Base de dados : MEDLINE
Pesquisa : A11.284.430.106.279 [Categoria DeCS]
Referências encontradas : 315 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 32 ir para página                         

  1 / 315 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28039056
[Au] Autor:Afanasieva K; Chopei M; Lozovik A; Semenova A; Lukash L; Sivolob A
[Ad] Endereço:Department of General and Molecular Genetics, Taras Shevchenko National University, 64/13, Volodymyrska Street, 01601, Kiev, Ukraine.
[Ti] Título:DNA loop domain organization in nucleoids from cells of different types.
[So] Source:Biochem Biophys Res Commun;483(1):142-146, 2017 Jan 29.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The loop domain organization of chromatin plays an important role in transcription regulation and thus may be assumed to vary in cells of different types. We investigated the kinetics of DNA loop migration during single cell gel electrophoresis (the comet assay) for nucleoids obtained from human lymphocytes, lymphoblasts and glioblastoma T98G cells. The results confirm our previous observation that there are three parts of DNA in nucleoids: DNA on the nucleoid surface, loops up to ∼150 kb inside the nucleoid, and larger loops that cannot migrate. However, the relative amounts of the three parts were found to be very different for different cell types. The distributions of the loop length up to 150 kb were shown to be exponential, with the distribution parameter, the loop density, to be dependent on the cell type.
[Mh] Termos MeSH primário: Ensaio Cometa/métodos
DNA/química
[Mh] Termos MeSH secundário: Adulto
Estruturas do Núcleo Celular/química
Feminino
Seres Humanos
Cinética
Linfócitos/citologia
Linfócitos/fisiologia
Masculino
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9007-49-2 (DNA)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170601
[Lr] Data última revisão:
170601
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170101
[St] Status:MEDLINE


  2 / 315 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27632380
[Au] Autor:Underwood JM; Becker KA; Stein GS; Nickerson JA
[Ad] Endereço:Department of Cell and Developmental Biology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, Massachusetts 01655.
[Ti] Título:The Ultrastructural Signature of Human Embryonic Stem Cells.
[So] Source:J Cell Biochem;118(4):764-774, 2017 Apr.
[Is] ISSN:1097-4644
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The epigenetics and molecular biology of human embryonic stem cells (hES cells) have received much more attention than their architecture. We present a more complete look at hES cells by electron microscopy, with a special emphasis on the architecture of the nucleus. We propose that there is an ultrastructural signature of pluripotent human cells. hES cell nuclei lack heterochromatin, including the peripheral heterochromatin, that is common in most somatic cell types. The absence of peripheral heterochromatin may be related to the absence of lamins A and C, proteins important for linking chromatin to the nuclear lamina and envelope. Lamins A and C expression and the development of peripheral heterochromatin were early steps in the development of embryoid bodies. While hES cell nuclei had abundant nuclear pores, they also had an abundance of nuclear pores in the cytoplasm in the form of annulate lamellae. These were not a residue of annulate lamellae from germ cells or the early embryos from which hES cells were derived. Subnuclear structures including nucleoli, interchromatin granule clusters, and Cajal bodies were observed in the nuclear interior. The architectural organization of human ES cell nuclei has important implications for cell structure-gene expression relationships and for the maintenance of pluripotency. J. Cell. Biochem. 118: 764-774, 2017. © 2016 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Células-Tronco Embrionárias Humanas/ultraestrutura
[Mh] Termos MeSH secundário: Linhagem Celular
Nucléolo Celular/ultraestrutura
Núcleo Celular/ultraestrutura
Estruturas do Núcleo Celular/ultraestrutura
Cromatina/ultraestrutura
Células-Tronco Embrionárias Humanas/metabolismo
Seres Humanos
Microscopia Eletrônica
Microscopia de Fluorescência
Poro Nuclear/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromatin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160916
[St] Status:MEDLINE
[do] DOI:10.1002/jcb.25736


