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[PMID]:29372649
[Au] Autor:Chamorro-Petronacci C; Perez-Sayáns M; Padín-Iruegas ME; Marichalar-Mendia X; Gallas-Torreira M; García García A
[Ad] Endereço:a Oral Medicine, Oral Surgery and Implantology Unit, Faculty of Medicine and Dentistry , Instituto de Investigación Sanitaria de Santiago (IDIS) , Santiago de Compostela , Spain.
[Ti] Título:Differential expression of snoRNAs in oral squamous cell carcinomas: new potential diagnostic markers.
[So] Source:J Enzyme Inhib Med Chem;33(1):424-427, 2018 Dec.
[Is] ISSN:1475-6374
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Small nucleolar RNAs (snoRNAs) are small non-coding RNA sequences whose most studied function is ribosome biogenesis. The altered expression of snoRNA is observed in tumoral processes such as breast cancer and multiple myeloma. However, we have not found any references to snoRNAs in oral squamous cell carcinomas (OSCC) in the literature at the time this article was written. MATERIAL AND METHODS: We have analyzed snoRNA expression in frozen OSCC tissue samples and have compared them to healthy controls. RNA was extracted from a total of eight OSCC samples and eight control samples, measuring the differential expression of small RNAs with the Affymetrix miRNA 4.1 Array Plate microarray platform. RESULTS: Results were analyzed using the Transcriptome Analysis Console 3.0 (TAC) software. We obtained a total of 16 deregulated snoRNAs of which one was over expressed and 15 were under expressed. SnoRNAs expression was altered in OSCC and could serve as a diagnostic marker.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/genética
Carcinoma de Células Escamosas/diagnóstico
Neoplasias Bucais/diagnóstico
Ribonucleoproteínas Nucleolares Pequenas/genética
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
Carcinoma de Células Escamosas/genética
Feminino
Expressão Gênica
Seres Humanos
Masculino
Meia-Idade
Neoplasias Bucais/genética
Análise de Sequência com Séries de Oligonucleotídeos
Ribonucleoproteínas Nucleolares Pequenas/isolamento & purificação
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (Ribonucleoproteins, Small Nucleolar)
[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:180127
[St] Status:MEDLINE
[do] DOI:10.1080/14756366.2018.1426574


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[PMID]:29174924
[Au] Autor:Liang D; Tatomer DC; Luo Z; Wu H; Yang L; Chen LL; Cherry S; Wilusz JE
[Ad] Endereço:Department of Biochemistry and Biophysics, University of Pennsylvania Perelman School of Medicine, Philadelphia, PA 19104, USA.
[Ti] Título:The Output of Protein-Coding Genes Shifts to Circular RNAs When the Pre-mRNA Processing Machinery Is Limiting.
[So] Source:Mol Cell;68(5):940-954.e3, 2017 Dec 07.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Many eukaryotic genes generate linear mRNAs and circular RNAs, but it is largely unknown how the ratio of linear to circular RNA is controlled or modulated. Using RNAi screening in Drosophila cells, we identify many core spliceosome and transcription termination factors that control the RNA outputs of reporter and endogenous genes. When spliceosome components were depleted or inhibited pharmacologically, the steady-state levels of circular RNAs increased while expression of their associated linear mRNAs concomitantly decreased. Upon inhibiting RNA polymerase II termination via depletion of the cleavage/polyadenylation machinery, circular RNA levels were similarly increased. This is because readthrough transcripts now extend into downstream genes and are subjected to backsplicing. In total, these results demonstrate that inhibition or slowing of canonical pre-mRNA processing events shifts the steady-state output of protein-coding genes toward circular RNAs. This is in part because nascent RNAs become directed into alternative pathways that lead to circular RNA production.
