H
Helen R. Saibil
Researcher at Birkbeck, University of London
Publications - 172
Citations - 18391
Helen R. Saibil is an academic researcher from Birkbeck, University of London. The author has contributed to research in topics: Protein folding & GroEL. The author has an hindex of 72, co-authored 161 publications receiving 16902 citations. Previous affiliations of Helen R. Saibil include University College London & University of London.
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Journal ArticleDOI
The protofilament structure of insulin amyloid fibrils
José L. Jiménez,Ewan J. Nettleton,Mario Bouchard,Carol V. Robinson,Christopher M. Dobson,Helen R. Saibil +5 more
TL;DR: Cryo-electron microscopy is used, combining single particle analysis and helical reconstruction, to characterize these fibrils and to study the three-dimensional (3D) arrangement of their component protofilaments, suggesting that very small, local changes in β-sheet twist are important in establishing the long-range coiling of the prot ofilaments into fibrILS of diverse morphology.
Journal ArticleDOI
Chaperone machines for protein folding, unfolding and disaggregation
TL;DR: The structural basis of their mechanism of action is being unravelled and typically involves massive displacements of 20–30 kDa domains over distances of 20-50 Å and rotations of up to 100°.
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A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state.
TL;DR: The small heat shock proteins (sHSPs) recently have been reported to have molecular chaperone activity in vitro; however, the mechanism of this activity is poorly defined, and it is found that HSP18.1 prevented aggregation of substrates and can be reactivated in the presence of rabbit reticulocyte or wheat germ extracts in an ATP‐dependent process.
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Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing.
José L. Jiménez,J I Guijarro,Elena V. Orlova,Jesús Zurdo,Christopher M. Dobson,Margaret Sunde,Helen R. Saibil +6 more
TL;DR: A model for the polypeptide packing as a basis for understanding the structure of amyloid fibrils in general is proposed.
Journal ArticleDOI
Atomic structure and hierarchical assembly of a cross-β amyloid fibril
Anthony W. P. Fitzpatrick,Galia T. Debelouchina,Marvin J. Bayro,Daniel K. Clare,Marc A. Caporini,Vikram S. Bajaj,Christopher P. Jaroniec,Luchun Wang,Vladimir Ladizhansky,Shirley A. Müller,Cait E. MacPhee,Christopher A. Waudby,Christopher A. Waudby,Helen R. Mott,Alfonso De Simone,Alfonso De Simone,Tuomas P. J. Knowles,Helen R. Saibil,Michele Vendruscolo,Elena V. Orlova,Robert G. Griffin,Christopher M. Dobson +21 more
TL;DR: Atomic-resolution structures of three amyloid polymorphs formed by an 11-residue peptide reveal the details of the packing interactions by which the constituent β-strands are assembled hierarchically into protofilaments, filaments, and mature fibrils.