Base de dados : MEDLINE
Pesquisa : A11.284.430.106.279.345.700 [Categoria DeCS]
Referências encontradas : 1497 [refinar]
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  1 / 1497 MEDLINE  
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[PMID]:28464286
[Au] Autor:García-Vilchis D; Aranda-Anzaldo A
[Ad] Endereço:Facultad de Medicina, Laboratorio de Biología Molecular y Neurociencias, Universidad Autónoma del Estado de México, Toluca 50180, Edo. Méx., Mexico.
[Ti] Título:DNA Length Modulates the Affinity of Fragments of Genomic DNA for the Nuclear Matrix In Vitro.
[So] Source:J Cell Biochem;118(12):4487-4497, 2017 Dec.
[Is] ISSN:1097-4644
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Classical observations have shown that during the interphase the chromosomal DNA of metazoans is organized in supercoiled loops attached to a compartment known as the nuclear matrix (NM). Fragments of chromosomal DNA able to bind the isolated NM in vitro are known as matrix associated/attachment/addressed regions or MARs. No specific consensus sequence or motif has been found that may constitute a universal, defining feature of MARs. On the other hand, high-salt resistant DNA-NM interactions in situ define true DNA loop anchorage regions or LARs, that might correspond to a subset of the potential MARs but are not necessarily identical to MARs characterized in vitro, since there are several examples of MARs able to bind the NM in vitro but which are not actually bound to the NM in situ. In the present work we assayed the capacity of two LARs, as well as of shorter fragments within such LARs, for binding to the NM in vitro. Paradoxically the isolated (≈2 kb) LARs cannot bind to the NM in vitro while their shorter (≈300 pb) sub-fragments and other non-related but equally short DNA fragments, bind to the NM in a high-salt resistant fashion. Our results suggest that the ability of a given DNA fragment for binding to the NM in vitro primarily depends on the length of the fragment, suggesting that binding to the NM is modulated by the local topology of the DNA fragment in suspension that it is known to depend on the DNA length. J. Cell. Biochem. 118: 4487-4497, 2017. © 2017 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: DNA/química
Hepatócitos/química
Regiões de Interação com a Matriz
Matriz Nuclear/química
[Mh] Termos MeSH secundário: Animais
DNA/metabolismo
Hepatócitos/metabolismo
Masculino
Matriz Nuclear/metabolismo
Ratos
Ratos Wistar
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9007-49-2 (DNA)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180102
[Lr] Data última revisão:
180102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1002/jcb.26106


  2 / 1497 MEDLINE  
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[PMID]:28724767
[Au] Autor:Klupp BG; Hellberg T; Granzow H; Franzke K; Dominguez Gonzalez B; Goodchild RE; Mettenleiter TC
[Ad] Endereço:Institute of Molecular Virology and Cell Biology, Friedrich-Loeffler-Institut, Greifswald-Insel Riems, Germany.
[Ti] Título:Integrity of the Linker of Nucleoskeleton and Cytoskeleton Is Required for Efficient Herpesvirus Nuclear Egress.
[So] Source:J Virol;91(19), 2017 Oct 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Herpesvirus capsids assemble in the nucleus, while final virion maturation proceeds in the cytoplasm. This requires that newly formed nucleocapsids cross the nuclear envelope (NE), which occurs by budding at the inner nuclear membrane (INM), release of the primary enveloped virion into the perinuclear space (PNS), and subsequent rapid fusion with the outer nuclear membrane (ONM). During this process, the NE remains intact, even at late stages of infection. In addition, the spacing between the INM and ONM is maintained, as is that between the primary virion envelope and nuclear membranes. The linker of nucleoskeleton and cytoskeleton (LINC) complex consists of INM proteins with a luminal SUN (Sad1/UNC-84 homology) domain connected to ONM proteins with a KASH (Klarsicht, ANC-1, SYNE homology) domain and is thought to be responsible for spacing the nuclear membranes. To investigate the role of the LINC complex during herpesvirus infection, we generated cell lines constitutively expressing dominant negative (dn) forms of SUN1 and SUN2. Ultrastructural analyses revealed a significant expansion of the PNS and the contiguous intracytoplasmic lumen, most likely representing endoplasmic reticulum (ER), especially in cells expressing dn-SUN2. After infection, primary virions accumulated in these expanded luminal regions, also very distant from the nucleus. The importance of the LINC complex was also confirmed by reduced progeny virus titers in cells expressing dn-SUN2. These data show that the intact LINC complex is required for efficient nuclear egress of herpesviruses, likely acting to promote fusion of primary enveloped virions with the ONM. While the viral factors for primary envelopment of nucleocapsids at the inner nuclear membrane are known to the point of high-resolution structures, the roles of cellular components and regulators remain enigmatic. Furthermore, the machinery responsible for fusion with the outer nuclear membrane is unsolved. We show here that dominant negative SUN2 interferes with efficient herpesvirus nuclear egress, apparently by interfering with fusion between the primary virion envelope and outer nuclear membrane. This identifies a new cellular component important for viral egress and implicates LINC complex integrity in nonconventional nuclear membrane trafficking.
[Mh] Termos MeSH primário: Transporte Ativo do Núcleo Celular/fisiologia
Citoesqueleto/metabolismo
Herpesviridae/crescimento & desenvolvimento
Membrana Nuclear/metabolismo
Matriz Nuclear/metabolismo
[Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular/genética
Animais
Linhagem Celular
Herpesviridae/metabolismo
Proteínas de Membrana/genética
Proteínas Associadas aos Microtúbulos/genética
Proteínas Nucleares/metabolismo
Coelhos
Suínos
Montagem de Vírus/fisiologia
Liberação de Vírus/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (Microtubule-Associated Proteins); 0 (Nuclear Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170721
[St] Status:MEDLINE