[Mh] Termos MeSH primário: Proteínas de Drosophila/genética
Drosophila melanogaster/genética
Precursores de RNA/biossíntese
Processamento de RNA
RNA Mensageiro/biossíntese
RNA/biossíntese
Spliceossomos/genética
Transcrição Genética
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Proteínas de Drosophila/biossíntese
Drosophila melanogaster/metabolismo
Lacase/biossíntese
Lacase/genética
RNA/genética
Interferência de RNA
RNA Polimerase II/metabolismo
Precursores de RNA/genética
Fatores de Processamento de RNA/genética
Fatores de Processamento de RNA/metabolismo
Estabilidade de RNA
RNA Mensageiro/genética
Ribonucleoproteínas Nucleolares Pequenas/genética
Ribonucleoproteínas Nucleolares Pequenas/metabolismo
Spliceossomos/metabolismo
Terminação da Transcrição Genética
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (RNA Precursors); 0 (RNA Splicing Factors); 0 (RNA, Messenger); 0 (RNA, circular); 0 (Ribonucleoproteins, Small Nucleolar); 0 (ribonucleoprotein, U3 small nucleolar); 63231-63-0 (RNA); EC 1.10.3.2 (Laccase); EC 2.7.7.- (RNA Polymerase II)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171226
[Lr] Data última revisão:
171226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE


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[PMID]:28672776
[Au] Autor:Ma T; Lu C; Guo Y; Zhang C; Du X
[Ad] Endereço:.
[Ti] Título:Human U3 protein 14a plays an anti-apoptotic role in cancer cells.
[So] Source:Biol Chem;398(11):1247-1257, 2017 Oct 26.
[Is] ISSN:1437-4315
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Human U three protein 14a (hUTP14a) binds p53 and promotes p53 degradation. Here, we report that hUTP14a plays an anti-apoptotic role in tumor cells through a p53-independent pathway. Knockdown of hUTP14a activated the intrinsic pathway of apoptosis and sensitized tumor cells to chemotherapeutic drug-induced apoptosis. In addition, the protein level of hUTP14a decreased upon chemotherapeutic drug- or irradiation-induced apoptosis. Importantly, the decrease of hUTP14a during induced apoptosis was not blocked by pan-caspase inhibitor z-VAD-FMK, indicating that the down-regulation of hUTP14a is an upstream event in apoptosis. Furthermore, ectopically expressed hUTP14a protected tumor cells from chemotherapeutic drug-induced apoptosis. In summary, our data showed that hUTP14a protected tumor cells from chemotherapeutic drug-induced apoptosis and thus might possess a potential as a target for anti-tumor therapy.
[Mh] Termos MeSH primário: Apoptose
Carcinoma Pulmonar de Células não Pequenas/metabolismo
Neoplasias Pulmonares/metabolismo
Ribonucleoproteínas Nucleolares Pequenas/metabolismo
[Mh] Termos MeSH secundário: Carcinoma Pulmonar de Células não Pequenas/patologia
Seres Humanos
Neoplasias Pulmonares/patologia
Células Tumorais Cultivadas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ribonucleoproteins, Small Nucleolar); 0 (U3 protein 14a, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170705
[St] Status:MEDLINE


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[PMID]:28576826
[Au] Autor:Tomkuviene M; Licyte J; Olendraite I; Liutkeviciute Z; Clouet-d'Orval B; Klimasauskas S
[Ad] Endereço:Department of Biological DNA Modification, Institute of Biotechnology, Vilnius University, Vilnius LT-10257, Lithuania.
[Ti] Título:Archaeal fibrillarin-Nop5 heterodimer 2'- -methylates RNA independently of the C/D guide RNP particle.
[So] Source:RNA;23(9):1329-1337, 2017 Sep.
[Is] ISSN:1469-9001
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Archaeal fibrillarin (aFib) is a well-characterized -adenosyl methionine (SAM)-dependent RNA 2'- -methyltransferase that is known to act in a large C/D ribonucleoprotein (RNP) complex together with Nop5 and L7Ae proteins and a box C/D guide RNA. In the reaction, the guide RNA serves to direct the methylation reaction to a specific site in tRNA or rRNA by sequence complementarity. Here we show that a aFib-Nop5 heterodimer can alone perform SAM-dependent 2'- -methylation of 16S and 23S ribosomal RNAs in vitro independently of L7Ae and C/D guide RNAs. Using tritium-labeling, mass spectrometry, and reverse transcription analysis, we identified three in vitro 2'- -methylated positions in the 16S rRNA of , positions lying outside of previously reported pyrococcal C/D RNP methylation sites. This newly discovered stand-alone activity of aFib-Nop5 may provide an example of an ancestral activity retained in enzymes that were recruited to larger complexes during evolution.
