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Pesquisa : G05.360.340.024.340.137 [Categoria DeCS]
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[PMID]:28636075
[Au] Autor:Fodor J; Köblös G; Kákai Á; Kárpáti Z; Molnár BP; Dankó T; Bozsik G; Bognár C; Szocs G; Fónagy A
[Ad] Endereço:Plant Protection Institute, Centre for Agricultural Research, Hungarian Academy of Sciences, Budapest, Hungary.
[Ti] Título:Molecular cloning, mRNA expression and biological activity of the pheromone biosynthesis activating neuropeptide (PBAN) from the European corn borer, Ostrinia nubilalis.
[So] Source:Insect Mol Biol;26(5):616-632, 2017 Oct.
[Is] ISSN:1365-2583
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Pheromone biosynthesis activating neuropeptide (PBAN) is a member of the pyrokinin (FXPRLamide) insect neuropeptides. Here, we report the cloning of the gene Ostnu-PBAN from the E and Z pheromone strains of the European corn borer (ECB), Ostrinia nubilalis (Lepidoptera: Crambidae), a major pest of maize. The Ostnu-PBAN genomic sequence is > 5 kb in length and consists of six exons. The deduced amino acid sequence revealed a 200-residue precursor protein including a signal peptide, a 24-amino acid (aa) diapause hormone, a 37-aa PBAN and three other FXPRLamide neuropeptides. Our in vivo assays suggest that the 37-aa synthetic Ostnu-PBAN is hormonally active in the pheromone gland. It restores sex pheromone production to normal levels in mated females and decapitated virgins of both E and Z cultures. The results of a real-time PCR analysis indicated that Ostnu-PBAN mRNA levels reached a plateau in the brain-suboesophageal ganglion complexes 1 day after eclosion, and mating did not affect the mRNA expression. Three size classes of Ostnu-PBAN mRNA (1.9, 2.0 and 2.1 kb) were obtained, differing only in the length of the 3' untranslated region. However, there was no correlation between sequence divergence and the pheromone composition, voltinism or geographical origin (Hungary, Slovenia, Sweden, Turkey) of ECB moths.
[Mh] Termos MeSH primário: Mariposas/genética
Neuropeptídeos/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sequência de Bases
Feminino
Componentes do Gene
Masculino
Dados de Sequência Molecular
Mariposas/química
Mariposas/crescimento & desenvolvimento
Mariposas/metabolismo
Neuropeptídeos/química
Neuropeptídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Neuropeptides); 0 (pheromone biosynthesis activating neuropeptide, Helicoverpa zea)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170622
[St] Status:MEDLINE
[do] DOI:10.1111/imb.12324


  2 / 963 MEDLINE  
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[PMID]:28234413
[Au] Autor:Chahad-Ehlers S; Arthur LP; Lima ALA; Gesto JSM; Torres FR; Peixoto AA; de Brito RA
[Ad] Endereço:Departamento de Genética e Evolução, Universidade Federal de São Carlos, São Carlos, Brazil.
[Ti] Título:Expanding the view of Clock and cycle gene evolution in Diptera.
[So] Source:Insect Mol Biol;26(3):317-331, 2017 Jun.
[Is] ISSN:1365-2583
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We expanded the view of Clock (Clk) and cycle (cyc) gene evolution in Diptera by studying the fruit fly Anastrepha fraterculus (Afra), a Brachycera. Despite the high conservation of clock genes amongst insect groups, striking structural and functional differences of some clocks have appeared throughout evolution. Clk and cyc nucleotide sequences and corresponding proteins were characterized, along with their mRNA expression data, to provide an evolutionary overview in the two major groups of Diptera: Lower Diptera and Higher Brachycera. We found that AfraCYC lacks the BMAL (Brain and muscle ARNT-like) C-terminus region (BCTR) domain and is constitutively expressed, suggesting that AfraCLK has the main transactivation function, which is corroborated by the presence of poly-Q repeats and an oscillatory pattern. Our analysis suggests that the loss of BCTR in CYC is not exclusive of drosophilids, as it also occurs in other Acalyptratae flies such as tephritids and drosophilids, however, but it is also present in some Calyptratae, such as Muscidae, Calliphoridae and Sarcophagidae. This indicates that BCTR is missing from CYC of all higher-level Brachycera and that it was lost during the evolution of Lower Brachycera. Thus, we can infer that CLK protein may play the main role in the CLK\CYC transcription complex in these flies, like in its Drosophila orthologues.
