World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

D-Index
88
Citations
25087
World Ranking
2729
National Ranking
197

Research.com Recognitions

  • 2015 - Member of Academia Europaea
  • 2006 - Fellow of the Royal Society, United Kingdom
  • Fellow of The Academy of Medical Sciences, United Kingdom
  • Member of the European Molecular Biology Organization (EMBO)
  • Fellow of The Academy of Medical Sciences, United Kingdom
  • Member of the European Molecular Biology Organization (EMBO)
  • Fellow of The Academy of Medical Sciences, United Kingdom
  • Member of the European Molecular Biology Organization (EMBO)

Overview

Helen R. Saibil is affiliated with Birkbeck, University of London in the United Kingdom. Their research primarily spans the broad domain of Biochemistry, Genetics and Molecular Biology, with a focus on Molecular Biology, Cell Biology, Public Health, Environmental and Occupational Health, Immunology, and Materials Chemistry.

Their scientific work covers several principal topics including:

  • Endoplasmic Reticulum Stress and Disease
  • Heat shock proteins research
  • Protein Structure and Dynamics
  • Prion Diseases and Protein Misfolding
  • Enzyme Structure and Function
  • Neurological diseases and metabolism
  • Advanced Electron Microscopy Techniques and Applications

Recent publications by Helen R. Saibil include:

  • "2.7 Å cryo-EM structure of ex vivo RML prion fibrils" (2022, Nature Communications)
  • "REMBI: Recommended Metadata for Biological Images-enabling reuse of microscopy data in biology" (2021, Nature Methods)
  • "Cryo-EM in molecular and cellular biology" (2022, Molecular Cell)
  • "A structural basis for prion strain diversity" (2023, Nature Chemical Biology)
  • "Cooperative amyloid fibre binding and disassembly by the Hsp70 disaggregase" (2022, The EMBO Journal)

Helen R. Saibil frequently collaborates with several researchers, including:

  • Szymon W. Manka
  • Adam Wenborn
  • Jemma Betts
  • Susan Joiner
  • John Collinge

Their research has been published in a variety of scientific venues, prominently including:

  • bioRxiv (Cold Spring Harbor Laboratory)
  • Faraday Discussions
  • Nature Communications
  • The EMBO Journal
  • Nature Methods

Helen R. Saibil has received notable recognitions such as:

  • Member of Academia Europaea (2015)
  • Fellow of the Royal Society, United Kingdom (2006)
  • Fellow of The Academy of Medical Sciences, United Kingdom
  • Member of the European Molecular Biology Organization (EMBO)

Best Publications

  • Chaperone machines for protein folding, unfolding and disaggregation

    Helen R. Saibil

  • The protofilament structure of insulin amyloid fibrils

    José L. Jiménez;Ewan J. Nettleton;Mario Bouchard;Carol V. Robinson

  • A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state.

    Garrett J. Lee;Alan M. Roseman;Helen R. Saibil;Elizabeth Vierling

  • Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing.

    J L Jiménez;J I Guijarro;E Orlova;J Zurdo

  • Atomic structure and hierarchical assembly of a cross-β amyloid fibril

    Anthony W. P. Fitzpatrick;Galia T. Debelouchina;Marvin J. Bayro;Daniel K. Clare

  • Hsp26: a temperature‐regulated chaperone

    Martin Haslbeck;Stefan Walke;Stefan Walke;Thusnelda Stromer;Monika Ehrnsperger;Monika Ehrnsperger

  • Structural Basis of Pore Formation by the Bacterial Toxin Pneumolysin

    Sarah J. Tilley;Elena V. Orlova;Robert J.C. Gilbert;Robert J.C. Gilbert;Peter W. Andrew

  • Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes

    Jonathan S. Weissman;Jonathan S. Weissman;Corinne M. Hohl;Corinne M. Hohl;Oleg Kovalenko;Yechezkel Kashi

  • The Chaperonin ATPase Cycle: Mechanism of Allosteric Switching and Movements of Substrate-Binding Domains in GroEL

    Alan M Roseman;Shaoxia Chen;Helen White;Kerstin Braig

  • The structural basis for membrane binding and pore formation by lymphocyte perforin

    Ruby H P Law;Natalya Lukoyanova;Ilia Voskoboinik;Ilia Voskoboinik;Tom T Caradoc-Davies

  • Reversible Conversion of Monomeric Human Prion Protein Between Native and Fibrilogenic Conformations

    G. S. Jackson;L. L. P. Hosszu;L. L. P. Hosszu;A. Power;A. F. Hill

  • Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.

    Shaoxia Chen;Alan M. Roseman;Allison S. Hunter;Stephen P. Wood

  • Structural basis for the regulated protease and chaperone function of DegP

    Tobias Krojer;Justyna Sawa;Eva Schäfer;Helen R. Saibil

  • Structure of a type IV secretion system core complex.

    Rémi Fronzes;Eva Schäfer;Eva Schäfer;Luchun Wang;Luchun Wang;Helen R. Saibil;Helen R. Saibil

  • Human Hsp70 Disaggregase Reverses Parkinson’s-Linked α-Synuclein Amyloid Fibrils

    Xuechao Gao;Xuechao Gao;Marta Carroni;Carmen Nussbaum-Krammer;Carmen Nussbaum-Krammer;Axel Mogk;Axel Mogk

  • T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol

    Victoria A. Lewis;Gillian M. Hynes;Dong Zheng;Dong Zheng;Helen Saibil;Helen Saibil

  • GroEL-GroES Cycling: ATP and Nonnative Polypeptide Direct Alternation of Folding-Active Rings

    Hays S. Rye;Hays S. Rye;Alan M. Roseman;Shaoxia Chen;Krystyna Furtak;Krystyna Furtak

  • Structure of an Hsp90-Cdc37-Cdk4 Complex

    Cara K. Vaughan;Ulrich Gohlke;Frank Sobott;Valerie M. Good

  • The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter.

    Ulrich Gohlke;Lee Pullan;Christopher A. McDevitt;Ida Porcelli

  • ATP-Bound States of GroEL Captured by Cryo-Electron Microscopy

    Neil A. Ranson;George W. Farr;George W. Farr;Alan M. Roseman;Brent Gowen

Frequent Co-Authors

Arthur L. Horwich
Arthur L. Horwich Yale University
Elena V. Orlova
Elena V. Orlova Birkbeck, University of London
James C. Whisstock
James C. Whisstock Monash University
Wayne A. Fenton
Wayne A. Fenton Yale University
Michael J. Blackman
Michael J. Blackman London School of Hygiene & Tropical Medicine
John Collinge
John Collinge University College London
Joseph A. Trapani
Joseph A. Trapani Peter MacCallum Cancer Centre
Christopher M. Dobson
Christopher M. Dobson University of Cambridge
Ilia Voskoboinik
Ilia Voskoboinik Peter MacCallum Cancer Centre
Carol V. Robinson
Carol V. Robinson University of Oxford

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