[Mh] Termos MeSH primário: Archaea/genética
Archaea/metabolismo
Proteínas Cromossômicas não Histona/metabolismo
RNA Arqueal/genética
RNA Arqueal/metabolismo
Ribonucleoproteínas Nucleolares Pequenas/metabolismo
Ribonucleoproteínas/metabolismo
[Mh] Termos MeSH secundário: Proteínas Cromossômicas não Histona/química
Metilação
Conformação de Ácido Nucleico
Ligação Proteica
Multimerização Proteica
RNA Ribossômico 16S/química
RNA Ribossômico 16S/genética
RNA Ribossômico 16S/metabolismo
RNA Ribossômico 23S/química
RNA Ribossômico 23S/genética
RNA Ribossômico 23S/metabolismo
Ribonucleoproteínas/química
Ribonucleoproteínas Nucleolares Pequenas/química
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromosomal Proteins, Non-Histone); 0 (RNA, Archaeal); 0 (RNA, Ribosomal, 16S); 0 (RNA, Ribosomal, 23S); 0 (Ribonucleoproteins); 0 (Ribonucleoproteins, Small Nucleolar); 0 (fibrillarin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170604
[St] Status:MEDLINE
[do] DOI:10.1261/rna.059832.116


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[PMID]:28505348
[Au] Autor:Rothé B; Manival X; Rolland N; Charron C; Senty-Ségault V; Branlant C; Charpentier B
[Ad] Endereço:Ingénierie Moléculaire et Physiopathologie Articulaire (IMoPA), UMR 7365 CNRS Université de Lorraine, Biopôle, Campus Biologie Santé, 9 avenue de la forêt de Haye, BP 20199, 54505 VandÅ“uvre-lès-Nancy, France.
[Ti] Título:Implication of the box C/D snoRNP assembly factor Rsa1p in U3 snoRNP assembly.
[So] Source:Nucleic Acids Res;45(12):7455-7473, 2017 Jul 07.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The U3 box C/D snoRNA is one key element of 90S pre-ribosome. It contains a 5΄ domain pairing with pre-rRNA and the U3B/C and U3C΄/D motifs for U3 packaging into a unique small nucleolar ribonucleoprotein particle (snoRNP). The RNA-binding protein Snu13/SNU13 nucleates on U3B/C the assembly of box C/D proteins Nop1p/FBL and Nop56p/NOP56, and the U3-specific protein Rrp9p/U3-55K. Snu13p/SNU13 has a much lower affinity for U3C΄/D but nevertheless forms on this motif an RNP with box C/D proteins Nop1p/FBL and Nop58p/NOP58. In this study, we characterized the influence of the RNP assembly protein Rsa1 in the early steps of U3 snoRNP biogenesis in yeast and we propose a refined model of U3 snoRNP biogenesis. While recombinant Snu13p enhances the binding of Rrp9p to U3B/C, we observed that Rsa1p has no effect on this activity but forms with Snu13p and Rrp9p a U3B/C pre-RNP. In contrast, we found that Rsa1p enhances Snu13p binding on U3C΄/D. RNA footprinting experiments indicate that this positive effect most likely occurs by direct contacts of Rsa1p with the U3 snoRNA 5΄ domain. In light of the recent U3 snoRNP cryo-EM structures, our data suggest that Rsa1p has a dual role by also preventing formation of a pre-mature functional U3 RNP.