  3 / 315 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27505896
[Au] Autor:Jorgens DM; Inman JL; Wojcik M; Robertson C; Palsdottir H; Tsai WT; Huang H; Bruni-Cardoso A; López CS; Bissell MJ; Xu K; Auer M
[Ad] Endereço:Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, MS Donner, Berkeley, CA 94720, USA.
[Ti] Título:Deep nuclear invaginations are linked to cytoskeletal filaments - integrated bioimaging of epithelial cells in 3D culture.
[So] Source:J Cell Sci;130(1):177-189, 2017 Jan 01.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The importance of context in regulation of gene expression is now an accepted principle; yet the mechanism by which the microenvironment communicates with the nucleus and chromatin in healthy tissues is poorly understood. A functional role for nuclear and cytoskeletal architecture is suggested by the phenotypic differences observed between epithelial and mesenchymal cells. Capitalizing on recent advances in cryogenic techniques, volume electron microscopy and super-resolution light microscopy, we studied human mammary epithelial cells in three-dimensional (3D) cultures forming growth-arrested acini. Intriguingly, we found deep nuclear invaginations and tunnels traversing the nucleus, encasing cytoskeletal actin and/or intermediate filaments, which connect to the outer nuclear envelope. The cytoskeleton is also connected both to other cells through desmosome adhesion complexes and to the extracellular matrix through hemidesmosomes. This finding supports a physical and/or mechanical link from the desmosomes and hemidesmosomes to the nucleus, which had previously been hypothesized but now is visualized for the first time. These unique structures, including the nuclear invaginations and the cytoskeletal connectivity to the cell nucleus, are consistent with a dynamic reciprocity between the nucleus and the outside of epithelial cells and tissues.
[Mh] Termos MeSH primário: Técnicas de Cultura de Células/métodos
Estruturas do Núcleo Celular/metabolismo
Citoesqueleto/metabolismo
Células Epiteliais/citologia
Células Epiteliais/metabolismo
Imagem Tridimensional
[Mh] Termos MeSH secundário: Actinas/metabolismo
Biomimética
Mama/citologia
Adesão Celular
Comunicação Celular
Pontos de Checagem do Ciclo Celular
Estruturas do Núcleo Celular/ultraestrutura
Citoesqueleto/ultraestrutura
Desmossomos/metabolismo
Desmossomos/ultraestrutura
Células Epiteliais/ultraestrutura
Espaço Extracelular/metabolismo
Feminino
Seres Humanos
Queratinas/metabolismo
Microscopia de Fluorescência
Membrana Nuclear/metabolismo
Membrana Nuclear/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 68238-35-7 (Keratins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170804
[Lr] Data última revisão:
170804
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160810
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.190967


  4 / 315 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26378184
[Au] Autor:Robert ME; Linthicum FH
[Ad] Endereço:Pasadena, California, USA.
[Ti] Título:Empirical Derivation of Correction Factors for Human Spiral Ganglion Cell Nucleus and Nucleolus Count Units.
[So] Source:Otolaryngol Head Neck Surg;154(1):157-63, 2016 Jan.
[Is] ISSN:1097-6817
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Profile count method for estimating cell number in sectioned tissue applies a correction factor for double count (resulting from transection during sectioning) of count units selected to represent the cell. For human spiral ganglion cell counts, we attempted to address apparent confusion between published correction factors for nucleus and nucleolus count units that are identical despite the role of count unit diameter in a commonly used correction factor formula. STUDY DESIGN: We examined a portion of human cochlea to empirically derive correction factors for the 2 count units, using 3-dimensional reconstruction software to identify double counts. SETTING: The Neurotology and House Histological Temporal Bone Laboratory at University of California at Los Angeles. SUBJECTS AND METHODS: Using a fully sectioned and stained human temporal bone, we identified and generated digital images of sections of the modiolar region of the lower first turn of cochlea, identified count units with a light microscope, labeled them on corresponding digital sections, and used 3-dimensional reconstruction software to identify double-counted count units. RESULTS: For 25 consecutive sections, we determined that double-count correction factors for nucleus count unit (0.91) and nucleolus count unit (0.92) matched the published factors. We discovered that nuclei and, therefore, spiral ganglion cells were undercounted by 6.3% when using nucleolus count units. CONCLUSION: We determined that correction factors for count units must include an element for undercounting spiral ganglion cells as well as the double-count element. We recommend a correction factor of 0.91 for the nucleus count unit and 0.98 for the nucleolus count unit when using 20-µm sections.
[Mh] Termos MeSH primário: Estruturas do Núcleo Celular
Gânglio Espiral da Cóclea/citologia
[Mh] Termos MeSH secundário: Contagem de Células
Seres Humanos
Meia-Idade
Gânglio Espiral da Cóclea/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Em] Mês de entrada:1605
[Cu] Atualização por classe:170309
[Lr] Data última revisão:
170309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150918
[St] Status:MEDLINE
[do] DOI:10.1177/0194599815603964


