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Showing 1 to 8 of 8 for “"CoREST"”.

  1. P120-Catenin Regulates Rest and Corest, and Modulates Mouse Embryonic Stem Cell Differentiation

    … binds to and negatively regulates REST and CoREST, that others have indicated form a repressive complex having diverse key roles in developmental and pathologic gene regulation. We thus provide the first evidence for a direct upstream modulator of REST/CoREST function. Using mouse embryonic …

    uthsc Repository record for P120-Catenin Regulates Rest and Corest, and Modulates Mouse Embryonic Stem Cell Differentiation (opens in a new tab)

  2. Efforts to Elucidate the Binding Interaction between Lysine-Specific Demethylase 1 (LSD1/KDM1) and CoREST and Their Roles in Breast Cancer

    … with a number of co-regulatory proteins. CoREST is one such important binding protein that endows LSD1 with the ability to associate with and demethylate nucleosomal substrates. </p><p>Given the significance of CoREST in directing LSD1 activity, herein we report our efforts to regulate …

    duke Repository record for Efforts to Elucidate the Binding Interaction between Lysine-Specific Demethylase 1 (LSD1/KDM1) and CoREST and Their Roles in Breast Cancer (opens in a new tab)

  3. Analysis and suppression of mutant sel-12 in Caenorhabditis elegans

    … is found to be an integral component of the CoREST transcriptional co-repressor complex. Further analysis of the other spr genes revealed that SPR-1 is the C. elegans homolog of the human CoREST protein, which is also a component of the CoREST complex. Based on the physical interaction of …

    lmu-germany Repository record for Analysis and suppression of mutant sel-12 in Caenorhabditis elegans (opens in a new tab)

  4. Characterisation of oncogenic pathways driving the pathogenesis of prostate cancer

    … demonstrated that TBX2 interacts with CoREST complex members LSD1 and ZNF217 and ChIP qPCR confirmed TBX2 shRNA reduced ZNF217 recruitment to E-cadherin and NDRG1 promoters. In accordance, targeting the LSD1/ZNF217 interaction via an allosteric LSD1 inhibitor phenocopied TBX2 knockdown …

    qu-belfast Repository record for Characterisation of oncogenic pathways driving the pathogenesis of prostate cancer (opens in a new tab)

  5. Simulating biochemical physics with computers

    … demethylase (LSD1) in complex with CoREST and protein-substrate interactions of LSD1 with histone H3 tail. MD simulations of LSD1•CoREST complex bound to a 16 a.a. of the Nterminal H3-tail peptide (H3-p16) were carried out using NAMD to study the conformational flexibility of the …

    umn Repository record for Simulating biochemical physics with computers (opens in a new tab)

  6. Lysine Specific Demethylase-1 and the Brahma Chromatin Remodeling Complex Regulate Conserved Signaling Pathways During Drosophila Wing Development

    … loss of Co-RE1 Silencing Transcription Factor (CoREST), an accessory protein required for LSD1 demethylase activity, results in a similar wing patterning phenotypes, suggesting that demethylase activity is required for proper cell-fate specification. By utilizing a variety of biochemical and …

    loyola-thes Repository record for Lysine Specific Demethylase-1 and the Brahma Chromatin Remodeling Complex Regulate Conserved Signaling Pathways During Drosophila Wing Development (opens in a new tab)

  7. Studies of the MYM-type zinc finger protein ZMYM3

    … deacetylase, LSD1, a histone demethylase, CoREST, a co-repressor of transcription, TFII-I, a transcription factor, and ZMYM3, an MYM-type zinc finger protein of unknown function. By making several truncation mutants of ZMYM3, I show that a C-terminal region containing a ‘PXP’ repeat motif …

    cambridge Repository record for Studies of the MYM-type zinc finger protein ZMYM3 (opens in a new tab)

  8. Functional characterization of CDY family proteins and their role in recognition of the heterochromatic histone H3K9me3 modification

    … (HDAC1, HDAC2) oder dem Repressorkomplex CoREST erreicht wird. Interessanterweise konnte in der vorliegenden Doktorarbeit ein weiterer Interaktionspartner von CDYL1 identifiziert werden: PRMT5. PRMT5 ist eine Argininmethyltransferase und in vitro Experimente bestätigen, dass PRMT5 CDYL1 …

    goettingen Repository record for Functional characterization of CDY family proteins and their role in recognition of the heterochromatic histone H3K9me3 modification (opens in a new tab)