Sheena E Radford

Has grant

Astbury Professor of Biophysics

University of Leeds

United Kingdom

Research Interests

Explore related searches

Professors in United Kingdom

Contact this professor

Get a free first email built on one of their papers, ready for you to edit and send yourself.

About

Sheena E Radford is the Astbury Professor of Biophysics at the University of Leeds, UK. Her research focuses on the biochemical mechanisms of amyloid formation and polymorphism, enzyme activity in crowded environments, and the development of innovative crosslinking techniques. Recent publications include studies on the modulation of enzyme activities and the dynamics of fibril assembly, contributing to a deeper understanding of protein interactions and structural classifications.

Recent Grants

Grant: Close

Seeing the Unseeable: How does protein dynamic disorder shape biology?

Open Date: 2021-01-01

Close Date: 2025-12-01

Grant: Close

Deciphering the function of intrinsically disordered protein regions in a cellular context

Open Date: 2020-11-01

Close Date: 2025-10-01

Grant: Close

Dynamic allostery of Sec machinery in protein transport and folding

Open Date: 2020-04-30

Close Date: 2023-04-29

Grant: Close

The structural biology of amyloid aggregation

Open Date: 2020-01-01

Close Date: 2022-12-01

Grant: Close

Targeting SurA Dynamics: An Achilles Heel in Bacterial Outer Membrane Biogenesis

Open Date: 2019-09-30

Close Date: 2022-09-29

Articles (27)

Year:

2025

Year:

2025

Year:

2025

Year:

2025

Year:

2025

Year:

2025

Year:

2025

Year:

2025

Year:

2025

Year:

2025

Year:

2024

Year:

2024

Year:

2024

Year:

2024

Year:

2023

Year:

2023

Year:

2023

Year:

2023

Year:

2023

Year:

2023

Year:

2023

Year:

2023

Year:

2022

Year:

2022

Year:

2022

Year:

2022

Year:

2022

Collaborators (18)

Martin Edwards

Assistant Professor

University of Arkansas at Fayetteville

UNITED STATES

Sheena E Radford

Research Interests

Explore related searches

Contact this professor

About

Recent Grants

Articles (27)

Structural and thermodynamic classification of amyloid polymorphs

In the flow, how fluid dynamics shapes amyloid formation

Protein-induced membrane asymmetry modulates OMP folding kinetics and stability

OmpA Specifically Modulates the Activity of Enzymes that Reside in the Crowded Bacterial Outer Membrane

Kinetic Steering of Amyloid Formation and Polymorphism by Canagliflozin, a Type-2 Diabetes Drug

How is the Amyloid Fold Built? Polymorphism and the Microscopic Mechanisms of Fibril Assembly.

Design and characterisation of photoactivatable and lysine reactive o-nitrobenzyl alcohol-based crosslinkers

Design and characterisation of photoactivatable and lysine reactive o-nitrobenzyl alcohol-based crosslinkers

High-throughput discovery of fluoroprobes that recognize amyloid fibril polymorphs

Protein-induced membrane asymmetry modulates OMP folding kinetics and stability

Single molecule delivery into living cells

Outer membrane protein assembly mediated by BAM-SurA complexes

A Potent Sybody Selectively Inhibits α-Synuclein Amyloid Formation by Binding to the P1 Region

Exploring a Role for Flow-Induced Aggregation Assays in Platform Formulation Optimisation for Antibody-Based Proteins

Mechanistic Study of the Conductance and Enhanced Single-Molecule Detection in a Polymer–Electrolyte Nanopore

Darobactin B stabilises a lateral-closed conformation of the BAM complex in E. coli cells

Protein–lipid charge interactions control the folding of outer membrane proteins into asymmetric membranes

The in-tissue molecular architecture of β-amyloid pathology in the mammalian brain

Disease-relevant β2-microglobulin variants share a common amyloid fold

Taking Charge: Metal Ions Accelerate Amyloid Aggregation in Sequence Variants of α-Synuclein

Dynamic coupling of fast channel gating with slow ATP-turnover underpins protein transport through the Sec translocon

Changing Shape of Molecules

Probing RNA Conformations Using a Polymer–Electrolyte Solid-State Nanopore

Single residue modulators of amyloid formation in the N-terminal P1-region of α-synuclein

Controlling amyloid formation of intrinsically disordered proteins and peptides: slowing down or speeding up?

Dimers of D76N-β2-microglobulin display potent antiamyloid aggregation activity

Trigger factor both holds and folds its client proteins

Collaborators (18)

Martin Edwards

Antreas C. Kalli

Jeanine Williams

Neil Ranson

Anastasia Zhuravleva

Christos Pliotas

Tomáš Fessl

Paolo Actis

Frank Sobott

Patricija van Oosten-Hawle

Eric Hewitt

Antonio N. Calabrese

Hassane El Mkami

Tara Sabir

David Brockwell

James C A Bardwell

Ian Collinson

Yue Ma

Make your next move.