Ted Hupp
Chair of Cancer Research
- Cancer Research UK Edinburgh Centre
- MRC Institute of Genetics & Molecular Medicine
Contact details
- Tel: +44 (0)131 651 8500
- Email: Ted.Hupp@ed.ac.uk
Address
- Street
-
Cancer Research UK Edinburgh Centre
MRC Institute of Genetics & Molecular Medicine
The University of Edinburgh
Western General Hospital
Crewe Road South - City
- Edinburgh
- Post code
- EH4 2XR
Background
Ted trained in Chemistry as an undergraduate at Bowling Green State University (Ohio USA) and acquired a PhD in the enzymology of protein-DNA interactions under supervision of Jon Kaguni at Michigan State University (USA). Interests in enzymology was applied to the p53 tumour suppressor protein working with David Lane in Dundee (UK) at the time when the p53 field developed its key concepts including p53’s transcription activation function, p53’s amenability to re-activation by biologics like peptides or monoclonal antibodies, and p53 protein regulation by covalent modifications like ubiquitination, acetylation, and phosphorylation. The Hupp lab is now building on this fundamental knowledge of the p53 pathway to identify dominant pro-oncogenic signals that inactivate p53 in human cancers.
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Emergent Role of IFITM1/3 towards Splicing Factor (SRSF1) and Antigen-Presenting Molecule (HLA-B) in Cervical Cancer
In:
Biomolecules, vol. 12, pp. 1090
DOI: https://doi.org/10.3390/biom12081090
Research output: Contribution to Journal › Article (E-pub ahead of print) -
Comparison of ATP-binding pockets and discovery of homologous recombination inhibitors
(10 pages)
In:
Bioorganic and Medicinal Chemistry, vol. 70
DOI: https://doi.org/10.1016/j.bmc.2022.116923
Research output: Contribution to Journal › Article (E-pub ahead of print) -
Multiparametric High-Content Cell Painting Identifies Copper Ionophores as Selective Modulators of Esophageal Cancer Phenotypes
In:
Acs chemical biology
DOI: https://doi.org/10.1021/acschembio.2c00301
Research output: Contribution to Journal › Article (E-pub ahead of print) -
Gorham-Stout case report: a multi-omic analysis reveals recurrent fusions as new potential drivers of the disease
In:
BMC Medical Genomics, vol. 15, pp. 128
DOI: https://doi.org/10.1186/s12920-022-01277-x
Research output: Contribution to Journal › Article (Published) -
Self-derived peptides from the SARS-CoV-2 spike glycoprotein disrupting shaping and stability of the homotrimer unit
In:
Biomedicine and Pharmacotherapy, vol. 151
DOI: https://doi.org/10.1016/j.biopha.2022.113190
Research output: Contribution to Journal › Article (E-pub ahead of print)