Base de dados : MEDLINE
Pesquisa : D12.776.835 [Categoria DeCS]
Referências encontradas : 11824 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 1183 ir para página                         

  1 / 11824 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28454764
[Au] Autor:Lupas AN; Alva V
[Ad] Endereço:Department of Protein Evolution, Max Planck Institute for Developmental Biology, 72076 Tübingen, Germany. Electronic address: andrei.lupas@tuebingen.mpg.de.
[Ti] Título:Ribosomal proteins as documents of the transition from unstructured (poly)peptides to folded proteins.
[So] Source:J Struct Biol;198(2):74-81, 2017 May.
[Is] ISSN:1095-8657
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:For the most part, contemporary proteins can be traced back to a basic set of a few thousand domain prototypes, many of which were already established in the Last Universal Common Ancestor of life on Earth, around 3.5 billion years ago. The origin of these domain prototypes, however, remains poorly understood. One hypothesis posits that they arose from an ancestral set of peptides, which acted as cofactors of RNA-mediated catalysis and replication. Initially, these peptides were entirely dependent on the RNA scaffold for their structure, but as their complexity increased, they became able to form structures by excluding water through hydrophobic contacts, making them independent of the RNA scaffold. Their ability to fold was thus an emergent property of peptide-RNA coevolution. The ribosome is the main survivor of this primordial RNA world and offers an excellent model system for retracing the steps that led to the folded proteins of today, due to its very slow rate of change. Close to the peptidyl transferase center, which is the oldest part of the ribosome, proteins are extended and largely devoid of secondary structure; further from the center, their secondary structure content increases and supersecondary topologies become common, although the proteins still largely lack a hydrophobic core; at the ribosomal periphery, supersecondary structures coalesce around hydrophobic cores, forming folds that resemble those seen in proteins of the cytosol. Collectively, ribosomal proteins thus offer a window onto the time when proteins were acquiring the ability to fold.
[Mh] Termos MeSH primário: Evolução Molecular
Origem da Vida
Dobramento de Proteína
Proteínas Ribossômicas/química
[Mh] Termos MeSH secundário: Peptídeos/química
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Peptides); 0 (Ribosomal Proteins)
[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:170430
[St] Status:MEDLINE


  2 / 11824 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29198719
[Au] Autor:Shaffer JR; Li J; Lee MK; Roosenboom J; Orlova E; Adhikari K; Gallo C; Poletti G; Schuler-Faccini L; Bortolini MC; Canizales-Quinteros S; Rothhammer F; Bedoya G; González-José R; Pfeffer PE; Wollenschlaeger CA; Hecht JT; Wehby GL; Moreno LM; Ding A; Jin L; Yang Y; Carlson JC; Leslie EJ; Feingold E; Marazita ML; Hinds DA; Cox TC; Wang S; Ruiz-Linares A; Weinberg SM; 23andMe Research Team
[Ad] Endereço:Department of Human Genetics, Graduate School of Public Health, University of Pittsburgh, Pittsburgh, PA 15261, USA.
[Ti] Título:Multiethnic GWAS Reveals Polygenic Architecture of Earlobe Attachment.
[So] Source:Am J Hum Genet;101(6):913-924, 2017 Dec 07.
[Is] ISSN:1537-6605
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The genetic basis of earlobe attachment has been a matter of debate since the early 20 century, such that geneticists argue both for and against polygenic inheritance. Recent genetic studies have identified a few loci associated with the trait, but large-scale analyses are still lacking. Here, we performed a genome-wide association study of lobe attachment in a multiethnic sample of 74,660 individuals from four cohorts (three with the trait scored by an expert rater and one with the trait self-reported). Meta-analysis of the three expert-rater-scored cohorts revealed six associated loci harboring numerous candidate genes, including EDAR, SP5, MRPS22, ADGRG6 (GPR126), KIAA1217, and PAX9. The large self-reported 23andMe cohort recapitulated each of these six loci. Moreover, meta-analysis across all four cohorts revealed a total of 49 significant (p < 5 × 10 ) loci. Annotation and enrichment analyses of these 49 loci showed strong evidence of genes involved in ear development and syndromes with auricular phenotypes. RNA sequencing data from both human fetal ear and mouse second branchial arch tissue confirmed that genes located among associated loci showed evidence of expression. These results provide strong evidence for the polygenic nature of earlobe attachment and offer insights into the biological basis of normal and abnormal ear development.
[Mh] Termos MeSH primário: Orelha/anatomia & histologia
Herança Multifatorial/genética
Locos de Características Quantitativas/genética
[Mh] Termos MeSH secundário: Adolescente
Adulto
Animais
Região Branquial/anatomia & histologia
Criança
Pré-Escolar
Proteínas de Ligação a DNA/genética
Receptor Edar/genética
Estudo de Associação Genômica Ampla
Genótipo
Seres Humanos
Camundongos
Meia-Idade
Proteínas Mitocondriais/genética
Fator de Transcrição PAX9/genética
Proteínas/genética
Receptores Acoplados a Proteínas-G/genética
Proteínas Ribossômicas/genética
Fatores de Transcrição/genética
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (EDAR protein, human); 0 (Edar Receptor); 0 (GPR126 protein, human); 0 (MRPS22 protein, human); 0 (Mitochondrial Proteins); 0 (PAX9 Transcription Factor); 0 (PAX9 protein, human); 0 (Proteins); 0 (Receptors, G-Protein-Coupled); 0 (Ribosomal Proteins); 0 (SKT protein, human); 0 (SP5 protein, human); 0 (Transcription Factors)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE


  3 / 11824 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29225165
[Au] Autor:Chakraborty A; Uechi T; Nakajima Y; Gazda HT; O'Donohue MF; Gleizes PE; Kenmochi N
[Ad] Endereço:Division of Molecular Genetics and Cancer, NU Centre for Science Education & Research, Nitte University, Mangalore 18, India. Electronic address: anirban@nitte.edu.in.
[Ti] Título:Cross talk between TP53 and c-Myc in the pathophysiology of Diamond-Blackfan anemia: Evidence from RPL11-deficient in vivo and in vitro models.
[So] Source:Biochem Biophys Res Commun;495(2):1839-1845, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mutations in genes encoding ribosomal proteins have been identified in Diamond-Blackfan anemia (DBA), a rare genetic disorder that presents with a prominent erythroid phenotype. TP53 has been implicated in the pathophysiology of DBA with ribosomal protein (RP) L11 playing a crucial role in the TP53 response. Interestingly, RPL11 also controls the transcriptional activity of c-Myc, an oncoprotein that positively regulates ribosome biogenesis. In the present study, we analyzed the consequences of rpl11 depletion on erythropoiesis and ribosome biogenesis in zebrafish. As expected, Rpl11-deficient zebrafish exhibited defects in ribosome biogenesis and an anemia phenotype. However, co-inhibition of Tp53 did not alleviate the erythroid aplasia in these fish. Next, we explored the role of c-Myc in RPL11-deficient cellular and animal models. c-Myc and its target nucleolar proteins showed upregulation and increased localization in the head region of Rpl11-deficient zebrafish, where the morphological abnormalities and tp53 expression were more pronounced. Interestingly, in blood cells derived from DBA patients with mutations in RPL11, the biogenesis of ribosomes was defective, but the expression level of c-Myc and its target nucleolar proteins was unchanged. The results suggest a model whereby RPL11 deficiency activates the synthesis of c-Myc target nucleolar proteins, which subsequently triggers a p53 response. These results further demonstrate that the induction of Tp53 mediates the morphological, but not erythroid, defects associated with RPL11 deficiency.
[Mh] Termos MeSH primário: Anemia de Diamond-Blackfan/fisiopatologia
Proteínas Ribossômicas/deficiência
[Mh] Termos MeSH secundário: Anemia de Diamond-Blackfan/genética
Anemia de Diamond-Blackfan/patologia
Animais
Modelos Animais de Doenças
Eritropoese/genética
Proteínas de Peixes/deficiência
Proteínas de Peixes/genética
Genes myc
Genes p53
Seres Humanos
Mutação
Processamento Pós-Transcricional do RNA
Proteínas Ribossômicas/genética
Peixe-Zebra
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fish Proteins); 0 (Ribosomal Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171212
[St] Status:MEDLINE


