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Bioimage

Bio-Image Summer School Paris 2005

Author name initial(s) from year to year Publication type Display format limit
20 Publications
1 Structural basis of pore formation by the bacterial toxin pneumolysin.
SJ. Tilley, EV. Orlova, RJC. Gilbert, PW. Andrew, HR. Saibil,
Cell (2005) 121-2 p.247
2 A mutant chaperonin with rearranged inter-ring electrostatic contacts and temperature-sensitive dissociation
BT. Sewell, RB. Best, SX. Chen, AM. Roseman, GW. Farr, AL. Horwich, HR. Saibil,
Nat. Struct. Mol. Biol. (2004) 11-11 p.1128
3 A domain in the N-terminal part of Hsp26 is essential for chaperone function and oligomerization
M. Haslbeck, A. Ignatiou, HR. Saibil, S. Helmich, E. Frenzl, T. Stromer, J. Buchner,
J. Mol. Biol. (2004) 343-2 p.445
4 Structure determination of macromolecular assemblies by single-particle analysis of cryo-electron micrographs
EV. Orlova, HR. Saibil,
Curr. Opin. Struct. Biol. (2004) 14-5 p.584
5 Recognition and separation of single particles with size variation by statistical analysis of their images
HE. White, HR. Saibil, A. Ignatiou, EV. Orlova,
J. Mol. Biol. (2004) 336-2 p.453
6 Location of auxilin within a clathrin cage
CJ. Smith, TR. Dafforn, H. Kent, CA. Sims, K. Khubchandani-aswani, L. Zhang, HR. Saibil, BMF. Pearse,
J. Mol. Biol. (2004) 336-2 p.461
7 Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes
GW. Farr, WA. Fenton, TK. Chaudhuri, DK. Clare, HR. Saibil, AL. Horwich,
Embo J. (2003) 22-13 p.3220
8 The chaperonin folding machine
HR. Saibil, NA. Ranson,
Trends Biochem.Sci. (2002) 27-12 p.627
9 The protofilament structure of insulin amyloid fibrils
JL. Jimenez, EJ. Nettleton, M. Bouchard, CV. Robinson, CM. Dobson, HR. Saibil,
Proc. Natl. Acad. Sci. U. S. A. (2002) 99-14 p.9196
10 Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding
HR. Saibil, AL. Horwich, WA. Fenton,
Adv. Protein Chem. (2002) 59- p.45
11 ATP-bound states of GroEL captured by cryo-electron microscopy
NA. Ranson, GW. Farr, AM. Roseman, B. Gowen, WA. Fenton, AL. Horwich, HR. Saibil,
Cell (2001) 107-7 p.869
12 Three-dimensional structure of an invertebrate rhodopsin and basis for ordered alignment in the photoreceptor membrane
A. Davies, BE. Gowen, AM. Krebs, GFX. Schertler, HR. Saibil,
J. Mol. Biol. (2001) 314-3 p.455
13 Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy
JL. Jimenez, G. Tennent, M. Pepys, HR. Saibil,
J. Mol. Biol. (2001) 311-2 p.241
14 Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain
J. Zurdo, JI. Guijarro, JL. Jimenez, HR. Saibil, CM. Dobson,
J. Mol. Biol. (2001) 311-2 p.325
15 Structures of unliganded and ATP-bound states of the Escherichia coli chaperonin GroEL by cryoelectron microscopy
AM. Roseman, NA. Ranson, GT. Brent, SD. Fuller, HR. Saibil,
J. Struct. Biol. (2001) 135-2 p.115
16 Purified components of the Escherichia coli Tat protein transport system form a double-layered ring structure
F. Sargent, U. Gohlke, E. De Leeuw, NR. Stanley, T. Palmer, HR. Saibil, BC. Berks,
Eur. J. Biochem. (2001) 268-12 p.3361
17 Macromolecular structure determination by cryo-electron microscopy
HR. Saibil,
Acta Crystallogr. Sect. D-Biol. Crystallogr. (2000) 56- p.1215
18 Conformational changes studied by cryo-electron microscopy
HR. Saibil,
Nat. Struct. Biol. (2000) 7-9 p.711
19 Domain rotations between open, closed and bullet-shaped forms of the thermosome, an archaeal chaperonin
G. Schoehn, M. Hayes, M. Cliff, AR. Clarke, HR. Saibil,
J. Mol. Biol. (2000) 301-2 p.323
20 Molecular chaperones: containers and surfaces for folding, stabilising or unfolding proteins
HR. Saibil,
Curr. Opin. Struct. Biol. (2000) 10-2 p.251

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