  3 / 1497 MEDLINE  
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[PMID]:27715428
[Au] Autor:Thorpe SD; Charpentier M
[Ad] Endereço:a Institute of Bioengineering, School of Engineering and Materials Science , Queen Mary University of London , London , UK.
[Ti] Título:Highlight on the dynamic organization of the nucleus.
[So] Source:Nucleus;8(1):2-10, 2017 Jan 02.
[Is] ISSN:1949-1042
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The last decade has seen rapid advances in our understanding of the proteins of the nuclear envelope, which have multiple roles including positioning the nucleus, maintaining its structural organization, and in events ranging from mitosis and meiosis to chromatin positioning and gene expression. Diverse new and stimulating results relating to nuclear organization and genome function from across kingdoms were presented in a session stream entitled "Dynamic Organization of the Nucleus" at this year's Society of Experimental Biology (SEB) meeting in Brighton, UK (July 2016). This was the first session stream run by the Nuclear Dynamics Special Interest Group, which was organized by David Evans, Katja Graumann (both Oxford Brookes University, UK) and Iris Meier (Ohio State University, USA). The session featured presentations on areas relating to nuclear organization across kingdoms including the nuclear envelope, chromatin organization, and genome function.
[Mh] Termos MeSH primário: Núcleo Celular/metabolismo
[Mh] Termos MeSH secundário: Animais
Cromatina/metabolismo
Genoma/genética
Seres Humanos
Membrana Nuclear/metabolismo
Matriz Nuclear/metabolismo
Células Vegetais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Chromatin)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170516
[Lr] Data última revisão:
170516
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161008
[St] Status:MEDLINE
[do] DOI:10.1080/19491034.2016.1243634


  4 / 1497 MEDLINE  
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[PMID]:27627025
[Au] Autor:Dobson JR; Hong D; Barutcu AR; Wu H; Imbalzano AN; Lian JB; Stein JL; van Wijnen AJ; Nickerson JA; Stein GS
[Ad] Endereço:Department of Cell and Developmental Biology, University of Massachusetts Medical School, Worcester, Massachusetts.
[Ti] Título:Identifying Nuclear Matrix-Attached DNA Across the Genome.
[So] Source:J Cell Physiol;232(6):1295-1305, 2017 Jun.
[Is] ISSN:1097-4652
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Experimental approaches to define the relationship between gene expression and nuclear matrix attachment regions (MARs) have given contrasting and method-specific results. We have developed a next generation sequencing strategy to identify MARs across the human genome (MAR-Seq). The method is based on crosslinking chromatin to its nuclear matrix attachment sites to minimize changes during biochemical processing. We used this method to compare nuclear matrix organization in MCF-10A mammary epithelial-like cells and MDA-MB-231 breast cancer cells and evaluated the results in the context of global gene expression (array analysis) and positional enrichment of gene-regulatory histone modifications (ChIP-Seq). In the normal-like cells, nuclear matrix-attached DNA was enriched in expressed genes, while in the breast cancer cells, it was enriched in non-expressed genes. In both cell lines, the chromatin modifications that mark transcriptional activation or repression were appropriately associated with gene expression. Using this new MAR-Seq approach, we provide the first genome-wide characterization of nuclear matrix attachment in mammalian cells and reveal that the nuclear matrix-associated genome is highly cell-context dependent. J. Cell. Physiol. 232: 1295-1305, 2017. © 2016 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: DNA/metabolismo
Genoma Humano
Regiões de Interação com a Matriz/genética
Matriz Nuclear/metabolismo
[Mh] Termos MeSH secundário: Neoplasias da Mama/genética
Linhagem Celular
Cromatina/metabolismo
Reagentes para Ligações Cruzadas/metabolismo
Feminino
Imunofluorescência
Regulação Neoplásica da Expressão Gênica
Histonas/metabolismo
Seres Humanos
Fases de Leitura Aberta/genética
Reprodutibilidade dos Testes
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromatin); 0 (Cross-Linking Reagents); 0 (Histones); 9007-49-2 (DNA)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160915
[St] Status:MEDLINE
[do] DOI:10.1002/jcp.25596