  4 / 11824 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28742285
[Au] Autor:Carlston CM; Afify ZA; Palumbos JC; Bagley H; Barbagelata C; Wooderchak-Donahue WL; Mao R; Carey JC
[Ad] Endereço:Department of Pathology, University of Utah, Salt Lake City, Utah.
[Ti] Título:Variable expressivity and incomplete penetrance in a large family with non-classical Diamond-Blackfan anemia associated with ribosomal protein L11 splicing variant.
[So] Source:Am J Med Genet A;173(10):2622-2627, 2017 Oct.
[Is] ISSN:1552-4833
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Diamond-Blackfan anemia (DBA) is a group of clinically and genetically heterogeneous bone marrow failure disorders with or without congenital anomalies. Variable expressivity and incomplete penetrance have been observed within affected families. Diamond-Blackfan anemia-7 (DBA7), caused by heterozygous mutations in ribosomal protein L11 (RPL11), accounts for approximately 5% of DBA. DBA7 is usually characterized by early-onset bone marrow failure often accompanied by congenital malformations, especially thumb defects. Here, we present the case of a 2-year-old boy with chronic mild normocytic anemia, short stature, bilateral underdevelopment of the thumbs, atrial septal defect, and hypospadias. Hematological testing revealed slightly decreased hematocrit and hemoglobin, normal HbF, and elevated eADA. Family history included maternal relatives with thumb defects, but the mother's thumbs were normal. Clinical exome sequencing detected a maternally-inherited RPL11 variant, c.396+3A>G, that is predicted to affect splicing. A family correlation study of the identified variant demonstrates segregation with thumb anomalies in the mother's family. RNA studies suggest that the variant produces an alternative transcript that is likely susceptible to nonsense-mediated decay. This report summarizes the prevalence of non-anemia findings in DBA7 and describes a non-classical familial presentation of DBA7 more associated with thumb anomalies than with anemia.
[Mh] Termos MeSH primário: Anemia de Diamond-Blackfan/genética
Mutação
Processamento de RNA
Proteínas Ribossômicas/genética
[Mh] Termos MeSH secundário: Adulto
Pré-Escolar
Feminino
Seres Humanos
Masculino
Linhagem
Penetrância
Fenótipo
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ribosomal Proteins); 0 (ribosomal protein L11)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180207
[Lr] Data última revisão:
180207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.1002/ajmg.a.38360


  5 / 11824 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29324785
[Au] Autor:Joerling J; Barth SA; Schlez K; Willems H; Herbst W; Ewers C
[Ad] Endereço:Institute of Hygiene and Infectious Diseases of Animals, Justus Liebig University Giessen, Giessen, Germany.
[Ti] Título:Phylogenetic diversity, antimicrobial susceptibility and virulence gene profiles of Brachyspira hyodysenteriae isolates from pigs in Germany.
[So] Source:PLoS One;13(1):e0190928, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Swine dysentery (SD) is an economically important diarrheal disease in pigs caused by different strongly hemolytic Brachyspira (B.) species, such as B. hyodysenteriae, B. suanatina and B. hampsonii. Possible associations of epidemiologic data, such as multilocus sequence types (STs) to virulence gene profiles and antimicrobial susceptibility are rather scarce, particularly for B. hyodysenteriae isolates from Germany. In this study, B. hyodysenteriae (n = 116) isolated from diarrheic pigs between 1990 and 2016 in Germany were investigated for their STs, susceptibility to the major drugs used for treatment of SD (tiamulin and valnemulin) and genes that were previously linked with virulence and encode for hemolysins (tlyA, tlyB, tlyC, hlyA, BHWA1_RS02885, BHWA1_RS09085, BHWA1_RS04705, and BHWA1_RS02195), outer membrane proteins (OMPs) (bhlp16, bhlp17.6, bhlp29.7, bhmp39f, and bhmp39h) as well as iron acquisition factors (ftnA and bitC). Multilocus sequence typing (MLST) revealed that 79.4% of the isolates belonged to only three STs, namely ST52 (41.4%), ST8 (12.1%), and ST112 (25.9%) which have been observed in other European countries before. Another 24 isolates belonged to twelve new STs (ST113-118, ST120-123, ST131, and ST193). The temporal distribution of STs revealed the presence of new STs as well as the regular presence of ST52 over three decades (1990s-2000s). The proportion of strains that showed resistance to both tiamulin und valnemulin (39.1%) varied considerably among the most frequent STs ranging from 0% (0/14 isolates resistant) in ST8 isolates to 46.7% (14/30), 52.1% (25/48), and 85.7% (6/7) in isolates belonging to ST112, ST52, and ST114, respectively. All hemolysin genes as well as the iron-related gene ftnA and the OMP gene bhlp29.7 were regularly present in the isolates, while the OMP genes bhlp17.6 and bhmp39h could not be detected. Sequence analysis of hemolysin genes of selected isolates revealed co-evolution of tlyB, BHWA1_RS02885, BHWA1_RS09085, and BHWA1_RS02195 with the core genome and suggested independent evolution of tlyA, tlyC, and hlyA. Our data indicate that in Germany, swine dysentery might be caused by a limited number of B. hyodysenteriae clonal groups. Major STs (ST8, ST52, and ST112) are shared with other countries in Europe suggesting a possible role of the European intra-Community trade of pigs in the dissemination of certain clones. The identification of several novel STs, some of which are single or double locus variants of ST52, may on the other hand hint towards an ongoing diversification of the pathogen in the studied area. The linkage of pleuromutilin susceptibility and sequence type of an isolate might reflect a clonal expansion of the underlying resistance mechanism, namely mutations in the ribosomal RNA genes. A linkage between single virulence-associated genes (VAGs) or even VAG patterns and the phylogenetic background of the isolates could not be established, since almost all VAGs were regularly present in the isolates.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Brachyspira hyodysenteriae/efeitos dos fármacos
Brachyspira hyodysenteriae/patogenicidade
Farmacorresistência Bacteriana/genética
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias/genética
Brachyspira hyodysenteriae/genética
Brachyspira hyodysenteriae/isolamento & purificação
Diterpenos/farmacologia
Disenteria/microbiologia
Disenteria/veterinária
Fezes/microbiologia
Alemanha
Infecções por Bactérias Gram-Negativas/microbiologia
Infecções por Bactérias Gram-Negativas/veterinária
Proteínas Hemolisinas/genética
Filogenia
Polimorfismo de Nucleotídeo Único
Proteínas Ribossômicas/genética
Sus scrofa
Suínos
Doenças dos Suínos/microbiologia
Virulência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (Diterpenes); 0 (Hemolysin Proteins); 0 (Ribosomal Proteins); 0 (ribosomal protein L3); 125-65-5 (pleuromutilin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180206
[Lr] Data última revisão:
180206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190928


