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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The immunopeptidome from a genomic perspective: Establishing the noncanonical landscape of MHC class I–associated peptides
(39 pages)
In:
Cancer Immunology Research, pp. 1-40
DOI: https://doi.org/10.1158/2326-6066.CIR-22-0621
Research output: Contribution to Journal › Article (E-pub ahead of print) -
Development of monoclonal antibodies targeting canine PD-L1 and PD-1 and their clinical relevance in Canine Apocrine Gland Anal Sac Adenocarcinoma
In:
Cancers, vol. 14
DOI: https://doi.org/10.3390/cancers14246188
Research output: Contribution to Journal › Article (E-pub ahead of print) -
Next-generation sequencing of a combinatorial peptide phage library screened against ubiquitin identifies peptide aptamers that can inhibit the in vitro ubiquitin transfer cascade
In:
Frontiers in Microbiology, vol. 13
DOI: https://doi.org/10.3389/fmicb.2022.875556
Research output: Contribution to Journal › Article (E-pub ahead of print) -
Identification of novel interferon responsive protein partners of human leukocyte antigen A (HLA-A) using cross-linking mass spectrometry (CLMS) approach
In:
Scientific Reports, vol. 12
DOI: https://doi.org/10.1038/s41598-022-21393-z
Research output: Contribution to Journal › Article (Published) -
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 (Published)