Neil Ranson
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About
Neil Ranson is a Professor at the University of Leeds, UK. His research focuses on protein dynamics, membrane protein folding, and amyloid formation, with recent articles exploring topics such as outer membrane protein assembly and the molecular architecture of β-amyloid pathology. He employs advanced techniques like CryoEM to investigate viral structures and their interactions, contributing significantly to our understanding of disease-related proteins and resistance mechanisms.
Recent Grants
Grant: Close
The structure and function of the beta-barrel assembly machinery: an Achilles heel of Gram-negative pathogens
Open Date: 2017-11-01
Close Date: 2022-10-31
Grant: Close
Exploiting the power of heterologous expression in plants to discover new virus structure.
Open Date: 2017-09-30
Close Date: 2020-09-29
Grant: Close
Bridging the gap between cell and structural biology at the University of Leeds
Open Date: 2017-09-01
Close Date: 2022-08-31
Grant: Close
The roles of the pre-genomic RNA in Hepatitis B Virus nucleocapsid assembly.
Open Date: 2016-06-30
Close Date: 2018-06-29
Grant: Close
The roles of the pre-genomic RNA in Hepatitis B Virus nucleocapsid assembly.
Open Date: 2016-06-30
Close Date: 2018-06-29
Positions (1)
Sheena Radford
University of Leeds
3 weeks ago
A 4-year PhD studentship is available at the University of Leeds, funded at the standard UKRI stipend rate and supported by a Wellcome-funded research programme. The project, starting in October 2026, focuses on understanding and controlling amyloid fibril polymorphism, a key factor in diseases such as Alzheimer’s, Parkinson’s, and type-2 diabetes. The studentship is jointly supervised by Prof Sheena Radford and Prof Neil Ranson in the Astbury Centre for Structural Molecular Biology. The research aims to unravel why proteins form amyloid fibrils and how this process leads to disease. Unlike the predictable folding of globular proteins, amyloid-forming proteins can assemble into multiple structures in vitro, but only a single, disease-specific structure is found in patients. The project will use a combination of biochemical and biophysical assays to map the pathways of protein aggregation and employ cryo-electron microscopy (cryoEM) to solve the structures formed during assembly. By integrating these data, the student will develop new models describing the molecular events underpinning amyloid assembly and investigate how solution conditions and cellular cofactors influence the selection of disease-specific amyloid structures. This research has the potential to accelerate diagnosis and enable patient-specific therapies for amyloid diseases. The successful candidate will join a dynamic team and gain experience in advanced techniques in biochemistry, biophysics, and structural biology. Applicants should have a strong background in a relevant field such as biochemistry, biophysics, or molecular biology, and demonstrate enthusiasm for research and learning new methods. Experience with biochemical or biophysical assays, or structural biology, is desirable but not essential. Funding is fully provided for four years, covering both stipend and tuition fees. Interested candidates should contact Prof Sheena Radford ([email protected]) or Prof Neil Ranson ([email protected]) with a CV to express interest. The application window is open for an October 2026 start.
3 weeks ago
Articles (14)
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2025
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2021
Collaborators (13)
Sergey V Melnikov
Newcastle University
Antreas C. Kalli
University of Leeds
Sheena E Radford
Astbury Professor of Biophysics
University of Leeds
Robert Hirt
Professor of Evolutionary Parasitology
Newcastle University
Frank Sainsbury
-
Kei Sakamoto
Professor
University of Copenhagen
Mikael Elofsson
Umea University
Juan Jose Lopez-Moya
Investigador Científico CSIC (associate professor)
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Patricija van Oosten-Hawle
Assistant Professor
University of North Carolina at Charlotte
Antonio N. Calabrese
University of Leeds
Benjamin Rowlinson
University of Leeds
Dipsikha Biswas
Københavns Universitet
Peter Stockley
Professor of Biological Chemistry
University of Leeds
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