[Mh] Termos MeSH primário: Fatores de Transcrição ARNTL/genética
Proteínas CLOCK/genética
Proteínas de Drosophila/genética
Drosophila/genética
Evolução Molecular
Tephritidae/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Feminino
Componentes do Gene
Masculino
Dados de Sequência Molecular
Tephritidae/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ARNTL Transcription Factors); 0 (CYCLE protein, Drosophila); 0 (Clk protein, Drosophila); 0 (Drosophila Proteins); EC 2.3.1.48 (CLOCK Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170828
[Lr] Data última revisão:
170828
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170225
[St] Status:MEDLINE
[do] DOI:10.1111/imb.12296


  3 / 963 MEDLINE  
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[PMID]:27830839
[Au] Autor:Dutkiewicz M; Stachowiak A; Swiatkowska A; Ciesiolka J
[Ad] Endereço:Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland.
[Ti] Título:Structure and function of RNA elements present in enteroviral genomes.
[So] Source:Acta Biochim Pol;63(4):623-630, 2016.
[Is] ISSN:1734-154X
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:Enteroviruses are small RNA(+) viruses that encode one open reading frame flanked by two extensive noncoding regions carrying structural RNA regulatory elements that control replication and translation processes. For a long time the central, coding region was thought to remain single-stranded and its only function was supposed to be as the template for polyprotein synthesis. It turned out, however, that the protein coding region also encodes important RNA structures crucial for the viral life cycle and virus persistence in the host cells. This review considers the RNA structures in enteroviral genomes identified and characterized to date.
[Mh] Termos MeSH primário: Enterovirus/genética
RNA Viral/genética
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Sequência de Bases
Componentes do Gene
Genoma Viral
Seres Humanos
Sequências Repetidas Invertidas
Biossíntese de Proteínas
Proteínas Virais/genética
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (RNA, Viral); 0 (Viral Proteins)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170119
[Lr] Data última revisão:
170119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161111
[St] Status:MEDLINE


  4 / 963 MEDLINE  
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[PMID]:27292444
[Au] Autor:Agarwal AM; Nussenzveig RH; Reading NS; Patel JL; Sangle N; Salama ME; Prchal JT; Perkins SL; Yaish HM; Christensen RD
[Ad] Endereço:Department of Pathology, University of Utah and ARUP Laboratories, Salt Lake City, UT, USA.
[Ti] Título:Clinical utility of next-generation sequencing in the diagnosis of hereditary haemolytic anaemias.
[So] Source:Br J Haematol;174(5):806-14, 2016 Sep.
[Is] ISSN:1365-2141
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Hereditary haemolytic anaemias are genetically and phenotypically heterogeneous disorders characterized by increased red cell destruction, with consequences ranging from innocuous to severe life-threatening anaemia. Diagnostic laboratories endeavour to assist clinicians reach the exact patient diagnosis by using tests principally based on morphological and biochemical techniques. However, these routine studies may be inconclusive, particularly in newborn infants and when transfusions have recently been administered. Large numbers and size of the potentially involved genes also impose a practical challenge for molecular diagnosis using routine sequencing approaches. To overcome these diagnostic shortcomings, we have utilized next-generation sequencing to provide a high-throughput, highly sensitive assay. We developed a panel interrogating 28 genes encoding cytoskeletal proteins and enzymes with sequencing coverage of the coding regions, splice site junctions, deep intronic and regulatory regions. We then evaluated 19 samples, including infants with unexplained extreme hyperbilirubinaemia and patients with transfusion-dependent haemolytic anaemia. Where possible, inheritance patterns of pathogenic mutations were determined by sequencing of immediate relatives. We conclude that this next-generation sequencing panel could be a cost-effective approach to molecular diagnosis of hereditary haemolytic anaemia, especially when the family history is uninformative or when routine laboratory testing fails to identify the causative haemolytic process.
