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[PMID]:28369060
[Au] Autor:Mendoza-García P; Hugosson F; Fallah M; Higgins ML; Iwasaki Y; Pfeifer K; Wolfstetter G; Varshney G; Popichenko D; Gergen JP; Hens K; Deplancke B; Palmer RH
[Ad] Endereço:Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
[Ti] Título:The Zic family homologue Odd-paired regulates Alk expression in Drosophila.
[So] Source:PLoS Genet;13(4):e1006617, 2017 Apr.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Anaplastic Lymphoma Kinase (Alk) receptor tyrosine kinase (RTK) plays a critical role in the specification of founder cells (FCs) in the Drosophila visceral mesoderm (VM) during embryogenesis. Reporter gene and CRISPR/Cas9 deletion analysis reveals enhancer regions in and upstream of the Alk locus that influence tissue-specific expression in the amnioserosa (AS), the VM and the epidermis. By performing high throughput yeast one-hybrid screens (Y1H) with a library of Drosophila transcription factors (TFs) we identify Odd-paired (Opa), the Drosophila homologue of the vertebrate Zic family of TFs, as a novel regulator of embryonic Alk expression. Further characterization identifies evolutionarily conserved Opa-binding cis-regulatory motifs in one of the Alk associated enhancer elements. Employing Alk reporter lines as well as CRISPR/Cas9-mediated removal of regulatory elements in the Alk locus, we show modulation of Alk expression by Opa in the embryonic AS, epidermis and VM. In addition, we identify enhancer elements that integrate input from additional TFs, such as Binou (Bin) and Bagpipe (Bap), to regulate VM expression of Alk in a combinatorial manner. Taken together, our data show that the Opa zinc finger TF is a novel regulator of embryonic Alk expression.
[Mh] Termos MeSH primário: Proteínas de Drosophila/genética
Drosophila melanogaster/embriologia
Regulação da Expressão Gênica no Desenvolvimento
Proteínas de Homeodomínio/genética
Receptores Proteína Tirosina Quinases/genética
Fatores de Transcrição/genética
[Mh] Termos MeSH secundário: Complexo 1 de Proteínas Adaptadoras/genética
Complexo 1 de Proteínas Adaptadoras/metabolismo
Subunidades beta do Complexo de Proteínas Adaptadoras/genética
Subunidades beta do Complexo de Proteínas Adaptadoras/metabolismo
Animais
Animais Geneticamente Modificados
Sítios de Ligação
Sistemas CRISPR-Cas
Proteínas de Drosophila/metabolismo
Drosophila melanogaster/genética
Embrião não Mamífero
Elementos Facilitadores Genéticos
Fatores de Transcrição Forkhead/genética
Fatores de Transcrição Forkhead/metabolismo
Proteínas de Homeodomínio/metabolismo
Regiões Promotoras Genéticas
Receptores Proteína Tirosina Quinases/metabolismo
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Protein Complex 1); 0 (Adaptor Protein Complex beta Subunits); 0 (Bap protein, Drosophila); 0 (Drosophila Proteins); 0 (Forkhead Transcription Factors); 0 (Homeodomain Proteins); 0 (Opa protein, Drosophila); 0 (Transcription Factors); 0 (biniou protein, Drosophila); EC 2.7.10.1 (Receptor Protein-Tyrosine Kinases); EC 2.7.10.1 (anaplastic lymphoma kinase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170516
[Lr] Data última revisão:
170516
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170404
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006617


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[PMID]:27889060
[Au] Autor:Assoum M; Philippe C; Isidor B; Perrin L; Makrythanasis P; Sondheimer N; Paris C; Douglas J; Lesca G; Antonarakis S; Hamamy H; Jouan T; Duffourd Y; Auvin S; Saunier A; Begtrup A; Nowak C; Chatron N; Ville D; Mireskandari K; Milani P; Jonveaux P; Lemeur G; Milh M; Amamoto M; Kato M; Nakashima M; Miyake N; Matsumoto N; Masri A; Thauvin-Robinet C; Rivière JB; Faivre L; Thevenon J
[Ad] Endereço:Equipe d'Accueil 4271, Génétique des Anomalies du Développement, Université de Bourgogne, 21079 Dijon, France.