  5 / 1497 MEDLINE  
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[PMID]:28026824
[Au] Autor:Wasag P; Lenartowski R
[Ad] Endereço:Zaklad Genetyki, Wydzial Biologii i Ochrony Srodowiska, UMK w Toruniu; Pracownia Izotopowa i Analizy Instrumentalnej, Wydzial Biologii i Ochrony Srodowiska, UMK w Toruniu.
[Ti] Título:Nuclear matrix - structure, function and pathogenesis.
[So] Source:Postepy Hig Med Dosw (Online);70(0):1206-1219, 2016 Dec 20.
[Is] ISSN:1732-2693
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:The nuclear matrix (NM), or nuclear skeleton, is the non-chromatin, ribonucleoproteinaceous framework that is resistant to high ionic strength buffers, nonionic detergents, and nucleolytic enzymes. The NM fulfills a structural role in eukaryotic cells and is responsible for maintaining the shape of the nucleus and the spatial organization of chromatin. Moreover, the NM participates in several cellular processes, such as DNA replication/repair, gene expression, RNA transport, cell signaling and differentiation, cell cycle regulation, apoptosis and carcinogenesis. Short nucleotide sequences called scaffold/matrix attachment regions (S/MAR) anchor the chromatin loops to the NM proteins (NMP). The NMP composition is dynamic and depends on the cell type and differentiation stage or metabolic activity. Alterations in the NMP composition affect anchoring of the S/MARs and thus alter gene expression. This review aims to systematize information about the skeletal structure of the nucleus, with particular emphasis on the organization of the NM and its role in selected cellular processes. We also discuss several diseases that are caused by aberrant NM structure or dysfunction of individual NM elements.
[Mh] Termos MeSH primário: Replicação do DNA
Matriz Nuclear/metabolismo
[Mh] Termos MeSH secundário: Sequência de Bases
Núcleo Celular/metabolismo
Cromatina/metabolismo
Seres Humanos
Regiões de Interação com a Matriz
Neoplasias/metabolismo
Proteínas Nucleares/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Chromatin); 0 (Nuclear Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161228
[St] Status:MEDLINE


  6 / 1497 MEDLINE  
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[PMID]:27851952
[Au] Autor:Zhu Q; Zheng F; Liu AP; Qian J; Fu C; Lin Y
[Ad] Endereço:Department of Mechanical Engineering, The University of Hong Kong, Hong Kong SAR, China.
[Ti] Título:Shape Transformation of the Nuclear Envelope during Closed Mitosis.
[So] Source:Biophys J;111(10):2309-2316, 2016 Nov 15.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The nuclear envelope (NE) in lower eukaryotes such as Schizosaccharomyces pombe undergoes large morphology changes during closed mitosis. However, which physical parameters are important in governing the shape evolution of the NE, and how defects in the dividing chromosomes/microtubules are reflected in those parameters, are fundamental questions that remain unresolved. In this study, we show that improper separation of chromosomes in genetically deficient cells leads to membrane tethering or asymmetric division in contrast to the formation of two equal-sized daughter nuclei in wild-type cells. We hypothesize that the poleward force is transmitted to the nuclear membrane through its physical contact with the separated sister chromatids at the two spindle poles. A theoretical model is developed to predict the morphology evolution of the NE where key factors such as the work done by the poleward force and bending and surface energies stored in the membrane have been taken into account. Interestingly, the predicted phase diagram, summarizing the dependence of nuclear shape on the size of the load transmission regions, and the pole-to-pole distance versus surface area relationship all quantitatively agree well with our experimental observations, suggesting that this model captures the essential physics involved in closed mitosis.
[Mh] Termos MeSH primário: Mitose
Modelos Biológicos
Membrana Nuclear/metabolismo
[Mh] Termos MeSH secundário: Cromossomos Fúngicos/metabolismo
Matriz Nuclear/metabolismo
Schizosaccharomyces/citologia
Schizosaccharomyces/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171115
[Lr] Data última revisão:
171115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161117
[St] Status:MEDLINE