[Mh] Termos MeSH primário: Anemia Hemolítica Congênita/diagnóstico
Sequenciamento de Nucleotídeos em Larga Escala/métodos
[Mh] Termos MeSH secundário: Adolescente
Adulto
Anemia Hemolítica Congênita/genética
Criança
Pré-Escolar
Proteínas do Citoesqueleto/genética
Enzimas/genética
Componentes do Gene/genética
Sequenciamento de Nucleotídeos em Larga Escala/economia
Seres Humanos
Hiperbilirrubinemia Hereditária/diagnóstico
Lactente
Recém-Nascido
Técnicas de Diagnóstico Molecular/economia
Técnicas de Diagnóstico Molecular/métodos
Mutação
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytoskeletal Proteins); 0 (Enzymes)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170606
[Lr] Data última revisão:
170606
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160614
[St] Status:MEDLINE
[do] DOI:10.1111/bjh.14131


  5 / 963 MEDLINE  
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[PMID]:26936952
[Au] Autor:Beran F; Rahfeld P; Luck K; Nagel R; Vogel H; Wielsch N; Irmisch S; Ramasamy S; Gershenzon J; Heckel DG; Köllner TG
[Ad] Endereço:Research Group Sequestration and Detoxification in Insects, Max Planck Institute for Chemical Ecology, 07745 Jena, Germany; fberan@ice.mpg.de.
[Ti] Título:Novel family of terpene synthases evolved from trans-isoprenyl diphosphate synthases in a flea beetle.
[So] Source:Proc Natl Acad Sci U S A;113(11):2922-7, 2016 Mar 15.
[Is] ISSN:1091-6490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sesquiterpenes play important roles in insect communication, for example as pheromones. However, no sesquiterpene synthases, the enzymes involved in construction of the basic carbon skeleton, have been identified in insects to date. We investigated the biosynthesis of the sesquiterpene (6R,7S)-himachala-9,11-diene in the crucifer flea beetle Phyllotreta striolata, a compound previously identified as a male-produced aggregation pheromone in several Phyllotreta species. A (6R,7S)-himachala-9,11-diene-producing sesquiterpene synthase activity was detected in crude beetle protein extracts, but only when (Z,E)-farnesyl diphosphate [(Z,E)-FPP] was offered as a substrate. No sequences resembling sesquiterpene synthases from plants, fungi, or bacteria were found in the P. striolata transcriptome, but we identified nine divergent putative trans-isoprenyl diphosphate synthase (trans-IDS) transcripts. Four of these putative trans-IDSs exhibited terpene synthase (TPS) activity when heterologously expressed. Recombinant PsTPS1 converted (Z,E)-FPP to (6R,7S)-himachala-9,11-diene and other sesquiterpenes observed in beetle extracts. RNAi-mediated knockdown of PsTPS1 mRNA in P. striolata males led to reduced emission of aggregation pheromone, confirming a significant role of PsTPS1 in pheromone biosynthesis. Two expressed enzymes showed genuine IDS activity, with PsIDS1 synthesizing (E,E)-FPP, whereas PsIDS3 produced neryl diphosphate, (Z,Z)-FPP, and (Z,E)-FPP. In a phylogenetic analysis, the PsTPS enzymes and PsIDS3 were clearly separated from a clade of known coleopteran trans-IDS enzymes including PsIDS1 and PsIDS2. However, the exon-intron structures of IDS and TPS genes in P. striolata are conserved, suggesting that this TPS gene family evolved from trans-IDS ancestors.
