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K. Papanikolopoulou, G. Schoehn, G. Schoehn, G. Schoehn, V. Forge, V. Forsyth, C. Riekel, Jean‐François Hernandez, R. Ruigrok, A. Mitraki (2005)
Amyloid Fibril Formation from Sequences of a Natural β-Structured Fibrous Protein, the Adenovirus Fiber*Journal of Biological Chemistry, 280
C. Jaroniec, C. MacPhee, V. Bajaj, M. McMahon, C. Dobson, R. Griffin (2004)
High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America, 101 3
C. Broder, M. Davidson, V. Forsyth, J. Howard, Sarah Lamb, S. Mason (2002)
On the reliability of C-H…O interactions in crystal engineering: Synthesis and structure of two hydrogen bonded phosphonium bis(aryloxide) saltsCrystal Growth & Design, 2
(2001)
Philos
V. Forsyth, S. Mason, J. Howard, M. Davidson, W. Fuller, D. Myles (2001)
A fast new diffractometer for chemical crystallography, small proteins and fiber diffractionNeutron News, 12
Michele McDonald, A. Kendall, Motomasa Tanaka, J. Weissman, G. Stubbs (2008)
Enclosed chambers for humidity control and sample containment in fiber diffractionJournal of Applied Crystallography, 41
(2010)
ILL : Neutrons for Science : D 22
H. Inouye, Katherine Gleason, Dong Zhang, S. Decatur, Daniel Kirschner (2010)
Differential effects of phe19 and phe20 on fibril formation by amyloidogenic peptide Aβ16–22 (Ac‐KLVFFAE‐NH2)Proteins: Structure, 78
R. Nelson, M. Sawaya, M. Balbirnie, A. Madsen, C. Riekel, Robert Grothe, D. Eisenberg (2005)
Structure of the cross-β spine of amyloid-like fibrilsNature, 435
V. Laux, P. Callow, D. Svergun, P. Timmins, V. Forsyth, M. Haertlein (2008)
Selective deuteration of tryptophan and methionine residues in maltose binding protein: a model system for neutron scatteringEuropean Biophysics Journal, 37
C. Dobson (2001)
The structural basis of protein folding and its links with human disease.Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 356 1406
H. White, J. Hodgkinson, T. Jahn, Sara Cohen-Krausz, Walraj Gosal, S. Müller, E. Orlova, S. Radford, H. Saibil (2009)
Globular Tetramers of β2-Microglobulin Assemble into Elaborate Amyloid FibrilsJournal of Molecular Biology, 389
M. Shotton, L. Pope, V. Forsyth, R. Denny, J. Archer, P. Langan, H. Ye, C. Boote (1998)
New Developments in Instrumentation for X-ray and Neutron Fibre Diffraction ExperimentsJournal of Applied Crystallography, 31
A. Mahendrasingam, V. Forsyth, R. Hussain, R. Greenall, W. Pigram, W. Fuller (1986)
Time-resolved X-ray diffraction studies of the B in equilibrium D structural transition in the DNA double helix.Science, 233 4760
K. Papanikolopoulou, V. Forge, P. Goeltz, A. Mitraki (2004)
Formation of Highly Stable Chimeric Trimers by Fusion of an Adenovirus Fiber Shaft Fragment with the Foldon Domain of Bacteriophage T4 Fibritin*Journal of Biological Chemistry, 279
T. Narayanan, O. Diat, P. Bösecke (2001)
SAXS and USAXS on the high brilliance beamline at the ESRFNuclear Instruments & Methods in Physics Research Section A-accelerators Spectrometers Detectors and Associated Equipment, 467
O. Makin, L. Serpell (2005)
Structures for amyloid fibrilsThe FEBS Journal, 272
Y. Nishiyama, G. Johnson, A. French, V. Forsyth, P. Langan (2008)
Neutron crystallography, molecular dynamics, and quantum mechanics studies of the nature of hydrogen bonding in cellulose Ibeta.Biomacromolecules, 9 11
K. Papanikolopoulou, S. Teixeira, H. Belrhali, V. Forsyth, A. Mitraki, M. Raaij (2004)
Adenovirus fibre shaft sequences fold into the native triple beta-spiral fold when N-terminally fused to the bacteriophage T4 fibritin foldon trimerisation motif.Journal of molecular biology, 342 1
T. Jahn, O. Makin, Kyle Morris, K. Marshall, P. Tian, P. Sikorski, L. Serpell (2010)