[Ti] Título:Autosomal-Recessive Mutations in AP3B2, Adaptor-Related Protein Complex 3 Beta 2 Subunit, Cause an Early-Onset Epileptic Encephalopathy with Optic Atrophy.
[So] Source:Am J Hum Genet;99(6):1368-1376, 2016 Dec 01.
[Is] ISSN:1537-6605
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Early-onset epileptic encephalopathy (EOEE) represents a heterogeneous group of severe disorders characterized by seizures, interictal epileptiform activity with a disorganized electroencephalography background, developmental regression or retardation, and onset before 1 year of age. Among a cohort of 57 individuals with epileptic encephalopathy, we ascertained two unrelated affected individuals with EOEE associated with developmental impairment and autosomal-recessive variants in AP3B2 by means of whole-exome sequencing. The targeted sequencing of AP3B2 in 86 unrelated individuals with EOEE led to the identification of an additional family. We gathered five additional families with eight affected individuals through the Matchmaker Exchange initiative by matching autosomal-recessive mutations in AP3B2. Reverse phenotyping of 12 affected individuals from eight families revealed a homogeneous EOEE phenotype characterized by severe developmental delay, poor visual contact with optic atrophy, and postnatal microcephaly. No spasticity, albinism, or hematological symptoms were reported. AP3B2 encodes the neuron-specific subunit of the AP-3 complex. Autosomal-recessive variations of AP3B1, the ubiquitous isoform, cause Hermansky-Pudlak syndrome type 2. The only isoform for the δ subunit of the AP-3 complex is encoded by AP3D1. Autosomal-recessive mutations in AP3D1 cause a severe disorder cumulating the symptoms of the AP3B1 and AP3B2 defects.
[Mh] Termos MeSH primário: Complexo 3 de Proteínas Adaptadoras/genética
Subunidades beta do Complexo de Proteínas Adaptadoras/genética
Epilepsia/complicações
Epilepsia/genética
Genes Recessivos/genética
Mutação
Atrofia Óptica/complicações
Atrofia Óptica/genética
[Mh] Termos MeSH secundário: Idade de Início
Criança
Pré-Escolar
Deficiências do Desenvolvimento/genética
Feminino
Seres Humanos
Lactente
Recém-Nascido
Masculino
Microcefalia/genética
Linhagem
Síndrome
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AP3B2 protein, human); 0 (Adaptor Protein Complex 3); 0 (Adaptor Protein Complex beta Subunits)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170830
[Lr] Data última revisão:
170830
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161128
[St] Status:MEDLINE


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[PMID]:27392064
[Au] Autor:Alford JE; Marongiu M; Watkins GL; Anderson EC
[Ad] Endereço:School of Life Sciences, University of Warwick, Coventry, United Kingdom.
[Ti] Título:Human Immunodeficiency Virus Type 2 (HIV-2) Gag Is Trafficked in an AP-3 and AP-5 Dependent Manner.
[So] Source:PLoS One;11(7):e0158941, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Although human immunodeficiency virus (HIV) types 1 and 2 are closely related lentiviruses with similar replication cycles, HIV-2 infection is associated with slower progression to AIDS, a higher proportion of long term non-progressors, and lower rates of transmission than HIV-1, likely as a consequence of a lower viral load during HIV-2 infection. A mechanistic explanation for the differential viral load remains unclear but knowledge of differences in particle production between HIV-1 and HIV-2 may help to shed light on this issue. In contrast to HIV-1, little is known about the assembly of HIV-2 particles, and the trafficking of HIV-2 Gag, the structural component of the virus, within cells. We have established that HIV-2 Gag accumulates in intracellular CD63 positive compartments, from which it may be delivered or recycled to the cell surface, or degraded. HIV-2 particle release was dependent on the adaptor protein complex AP-3 and the newly identified AP-5 complex, but much less so on AP-1. In contrast, HIV-1 particle release required AP-1 and AP-3, but not AP-5. AP-2, an essential component of clathrin-mediated endocytosis, which was previously shown to be inhibitory to HIV-1 particle release, had no effect on HIV-2. The differential requirement for adaptor protein complexes confirmed that HIV-1 and HIV-2 Gag have distinct cellular trafficking pathways, and that HIV-2 particles may be more susceptible to degradation prior to release.