[Mh] Termos MeSH primário: Regulação Fúngica da Expressão Gênica
Precursores de RNA/genética
RNA Nucleolar Pequeno/genética
Ribonucleoproteínas Nucleares Pequenas/genética
Ribonucleoproteínas Nucleolares Pequenas/genética
Proteínas Ribossômicas/genética
Proteínas de Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: Sequência de Bases
Sítios de Ligação
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
Conformação de Ácido Nucleico
Ligação Proteica
Precursores de RNA/metabolismo
RNA Nucleolar Pequeno/metabolismo
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Ribonucleoproteínas Nucleares Pequenas/metabolismo
Ribonucleoproteínas Nucleolares Pequenas/metabolismo
Proteínas Ribossômicas/metabolismo
Ribossomos/genética
Ribossomos/metabolismo
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (NOP1 protein, S cerevisiae); 0 (NOP56 protein, S cerevisiae); 0 (Nuclear Proteins); 0 (RNA Precursors); 0 (RNA, Small Nucleolar); 0 (RNA, U3 small nucleolar); 0 (RSA1 protein, S cerevisiae); 0 (Recombinant Proteins); 0 (Ribonucleoproteins, Small Nuclear); 0 (Ribonucleoproteins, Small Nucleolar); 0 (Ribosomal Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (Snu13 protein, S cerevisiae); 0 (ribonucleoprotein, U3 small nucleolar)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170516
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx424


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[PMID]:28436950
[Au] Autor:von Morgen P; Burdova K; Flower TG; O'Reilly NJ; Boulton SJ; Smerdon SJ; Macurek L; Horejsí Z
[Ad] Endereço:Department of Cancer Cell Biology, Institute of Molecular Genetics of the ASCR, Prague, Czech Republic.
[Ti] Título:MRE11 stability is regulated by CK2-dependent interaction with R2TP complex.
[So] Source:Oncogene;36(34):4943-4950, 2017 Aug 24.
[Is] ISSN:1476-5594
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The MRN (MRE11-RAD50-NBS1) complex is essential for repair of DNA double-strand breaks and stalled replication forks. Mutations of the MRN complex subunit MRE11 cause the hereditary cancer-susceptibility disease ataxia-telangiectasia-like disorder (ATLD). Here we show that MRE11 directly interacts with PIH1D1, a subunit of heat-shock protein 90 cochaperone R2TP complex, which is required for the assembly of large protein complexes, such as RNA polymerase II, small nucleolar ribonucleoproteins and mammalian target of rapamycin complex 1. The MRE11-PIH1D1 interaction is dependent on casein kinase 2 (CK2) phosphorylation of two acidic sequences within the MRE11 C terminus containing serines 558/561 and 688/689. Conversely, the PIH1D1 phospho-binding domain PIH-N is required for association with MRE11 phosphorylated by CK2. Consistent with these findings, depletion of PIH1D1 resulted in MRE11 destabilization and affected DNA-damage repair processes dependent on MRE11. Additionally, mutations of serines 688/689, which abolish PIH1D1 binding, also resulted in decreased MRE11 stability. As depletion of R2TP frequently leads to instability of its substrates and as truncation mutation of MRE11 lacking serines 688/689 leads to decreased levels of the MRN complex both in ATLD patients and an ATLD mouse model, our results suggest that the MRN complex is a novel R2TP complex substrate and that their interaction is regulated by CK2 phosphorylation.
[Mh] Termos MeSH primário: Proteínas Reguladoras de Apoptose/metabolismo
Caseína Quinase II/metabolismo
Proteínas de Ligação a DNA/metabolismo
[Mh] Termos MeSH secundário: Animais
Ataxia Telangiectasia/metabolismo
Proteínas Mutadas de Ataxia Telangiectasia/metabolismo
Núcleo Celular/metabolismo
Dano ao DNA/fisiologia
Reparo do DNA/fisiologia
Enzimas Reparadoras do DNA/metabolismo
Proteínas de Choque Térmico/metabolismo
Seres Humanos
Camundongos
Mutação/fisiologia
Proteínas Nucleares/metabolismo
Fosforilação/fisiologia
Ligação Proteica/fisiologia
RNA Polimerase II/metabolismo
Ribonucleoproteínas Nucleolares Pequenas/metabolismo
Serina/metabolismo
Serina-Treonina Quinases TOR/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apoptosis Regulatory Proteins); 0 (DNA-Binding Proteins); 0 (Heat-Shock Proteins); 0 (Nuclear Proteins); 0 (Ribonucleoproteins, Small Nucleolar); 452VLY9402 (Serine); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.11.1 (Ataxia Telangiectasia Mutated Proteins); EC 2.7.11.1 (Casein Kinase II); EC 2.7.7.- (RNA Polymerase II); EC 6.5.1.- (DNA Repair Enzymes)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170425
[St] Status:MEDLINE
[do] DOI:10.1038/onc.2017.99


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[PMID]:28218222
[Au] Autor:Zhang JY; Xu D; Liu ZZ; Li Y; Wang LJ; Xing BC
[Ad] Endereço:Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Hepatopancreatobiliary Surgery Department I, Peking University Cancer Hospital and Institute, Beijing 100142, China.