[Mh] Termos MeSH primário: Alquil e Aril Transferases/classificação
Coleópteros/enzimologia
Genes de Insetos
Proteínas de Insetos/classificação
Família Multigênica
Feromônios/biossíntese
Sesquiterpenos/metabolismo
[Mh] Termos MeSH secundário: Alquil e Aril Transferases/genética
Alquil e Aril Transferases/isolamento & purificação
Sequência de Aminoácidos
Animais
Clonagem Molecular
Coleópteros/classificação
Coleópteros/genética
Evolução Molecular
Feminino
Componentes do Gene
Especiação Genética
Proteínas de Insetos/genética
Proteínas de Insetos/isolamento & purificação
Masculino
Dados de Sequência Molecular
Fases de Leitura Aberta/genética
Filogenia
Proteínas Recombinantes de Fusão/metabolismo
Homologia de Sequência de Aminoácidos
Transcriptoma
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 ((6R,7S)-himachala-9,11-diene); 0 (Insect Proteins); 0 (Pheromones); 0 (Recombinant Fusion Proteins); 0 (Sesquiterpenes); EC 2.5.- (Alkyl and Aryl Transferases); EC 2.5.1.- (terpene synthase)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160304
[St] Status:MEDLINE
[do] DOI:10.1073/pnas.1523468113


  6 / 963 MEDLINE  
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[PMID]:26523948
[Au] Autor:Burle-Caldas Gde A; Grazielle-Silva V; Laibida LA; DaRocha WD; Teixeira SM
[Ad] Endereço:Departamento de Bioquímica e Imunologia, Universidade Federal de Minas Gerais, Belo Horizonte, MG, Brazil.
[Ti] Título:Expanding the tool box for genetic manipulation of Trypanosoma cruzi.
[So] Source:Mol Biochem Parasitol;203(1-2):25-33, 2015 Sep-Oct.
[Is] ISSN:1872-9428
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Trypanosoma cruzi is a protozoan parasite that causes Chagas disease, an illness that affects 6-7 million people and for which there is no effective drug therapy or vaccine. The publication of its complete genome sequence allowed a rapid advance in molecular studies including in silico screening of genes involved with pathogenicity as well as molecular targets for the development of new diagnostic methods, drug therapies and prophylactic vaccines. Alongside with in silico genomic analyses, methods to study gene function in this parasite such as gene deletion, overexpression, mutant complementation and reporter gene expression have been largely explored. More recently, the use of genome-wide strategies is producing a shift towards a global perspective on gene function studies, with the examination of the expression and biological roles of gene networks in different stages of the parasite life cycle and under different contexts of host parasite interactions. Here we describe the molecular tools and protocols currently available to perform genetic manipulation of the T. cruzi genome, with emphasis on recently described strategies of gene editing that will facilitate large-scale functional genomic analyses. These new methodologies are long overdue, since more efficient protocols for genetic manipulation in T. cruzi are urgently needed for a better understanding of the biology of this parasite and molecular processes involved with the complex and often harmful, interaction with its human host.
[Mh] Termos MeSH primário: Doença de Chagas/parasitologia
Regulação da Expressão Gênica
Técnicas de Silenciamento de Genes/métodos
Marcação de Genes/métodos
Genoma de Protozoário/genética
Trypanosoma cruzi/genética
[Mh] Termos MeSH secundário: Componentes do Gene
Redes Reguladoras de Genes
Genes Reporter
Interações Hospedeiro-Parasita/genética
Interações Hospedeiro-Parasita/fisiologia
Seres Humanos
Estágios do Ciclo de Vida
RNA Líder para Processamento/genética
Trypanosoma cruzi/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (RNA, Spliced Leader)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:151215
[Lr] Data última revisão:
151215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151103
[St] Status:MEDLINE


  7 / 963 MEDLINE  
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[PMID]:26504242
[Au] Autor:Gupta RK; Luong TT; Lee CY
[Ad] Endereço:Department of Microbiology and Immunology, University of Arkansas for Medical Sciences, Little Rock, AR 72205.
