Helen Walden awarded Colworth Medal
Many congratulations to MRC-PPU PI Helen Walden who has been awarded the prestigious Colworth Medal.
The Colworth Medal is sponsored by Unilever and presented by the Biochemical Society, and is the most distinguished award that a biochemical researcher in the early stages of their independent research can receive in the UK. In addition to the medal, Helen will receive an honorarium of £3,000 and an invitation to present two lectures, one at a Biochemical Society meeting and another at the Unilever research laboratory.
Helen's research focuses on understanding the fundamentals of the ubiquitylation system and how it is linked to disease mechanisms. Helen has made a series of wonderful discoveries that have resulted in a much better understanding of three important areas of the ubiquitylation system namely the E1 activating enzyme, and the E3 ubiquitin ligases, FANCL and Parkin. As a result of this work Helen has been able to establish a growing international reputation as a leader in the ubiquitylation area and published numerous highly cited research papers. In 2012 Helen also received an esteemed and highly sought after Young Investigator Award from the European Molecular Biology Organisation (EMBO).
Helen did her undergraduate training at the University of Bath before moving to St Andrews to perform her PhD with Professor Garry Taylor, where she worked on unravelling the structural basis of protein thermo-stability through X-ray analysis of thermostable proteins. Helen next undertook a postdoc, in the laboratory of Brenda Schulman at the St Jude Children's hospital in Memphis (Dr Schulman's first postdoc), to work on the ubiquitylation system. During this period Helen solved the first structure of an E1 activating enzyme, namely the heterodimeric E1 enzyme (APPBP1-UBA3). E1 enzymes play an important role in regulating ubiquitylation as they catalyse the first step in the ubiquitylation pathway. The dramatic structure and the analysis that Helen revealed the catalytic mechanism by which E1 functions.
In 2005 Helen then set up her own research group at the Cancer Research UK London Research Institute at Lincoln's Inn fields. Here, Helen focused mainly on understanding two important E3 ligases namely Parkin and FANCL, biologically important enzymes that are mutated in patients with Parkinson's disease and Fanconi Anemia respectively. These were very challenging projects but Helen made great strides in elucidating the structures of these components and working out how they are regulated and function. For example, in a landmark publication in 2011 Helen reported that a key regulatory role for the N-terminal ubiquitin-like domain of Parkin operated by binding to the catalytic domain as an auto-inhibitory domain. This discovery has provided great insights into how Parkin is regulated and functions. In another beautiful Nature Structural Molecular Biology paper in 2010, Helen was able to devise a strategy to express, crystallise and solve the structure or the Drosophila FANCL E3 ligase which reveals that the architecture of the domains turned out to be fundamentally different from previous sequence-based predictions. In 2013 Helen moved her laboratory to the MRC-PPU where she is continuing her work to better understand Parkin and FANCL and how these enzymes are linked to disease.
Commenting on the award Helen said 'I am absolutely thrilled to be awarded the Colworth Medal. It is a wonderful endorsement of the efforts in my lab to understand the molecular processes underlying protein regulation.' MRC-PPU Director Dario Alessi stated 'This is fantastic recognition for the ambitious and important research that Helen has undertaken to date. Her work has provided fabulous insights into key biochemical processes that are of great relevance to better understanding and treating diseases such as cancer and Parkinson's disease. I am delighted that we have been able to recruit Helen to our Unit. Helen's talent and ambitious future research plans particularly excite me. These show great promise and are likely to provide critical knowledge that could lead to improved strategies to better treat disease in the future.
Helen is the tenth principal investigator working within the College of Life Sciences at the University of Dundee to be awarded the Colworth medal. The previous recipients are Philip Cohen (1977), David M.J. Lilley (1982), Pete Downes (1987), Michael Ferguson (1991), Angus Lamond (1992), Dario Alessi (2000), Tom Owen-Hughes (2002), Frank Sargent (2007) and John Rouse (2008). In addition two other researchers who trained within the MRC-PPU, namely Nicholas C. Tonks (1993) and David Barford (1998), have also been awarded the Colworth medal.
