Contact information
adan.pintofernandez@ndm.ox.ac.uk
COI-The Wellcome Centre for Human Genetics and NDM Research Building, Old Road Campus
Adán Pinto-Fernández
PhD
Career Development Fellow at Chinese Academy of Medical Sciences Oxford Institute (CAMS) - Nuffield Department of Medicine
TRANSLATIONAL STUDIES OF THE UBIQUITIN SYSTEM - CANCER IMMUNOLOGY
Current research involves the study of the roles of a class of druggable enzymes called deubiquitylating enzymes (DUBs) in cancer inflammation using advanced proteomics, lipidomics, and immunology techniques as main tools.
For instance, we have recently discovered that cancer cells lacking the DUB USP18, a negative regulator of the interferon pathway, are more antigenic and radiosensitive. At a molecular level, USP18-deficient cells accumulate innate immune ligands such as dsRNA, enhance the antigen presentation machinery, and hence they can activate more efficiently cytotoxic T cells, resulting in enhanced T cell killing and immunotherapy responses.
Pinto-Fernandez, A., Salio, M., Partridge, T. et al. Deletion of the deISGylating enzyme USP18 enhances tumour cell antigenicity and radiosensitivity. Br J Cancer 124, 817–830 (2021). https://doi.org/10.1038/s41416-020-01167-y
Recent publications
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Covalent Fragment Screening and Optimization Identifies the Chloroacetohydrazide Scaffold as Inhibitors for Ubiquitin C-terminal Hydrolase L1
Journal article
Imhoff RD. et al, (2024), Journal of Medicinal Chemistry
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USP16 is an ISG15 cross-reactive deubiquitinase targeting a subset of metabolic pathway-related proteins
Preprint
Gan J. et al, (2023)
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Structural basis for SMAC-mediated antagonism of caspase inhibition by the giant ubiquitin ligase BIRC6
Journal article
Dietz L. et al, (2023), Science, 379, 1112 - 1117
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Structural Premise of Selective Deubiquitinase USP30 Inhibition by Small-Molecule Benzosulfonamides
Preprint
O’Brien DP. et al, (2022)
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Structural basis for antagonism of the ubiquitin ligase BIRC6 by SMAC
Preprint
Dietz L. et al, (2022)