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  1. Book ; Online ; Thesis: Funktionelle Charakterisierung der C-terminalen Domänen des Korepressors N-CoR

    Ducasse, Miryam

    2006  

    Author's details von Miryam Ducasse
    Language English
    Size Online-Ressource
    Document type Book ; Online ; Thesis
    Thesis / German Habilitation thesis Univ., Diss--Frankfurt (Main), 2006
    Database Former special subject collection: coastal and deep sea fishing

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  2. Book ; Online ; Thesis: Funktionelle Charakterisierung der C-terminalen Domänen des Korepressors N-CoR

    Ducasse, Miryam [Verfasser]

    2006  

    Author's details von Miryam Ducasse
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language English
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  3. Article ; Online: Altered stoichiometry and nuclear delocalization of NonO and PSF promote cellular senescence.

    Huang, Ching-Jung / Das, Utsab / Xie, Weijun / Ducasse, Miryam / Tucker, Haley O

    Aging

    2017  Volume 8, Issue 12, Page(s) 3356–3374

    Abstract: While cellular senescence is a critical mechanism to prevent malignant transformation of potentially mutated cells, persistence of senescent cells can also promote cancer and aging phenotypes. NonO/p54nrb and PSF are multifunctional hnRNPs typically ... ...

    Abstract While cellular senescence is a critical mechanism to prevent malignant transformation of potentially mutated cells, persistence of senescent cells can also promote cancer and aging phenotypes. NonO/p54nrb and PSF are multifunctional hnRNPs typically found as a complex exclusively within the nuclei of all mammalian cells. We demonstrate here that either increase or reduction of expression of either factor results in cellular senescence. Coincident with this, we observe expulsion of NonO and PSF-containing nuclear paraspeckles and posttranslational modification at G2/M. That senescence is mediated most robustly by overexpression of a cytoplasmic C-truncated form of NonO further indicated that translocation of NonO and PSF from the nucleus is critical to senescence induction. Modulation of NonO and PSF expression just prior to or coincident with senescence induction disrupts the normally heterodimeric NonO-PSF nuclear complex resulting in a dramatic shift in stoichiometry to heterotetramers and monomer with highest accumulation within the cytoplasm. This is accompanied by prototypic cell cycle checkpoint activation and chromatin condensation. These observations identify yet another role for these multifunctional factors and provide a hitherto unprecedented mechanism for cellular senescence and nuclear-cytoplasmic trafficking.
    MeSH term(s) Animals ; Cell Line ; Cellular Senescence/physiology ; Cytoplasm/physiology ; DNA Damage ; Gene Expression Regulation ; Humans ; Mitosis ; Mutation ; Nuclear Matrix-Associated Proteins/genetics ; Nuclear Matrix-Associated Proteins/metabolism ; Octamer Transcription Factors/genetics ; Octamer Transcription Factors/metabolism ; PTB-Associated Splicing Factor/genetics ; PTB-Associated Splicing Factor/metabolism ; Plasmids ; Protein Processing, Post-Translational ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Telomere Shortening ; Transformation, Genetic ; Up-Regulation
    Chemical Substances NONO protein, human ; Nuclear Matrix-Associated Proteins ; Octamer Transcription Factors ; PTB-Associated Splicing Factor ; RNA-Binding Proteins
    Language English
    Publishing date 2017-01-27
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 1945-4589
    ISSN (online) 1945-4589
    DOI 10.18632/aging.101125
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Epigenetic aberrations and cancer.

    Ducasse, Miryam / Brown, Mark A

    Molecular cancer

    2006  Volume 5, Page(s) 60

    Abstract: The correlation between epigenetic aberrations and disease underscores the importance of epigenetic mechanisms. Here, we review recent findings regarding chromatin modifications and their relevance to cancer. ...