[Ti] Título:Human U Three Protein 14a Expression is Increased in Hepatocellular Carcinoma and Associated with Poor Prognosis.
[So] Source:Chin Med J (Engl);130(4):470-476, 2017 02 20.
[Is] ISSN:0366-6999
[Cp] País de publicação:China
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Human U three protein 14a (hUTP14a) promotes p53 degradation. Moreover, hUTP14a expression is upregulated in several types of tumors. However, the expression pattern of hUTP14a in hepatocellular carcinoma (HCC) remains unknown. The aim of this study was to investigate hUTP14a expression and its prognostic value in HCC. METHODS: The hUTP14a expression was evaluated using immunohistochemistry (IHC) in HCC tissue specimens. The correlations between hUTP14a expression and clinicopathological variables were analyzed. The Kaplan-Meier method was used to analyze the association between hUTP14a expression and survival. Independent prognostic factors associated with overall survival (OS) and disease-free survival (DFS) were analyzed using the Cox proportional-hazards regression model. RESULTS: The IHC data revealed that the hUTP14a positivity rate in HCC tissue specimens was significantly higher than that in nontumorous tissue specimens (89.9% vs. 72.7%, P < 0.05). The hUTP14a expression was detected in both the nucleolus and the cytoplasm. The positivity rate of nucleolar hUTP14a expression in HCC tissue specimens was higher than that in the nontumorous tissue specimens (29.3% vs. 10.1%, P < 0.05). No significant difference was found between HCC and nontumorous tissue specimens of cytoplasmic hUTP14a expression (60.6% vs. 62.6%, P > 0.05). In addition, no significant correlation was found between nucleolar hUTP14a expression and other clinicopathological variables. The 5-year OS and DFS rates in patients with positive nucleolar hUTP14a expression were significantly lower than those in patients with negative hUTP14a expression (P = 0.004 for OS, P = 0.003 for DFS). Multivariate analysis showed that nucleolar hUTP14a expression was an independent prognostic factor for OS (P = 0.004) and DFS (P < 0.001). CONCLUSIONS: The positivity rate of hUTP14a expression was significantly higher in HCC specimens. Positive expression of nucleolar hUTP14a might act as a novel prognostic predictor for patients with HCC.
[Mh] Termos MeSH primário: Carcinoma Hepatocelular/metabolismo
Carcinoma Hepatocelular/patologia
Neoplasias Hepáticas/metabolismo
Neoplasias Hepáticas/patologia
Ribonucleoproteínas Nucleolares Pequenas/metabolismo
[Mh] Termos MeSH secundário: Adulto
Idoso
Idoso de 80 Anos ou mais
Biomarcadores Tumorais/genética
Biomarcadores Tumorais/metabolismo
Carcinoma Hepatocelular/mortalidade
Intervalo Livre de Doença
Feminino
Seres Humanos
Imuno-Histoquímica
Estimativa de Kaplan-Meier
Neoplasias Hepáticas/mortalidade
Masculino
Meia-Idade
Análise Multivariada
Prognóstico
Modelos de Riscos Proporcionais
Ribonucleoproteínas Nucleolares Pequenas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (Ribonucleoproteins, Small Nucleolar)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170323
[Lr] Data última revisão:
170323
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170221
[St] Status:MEDLINE
[do] DOI:10.4103/0366-6999.199839


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[PMID]:28082392
[Au] Autor:Wells GR; Weichmann F; Sloan KE; Colvin D; Watkins NJ; Schneider C
[Ad] Endereço:Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, NE2 4HH, UK.
[Ti] Título:The ribosome biogenesis factor yUtp23/hUTP23 coordinates key interactions in the yeast and human pre-40S particle and hUTP23 contains an essential PIN domain.
