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Chemistry

D-Index
104
Citations
36210
World Ranking
1071
National Ranking
55

Overview

Sheena E. Radford is affiliated with the University of Leeds in the United Kingdom. The research focus covers primarily Biochemistry, Genetics and Molecular Biology with significant contributions to Medicine. Their work extensively explores Molecular Biology, Physiology, Neurology, Genetics, and Materials Chemistry.

The research topics addressed include:

  • Alzheimer's disease research and treatments
  • Protein Structure and Dynamics
  • RNA and protein synthesis mechanisms
  • Bacterial Genetics and Biotechnology
  • Parkinson's Disease Mechanisms and Treatments
  • Lipid Membrane Structure and Behavior
  • Enzyme Structure and Function

Frequent publication venues for this scientist highlight a diverse presence in the scientific community, including:

  • bioRxiv (Cold Spring Harbor Laboratory)
  • Nature Communications
  • Trends in Biochemical Sciences
  • Biophysical Journal
  • Journal of Molecular Biology

Among recent papers authored or co-authored, the following are notable:

  • "A short motif in the N-terminal region of α-synuclein is critical for both aggregation and function," 2020, Nature Structural & Molecular Biology
  • "Proteostasis of Islet Amyloid Polypeptide: A Molecular Perspective of Risk Factors and Protective Strategies for Type II Diabetes," 2021, Chemical Reviews
  • "Role of the lipid bilayer in outer membrane protein folding in Gram-negative bacteria," 2020, Journal of Biological Chemistry
  • "De novo design of transmembrane β barrels," 2021, Science
  • "Visualizing and trapping transient oligomers in amyloid assembly pathways," 2020, Biophysical Chemistry

Frequent collaborators in research include:

  • David J. Brockwell
  • Neil A. Ranson
  • Antonio N. Calabrese
  • Jonathan Machin
  • Jim E. Horne

Best Publications

  • Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

    David R. Booth;Margaret Sunde;Vittorio Bellotti;Vittorio Bellotti;Carol V. Robinson

  • Responsive gels formed by the spontaneous self-assembly of peptides into polymeric β-sheet tapes

    A. Aggeli;M. Bell;N. Boden;J. N. Keen

  • Nucleation of protein fibrillation by nanoparticles

    Sara Linse;Celia Cabaleiro-Lago;Wei-Feng Xue;Iseult Lynch

  • A new era for understanding amyloid structures and disease.

    Matthew G Iadanza;Matthew P Jackson;Eric W Hewitt;Neil A Ranson

  • The folding of hen lysozyme involves partially structured intermediates and multiple pathways.

    Sheena E. Radford;Christopher M. Dobson;Philip A. Evans

  • Detection of transient protein folding populations by mass spectrometry.

    Andrew Miranker;Carol V. Robinson;Sheena E. Radford;Robin T. Aplin

  • pH as a Trigger of Peptide β-Sheet Self-Assembly and Reversible Switching between Nematic and Isotropic Phases

    Amalia Aggeli;Mark Bell;Lisa M. Carrick;Colin W. G. Fishwick

  • Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly.

    Wei-Feng Xue;Steve W. Homans;Sheena E. Radford

  • Folding versus aggregation: Polypeptide conformations on competing pathways

    Thomas R. Jahn;Sheena E. Radford

  • The Yin and Yang of protein folding.

    Thomas R. Jahn;Sheena E. Radford

  • Pulling geometry defines the mechanical resistance of a β-sheet protein

    David J Brockwell;Emanuele Paci;Rebecca C Zinober;Godfrey S Beddard

  • Fibril fragmentation enhances amyloid cytotoxicity.

    Wei-Feng Xue;Andrew L. Hellewell;Walraj S. Gosal;Steve W. Homans

  • Understanding how proteins fold: the lysozyme story so far.

    Christopher M. Dobson;Philip A. Evans;Sheena E. Radford

  • Competing Pathways Determine Fibril Morphology in the Self-assembly of β2-Microglobulin into Amyloid

    Walraj S. Gosal;Isobel J. Morten;Eric W. Hewitt;D. Alastair Smith

  • Deciphering drift time measurements from travelling wave ion mobility spectrometry-mass spectrometry studies

    David P. Smith;Tom W. Knapman;Iain Campuzano;Richard W. Malham

  • Partially unfolded states of beta(2)-microglobulin and amyloid formation in vitro.

    Victoria J. McParland;Neil M. Kad;Arnout P. Kalverda;Anthony Brown

  • Amyloid formation under physiological conditions proceeds via a native-like folding intermediate

    Thomas R Jahn;Martin J Parker;Steve W Homans;Sheena E Radford

  • A partially folded state of hen egg white lysozyme in trifluoroethanol: structural characterization and implications for protein folding.

    Matthias Buck;Sheena E. Radford;Christopher M. Dobson

  • An expanding arsenal of experimental methods yields an explosion of insights into protein folding mechanisms

    Alice I Bartlett;Sheena E Radford

  • Im7 folding mechanism: misfolding on a path to the native state.

    Andrew P. Capaldi;Colin Kleanthous;Sheena E. Radford

  • Demonstration by NMR of folding domains in lysozyme.

    Andrew Miranker;Sheena E. Radford;Martin Karplus;Christopher M. Dobson

Frequent Co-Authors

Alison E. Ashcroft
Alison E. Ashcroft University of Leeds
Christopher M. Dobson
Christopher M. Dobson University of Cambridge
Carol V. Robinson
Carol V. Robinson University of Oxford
Colin Kleanthous
Colin Kleanthous University of Oxford
Richard N. Perham
Richard N. Perham University of Cambridge
Peter G. Stockley
Peter G. Stockley University of Leeds
Geoffrey R. Moore
Geoffrey R. Moore University of East Anglia
Gabriel Waksman
Gabriel Waksman University College London
Daniel P. Raleigh
Daniel P. Raleigh Stony Brook University

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