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Showing 1 to 5 of 5 for “"histone reader"”.

  1. Role of P300 Zz Domain In Chromatin Association and Histone Acetylation

    … to bind to chromatin and to acetylate the histone substrates. However, the molecular mechanisms underlying the regulation of these processes are not fully understood.</p> <p>Through combination of various biochemical, biophysical and molecular approaches, we show that the ZZ-type zinc …

    uthsc Repository record for Role of P300 Zz Domain In Chromatin Association and Histone Acetylation (opens in a new tab)

  2. Trim24 As An Oncogene In The Mammary Gland

    … acts as a co-regulator of estrogen receptor, a histone reader with tandem PHD and Bromo domains, and a ubiquitin E3-ligase targeting p53 by its RING domain. TRIM24 is over-expressed in human breast cancers, which is correlated with poor patient survival. Previous in cellulo studies in our lab …

    uthsc Repository record for Trim24 As An Oncogene In The Mammary Gland (opens in a new tab)

  3. Trim24 Promotes Mammary Tumor Development By Upregulating Metabolic Reducing Power

    … for p53, a nuclear receptor co-regulator, and a histone reader. Over expression of TRIM24 correlates with poor overall survival of breast cancer patients. Previously, our lab created a mouse model that conditionally over-expresses (COE) TRIM24 protein in mammary epithelia …

    uthsc Repository record for Trim24 Promotes Mammary Tumor Development By Upregulating Metabolic Reducing Power (opens in a new tab)

  4. Trim24 Orchestrates Metabolic Reprogramming and Emt In Breast Cancer

    … of nuclear receptors and a PHD/Bromodomain reader of specific histone modifications. TRIM24 expression correlates with poor prognosis of breast cancer, but the mechanisms of TRIM24-mediated oncogenesis are unknown. In the first part of my thesis, I found that TRIM24 is aberrantly expressed …

    uthsc Repository record for Trim24 Orchestrates Metabolic Reprogramming and Emt In Breast Cancer (opens in a new tab)

  5. Structural Insights into the Mechanisms Controlling the Modification and the Readout of Histone H3.1

    The histone H3.1 is the canonical histone H3 inserted into new nucleosomes during replication. The unstructured N-terminal region (also referred to as the tail) of histone H3.1 is decorated by many post-translational modifications (PTMs). These PTMs serve as epigenetic signals coordinating …

    ottawa-retro Repository record for Structural Insights into the Mechanisms Controlling the Modification and the Readout of Histone H3.1 (opens in a new tab)