We are delighted to announce that Helen Walden and her PhD student Mark Frost have joined the MRC Protein Phosphorylation and Ubiquitylation Unit (MRC-PPU). Helen has relocated her laboratory from the CRUK London Research Institute at Lincoln's Inn fields.
Helen will take up a senior group leader position within the MRC-PPU.
Helen's research centres on understanding how post-translational modification of proteins by ubiquitylation impacts on cellular process, related to understanding diseases such as cancer and Parkinson's.
Highlights of Helen's recent work include analysing the structure of the Parkinson's disease E3 ligase termed Parkin. This has revealed how Parkin is regulated and maintained in an inactive conformation via an auto-inhibitory interaction of a UBL domain with the catalytic E3 ligase domain. This work has also revealed how disease-causing mutations affect Parkin by interfering with the catalytic mechanism as well as by disrupting the ability of Parkin adopt and auto-inhibited conformation.
Helen has also undertaken ground-breaking structural and functional analysis of the a critical E3 ligase termed FANCL that is mutated in patients with Fanconi Anemia and that plays a critical role in the DNA Repair pathway.
Helen has very exciting plans to continue unravelling the role and molecular mechanism by which ubiquitylation controls fundamental biological processes of high relevance to understanding human diseases. She will employ a blend of the state of the art X-ray crystallographic and biochemical techniques to achieve her aims.
Helen will take up a senior group leader position within the MRC-PPU.
Helen's research centres on understanding how post-translational modification of proteins by ubiquitylation impacts on cellular process, related to understanding diseases such as cancer and Parkinson's.
Highlights of Helen's recent work include analysing the structure of the Parkinson's disease E3 ligase termed Parkin. This has revealed how Parkin is regulated and maintained in an inactive conformation via an auto-inhibitory interaction of a UBL domain with the catalytic E3 ligase domain. This work has also revealed how disease-causing mutations affect Parkin by interfering with the catalytic mechanism as well as by disrupting the ability of Parkin adopt and auto-inhibited conformation.
Helen has also undertaken ground-breaking structural and functional analysis of the a critical E3 ligase termed FANCL that is mutated in patients with Fanconi Anemia and that plays a critical role in the DNA Repair pathway.
Helen has very exciting plans to continue unravelling the role and molecular mechanism by which ubiquitylation controls fundamental biological processes of high relevance to understanding human diseases. She will employ a blend of the state of the art X-ray crystallographic and biochemical techniques to achieve her aims.