein, human); 0 (Small Ubiquitin-Related Modifier Proteins); 0 (Ubiquitins); 0 (Xenopus Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171228
[Lr] Data última revisão:
171228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.789982



página 1 de 2408 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