  5 / 315 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:26286192
[Au] Autor:Lee JH; Jeong SA; Khadka P; Hong J; Chung IK
[Ad] Endereço:Departments of Systems Biology and Integrated Omics for Biomedical Science, Yonsei University, Seoul 120-749, Korea.
[Ti] Título:Involvement of SRSF11 in cell cycle-specific recruitment of telomerase to telomeres at nuclear speckles.
[So] Source:Nucleic Acids Res;43(17):8435-51, 2015 Sep 30.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Telomerase, a unique ribonucleoprotein complex that contains the telomerase reverse transcriptase (TERT), the telomerase RNA component (TERC) and the TERC-binding protein dyskerin, is required for continued cell proliferation in stem cells and cancer cells. Here we identify SRSF11 as a novel TERC-binding protein that localizes to nuclear speckles, subnuclear structures that are enriched in pre-messenger RNA splicing factors. SRSF11 associates with active telomerase enzyme through an interaction with TERC and directs it to nuclear speckles specifically during S phase of the cell cycle. On the other hand, a subset of telomeres is shown to be constitutively present at nuclear speckles irrespective of cell cycle phase, suggesting that nuclear speckles could be the nuclear sites for telomerase recruitment to telomeres. SRSF11 also associates with telomeres through an interaction with TRF2, which facilitates translocation of telomerase to telomeres. Depletion of SRSF11 prevents telomerase from associating with nuclear speckles and disrupts telomerase recruitment to telomeres, thereby abrogating telomere elongation by telomerase. These findings suggest that SRSF11 acts as a nuclear speckle-targeting factor that is essential for telomerase association with telomeres through the interactions with TERC and TRF2, and provides a potential target for modulating telomerase activity in cancer.
[Mh] Termos MeSH primário: Ciclo Celular
Estruturas do Núcleo Celular/enzimologia
Fatores de Processamento de Serina-Arginina/metabolismo
Telomerase/metabolismo
Telômero/enzimologia
[Mh] Termos MeSH secundário: Ciclo Celular/genética
Linhagem Celular Tumoral
Estruturas do Núcleo Celular/genética
Células HeLa
Seres Humanos
Domínios e Motivos de Interação entre Proteínas
RNA/metabolismo
Fatores de Processamento de Serina-Arginina/química
Telomerase/química
Homeostase do Telômero
Proteína 2 de Ligação a Repetições Teloméricas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (SFRS11 protein, human); 0 (Telomeric Repeat Binding Protein 2); 0 (telomerase RNA); 170974-22-8 (Serine-Arginine Splicing Factors); 63231-63-0 (RNA); EC 2.7.7.49 (Telomerase)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:160316
[Lr] Data última revisão:
160316
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150820
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkv844