[Mh] Termos MeSH primário: Complexo 3 de Proteínas Adaptadoras/metabolismo
Subunidades beta do Complexo de Proteínas Adaptadoras/metabolismo
Proteínas Adaptadoras de Transporte Vesicular/metabolismo
HIV-2/metabolismo
Vírion/metabolismo
Produtos do Gene gag do Vírus da Imunodeficiência Humana/metabolismo
[Mh] Termos MeSH secundário: Complexo 3 de Proteínas Adaptadoras/genética
Subunidades beta do Complexo de Proteínas Adaptadoras/genética
Proteínas Adaptadoras de Transporte Vesicular/genética
HIV-1/genética
HIV-1/metabolismo
HIV-2/genética
Células HeLa
Seres Humanos
Transporte Proteico
Tetraspanina 30/genética
Tetraspanina 30/metabolismo
Vírion/genética
Produtos do Gene gag do Vírus da Imunodeficiência Humana/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AP3B1 protein, human); 0 (AP5B1 protein, human); 0 (Adaptor Protein Complex 3); 0 (Adaptor Protein Complex beta Subunits); 0 (Adaptor Proteins, Vesicular Transport); 0 (CD63 protein, human); 0 (Tetraspanin 30); 0 (gag Gene Products, Human Immunodeficiency Virus)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160709
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0158941


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[PMID]:26643602
[Au] Autor:Shang D; Dong L; Zeng L; Yang R; Xu J; Wu Y; Xu R; Tao H; Zhang N
[Ad] Endereço:Department of Stomatology, the First Affiliated Hospital, School of Medicine, Xi'an Jiaotong University, Xi'an, China.
[Ti] Título:Two-stage comprehensive evaluation of genetic susceptibility of common variants in FBXO38, AP3B2 and WHAMM to severe chronic periodontitis.
[So] Source:Sci Rep;5:17882, 2015 Dec 08.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Chronic periodontitis is an oral disorder characterized with gingival inflammation and bone destruction. As the sixth-most prevalent condition affecting more than 743 million people around the world, it is classified as one of the seven destructive oral disorders. Early genetic epidemiological evidence indicated a major role for genetics in periodontal disease development. In this study, we conducted a two-stage comprehensive evaluation of the genetic susceptibility of FBXO38, AP3B2 and WHAMM with the diagnosis of severe chronic periodontitis. A total of 5,065 study subjects from the Han Chinese population consisting of 1,264 cases and 3,801 healthy controls were recruited, and 65 single nucleotide markers related to the three candidate genes were genotyped to investigate the susceptibility of patients with these polymorphisms to severe chronic periodontitis. To increase the coverage of genetic markers, we implemented imputation techniques to extend the number of tested makers to 416. Single marker and haplotype-based analyses were performed, and significant results were obtained for FBXO38 (rs10043775, P = 0.0009) and AP3B2 (rs11631963-rs11637433, CA, P = 9.98 × 10(-5); rs1864699-rs2099259-rs2278355, ATC, P = 3.84 × 10(-8)). Our findings provide direct evidence for the association of FBXO38 and AP3B2 with severe chronic periodontitis in the Han Chinese population.
[Mh] Termos MeSH primário: Complexo 3 de Proteínas Adaptadoras/genética
Subunidades beta do Complexo de Proteínas Adaptadoras/genética
Periodontite Crônica/epidemiologia
Periodontite Crônica/genética
Estudos de Associação Genética
Predisposição Genética para Doença
Variação Genética
Proteínas de Membrana/genética
Proteínas Associadas aos Microtúbulos/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Estudos de Casos e Controles
Cromossomos Humanos Par 15
Cromossomos Humanos Par 5
Periodontite Crônica/diagnóstico
Feminino
Genótipo
Haplótipos
Seres Humanos
Desequilíbrio de Ligação
Masculino
Meia-Idade
Polimorfismo de Nucleotídeo Único
Vigilância da População
Índice de Gravidade de Doença
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (AP3B2 protein, human); 0 (Adaptor Protein Complex 3); 0 (Adaptor Protein Complex beta Subunits); 0 (Membrane Proteins); 0 (Microtubule-Associated Proteins); 0 (WHAMM protein, human)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151209
[St] Status:MEDLINE
[do] DOI:10.1038/srep17882


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[PMID]:26377319
[Au] Autor:Jarius S; Wildemann B
[Ad] Endereço:Molecular Neuroimmunology Group, Department of Neurology, University of Heidelberg, Otto Meyerhof Center, Im Neuenheimer Feld 350, D-69120, Heidelberg, Germany. sven.jarius@med.uni-heidelberg.de.
