Helen Walden | |
---|---|
![]() Helen Walden | |
Nationality | English |
Known for | Study of Ubiquitination |
Awards | Colworth Medal (2015) EMBO Member (2022) |
Scientific career | |
Fields | Structural biology |
Helen Walden FRSE is an English structural biologist who received the Colworth medal from the Biochemical Society in 2015. [1] [2] She was awarded European Molecular Biology Organization (EMBO) membership in 2022. She is a Professor of Structural Biology at the University of Glasgow and has made significant contributions to the Ubiquitination field. [3]
Helen Walden studied for a BSc in Biochemistry at the University of Bath. She moved to the University of St Andrews and was awarded a PhD for investigating the structural basis of protein hyperthermostability. After a postdoctoral fellowship at St Jude's Children's Research Hospital, Walden moved to London to set up a lab at the Cancer Research UK London Research Institute (and now part of the Francis Crick Institute). After tenure, Walden moved to the MRC-Phosphorylation and Ubiquitylation Unit at the University of Dundee where in 2016 she was promoted to professor. [4] In 2017, Walden relocated her lab to the University of Glasgow as Professor of Structural Biology. [3]
At St Jude's Children's Research Hospital, Helen Walden developed her interest in the mechanisms of ubiquitination, solving the structure of the E1 for Nedd8. [5] [6] In London, Walden studied the specificity and regulation of E3 ubiquitin ligases. [7] [8] In recent years Walden has studied the mechanism and disease association of E2-conjugating enzymes. [9] Walden has investigated the role of Parkin in Parkinson's disease. [10] [11] Her study of the Fanconi Anemia pathway has allowed Walden to begin developing small molecules to target the pathway. [12]
Helen Walden | |
---|---|
![]() Helen Walden | |
Nationality | English |
Known for | Study of Ubiquitination |
Awards | Colworth Medal (2015) EMBO Member (2022) |
Scientific career | |
Fields | Structural biology |
Helen Walden FRSE is an English structural biologist who received the Colworth medal from the Biochemical Society in 2015. [1] [2] She was awarded European Molecular Biology Organization (EMBO) membership in 2022. She is a Professor of Structural Biology at the University of Glasgow and has made significant contributions to the Ubiquitination field. [3]
Helen Walden studied for a BSc in Biochemistry at the University of Bath. She moved to the University of St Andrews and was awarded a PhD for investigating the structural basis of protein hyperthermostability. After a postdoctoral fellowship at St Jude's Children's Research Hospital, Walden moved to London to set up a lab at the Cancer Research UK London Research Institute (and now part of the Francis Crick Institute). After tenure, Walden moved to the MRC-Phosphorylation and Ubiquitylation Unit at the University of Dundee where in 2016 she was promoted to professor. [4] In 2017, Walden relocated her lab to the University of Glasgow as Professor of Structural Biology. [3]
At St Jude's Children's Research Hospital, Helen Walden developed her interest in the mechanisms of ubiquitination, solving the structure of the E1 for Nedd8. [5] [6] In London, Walden studied the specificity and regulation of E3 ubiquitin ligases. [7] [8] In recent years Walden has studied the mechanism and disease association of E2-conjugating enzymes. [9] Walden has investigated the role of Parkin in Parkinson's disease. [10] [11] Her study of the Fanconi Anemia pathway has allowed Walden to begin developing small molecules to target the pathway. [12]