  6 / 315 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:25870410
[Au] Autor:Yeoh LM; Goodman CD; Hall NE; van Dooren GG; McFadden GI; Ralph SA
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, Victoria 3010, Australia School of BioSciences, The University of Melbourne, Parkville, Victoria 3010, Australia.
[Ti] Título:A serine-arginine-rich (SR) splicing factor modulates alternative splicing of over a thousand genes in Toxoplasma gondii.
[So] Source:Nucleic Acids Res;43(9):4661-75, 2015 May 19.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Single genes are often subject to alternative splicing, which generates alternative mature mRNAs. This phenomenon is widespread in animals, and observed in over 90% of human genes. Recent data suggest it may also be common in Apicomplexa. These parasites have small genomes, and economy of DNA is evolutionarily favoured in this phylum. We investigated the mechanism of alternative splicing in Toxoplasma gondii, and have identified and localized TgSR3, a homologue of ASF/SF2 (alternative-splicing factor/splicing factor 2, a serine-arginine-rich, or SR protein) to a subnuclear compartment. In addition, we conditionally overexpressed this protein, which was deleterious to growth. qRT-PCR was used to confirm perturbation of splicing in a known alternatively-spliced gene. We performed high-throughput RNA-seq to determine the extent of splicing modulated by this protein. Current RNA-seq algorithms are poorly suited to compact parasite genomes, and hence we complemented existing tools by writing a new program, GeneGuillotine, that addresses this deficiency by segregating overlapping reads into distinct genes. In order to identify the extent of alternative splicing, we released another program, JunctionJuror, that detects changes in intron junctions. Using this program, we identified about 2000 genes that were constitutively alternatively spliced in T. gondii. Overexpressing the splice regulator TgSR3 perturbed alternative splicing in over 1000 genes.
[Mh] Termos MeSH primário: Processamento Alternativo
Proteínas Nucleares/metabolismo
Proteínas de Protozoários/metabolismo
Proteínas de Ligação a RNA/metabolismo
Toxoplasma/genética
[Mh] Termos MeSH secundário: Estruturas do Núcleo Celular/química
Expressão Gênica
Proteínas Nucleares/análise
Proteínas Nucleares/classificação
Proteínas Nucleares/genética
Plasmodium falciparum/genética
Proteínas de Protozoários/análise
Proteínas de Protozoários/classificação
Proteínas de Protozoários/genética
Proteínas de Ligação a RNA/análise
Proteínas de Ligação a RNA/classificação
Proteínas de Ligação a RNA/genética
Fatores de Processamento de Serina-Arginina
Software
Toxoplasma/crescimento & desenvolvimento
Toxoplasma/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Nuclear Proteins); 0 (Protozoan Proteins); 0 (RNA-Binding Proteins); 170974-22-8 (Serine-Arginine Splicing Factors)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150415
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkv311


  7 / 315 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:25848798
[Au] Autor:Sidik SM; Salsman J; Dellaire G; Rohde JR
[Ad] Endereço:Department of Microbiology and Immunology, Dalhousie University, Halifax, NS, Canada.
[Ti] Título:Shigella infection interferes with SUMOylation and increases PML-NB number.
[So] Source:PLoS One;10(4):e0122585, 2015.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Shigellosis is a severe diarrheal disease that affects hundreds of thousands of individuals resulting in significant morbidity and mortality worldwide. Shigellosis is caused by Shigella spp., a gram-negative bacterium that uses a Type 3 Secretion System (T3SS) to deliver effector proteins into the cytosol of infected human cells. Shigella infection triggers multiple signaling programs that result in a robust host transcriptional response that includes the induction of multiple proinflammatory cytokines. PML nuclear bodies (PML-NBs) are dynamic subnuclear structures that coordinate immune signaling programs and have a demonstrated role in controlling viral infection. We show that PML-NB number increases upon Shigella infection. We examined the effects of Shigella infection on SUMOylation and found that upon Shigella infection the localization of SUMOylated proteins is altered and the level of SUMOylated proteins decreases. Although Shigella infection does not alter the abundance of SUMO activating enzymes SAE1 or SAE2, it dramatically decreases the level of the SUMO conjugating enzyme Ubc9. All Shigella-induced alterations to the SUMOylation system are dependent upon a T3SS. Thus, we demonstrate that Shigella uses one or more T3SS effectors to influence both PML-NB number and the SUMOylation machinery in human cells.
[Mh] Termos MeSH primário: Estruturas do Núcleo Celular/metabolismo
Estruturas do Núcleo Celular/microbiologia
Shigella flexneri/fisiologia
Sumoilação
[Mh] Termos MeSH secundário: Estruturas do Núcleo Celular/imunologia
Células HeLa
Seres Humanos
Transporte Proteico
Proteína SUMO-1/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (SUMO-1 Protein); 0 (SUMO1 protein, human)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150408
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0122585