[Ti] Título:'Medusa head ataxia': the expanding spectrum of Purkinje cell antibodies in autoimmune cerebellar ataxia. Part 3: Anti-Yo/CDR2, anti-Nb/AP3B2, PCA-2, anti-Tr/DNER, other antibodies, diagnostic pitfalls, summary and outlook.
[So] Source:J Neuroinflammation;12:168, 2015 Sep 17.
[Is] ISSN:1742-2094
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Serological testing for anti-neural autoantibodies is important in patients presenting with idiopathic cerebellar ataxia, since these autoantibodies may indicate cancer, determine treatment and predict prognosis. While some of them target nuclear antigens present in all or most CNS neurons (e.g. anti-Hu, anti-Ri), others more specifically target antigens present in the cytoplasm or plasma membrane of Purkinje cells (PC). In this series of articles, we provide a detailed review of the clinical and paraclinical features, oncological, therapeutic and prognostic implications, pathogenetic relevance, and differential laboratory diagnosis of the 12 most common PC autoantibodies (often referred to as 'Medusa head antibodies' due to their characteristic somatodendritic binding pattern when tested by immunohistochemistry). To assist immunologists and neurologists in diagnosing these disorders, typical high-resolution immunohistochemical images of all 12 reactivities are presented, diagnostic pitfalls discussed and all currently available assays reviewed. Of note, most of these antibodies target antigens involved in the mGluR1/calcium pathway essential for PC function and survival. Many of the antigens also play a role in spinocerebellar ataxia. Part 1 focuses on anti-metabotropic glutamate receptor 1-, anti-Homer protein homolog 3-, anti-Sj/inositol 1,4,5-trisphosphate receptor- and anti-carbonic anhydrase-related protein VIII-associated autoimmune cerebellar ataxia (ACA); part 2 covers anti-protein kinase C gamma-, anti-glutamate receptor delta-2-, anti-Ca/RhoGTPase-activating protein 26- and anti-voltage-gated calcium channel-associated ACA; and part 3 reviews the current knowledge on anti-Tr/delta notch-like epidermal growth factor-related receptor-, anti-Nb/AP3B2-, anti-Yo/cerebellar degeneration-related protein 2- and Purkinje cell antibody 2-associated ACA, discusses differential diagnostic aspects and provides a summary and outlook.
[Mh] Termos MeSH primário: Complexo 3 de Proteínas Adaptadoras/imunologia
Subunidades beta do Complexo de Proteínas Adaptadoras/imunologia
Autoanticorpos/metabolismo
Ataxia Cerebelar
Proteínas do Tecido Nervoso/imunologia
Receptores de Superfície Celular/imunologia
[Mh] Termos MeSH secundário: Ataxia Cerebelar/diagnóstico
Ataxia Cerebelar/imunologia
Ataxia Cerebelar/metabolismo
Seres Humanos
Células de Purkinje
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (AP3B2 protein, human); 0 (Adaptor Protein Complex 3); 0 (Adaptor Protein Complex beta Subunits); 0 (Autoantibodies); 0 (CDR2 protein, human); 0 (DNER protein, human); 0 (Nerve Tissue Proteins); 0 (Purkinje cell protein L7); 0 (Receptors, Cell Surface)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150918
[St] Status:MEDLINE
[do] DOI:10.1186/s12974-015-0358-9


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[PMID]:26043821
[Au] Autor:Danelishvili L; Bermudez LE
[Ad] Endereço:Department of Biomedical Sciences, College of Veterinary Medicine, USA.
[Ti] Título:Mycobacterium avium MAV_2941 mimics phosphoinositol-3-kinase to interfere with macrophage phagosome maturation.
[So] Source:Microbes Infect;17(9):628-37, 2015 Sep.