  7 / 1497 MEDLINE  
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[PMID]:27663546
[Au] Autor:Alfadhli A; Mack A; Harper L; Berk S; Ritchie C; Barklis E
[Ad] Endereço:Oregon Health & Sciences University, 3181 SW Sam Jackson Park Road, Portland, OR 97239, United States.
[Ti] Título:Analysis of quinolinequinone reactivity, cytotoxicity, and anti-HIV-1 properties.
[So] Source:Bioorg Med Chem;24(21):5618-5625, 2016 Nov 01.
[Is] ISSN:1464-3391
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We have analyzed a set of quinolinequinones with respect to their reactivities, cytotoxicities, and anti-HIV-1 properties. Most of the quinolinequinones were reactive with glutathione, and several acted as sulfhydryl crosslinking agents. Quinolinequinones inhibited binding of the HIV-1 matrix protein to RNA to varying degrees, and several quinolinequinones showed the capacity to crosslink HIV-1 matrix proteins in vitro, and HIV-1 structural proteins in virus particles. Cytotoxicity assays yielded quinolinequinone CC values in the low micromolar range, reducing the potential therapeutic value of these compounds. However, one compound, 6,7-dichloro-5,8-quinolinequinone potently inactivated HIV-1, suggesting that quinolinequinones may prove useful in the preparation of inactivated virus vaccines or for other virucidal purposes.
[Mh] Termos MeSH primário: Fármacos Anti-HIV/farmacologia
HIV-1/efeitos dos fármacos
Quinolinas/farmacologia
[Mh] Termos MeSH secundário: Fármacos Anti-HIV/síntese química
Fármacos Anti-HIV/química
Proliferação Celular/efeitos dos fármacos
Células Cultivadas
Relação Dose-Resposta a Droga
Células HEK293
Seres Humanos
Testes de Sensibilidade Microbiana
Estrutura Molecular
Matriz Nuclear/efeitos dos fármacos
Quinolinas/síntese química
Quinolinas/química
RNA Viral/antagonistas & inibidores
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-HIV Agents); 0 (Quinolines); 0 (RNA, Viral)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160925
[St] Status:MEDLINE


  8 / 1497 MEDLINE  
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[PMID]:27591260
[Au] Autor:Meier I
[Ad] Endereço:Department of Molecular Genetics and Center for RNA Biology, The Ohio State University, 520 Aronoff Laboratory, 318 W 12th Avenue, Columbus, OH 43210, USA meier.56@osu.edu.
[Ti] Título:LINCing the eukaryotic tree of life - towards a broad evolutionary comparison of nucleocytoplasmic bridging complexes.
[So] Source:J Cell Sci;129(19):3523-3531, 2016 Oct 01.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The nuclear envelope is much more than a simple barrier between nucleoplasm and cytoplasm. Nuclear envelope bridging complexes are protein complexes spanning both the inner and outer nuclear envelope membranes, thus directly connecting the cytoplasm with the nucleoplasm. In metazoans, they are involved in connecting the cytoskeleton with the nucleoskeleton, and act as anchoring platforms at the nuclear envelope for the positioning and moving of both nuclei and chromosomes. Recently, nucleocytoplasmic bridging complexes have also been identified in more evolutionarily diverse organisms, including land plants. Here, I discuss similarities and differences among and between eukaryotic supergroups, specifically of the proteins forming the cytoplasmic surface of these complexes. I am proposing a structure and function for a hypothetical ancestral nucleocytoplasmic bridging complex in the last eukaryotic common ancestor, with the goal to stimulate research in more diverse emerging model organisms.
[Mh] Termos MeSH primário: Citoesqueleto/metabolismo
Eucariotos/metabolismo
Evolução Molecular
Complexos Multiproteicos/metabolismo
Matriz Nuclear/metabolismo
[Mh] Termos MeSH secundário: Animais
Centrossomo/metabolismo
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Multiprotein Complexes)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170731
[Lr] Data última revisão:
170731
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160904
[St] Status:MEDLINE