  8 / 315 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:25631093
[Au] Autor:Zheng Y; Gu H
[Ad] Endereço:Department of Biological Sciences, Wayne State University, Detroit, Michigan, USA.
[Ti] Título:Identification of three redundant segments responsible for herpes simplex virus 1 ICP0 to fuse with ND10 nuclear bodies.
[So] Source:J Virol;89(8):4214-26, 2015 Apr.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: Infected cell protein 0 (ICP0) of herpes simplex virus 1 (HSV-1) is a key regulator in both lytic and latent infections. In lytic infection, an important early event is the colocalization of ICP0 to nuclear domain 10 (ND10), the discrete nuclear bodies that impose restrictions on viral expression. ICP0 contains an E3 ubiquitin ligase that degrades promyelocytic leukemia protein (PML) and Sp100, two major components of ND10, and disperses ND10 to alleviate repression. We previously reported that the association between ICP0 and ND10 is a dynamic process that includes three steps: adhesion, fusion, and retention. ICP0 residues 245 to 474, defined as ND10 entry signal (ND10-ES), is a region required for the fusion step. Without ND10-ES, ICP0 adheres at the ND10 surface but fails to enter. In the present study, we focus on characterizing ND10-ES. Here we report the following. (i) Fusion of ICP0 with ND10 relies on specific sequences located within ND10-ES. Replacement of ND10-ES by the corresponding region from ORF61 of varicella-zoster virus did not rescue ND10 fusion. (ii) Three tandem ND10 fusion segments (ND10-FS1, ND10-FS2, and ND10-FS3), encompassing 200 amino acids within ND10-ES, redundantly facilitate fusion. Each of the three segments is sufficient to independently drive the fusion process, but none of the segments by themselves are necessary for ND10 fusion. Only when all three segments are deleted is fusion blocked. (iii) The SUMO interaction motif located within ND10-FS2 is not required for ND10 fusion but is required for the complete degradation of PML, suggesting that PML degradation and ND10 fusion are regulated by different molecular mechanisms. IMPORTANCE: ND10 nuclear bodies are part of the cell-intrinsic antiviral defenses that restrict viral gene expression upon virus infection. As a countermeasure, infected cell protein 0 (ICP0) of herpes simplex virus 1 (HSV-1) localizes to ND10s, degrades the ND10 organizer, and disperses ND10 components in order to alleviate repression. We studied the ICP0-ND10 association to delineate elements important for this dynamic interaction and to understand its role in viral replication and host defense. In this work, we show that ICP0 contains three redundant segments to ensure an effective mergence of ICP0 with ND10 nuclear bodies. This is the first study to systematically investigate ICP0 elements that are important for ICP0-ND10 fusion.
[Mh] Termos MeSH primário: Estruturas do Núcleo Celular/metabolismo
Regulação Viral da Expressão Gênica/fisiologia
Herpes Simples/genética
Proteínas Imediatamente Precoces/genética
Ubiquitina-Proteína Ligases/genética
[Mh] Termos MeSH secundário: Antígenos Nucleares/metabolismo
Autoantígenos/metabolismo
Western Blotting
Primers do DNA/genética
Regulação Viral da Expressão Gênica/genética
Herpes Simples/metabolismo
Seres Humanos
Proteínas Imediatamente Precoces/metabolismo
Imunoprecipitação
Microscopia Confocal
Proteínas Nucleares/metabolismo
Reação em Cadeia da Polimerase
Proteína da Leucemia Promielocítica
Fatores de Transcrição/metabolismo
Proteínas Supressoras de Tumor/metabolismo
Ubiquitina-Proteína Ligases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antigens, Nuclear); 0 (Autoantigens); 0 (DNA Primers); 0 (Immediate-Early Proteins); 0 (Nuclear Proteins); 0 (Promyelocytic Leukemia Protein); 0 (Transcription Factors); 0 (Tumor Suppressor Proteins); 135844-47-2 (Sp100 protein, human); 143220-95-5 (PML protein, human); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.3.2.27 (Vmw110 protein, Human herpesvirus 1)
[Em] Mês de entrada:1505
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150130
[St] Status:MEDLINE
[do] DOI:10.1128/JVI.03658-14