[Ti] Título:RNAIII of the Staphylococcus aureus agr system activates global regulator MgrA by stabilizing mRNA.
[So] Source:Proc Natl Acad Sci U S A;112(45):14036-41, 2015 Nov 10.
[Is] ISSN:1091-6490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:RNAIII, the effector of the agr quorum-sensing system, plays a key role in virulence gene regulation in Staphylococcus aureus, but how RNAIII transcriptionally regulates its downstream genes is not completely understood. Here, we show that RNAIII stabilizes mgrA mRNA, thereby increasing the production of MgrA, a global transcriptional regulator that affects the expression of many genes. The mgrA gene is transcribed from two promoters, P1 and P2, to produce two mRNA transcripts with long 5' UTR. Two adjacent regions of the mgrA mRNA UTR transcribed from the upstream P2 promoter, but not the P1 promoter, form a stable complex with two regions of RNAIII near the 5' and 3' ends. We further demonstrate that the interaction has several biological effects. We propose that MgrA can serve as an intermediary regulator through which agr exerts its regulatory function.
[Mh] Termos MeSH primário: Regulação Bacteriana da Expressão Gênica/genética
Percepção de Quorum/genética
RNA Bacteriano/metabolismo
Elementos Reguladores de Transcrição/genética
Staphylococcus aureus/enzimologia
[Mh] Termos MeSH secundário: Pareamento de Bases
Sequência de Bases
Western Blotting
Ensaio de Desvio de Mobilidade Eletroforética
Componentes do Gene
Dados de Sequência Molecular
Regiões Promotoras Genéticas/genética
Reação em Cadeia da Polimerase em Tempo Real
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (RNA, Bacterial); 0 (RNAIII, Staphylococcus aureus)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151028
[St] Status:MEDLINE
[do] DOI:10.1073/pnas.1509251112


  8 / 963 MEDLINE  
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[PMID]:26152174
[Au] Autor:Casane D; Fumey J; Laurenti P
[Ad] Endereço:Laboratoire Évolution, génomes, comportement, écologie, CNRS université Paris-Sud UMR 9191, IRD UMR 247, Avenue de la Terrasse, bâtiment 13, boîte postale 1, 91198 Gif-sur-Yvette, France - Université Paris-Diderot, Sorbonne Paris-Cité, Paris, France.
[Ti] Título:[ENCODE apophenia or a panglossian analysis of the human genome].
[Ti] Título:L'apophénie d'ENCODE ou Pangloss examine le génome humain..
[So] Source:Med Sci (Paris);31(6-7):680-6, 2015 Jun-Jul.
[Is] ISSN:0767-0974
[Cp] País de publicação:France
[La] Idioma:fre
[Ab] Resumo:In September 2012, a batch of more than 30 articles presenting the results of the ENCODE (Encyclopaedia of DNA Elements) project was released. Many of these articles appeared in Nature and Science, the two most prestigious interdisciplinary scientific journals. Since that time, hundreds of other articles dedicated to the further analyses of the Encode data have been published. The time of hundreds of scientists and hundreds of millions of dollars were not invested in vain since this project had led to an apparent paradigm shift: contrary to the classical view, 80% of the human genome is not junk DNA, but is functional. This hypothesis has been criticized by evolutionary biologists, sometimes eagerly, and detailed refutations have been published in specialized journals with impact factors far below those that published the main contribution of the Encode project to our understanding of genome architecture. In 2014, the Encode consortium released a new batch of articles that neither suggested that 80% of the genome is functional nor commented on the disappearance of their 2012 scientific breakthrough. Unfortunately, by that time many biologists had accepted the idea that 80% of the genome is functional, or at least, that this idea is a valid alternative to the long held evolutionary genetic view that it is not. In order to understand the dynamics of the genome, it is necessary to re-examine the basics of evolutionary genetics because, not only are they well established, they also will allow us to avoid the pitfall of a panglossian interpretation of Encode. Actually, the architecture of the genome and its dynamics are the product of trade-offs between various evolutionary forces, and many structural features are not related to functional properties. In other words, evolution does not produce the best of all worlds, not even the best of all possible worlds, but only one possible world.