  6 / 11824 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29237735
[Au] Autor:Dougherty JD
[Ad] Endereço:Departments of Genetics and Psychiatry, Washington University School of Medicine, St. Louis, Missouri 63110 jdougherty@genetics.wustl.edu.
[Ti] Título:The Expanding Toolkit of Translating Ribosome Affinity Purification.
[So] Source:J Neurosci;37(50):12079-12087, 2017 Dec 13.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Translating ribosome affinity purification is a method initially developed for profiling mRNA from genetically defined cell types in complex tissues. It has been applied both to identify target molecules in cell types that are important for controlling a variety of behaviors in the brain, and to understand the molecular consequences on those cells due to experimental manipulations, ranging from drugs of abuse to disease-causing mutations. Since its inception, a variety of methodological advances are opening new avenues of investigation. These advances include a variety of new methods for targeting cells for translating ribosome affinity purification by features such as their projections or activity, additional tags and mouse reagents increasing the flexibility of the system, and new modifications of the method specifically focused on studying the regulation of translation. The latter includes methods to assess cell type-specific regulation of translation in specific subcellular compartments. Here, I provide a summary of these recent advances and resources, highlighting both new experimental opportunities and areas for future technical development.
[Mh] Termos MeSH primário: Fracionamento Celular/métodos
Perfilação da Expressão Gênica/métodos
Ensaios de Triagem em Larga Escala/métodos
Separação Imunomagnética/métodos
Neuroglia/ultraestrutura
Neurônios/ultraestrutura
Biossíntese de Proteínas
Ribossomos
[Mh] Termos MeSH secundário: Marcadores de Afinidade
Animais
Encéfalo/citologia
Fracionamento Celular/tendências
Linhagem Celular
Cromossomos Artificiais Bacterianos
Dependovirus/genética
Eletroporação
Imunofluorescência
Previsões
Genes Reporter
Vetores Genéticos/genética
Proteínas de Fluorescência Verde/análise
Proteínas de Fluorescência Verde/genética
Camundongos
Neuroglia/metabolismo
Neurônios/classificação
Neurônios/metabolismo
Fases de Leitura Aberta/genética
RNA Mensageiro/genética
RNA Mensageiro/isolamento & purificação
Proteínas Recombinantes de Fusão/análise
Proteínas Ribossômicas/análise
Proteínas Ribossômicas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Affinity Labels); 0 (RNA, Messenger); 0 (Recombinant Fusion Proteins); 0 (Ribosomal Proteins); 147336-22-9 (Green Fluorescent Proteins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180130
[Lr] Data última revisão:
180130
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171215
[St] Status:MEDLINE
[do] DOI:10.1523/JNEUROSCI.1929-17.2017


