Hogg Laboratory
Proteins are responsible for all of life’s processes. The Hogg Laboratory investigates how proteins work in health and disease, focusing on a type of regulation that they discovered involving the disulphide bonds in proteins.
About the Hogg Laboratory
Protein structure is defined by two types of covalent bonds: the peptide bonds that link the amino acid residues and disulphide bonds that link pairs of cysteine amino acids. Since the discovery of disulphide bonds 60 years ago they were long thought to be fully formed and inert in the mature protein. The Hogg lab has discovered that disulphide bonds are neither fully formed nor inert in proteins and are remarkably dynamic bonds that control protein function. They are focused on understanding this biology and exploiting it for new treatments for cancer. They have developed novel diagnostics and therapeutics that are being trialled in cancer patients and have led to three spin-out companies.
Centre for Cancer Innovations
- Biochemistry
- Cancer drug development
- Protein chemistry
- Cell biology
- Medical imaging
Disulfide bonds as switches for protein function
Allosteric Disulfide Bonds
Phosphoglycerate kinase acts in tumour angiogenesis as a disulphide reductase
A first-in-human study of [68Ga]Ga-CDI: a positron emitting radiopharmaceutical for imaging tumour cell death
Fibrinogen function achieved through multiple covalent states
People
-
Professor Philip Hogg
Head of Centre for Cancer Innovations
-
Dr Diego Butera
-
Dr Aster Pijning
-
Dr Mark Schreuder
-
Mr Kenny Liu
-
Dr Wick Lakshantha
Student Opportunities
Postgraduate students and postdoctoral scientists can work alongside international authorities on protein function and researchers who have successfully developed and commercialised their discoveries. To learn more about student opportunities in the Hogg lab and for all general enquiries relating to our work, please contact Professor Philip Hogg.
