Browsing by Subject "p53"
Now showing items 1-6 of 6
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Characterization of Structures and Dynamics of Intrinsically Disordered Domain and Proteins Using Time Resolved-Hydrogen Deuterium Exchange Mass Spectrometry
(2017-07-27)Proteins are inherently dynamic. Virtually all of the processes that underlie biological activity, including binding partner recognition, catalysis and allostery among many others, require transient adoption of specific ... -
Identifying Substrates, Interacting Partners and Cofactors of Pirh2: Characterizing the Pirh2-PKCdelta Interaction
(2014-07-09)p53 is a central player in the cellular response to stress, allowing cells to cope in the presence of diverse stress signals including DNA damage and oncogene activation. In response to stress, p53 acts as a transcription ... -
Investigating the Anti-Cancer Effects of Small Molecule MEI-1 as a Potential MDM2 Inhibitor
(2021-11-15)MDM2 is an oncogenic E3 ligase found to be overexpressed in a number of human cancers, leading to poor prognosis. MDM2 overexpression inhibits the function of the tumour suppressor p53, which ubiquitinates p53 and tags it ... -
Investigation of EPO-Mediated Rescue From P53-Dependent Apoptosis in DA3-EPOR Cells
(2016-11-25)The usage of recombinant human erythropoietin in clinics to treat cancer-associated anemia has shown unfortunate unforeseen tumour response to cytokine treatment. Although other cytokines have previously been shown to have ... -
Mechanisms of p53-induced mitochondrial biogenesis in skeletal muscle
p53 is a pleiotropic protein that is mutated in many types of cancers. It is involved in regulating various distinct cellular pathways including apoptosis, cell cycle arrest, senescence, autophagy, angiogenesis, and most ... -
Structural and Functional Characterization of the Human Mdm2 and MdmX RING Domains
(2015-08-28)Human E3 ligase Mdm2 is an oncogene. Its amplification and overexpression have been found in many types of cancers. Mdm2 inhibits tumour suppressor p53 by regulating its stability through Mdm2 RING-mediated ubiquitination. ...