The Colworth Medal is awarded annually since 1963, and Helen will be the 52nd recipient. Helen is only the third female researcher to receive this accolade.
The Colworth Medal is sponsored by Unilever and presented by the Biochemical Society, and is the most distinguished award that a biochemical researcher in the early stages of their independent research can receive in the UK. In addition to the medal, Helen will receive an honorarium of £3,000 and an invitation to present two lectures, one at a Biochemical Society meeting and another at the Unilever research laboratory.
Helen's research focuses on understanding the fundamentals of the ubiquitylation system and how it is linked to disease mechanisms. Helen has made a series of wonderful discoveries that have resulted in a much better understanding of three important areas of the ubiquitylation system namely the E1 activating enzyme, and the E3 ubiquitin ligases, FANCL and Parkin. As a result of this work Helen has been able to establish a growing international reputation as a leader in the ubiquitylation area and published numerous highly cited research papers. In 2012 Helen also received an esteemed and highly sought after Young Investigator Award from the European Molecular Biology Organisation (EMBO).
Helen did her undergraduate training at the University of Bath before moving to St Andrews to perform her PhD with Professor Garry Taylor, where she worked on unravelling the structural basis of protein thermo-stability through X-ray analysis of thermostable proteins. Helen next undertook a postdoc, in the laboratory of Brenda Schulman at the St Jude Children's hospital in Memphis (Dr Schulman's first postdoc), to work on the ubiquitylation system. During this period Helen solved the first structure of an E1 activating enzyme, namely the heterodimeric E1 enzyme (APPBP1-UBA3). E1 enzymes play an important role in regulating ubiquitylation as they catalyse the first step in the ubiquitylation pathway. The dramatic structure and the analysis that Helen revealed the catalytic mechanism by which E1 functions.
In 2005 Helen then set up her own research group at the Cancer Research UK London Research Institute at Lincoln's Inn fields. Here, Helen focused mainly on understanding two important E3 ligases namely Parkin and FANCL, biologically important enzymes that are mutated in patients with Parkinson's disease and Fanconi Anemia respectively. These were very challenging projects but Helen made great strides in elucidating the structures of these components and working out how they are regulated and function. For example, in a landmark publication in 2011 Helen reported that a key regulatory role for the N-terminal ubiquitin-like domain of Parkin operated by binding to the catalytic domain as an auto-inhibitory domain. This discovery has provided great insights into how Parkin is regulated and functions. In another beautiful Nature Structural Molecular Biology paper in 2010, Helen was able to devise a strategy to express, crystallise and solve the structure or the Drosophila FANCL E3 ligase which reveals that the architecture of the domains turned out to be fundamentally different from previous sequence-based predictions. In 2013 Helen moved her laboratory to the MRC-PPU where she is continuing her work to better understand Parkin and FANCL and how these enzymes are linked to disease.
Commenting on the award Helen said 'I am absolutely thrilled to be awarded the Colworth Medal. It is a wonderful endorsement of the efforts in my lab to understand the molecular processes underlying protein regulation.' MRC-PPU Director Dario Alessi stated 'This is fantastic recognition for the ambitious and important research that Helen has undertaken to date. Her work has provided fabulous insights into key biochemical processes that are of great relevance to better understanding and treating diseases such as cancer and Parkinson's disease. I am delighted that we have been able to recruit Helen to our Unit. Helen's talent and ambitious future research plans particularly excite me. These show great promise and are likely to provide critical knowledge that could lead to improved strategies to better treat disease in the future.
Helen is the tenth principal investigator working within the College of Life Sciences at the University of Dundee to be awarded the Colworth medal. The previous recipients are Philip Cohen (1977), David M.J. Lilley (1982), Pete Downes (1987), Michael Ferguson (1991), Angus Lamond (1992), Dario Alessi (2000), Tom Owen-Hughes (2002), Frank Sargent (2007) and John Rouse (2008). In addition two other researchers who trained within the MRC-PPU, namely Nicholas C. Tonks (1993) and David Barford (1998), have also been awarded the Colworth medal.
The Colworth Medal is awarded annually since 1963, and Helen will be the 52nd recipient. Helen is only the third female researcher to receive this accolade.