[Is] ISSN:1769-714X
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Mycobacterium avium subsp hominissuis (M. avium) is a pathogen that infects and survives in macrophages. Previously, we have identified the M. avium MAV_2941 gene encoding a 73 amino acid protein exported by the oligopeptide transporter OppA to the macrophage cytoplasm. Mutations in MAV_2941 were associated with significant impairment of M. avium growth in THP-1 macrophages. In this study, we investigated the molecular mechanism of MAV_2941 action and demonstrated that MAV_2941 interacts with the vesicle trafficking proteins syntaxin-8 (STX8), adaptor-related protein complex 3 (AP-3) complex subunit beta-1 (AP3B1) and Archain 1 (ARCN1) in mononuclear phagocytic cells. Sequencing analysis revealed that the binding site of MAV_2941 is structurally homologous to the human phosphatidylinositol 3-kinase (PI3K) chiefly in the region recognized by vesicle trafficking proteins. The ß3A subunit of AP-3, encoded by AP3B1, is essential for trafficking cargo proteins, including lysosomal-associated membrane protein 1 (LAMP-1), to the phagosome and lysosome-related organelles. Here, we show that while the heat-killed M. avium when ingested by macrophages co-localizes with LAMP-1 protein, transfection of MAV_2941 in macrophages results in significant decrease of LAMP-1 co-localization with the heat-killed M. avium phagosomes. Mutated MAV_2941, where the amino acids homologous to the binding region of PI3K were changed, failed to interact with trafficking proteins. Inactivation of the AP3B1 gene led to alteration in the trafficking of LAMP-1. These results suggest that M. avium MAV_2941 interferes with the protein trafficking within macrophages altering the maturation of phagosome.
[Mh] Termos MeSH primário: Proteínas de Bactérias
Macrófagos
Complexo Mycobacterium avium/genética
Fagossomos
Fosfatidilinositol 3-Quinases
[Mh] Termos MeSH secundário: Complexo 3 de Proteínas Adaptadoras/metabolismo
Subunidades beta do Complexo de Proteínas Adaptadoras/metabolismo
Sequência de Aminoácidos
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Proteínas de Bactérias/farmacologia
Sítios de Ligação
Linhagem Celular
Seres Humanos
Macrófagos/metabolismo
Macrófagos/microbiologia
Modelos Moleculares
Dados de Sequência Molecular
Infecção por Mycobacterium avium-intracellulare/microbiologia
Fagossomos/efeitos dos fármacos
Fagossomos/metabolismo
Fosfatidilinositol 3-Quinases/química
Fosfatidilinositol 3-Quinases/genética
Transporte Proteico/efeitos dos fármacos
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (AP3B1 protein, human); 0 (Adaptor Protein Complex 3); 0 (Adaptor Protein Complex beta Subunits); 0 (Bacterial Proteins); EC 2.7.1.- (Phosphatidylinositol 3-Kinases)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:161020
[Lr] Data última revisão:
161020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150606
[St] Status:MEDLINE


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[PMID]:25980904
[Au] Autor:Gao L; Zhu L; Huang L; Zhou J
[Ad] Endereço:Department of Hematology, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, Hubei, People's Republic of China.
[Ti] Título:Synergistic defects of UNC13D and AP3B1 leading to adult hemophagocytic lymphohistiocytosis.
[So] Source:Int J Hematol;102(4):488-92, 2015 Oct.
[Is] ISSN:1865-3774
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:A 32-year-old man of non-consanguineous Chinese parentage, with high-grade fever, rash, joint pain, nausea, and vomiting, was diagnosed as adult-onset still's disease at his initial admission. Although prednisone had been taken, the patient presented with recurrent high-grade fever, rash, splenomegaly, hypertriglyceridemia, cryptogenic hepatitis, apparently elevated levels of serum ferritin(>20,000 µg/L), which met the proposed HLH diagnostic criteria, 2009. Sequence analysis of genomic DNA from the patient's peripheral blood demonstrated heterozygous for UNC13D mutation: c. 1232 G>A, and AP3B1 mutation: c. 1075 A>G, which were predicted to be pathogenic. Unfortunately, at the time, molecular confirmation results for HLH were obtained, and this patient had died from progressive HLH disease with multiple organ dysfunction syndrome caused by shock. FHL should be considered in the differential diagnosis of adults who present with adult-onset still's disease-like symptoms.