    Abstract The correlation between epigenetic aberrations and disease underscores the importance of epigenetic mechanisms. Here, we review recent findings regarding chromatin modifications and their relevance to cancer.
    MeSH term(s) Adenosine Triphosphate/metabolism ; Animals ; Chromatin/chemistry ; Chromatin/metabolism ; DNA Methylation ; Epigenesis, Genetic ; Gene Expression Regulation ; Histones/metabolism ; Humans ; Mice ; Neoplasms/genetics ; Nucleosomes/chemistry ; RNA, Untranslated/physiology
    Chemical Substances Chromatin ; Histones ; Nucleosomes ; RNA, Untranslated ; Adenosine Triphosphate (8L70Q75FXE)
    Language English
    Publishing date 2006-11-08
    Publishing country England
    Document type Journal Article ; Review
    ISSN 1476-4598
    ISSN (online) 1476-4598
    DOI 10.1186/1476-4598-5-60
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Inter-library loan at ZB MED

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  5. Article ; Online: Epigenetic aberrations and cancer

    Brown Mark A / Ducasse Miryam

    Molecular Cancer, Vol 5, Iss 1, p

    2006  Volume 60

    Abstract: Abstract The correlation between epigenetic aberrations and disease underscores the importance of epigenetic mechanisms. Here, we review recent findings regarding chromatin modifications and their relevance to cancer. ...

    Abstract Abstract The correlation between epigenetic aberrations and disease underscores the importance of epigenetic mechanisms. Here, we review recent findings regarding chromatin modifications and their relevance to cancer.
    Keywords Neoplasms. Tumors. Oncology. Including cancer and carcinogens ; RC254-282 ; Internal medicine ; RC31-1245 ; Medicine ; R ; DOAJ:Oncology ; DOAJ:Medicine (General) ; DOAJ:Health Sciences
    Language English
    Publishing date 2006-11-01T00:00:00Z
    Publisher BioMed Central
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  6. Article: SUMOylation of the corepressor N-CoR modulates its capacity to repress transcription.

    Tiefenbach, Jens / Novac, Natalia / Ducasse, Miryam / Eck, Maresa / Melchior, Frauke / Heinzel, Thorsten

    Molecular biology of the cell

    2006  Volume 17, Issue 4, Page(s) 1643–1651

    Abstract: In the absence of ligands the corepressor N-CoR mediates transcriptional repression by some nuclear hormone receptors. Several protein-protein interactions of N-CoR are known, of which mainly complex formation with histone deacetylases (HDACs) leads to ... ...

    Abstract In the absence of ligands the corepressor N-CoR mediates transcriptional repression by some nuclear hormone receptors. Several protein-protein interactions of N-CoR are known, of which mainly complex formation with histone deacetylases (HDACs) leads to the repression of target genes. On the other hand, the role of posttranslational modifications in corepressor function is not well established. Here, we show that N-CoR is modified by Sumo-1. We found SUMO-E2-conjugating enzyme Ubc9 and SUMO-E3 ligase Pias1 as novel N-CoR interaction partners. The SANT1 domain of N-CoR was found to mediate this interaction. We show that K152, K1117, and K1330 of N-CoR can be conjugated to SUMO and that mutation of all sites is necessary to fully block SUMOylation in vitro. Because these lysine residues are located within repression domains I and III, respectively, we investigated a possible correlation between the functions of the repression domains and SUMOylation. Coexpression of Ubc9 protein resulted in enhanced N-CoR-dependent transcriptional repression. Studies using SUMOylation-deficient N-CoR RDI mutants suggest that SUMO modification contributes to repression by N-CoR. Mutation of K152 to R in RD1, for example, not only significantly reduced repression of a reporter gene, but also abolished the effect of Ubc9 on transcriptional repression.
    MeSH term(s) Amino Acid Sequence ; Animals ; Mice ; Mucoproteins/chemistry ; Mucoproteins/genetics ; Mucoproteins/metabolism ; Mutation ; Nuclear Proteins/chemistry ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Nuclear Receptor Co-Repressor 1 ; Protein Inhibitors of Activated STAT/metabolism ; Protein Modification, Translational ; Protein Structure, Tertiary ; Repressor Proteins/chemistry ; Repressor Proteins/genetics ; Repressor Proteins/metabolism ; SUMO-1 Protein/metabolism ; Transcription, Genetic ; Two-Hybrid System Techniques ; Ubiquitin-Conjugating Enzymes/metabolism
    Chemical Substances Mucoproteins ; Ncor1 protein, mouse ; Nuclear Proteins ; Nuclear Receptor Co-Repressor 1 ; Protein Inhibitors of Activated STAT ; Repressor Proteins ; SUMO-1 Protein ; lysin, gastropoda ; Ubiquitin-Conjugating Enzymes (EC 2.3.2.23) ; ubiquitin-conjugating enzyme UBC9 (EC 6.3.2.-)
    Language English
    Publishing date 2006-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E05-07-0610
    Database MEDical Literature Analysis and Retrieval System OnLINE

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