14th International Conference on the Chemistry of Antibiotics and other Bioactive Compounds, 13-16 October 2015, Texas, USA


Philip Thomas, University of Texas, Southwestern Medical Center, USA

Philip ThomasI have a thirty year-long interest in the molecular basis of disease and assay development for discovery biology.    In my laboratory, over the past twenty two years, we have focused, utilizing biochemical and biophysical approaches, on understanding aberrant protein folding and regulation of protein expression as a basis of disease.  Significant results from these efforts include description of the folding defect of mutant CFTR that is the molecular basis of most cases of CF, structural determination of the ATP binding domain of CFTR, elucidation of the mechano-chemistry of CFTR and related ABC transporters, and related structural studies of the regulation of CFTR gating by the R domain.  Related to these interests are parallel studies of quality control and the regulation of expression of disease associated proteins.  Our studies have shed light on the recognition of substrates, including alpha synuclein, by the 20S proteasome—providing mechanistic insight into the protease and revealing the contribution of partial degradation to the disease process.  The group also has developed facile assays for monitoring protein folding and production and has utilized these to identify small molecule “correctors” of mutant CFTR folding and establish a connection between SOD1 and TDP43 two proteins that misfold in amyotrophic lateral sclerosis, revealing a novel pathway for possible therapeutic intervention.

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Supporting Journal

Bioorganic & Medicinal Chemistry Letters