[So] Source:Nucleic Acids Res;45(8):4796-4809, 2017 May 05.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Two proteins with PIN endonuclease domains, yUtp24(Fcf1)/hUTP24 and yUtp23/hUTP23 are essential for early pre-ribosomal (r)RNA cleavages at sites A0, A1/1 and A2/2a in yeast and humans. The yUtp24/hUTP24 PIN endonuclease is proposed to cleave at sites A1/1 and A2/2a, but the enzyme cleaving at site A0 is not known. Yeast yUtp23 contains a degenerate, non-essential PIN domain and functions together with the snR30 snoRNA, while human hUTP23 is associated with U17, the human snR30 counterpart. Using in vivo RNA-protein crosslinking and gel shift experiments, we reveal that yUtp23/hUTP23 makes direct contacts with expansion sequence 6 (ES6) in the 18S rRNA sequence and that yUtp23 interacts with the 3΄ half of the snR30 snoRNA. Protein-protein interaction studies further demonstrated that yeast yUtp23 and human hUTP23 directly interact with the H/ACA snoRNP protein yNhp2/hNHP2, the RNA helicase yRok1/hROK1(DDX52), the ribosome biogenesis factor yRrp7/hRRP7 and yUtp24/hUTP24. yUtp23/hUTP23 could therefore be central to the coordinated integration and release of ES6 binding factors and likely plays a pivotal role in remodeling this pre-rRNA region in both yeast and humans. Finally, studies using RNAi-rescue systems in human cells revealed that intact PIN domain and Zinc finger motifs in human hUTP23 are essential for 18S rRNA maturation.
[Mh] Termos MeSH primário: Proteínas Nucleares/biossíntese
Conformação de Ácido Nucleico
Ribossomos/genética
Proteínas de Saccharomyces cerevisiae/biossíntese
[Mh] Termos MeSH secundário: Seres Humanos
Proteínas Nucleares/química
Proteínas Nucleares/genética
Ligação Proteica
Domínios Proteicos/genética
Mapas de Interação de Proteínas/genética
Precursores de RNA/genética
RNA Ribossômico 18S/química
RNA Ribossômico 18S/genética
RNA Nucleolar Pequeno/biossíntese
RNA Nucleolar Pequeno/química
RNA Nucleolar Pequeno/genética
Ribonucleoproteínas Nucleolares Pequenas/biossíntese
Ribonucleoproteínas Nucleolares Pequenas/química
Ribonucleoproteínas Nucleolares Pequenas/genética
Ribossomos/química
Saccharomyces cerevisiae/química
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nuclear Proteins); 0 (RNA Precursors); 0 (RNA, Ribosomal, 18S); 0 (RNA, Small Nucleolar); 0 (Ribonucleoproteins, Small Nucleolar); 0 (Saccharomyces cerevisiae Proteins); 0 (Utp23 protein, S cerevisiae)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170114
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkw1344


  9 / 332 MEDLINE  
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[PMID]:28031372
[Au] Autor:Gumienny R; Jedlinski DJ; Schmidt A; Gypas F; Martin G; Vina-Vilaseca A; Zavolan M
[Ad] Endereço:Computational and Systems Biology, Biozentrum, University of Basel, Switzerland.
[Ti] Título:High-throughput identification of C/D box snoRNA targets with CLIP and RiboMeth-seq.
[So] Source:Nucleic Acids Res;45(5):2341-2353, 2017 Mar 17.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:High-throughput sequencing has greatly facilitated the discovery of long and short non-coding RNAs (ncRNAs), which frequently guide ribonucleoprotein complexes to RNA targets, to modulate their metabolism and expression. However, for many ncRNAs, the targets remain to be discovered. In this study, we developed computational methods to map C/D box snoRNA target sites using data from core small nucleolar ribonucleoprotein crosslinking and immunoprecipitation and from transcriptome-wide mapping of 2΄-O-ribose methylation sites. We thereby assigned the snoRNA guide to a known methylation site in the 18S rRNA, we uncovered a novel partially methylated site in the 28S ribosomal RNA, and we captured a site in the 28S rRNA in interaction with multiple snoRNAs. Although we also captured mRNAs in interaction with snoRNAs, we did not detect 2΄-O-methylation of these targets. Our study provides an integrated approach to the comprehensive characterization of 2΄-O-methylation targets of snoRNAs in species beyond those in which these interactions have been traditionally studied and contributes to the rapidly developing field of 'epitranscriptomics'.