  9 / 1497 MEDLINE  
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[PMID]:27307582
[Au] Autor:Auld AL; Folker ES
[Ad] Endereço:Department of Biology, Boston College, Chestnut Hill, MA 02467.
[Ti] Título:Nucleus-dependent sarcomere assembly is mediated by the LINC complex.
[So] Source:Mol Biol Cell;27(15):2351-9, 2016 08 01.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Two defining characteristics of muscle cells are the many precisely positioned nuclei and the linearly arranged sarcomeres, yet the relationship between these two features is not known. We show that nuclear positioning precedes sarcomere formation. Furthermore, ZASP-GFP, a Z-line protein, colocalizes with F-actin in puncta at the cytoplasmic face of nuclei before sarcomere assembly. In embryos with mispositioned nuclei, ZASP-GFP is still recruited to the nuclei before its incorporation into sarcomeres. Furthermore, the first sarcomeres appear in positions close to the nuclei, regardless of nuclear position. These data suggest that the interaction between sarcomere proteins and nuclei is not dependent on properly positioned nuclei. Mechanistically, ZASP-GFP localization to the cytoplasmic face of the nucleus did require the linker of nucleoskeleton and cytoskeleton (LINC) complex. Muscle-specific depletion of klarsicht (nesprin) or klariod (SUN) blocked the recruitment of ZASP-GFP to the nucleus during the early stages of sarcomere assembly. As a result, sarcomeres were poorly formed and the general myofibril network was less stable, incomplete, and/or torn. These data suggest that the nucleus, through the LINC complex, is crucial for the proper assembly and stability of the sarcomere network.
[Mh] Termos MeSH primário: Sarcômeros/metabolismo
Sarcômeros/fisiologia
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/metabolismo
Actinas/metabolismo
Animais
Proteínas de Transporte/metabolismo
Núcleo Celular/metabolismo
Citoesqueleto/metabolismo
Drosophila/metabolismo
Proteínas de Drosophila/metabolismo
Proteínas com Domínio LIM/metabolismo
Proteínas de Membrana Transportadoras/metabolismo
Proteínas dos Microfilamentos/metabolismo
Microtúbulos/metabolismo
Miofibrilas/metabolismo
Proteínas do Tecido Nervoso/metabolismo
Matriz Nuclear/metabolismo
Proteínas Nucleares/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Actins); 0 (Carrier Proteins); 0 (Drosophila Proteins); 0 (LIM Domain Proteins); 0 (Membrane Transport Proteins); 0 (Microfilament Proteins); 0 (Nerve Tissue Proteins); 0 (Nuclear Proteins); 0 (Zasp protein, Drosophila); 0 (klar protein, Drosophila)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171125
[Lr] Data última revisão:
171125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160617
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E16-01-0021


  10 / 1497 MEDLINE  
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[PMID]:27081072
[Au] Autor:Kosinski J; Mosalaganti S; von Appen A; Teimer R; DiGuilio AL; Wan W; Bui KH; Hagen WJ; Briggs JA; Glavy JS; Hurt E; Beck M
[Ad] Endereço:Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
[Ti] Título:Molecular architecture of the inner ring scaffold of the human nuclear pore complex.
[So] Source:Science;352(6283):363-5, 2016 Apr 15.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nuclear pore complexes (NPCs) are 110-megadalton assemblies that mediate nucleocytoplasmic transport. NPCs are built from multiple copies of ~30 different nucleoporins, and understanding how these nucleoporins assemble into the NPC scaffold imposes a formidable challenge. Recently, it has been shown how the Y complex, a prominent NPC module, forms the outer rings of the nuclear pore. However, the organization of the inner ring has remained unknown until now. We used molecular modeling combined with cross-linking mass spectrometry and cryo-electron tomography to obtain a composite structure of the inner ring. This architectural map explains the vast majority of the electron density of the scaffold. We conclude that despite obvious differences in morphology and composition, the higher-order structure of the inner and outer rings is unexpectedly similar.
[Mh] Termos MeSH primário: Complexo de Proteínas Formadoras de Poros Nucleares/metabolismo
Poro Nuclear/metabolismo
Poro Nuclear/ultraestrutura
[Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular
Microscopia Crioeletrônica
Tomografia com Microscopia Eletrônica
Células HeLa
Seres Humanos
Espectrometria de Massas
Modelos Moleculares
Matriz Nuclear/metabolismo
Matriz Nuclear/ultraestrutura
Complexo de Proteínas Formadoras de Poros Nucleares/química
Complexo de Proteínas Formadoras de Poros Nucleares/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Nuclear Pore Complex Proteins); 0 (Nup93 protein, human)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:170418
[Lr] Data última revisão:
170418
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160416
[St] Status:MEDLINE
[do] DOI:10.1126/science.aaf0643



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