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@igmm.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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An allostatic mechanism for M2 pyruvate kinase as an amino-acid sensor
(17 pages)
In:
Biochemical Journal, vol. 475, no. 10, pp. 1821-1837
DOI: https://doi.org/10.1042/BCJ20180171
Contribution To journal › Article (E-pub ahead of print) -
Evidence for allosteric effects on p53 oligomerization induced by phosphorylation
(8 pages)
In:
Protein Science, vol. 27, no. 2, pp. 523-530
DOI: https://doi.org/10.1002/pro.3344
Contribution To journal › Article (Published) -
The sequence-specific peptide-binding activity of the protein sulfide isomerase AGR2 directs its stable binding to the oncogenic receptor EpCAM
In:
Molecular and Cellular Proteomics
DOI: https://doi.org/10.1074/mcp.RA118.000573
Contribution To journal › Article (E-pub ahead of print) -
Mono-substituted Hydrocarbon Diastereomer Combinations Reveal Stapled Peptides with High Structural Fidelity
In:
Chemistry - A European Journal
DOI: https://doi.org/10.1002/chem.201705983
Contribution To journal › Article (E-pub ahead of print) -
Regulation of Transcriptional Activators by DNA-Binding Domain Ubiquitination
In:
Cell Death and Differentiation
DOI: https://doi.org/10.1038/cdd.2017.42
Contribution To journal › Article (Published)