[Mh] Termos MeSH primário: DNA/genética
Enciclopédias como Assunto
Componentes do Gene
Genoma Humano
Editoração
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Filogenia
Editoração/ética
Editoração/normas
Má Conduta Científica
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE
[Nm] Nome de substância:
9007-49-2 (DNA)
[Em] Mês de entrada:1509
[Cu] Atualização por classe:150708
[Lr] Data última revisão:
150708
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150709
[St] Status:MEDLINE
[do] DOI:10.1051/medsci/20153106023


  9 / 963 MEDLINE  
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[PMID]:26046368
[Au] Autor:Hira A; Yoshida K; Sato K; Okuno Y; Shiraishi Y; Chiba K; Tanaka H; Miyano S; Shimamoto A; Tahara H; Ito E; Kojima S; Kurumizaka H; Ogawa S; Takata M; Yabe H; Yabe M
[Ad] Endereço:Laboratory of DNA Damage Signaling, Department of Late Effects Studies, Radiation Biology Center, Kyoto University, Kyoto 606-8501, Japan.
[Ti] Título:Mutations in the gene encoding the E2 conjugating enzyme UBE2T cause Fanconi anemia.
[So] Source:Am J Hum Genet;96(6):1001-7, 2015 Jun 04.
[Is] ISSN:1537-6605
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Fanconi anemia (FA) is a rare genetic disorder characterized by genome instability, increased cancer susceptibility, progressive bone marrow failure (BMF), and various developmental abnormalities resulting from the defective FA pathway. FA is caused by mutations in genes that mediate repair processes of interstrand crosslinks and/or DNA adducts generated by endogenous aldehydes. The UBE2T E2 ubiquitin conjugating enzyme acts in FANCD2/FANCI monoubiquitination, a critical event in the pathway. Here we identified two unrelated FA-affected individuals, each harboring biallelic mutations in UBE2T. They both produced a defective UBE2T protein with the same missense alteration (p.Gln2Glu) that abolished FANCD2 monoubiquitination and interaction with FANCL. We suggest this FA complementation group be named FA-T.
[Mh] Termos MeSH primário: Anemia de Fanconi/genética
Anemia de Fanconi/patologia
Modelos Moleculares
Mutação de Sentido Incorreto/genética
Enzimas de Conjugação de Ubiquitina/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sequência de Bases
Criança
Pré-Escolar
Proteína do Grupo de Complementação L da Anemia de Fanconi/metabolismo
Feminino
Componentes do Gene
Genótipo
Seres Humanos
Japão
Masculino
Dados de Sequência Molecular
Linhagem
Conformação Proteica
Alinhamento de Sequência
Análise de Sequência de DNA
Enzimas de Conjugação de Ubiquitina/química
Enzimas de Conjugação de Ubiquitina/metabolismo
Ubiquitinação/genética
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 2.3.2.23 (UBE2T protein, human); EC 2.3.2.23 (Ubiquitin-Conjugating Enzymes); EC 2.3.2.27 (FANCL protein, human); EC 2.3.2.27 (Fanconi Anemia Complementation Group L Protein)
[Em] Mês de entrada:1508
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150606
[St] Status:MEDLINE


  10 / 963 MEDLINE  
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[PMID]:26046367
[Au] Autor:Dazzo E; Fanciulli M; Serioli E; Minervini G; Pulitano P; Binelli S; Di Bonaventura C; Luisi C; Pasini E; Striano S; Striano P; Coppola G; Chiavegato A; Radovic S; Spadotto A; Uzzau S; La Neve A; Giallonardo AT; Mecarelli O; Tosatto SC; Ottman R; Michelucci R; Nobile C
[Ad] Endereço:Section of Padua, Institute of Neuroscience, Consiglio Nazionale delle Ricerche, 35121 Padova, Italy.