  9 / 315 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:25240882
[Au] Autor:Merry CR; Niland C; Khalil AM
[Ad] Endereço:Department of Biochemistry, Case Western Reserve University School of Medicine, Cleveland, OH, USA.
[Ti] Título:Diverse functions and mechanisms of mammalian long noncoding RNAs.
[So] Source:Methods Mol Biol;1206:1-14, 2015.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Long noncoding RNAs are becoming increasingly appreciated as major players in gene regulation. They have been reported to play diverse roles in many biological processes. Here, we discuss their discovery, features, and known functions in cells. While not comprehensive, this chapter should serve to illustrate the power and promise of studying long noncoding RNAs.
[Mh] Termos MeSH primário: Mamíferos/genética
RNA Longo não Codificante/fisiologia
[Mh] Termos MeSH secundário: Processamento Alternativo
Animais
Estruturas do Núcleo Celular/genética
Epigênese Genética
Feminino
Regulação da Expressão Gênica
Impressão Genômica
Seres Humanos
Neoplasias/genética
Doenças do Sistema Nervoso/genética
RNA Longo não Codificante/classificação
Inativação do Cromossomo X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Long Noncoding)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:151209
[Lr] Data última revisão:
151209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140922
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-1369-5_1


  10 / 315 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
[PMID]:25842866
[Au] Autor:Nosov GA; Kibanov MV; Olenina LV
[Ti] Título:[Dynamic properties of germinal granule ping-body in the testes of Drosophila melanogaster].
[So] Source:Mol Biol (Mosk);48(5):805-13, 2014 Sep-Oct.
[Is] ISSN:0026-8984
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:Here we investigated dynamic properties of the piNG-body, large perinuclear granule that was discovered previously in spermatocytes of Drosophila. The piNG-body contains ribonucleoprotein complexes involved in piRNA-silencing of genome repeats including transposons in premeiotic spermatocytes with aid of short piRNAs. Confocal microscopy of fixed and native preparations demonstrates that the piNG-body is mobile structure which does not occupy a stationary position near nuclear surface relative to chromosomal territories. FRAP-analysis reveals a high exchange rate of RNA helicase Vasa in the piNG-body and small perinuclear granules with the cytozol Vasa pool. Disruption of microtubule assembly of cytoskeleton does not affect to stability of the piNG-body and small granules. We suppose that the combination of piNG-body mobility and permanent molecular exchange of Vasa protein provides an efficient "scanning" of total volume of the cytoplasm of primary spermatocytes and timely recognition and destruction of unwanted transcripts of the repetitive elements of genome.
[Mh] Termos MeSH primário: Microcorpos/genética
Testículo/citologia
Testículo/fisiologia
[Mh] Termos MeSH secundário: Animais
Estruturas do Núcleo Celular/metabolismo
RNA Helicases DEAD-box/genética
RNA Helicases DEAD-box/metabolismo
Proteínas de Drosophila/genética
Proteínas de Drosophila/metabolismo
Drosophila melanogaster
Recuperação de Fluorescência Após Fotodegradação
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Masculino
Microcorpos/metabolismo
Microcorpos/ultraestrutura
Microscopia Confocal
Microtúbulos/metabolismo
RNA Interferente Pequeno
Ribonucleoproteínas/genética
Ribonucleoproteínas/metabolismo
Espermatócitos/metabolismo
Espermatócitos/ultraestrutura
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (RNA, Small Interfering); 0 (Ribonucleoproteins); 147336-22-9 (Green Fluorescent Proteins); EC 3.6.1.- (vas protein, Drosophila); EC 3.6.4.13 (DEAD-box RNA Helicases)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:150406
[Lr] Data última revisão:
150406
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150407
[St] Status:MEDLINE



página 1 de 32 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