Helen R Saibil

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

Hays S. Rye, Alan M. Roseman, +4 authors Arthur L Horwich
Cell
1999

The double-ring chaperonin GroEL mediates protein folding in the central cavity of a ring bound by ATP and GroES, but it is unclear how GroEL cycles from one folding-active complex to the next. We… (More)

Structural basis for the regulated protease and chaperone function of DegP

Tobias Krojer, Justyna Sawa, Eva R Schäfer, Helen R Saibil, Michael Ehrmann, Tim Clausen
Nature
2008

All organisms have to monitor the folding state of cellular proteins precisely. The heat-shock protein DegP is a protein quality control factor in the bacterial envelope that is involved in… (More)

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
The EMBO journal
1997

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. We found that HSP18.1, a… (More)

Structural Basis of Pore Formation by the Bacterial Toxin Pneumolysin

Sarah J. Tilley, Elena V Orlova, Robert J C Gilbert, P. W. Andrew, Helen R Saibil
Cell
2005

The bacterial toxin pneumolysin is released as a soluble monomer that kills target cells by assembling into large oligomeric rings and forming pores in cholesterol-containing membranes. Using cryo-EM… (More)

The protofilament structure of insulin amyloid fibrils.

José Luis Domínguez Jiménez, Ewan J Nettleton, Mario Bouchard, Carol V Robinson, Christopher M. Dobson, Helen R Saibil
Proceedings of the National Academy of Sciences…
2002

Under solution conditions where the native state is destabilized, the largely helical polypeptide hormone insulin readily aggregates to form amyloid fibrils with a characteristic cross-beta… (More)

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

Neil A. Ranson, George W. Farr, +4 authors Helen R Saibil
Cell
2001

The chaperonin GroEL drives its protein-folding cycle by cooperatively binding ATP to one of its two rings, priming that ring to become folding-active upon GroES binding, while simultaneously… (More)

Hsp26: a temperature-regulated chaperone.

Martin Haslbeck, Stefan Walke, +5 authors Johannes Buchner
The EMBO journal
1999

Small heat shock proteins (sHsps) are a conserved protein family, with members found in all organisms analysed so far. Several sHsps have been shown to exhibit chaperone activity and protect proteins… (More)

Interaction between prion protein and toxic amyloid β assemblies can be therapeutically targeted at multiple sites

Darragh B. Freir, Andrew J. Nicoll, +11 authors John Collinge
Nature communications
2011

A role for PrP in the toxic effect of oligomeric forms of Aβ, implicated in Alzheimer's disease (AD), has been suggested but remains controversial. Here we show that PrP is required for the… (More)

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

Alan M. Roseman, Shaoxia Chen, H. P. Esmonde White, Kerstin Braig, Helen R Saibil
Cell
1996

Chaperonin-assisted protein folding proceeds through cycles of ATP binding and hydrolysis by the large chaperonin GroEL, which undergoes major allosteric rearrangements. Interaction between the two… (More)

Allosteric signaling of ATP hydrolysis in GroEL–GroES complexes

Neil A. Ranson, Daniel Kofi Clare, George W. Farr, David Houldershaw, Arthur L Horwich, Helen R Saibil
Nature Structural &Molecular Biology
2006

The double-ring chaperonin GroEL and its lid-like cochaperonin GroES form asymmetric complexes that, in the ATP-bound state, mediate productive folding in a hydrophilic, GroES-encapsulated chamber,… (More)

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