[Ti] Título:Heterozygous reelin mutations cause autosomal-dominant lateral temporal epilepsy.
[So] Source:Am J Hum Genet;96(6):992-1000, 2015 Jun 04.
[Is] ISSN:1537-6605
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Autosomal-dominant lateral temporal epilepsy (ADLTE) is a genetic epilepsy syndrome clinically characterized by focal seizures with prominent auditory symptoms. ADLTE is genetically heterogeneous, and mutations in LGI1 account for fewer than 50% of affected families. Here, we report the identification of causal mutations in reelin (RELN) in seven ADLTE-affected families without LGI1 mutations. We initially investigated 13 ADLTE-affected families by performing SNP-array linkage analysis and whole-exome sequencing and identified three heterozygous missense mutations co-segregating with the syndrome. Subsequent analysis of 15 small ADLTE-affected families revealed four additional missense mutations. 3D modeling predicted that all mutations have structural effects on protein-domain folding. Overall, RELN mutations occurred in 7/40 (17.5%) ADLTE-affected families. RELN encodes a secreted protein, Reelin, which has important functions in both the developing and adult brain and is also found in the blood serum. We show that ADLTE-related mutations significantly decrease serum levels of Reelin, suggesting an inhibitory effect of mutations on protein secretion. We also show that Reelin and LGI1 co-localize in a subset of rat brain neurons, supporting an involvement of both proteins in a common molecular pathway underlying ADLTE. Homozygous RELN mutations are known to cause lissencephaly with cerebellar hypoplasia. Our findings extend the spectrum of neurological disorders associated with RELN mutations and establish a link between RELN and LGI1, which play key regulatory roles in both the developing and adult brain.
[Mh] Termos MeSH primário: Moléculas de Adesão Celular Neuronais/genética
Epilepsia do Lobo Frontal/genética
Epilepsia do Lobo Frontal/patologia
Proteínas da Matriz Extracelular/genética
Modelos Moleculares
Mutação de Sentido Incorreto/genética
Proteínas do Tecido Nervoso/genética
Serina Endopeptidases/genética
Transtornos do Sono-Vigília/genética
Transtornos do Sono-Vigília/patologia
[Mh] Termos MeSH secundário: Animais
Sequência de Bases
Moléculas de Adesão Celular Neuronais/sangue
Moléculas de Adesão Celular Neuronais/química
Moléculas de Adesão Celular Neuronais/metabolismo
Mapeamento Cromossômico
Exoma
Proteínas da Matriz Extracelular/sangue
Proteínas da Matriz Extracelular/química
Proteínas da Matriz Extracelular/metabolismo
Imunofluorescência
Componentes do Gene
Seres Humanos
Immunoblotting
Dados de Sequência Molecular
Proteínas do Tecido Nervoso/sangue
Proteínas do Tecido Nervoso/química
Proteínas do Tecido Nervoso/metabolismo
Linhagem
Polimorfismo de Nucleotídeo Único/genética
Conformação Proteica
Dobramento de Proteína
Proteínas/metabolismo
Ratos
Análise de Sequência de DNA
Serina Endopeptidases/sangue
Serina Endopeptidases/química
Serina Endopeptidases/metabolismo
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cell Adhesion Molecules, Neuronal); 0 (Extracellular Matrix Proteins); 0 (Lgi1 protein, rat); 0 (Nerve Tissue Proteins); 0 (Proteins); EC 3.4.21.- (Serine Endopeptidases); EC 3.4.21.- (reelin protein)
[Em] Mês de entrada:1508
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150606
[St] Status:MEDLINE



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