[Mh] Termos MeSH primário: Complexo 3 de Proteínas Adaptadoras/genética
Subunidades beta do Complexo de Proteínas Adaptadoras/genética
Linfo-Histiocitose Hemofagocítica/genética
Proteínas de Membrana/genética
Mutação
[Mh] Termos MeSH secundário: Adulto
Seres Humanos
Masculino
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (AP3B1 protein, human); 0 (Adaptor Protein Complex 3); 0 (Adaptor Protein Complex beta Subunits); 0 (Membrane Proteins); 0 (UNC13D protein, human)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150519
[St] Status:MEDLINE
[do] DOI:10.1007/s12185-015-1807-z


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[PMID]:25615951
[Au] Autor:Martín-Quirós A; Nevola L; Eckelt K; Madurga S; Gorostiza P; Giralt E
[Ad] Endereço:Institute for Bioengineering of Catalonia (IBEC), Barcelona 08028, Spain.
[Ti] Título:Absence of a stable secondary structure is not a limitation for photoswitchable inhibitors of ß-arrestin/ß-Adaptin 2 protein-protein interaction.
[So] Source:Chem Biol;22(1):31-7, 2015 Jan 22.
[Is] ISSN:1879-1301
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Many protein-protein interactions (PPIs) are mediated by short, often helical, linear peptides. Molecules mimicking these peptides have been used to inhibit their PPIs. Recently, photoswitchable peptides with little secondary structure have been developed as modulators of clathrin-mediated endocytosis. Here we perform a systematic analysis of a series of azobenzene-crosslinked peptides based on a ß-arrestin P-long 20-mer peptide (BAP-long) sequence to assess the relevance of secondary structure in their interaction with ß-adaptin 2 and to identify the design requirements for photoswitchable inhibitors of PPI (PIPPIs). We observe that flexible structures show a greater inhibitory capacity and enhanced photoswitching ability and that the absence of helical structures in free inhibitor peptide is not a limitation for PIPPI candidates. Therefore, our PIPPIs expand the field of potential inhibitors of PPIs to the wide group of flexible peptides, and we argue against using a stable secondary structure as a sole criterion when designing PIPPI candidates.
[Mh] Termos MeSH primário: Subunidades beta do Complexo de Proteínas Adaptadoras/metabolismo
Arrestinas/metabolismo
[Mh] Termos MeSH secundário: Subunidades beta do Complexo de Proteínas Adaptadoras/antagonistas & inibidores
Sequência de Aminoácidos
Arrestinas/antagonistas & inibidores
Compostos Azo/química
Dicroísmo Circular
Desenho de Drogas
Isomerismo
Cinética
Dados de Sequência Molecular
Peptídeos/química
Peptídeos/farmacologia
Domínios e Motivos de Interação entre Proteínas/efeitos dos fármacos
Estrutura Secundária de Proteína
Raios Ultravioleta
beta-Arrestinas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Protein Complex beta Subunits); 0 (Arrestins); 0 (Azo Compounds); 0 (Peptides); 0 (beta-Arrestins); F0U1H6UG5C (azobenzene)
[Em] Mês de entrada:1509
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150124
[St] Status:MEDLINE


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[PMID]:25449265
[Au] Autor:Hirata Y; Funato Y; Miki H
[Ad] Endereço:Department of Cellular Regulation, Research Institute for Microbial Diseases, Osaka University, 3-1 Yamadaoka, Suita, Osaka 565-0871, Japan; Laboratory of Health Chemistry, Graduate School of Pharmaceutical Sciences, Tohoku University, 6-3 Aoba, Aramaki, Aoba-ku, Sendai, Miyagi 980-8578, Japan.
[Ti] Título:Basolateral sorting of the Mg²âº transporter CNNM4 requires interaction with AP-1A and AP-1B.
[So] Source:Biochem Biophys Res Commun;455(3-4):184-9, 2014 Dec 12.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ancient conserved domain protein/cyclin M (CNNM) 4 is an evolutionarily conserved Mg(2+) transporter that localizes at the basolateral membrane of the intestinal epithelia. Here, we show the complementary importance of clathrin adaptor protein (AP) complexes AP-1A and AP-1B in basolateral sorting of CNNM4. We first confirmed the basolateral localization of both endogenous and ectopically expressed CNNM4 in Madin-Darby Canine Kidney cells, which form highly polarized epithelia in culture. Single knockdown of µ1B, a cargo-recognition subunit of AP-1B, did not affect basolateral localization, but simultaneous knockdown of the µ1A subunit of AP-1A abrogated localization. Mutational analyses showed the importance of three conserved dileucine motifs in CNNM4 for both basolateral sorting and interaction with µ1A and µ1B. These results imply that CNNM4 is sorted to the basolateral membrane by the complementary function of AP-1A and AP-1B.