[Mh] Termos MeSH primário: Algoritmos
Sequenciamento de Nucleotídeos em Larga Escala/métodos
RNA Guia/genética
RNA Nucleolar Pequeno/genética
Ribonucleoproteínas Nucleolares Pequenas/genética
Transcriptoma
[Mh] Termos MeSH secundário: Sequência de Bases
Reagentes para Ligações Cruzadas/química
Bases de Dados Genéticas
Imunoprecipitação
Metilação
Ligação Proteica
RNA Guia/metabolismo
RNA Ribossômico 18S/genética
RNA Ribossômico 18S/metabolismo
RNA Ribossômico 28S/genética
RNA Ribossômico 28S/metabolismo
RNA Nucleolar Pequeno/metabolismo
Ribonucleoproteínas Nucleolares Pequenas/metabolismo
Ribose/metabolismo
Software
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cross-Linking Reagents); 0 (RNA, Guide); 0 (RNA, Ribosomal, 18S); 0 (RNA, Ribosomal, 28S); 0 (RNA, Small Nucleolar); 0 (Ribonucleoproteins, Small Nucleolar); 681HV46001 (Ribose)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170718
[Lr] Data última revisão:
170718
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161230
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkw1321


  10 / 332 MEDLINE  
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[PMID]:27864990
[Au] Autor:Tall F; Dechomet M; Riviere S; Cottin V; Ballot E; Tiev KP; Montin R; Morin C; Chantran Y; Grange C; Jullien D; Ninet J; Chretien P; Cabane J; Fabien N; Johanet C
[Ad] Endereço:Immunology Department, AP-HP Saint-Antoine Hospital, Paris, France.
[Ti] Título:The Clinical Relevance of Antifibrillarin (anti-U3-RNP) Autoantibodies in Systemic Sclerosis.
[So] Source:Scand J Immunol;85(1):73-79, 2017 Jan.
[Is] ISSN:1365-3083
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Systemic sclerosis (SSc) is a heterogeneous autoimmune disease associated with several antinuclear autoantibodies useful to diagnosis and prognosis. The aim of the present multicentric study was to determine the clinical relevance of antifibrillarin autoantibodies (AFA) in patients with SSc. The clinical features of 37 patients with SSc positive for AFA (AFA+) and 139 SSc patients without AFA (AFA-) were collected retrospectively from medical records to enable a comparison between AFA- and AFA+ patients. Antifibrillarin autoantibodies were screened by an indirect immunofluorescence technique using HEp2 cells and identified by an in-house Western blot technique and/or an EliA test. Comparing AFA+ and AFA- patients, AFA+ patients were significantly younger at disease onset (36.9 versus 42.9; P = 0.02), more frequently male (P = 0.02) and of Afro-Caribbean descent (65% versus 7.7%; P < 0.001). At diagnosis, the Rodnan skin score evaluating the cutaneous manifestations was higher (13.3 versus 8.7; P = 0.01) and myositis was also more common in the AFA+ group (31.4% versus 12.2%; P < 0.01). Patients with AFA+ were not associated with diffuse cutaneous SSc or with lung involvement and no difference in survival was observed. Antifibrillarin autoantibodies are associated with patients of Afro-Caribbean origin and can identify patients with SSc who are younger at disease onset and display a higher prevalence of myositis.
[Mh] Termos MeSH primário: Autoanticorpos/sangue
Proteínas Cromossômicas não Histona/imunologia
Escleroderma Sistêmico/diagnóstico
Escleroderma Sistêmico/imunologia
[Mh] Termos MeSH secundário: Adulto
Linhagem Celular
Grupos Étnicos
Feminino
França
Seres Humanos
Masculino
Meia-Idade
Miosite/diagnóstico
Miosite/imunologia
Prevalência
Estudos Retrospectivos
Ribonucleoproteínas Nucleolares Pequenas/imunologia
Análise de Sobrevida
[Pt] Tipo de publicação:JOURNAL ARTICLE; MULTICENTER STUDY; OBSERVATIONAL STUDY
[Nm] Nome de substância:
0 (Autoantibodies); 0 (Chromosomal Proteins, Non-Histone); 0 (Ribonucleoproteins, Small Nucleolar); 0 (fibrillarin); 0 (ribonucleoprotein, U3 small nucleolar)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170315
[Lr] Data última revisão:
170315
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161120
[St] Status:MEDLINE
[do] DOI:10.1111/sji.12510



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