  7 / 11824 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28741571
[Au] Autor:Liu Y; Deisenroth C; Zhang Y
[Ad] Endereço:Department of Radiation Oncology and Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
[Ti] Título:RP-MDM2-p53 Pathway: Linking Ribosomal Biogenesis and Tumor Surveillance.
[So] Source:Trends Cancer;2(4):191-204, 2016 Apr.
[Is] ISSN:2405-8025
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ribosomal biogenesis is tightly associated with cellular activities, such as growth, proliferation, and cell cycle progression. Perturbations in ribosomal biogenesis can initiate so-called nucleolar stress. The process through which ribosomal proteins (RPs) transduce nucleolar stress signals via MDM2 to p53 has been described as a crucial tumor-suppression mechanism. In this review we focus on recent progress pertaining to the function and mechanism of RPs in association with the MDM2-p53 tumor-suppression network, and the potential implications this surveillance network has for cancer development.
[Mh] Termos MeSH primário: Neoplasias/metabolismo
Proteínas Proto-Oncogênicas c-mdm2/metabolismo
Proteínas Ribossômicas/metabolismo
Proteína Supressora de Tumor p53/metabolismo
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Ribosomal Proteins); 0 (Tumor Suppressor Protein p53); EC 2.3.2.27 (Proto-Oncogene Proteins c-mdm2)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180117
[Lr] Data última revisão:
180117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE


  8 / 11824 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29211986
[Au] Autor:Jamiolkowski RM; Chen C; Cooperman BS; Goldman YE
[Ad] Endereço:Pennsylvania Muscle Institute, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, Pennsylvania.
[Ti] Título:tRNA Fluctuations Observed on Stalled Ribosomes Are Suppressed during Ongoing Protein Synthesis.
[So] Source:Biophys J;113(11):2326-2335, 2017 Dec 05.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The pretranslocation complex of the ribosome can undergo spontaneous fluctuations of messenger RNA and transfer RNAs (tRNAs) between classical and hybrid states, and occupation of the hybrid tRNA positions has been proposed to precede translocation. The classical and hybrid state tRNA positions have been extensively characterized when the ribosome is stalled along the messenger RNA by either the absence or delayed addition of elongation factor G (EF-G), or by the presence of antibiotics or GTP analogs that block translocation. However, during multiple ongoing elongation cycles when both EF-G and ternary complexes are present, EF-G can bind to the pretranslocation complex much faster than the timescale of the classic-hybrid transitions. Using single-molecule fluorescence resonance energy transfer between adjacent tRNAs and between A-site tRNA and ribosomal protein L11, we found that the tRNAs do not fluctuate between the hybrid and classical states, but instead adopt a position with fluorescence resonance energy transfer efficiencies between those of the stalled classical and hybrid states.
[Mh] Termos MeSH primário: Biossíntese de Proteínas
RNA de Transferência/genética
Ribossomos/genética
Ribossomos/metabolismo
[Mh] Termos MeSH secundário: Transferência Ressonante de Energia de Fluorescência
Fator G para Elongação de Peptídeos/metabolismo
Proteínas Ribossômicas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptide Elongation Factor G); 0 (Ribosomal Proteins); 0 (ribosomal protein L11); 9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180104
[Lr] Data última revisão:
180104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE


  9 / 11824 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29192214
[Au] Autor:Pelletier J; Thomas G; Volarevic S
[Ad] Endereço:Laboratory of Cancer Metabolism, Institut d'Investigació Biomèdica de Bellvitge (IDIBELL), Hospital Duran i Reynals, 08908 L'Hospitalet de Llobregat, Barcelona, Catalonia, Spain.
[Ti] Título:Ribosome biogenesis in cancer: new players and therapeutic avenues.
[So] Source:Nat Rev Cancer;18(1):51-63, 2018 Jan.
[Is] ISSN:1474-1768
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The ribosome is a complex molecular machine composed of numerous distinct proteins and nucleic acids and is responsible for protein synthesis in every living cell. Ribosome biogenesis is one of the most multifaceted and energy- demanding processes in biology, involving a large number of assembly and maturation factors, the functions of which are orchestrated by multiple cellular inputs, including mitogenic signals and nutrient availability. Although causal associations between inherited mutations affecting ribosome biogenesis and elevated cancer risk have been established over the past decade, mechanistic data have emerged suggesting a broader role for dysregulated ribosome biogenesis in the development and progression of most spontaneous cancers. In this Opinion article, we highlight the most recent findings that provide new insights into the molecular basis of ribosome biogenesis in cancer and offer our perspective on how these observations present opportunities for the design of new targeted cancer treatments.
[Mh] Termos MeSH primário: Neoplasias/patologia
Biossíntese de Proteínas/fisiologia
Ribossomos/fisiologia
[Mh] Termos MeSH secundário: Animais
Proliferação Celular/fisiologia
Seres Humanos
Neoplasias/metabolismo
Proteínas Ribossômicas/metabolismo
Ribossomos/metabolismo
Transdução de Sinais/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Ribosomal Proteins)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171227
[Lr] Data última revisão:
171227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171202
[St] Status:MEDLINE
[do] DOI:10.1038/nrc.2017.104


  10 / 11824 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29053787
[Au] Autor:Devoy A; Kalmar B; Stewart M; Park H; Burke B; Noy SJ; Redhead Y; Humphrey J; Lo K; Jaeger J; Mejia Maza A; Sivakumar P; Bertolin C; Soraru G; Plagnol V; Greensmith L; Acevedo Arozena A; Isaacs AM; Davies B; Fratta P; Fisher EMC
[Ad] Endereço:Department of Neurodegenerative Disease, UCL Institute of Neurology, Queen Square, London WC1N 3BG, UK.
[Ti] Título:Humanized mutant FUS drives progressive motor neuron degeneration without aggregation in 'FUSDelta14' knockin mice.
[So] Source:Brain;140(11):2797-2805, 2017 Nov 01.
[Is] ISSN:1460-2156
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mutations in FUS are causative for amyotrophic lateral sclerosis with a dominant mode of inheritance. In trying to model FUS-amyotrophic lateral sclerosis (ALS) in mouse it is clear that FUS is dosage-sensitive and effects arise from overexpression per se in transgenic strains. Novel models are required that maintain physiological levels of FUS expression and that recapitulate the human disease-with progressive loss of motor neurons in heterozygous animals. Here, we describe a new humanized FUS-ALS mouse with a frameshift mutation, which fulfils both criteria: the FUS Delta14 mouse. Heterozygous animals express mutant humanized FUS protein at physiological levels and have adult onset progressive motor neuron loss and denervation of neuromuscular junctions. Additionally, we generated a novel antibody to the unique human frameshift peptide epitope, allowing specific identification of mutant FUS only. Using our new FUSDelta14 ALS mouse-antibody system we show that neurodegeneration occurs in the absence of FUS protein aggregation. FUS mislocalization increases as disease progresses, and mutant FUS accumulates at the rough endoplasmic reticulum. Further, transcriptomic analyses show progressive changes in ribosomal protein levels and mitochondrial function as early disease stages are initiated. Thus, our new physiological mouse model has provided novel insight into the early pathogenesis of FUS-ALS.
[Mh] Termos MeSH primário: Esclerose Amiotrófica Lateral/genética
Modelos Animais de Doenças
Mutação da Fase de Leitura
Camundongos
Agregação Patológica de Proteínas/genética
Proteína FUS de Ligação a RNA/genética
[Mh] Termos MeSH secundário: Esclerose Amiotrófica Lateral/metabolismo
Animais
Retículo Endoplasmático Rugoso/metabolismo
Dosagem de Genes
Perfilação da Expressão Gênica
Técnicas de Introdução de Genes
Heterozigoto
Seres Humanos
Mitocôndrias/metabolismo
Neurônios Motores/metabolismo
Junção Neuromuscular/metabolismo
Agregação Patológica de Proteínas/metabolismo
Proteína FUS de Ligação a RNA/metabolismo
Proteínas Ribossômicas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA-Binding Protein FUS); 0 (Ribosomal Proteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:171021
[St] Status:MEDLINE
[do] DOI:10.1093/brain/awx248



página 1 de 1183 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