[Mh] Termos MeSH primário: Complexo 1 de Proteínas Adaptadoras/fisiologia
Subunidades beta do Complexo de Proteínas Adaptadoras/fisiologia
Subunidades mu do Complexo de Proteínas Adaptadoras/fisiologia
Proteínas de Transporte de Cátions/metabolismo
Regulação da Expressão Gênica
Magnésio/química
[Mh] Termos MeSH secundário: Complexo 1 de Proteínas Adaptadoras/química
Subunidades beta do Complexo de Proteínas Adaptadoras/química
Subunidades mu do Complexo de Proteínas Adaptadoras/química
Motivos de Aminoácidos
Sequência de Aminoácidos
Animais
Biotinilação
Células COS
Linhagem Celular
Membrana Celular/metabolismo
Cercopithecus aethiops
DNA Complementar/metabolismo
Cães
Seres Humanos
Proteínas de Membrana Transportadoras/metabolismo
Microscopia de Fluorescência
Dados de Sequência Molecular
Mutação
Transporte Proteico
Interferência de RNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (AP1B1 protein, human); 0 (Adaptor Protein Complex 1); 0 (Adaptor Protein Complex beta Subunits); 0 (Adaptor Protein Complex mu Subunits); 0 (CNNM4 protein, human); 0 (Cation Transport Proteins); 0 (DNA, Complementary); 0 (Membrane Transport Proteins); I38ZP9992A (Magnesium)
[Em] Mês de entrada:1502
[Cu] Atualização por classe:141206
[Lr] Data última revisão:
141206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141203
[St] Status:MEDLINE


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[PMID]:25410111
[Au] Autor:Evstratova A; Chamberland S; Faundez V; Tóth K
[Ad] Endereço:Department of Psychiatry and Neuroscience, Quebec Mental Health Institute, Université Laval, Quebec City, Quebec, Canada G1J 2G3.
[Ti] Título:Vesicles derived via AP-3-dependent recycling contribute to asynchronous release and influence information transfer.
[So] Source:Nat Commun;5:5530, 2014 Nov 20.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Action potentials trigger synchronous and asynchronous neurotransmitter release. Temporal properties of both types of release could be altered in an activity-dependent manner. While the effects of activity-dependent changes in synchronous release on postsynaptic signal integration have been studied, the contribution of asynchronous release to information transfer during natural stimulus patterns is unknown. Here we find that during trains of stimulations, asynchronous release contributes to the precision of action potential firing. Our data show that this form of release is selectively diminished in AP-3b2 KO animals, which lack functional neuronal AP-3, an adaptor protein regulating vesicle formation from endosomes generated during bulk endocytosis. We find that in the absence of neuronal AP-3, asynchronous release is attenuated and the activity-dependent increase in the precision of action potential timing is compromised. Lack of asynchronous release decreases the capacity of synaptic information transfer and renders synaptic communication less reliable in response to natural stimulus patterns.
[Mh] Termos MeSH primário: Potenciais de Ação
Complexo 3 de Proteínas Adaptadoras/genética
Subunidades beta do Complexo de Proteínas Adaptadoras/genética
Transmissão Sináptica
Vesículas Sinápticas/metabolismo
[Mh] Termos MeSH secundário: Complexo 3 de Proteínas Adaptadoras/metabolismo
Subunidades beta do Complexo de Proteínas Adaptadoras/metabolismo
Animais
Endocitose
Endossomos/metabolismo
Camundongos
Camundongos Knockout
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (AP-3b2 adaptor protein, mouse); 0 (Adaptor Protein Complex 3); 0 (Adaptor Protein Complex beta Subunits)
[Em] Mês de entrada:1511
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141121
[St] Status:MEDLINE
[do] DOI:10.1038/ncomms6530



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