The common architecture of cross-beta amyloid.Journal of molecular biology, 395 4
B. Ahrens, Matthew Davidson, V. Forsyth, M. Mahon, Andrew Johnson, Sax Mason, R. Price, P. Raithby (2001)
Neutron diffraction study of a phenol.nitroxide radical adduct: a structural model for hydrogen atom abstraction by peroxyl radicals from vitamin E and related phenolic antioxidants.Journal of the American Chemical Society, 123 37
L. Pope, M. Shotton, T. Forsyth, D. Hughes, R. Denny, W. Fuller (1998)
Structural polymorphism in a tubercidin analogue of the DNA double helix.Biophysical chemistry, 70 2
P. Callow, A. Sukhodub, James Taylor, G. Kneale (2007)
Shape and Subunit Organisation of the DNA Methyltransferase M.AhdI by Small-angle Neutron ScatteringJournal of Molecular Biology, 369
M. Raaij, A. Mitraki, Gilles Lavigne, S. Cusack (1999)
A triple β-spiral in the adenovirus fibre shaft reveals a new structural motif for a fibrous proteinNature, 401
H. Wille, Wen Bian, Michele McDonald, A. Kendall, David Colby, Lillian Bloch, J. Ollesch, Alexander Borovinskiy, F. Cohen, S. Prusiner, G. Stubbs (2009)
Natural and synthetic prion structure from X-ray fiber diffractionProceedings of the National Academy of Sciences, 106
L. Serpell (2000)
Alzheimer's amyloid fibrils: structure and assembly.Biochimica et biophysica acta, 1502 1
M. Sawaya, S. Sambashivan, R. Nelson, M. Ivanova, Stuart Sievers, M. Apostol, Michael Thompson, M. Balbirnie, Jed Wiltzius, Heather Mcfarlane, A. Madsen, C. Riekel, D. Eisenberg (2007)
Atomic structures of amyloid cross-β spines reveal varied steric zippersNature, 447
A. Paravastu, Isam Qahwash, R. Leapman, S. Meredith, R. Tycko (2009)
Seeded growth of β-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structureProceedings of the National Academy of Sciences, 106
Soichi Wakatsuki, H. Belrhali, Edward Mitchell, Wim Burmeister, Sean McSweeney, R. Kahn, Dominique Bourgeois, Min Yao, T. Tomizaki, P. Théveneau (1998)
ID14 'Quadriga', a Beamline for Protein Crystallography at the ESRF.Journal of synchrotron radiation, 5 Pt 3
J. Sanchez-Weatherby, M. Bowler, J. Huet, A. Gobbo, F. Felisaz, Bernard Lavault, R. Moya, J. Kadlec, R. Ravelli, F. Cipriani (2009)
Improving diffraction by humidity control: a novel device compatible with X-ray beamlines.Acta crystallographica. Section D, Biological crystallography, 65 Pt 12
M. Jasnin, M. Moulin, M. Haertlein, G. Zaccai, M. Tehei (2008)
In vivo measurement of internal and global macromolecular motions in Escherichia coli.Biophysical journal, 95 2
M. Sunde, L. Serpell, M. Bartlam, P. Fraser, M. Pepys, C. Blake (1997)
Common core structure of amyloid fibrils by synchrotron X-ray diffraction.Journal of molecular biology, 273 3
M. Pepys (2001)
Pathogenesis, diagnosis and treatment of systemic amyloidosis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 356 1406
V. Forsyth, A. Mahendrasingam, W. Pigram, R. Greenall, K. Bellamy, W. Fuller, S. Mason (1989)
Neutron fibre diffraction study of DNA hydration.International journal of biological macromolecules, 11 4
S. Teixeira, M. Blakeley, R. Leal, E. Mitchell, V. Forsyth (2008)
A preliminary neutron crystallographic study of thaumatin.Acta crystallographica. Section F, Structural biology and crystallization communications, 64 Pt 5
P. Langan, V. Forsyth, A. Mahendrasingam, W. Pigram, S. Mason, W. Fuller (1992)
A high angle neutron fibre diffraction study of the hydration of the A conformation of the DNA double helix.Journal of biomolecular structure & dynamics, 10 3
(2001)
Opportunities for Neutron Scattering in the 3rd Millennium
Mark Shotton, Lisa Pope, Trevor Forsyth, Paul Langan, Richard Denny, U. Giesen, Marie-Therese Dauvergne, Watson Fuller (1997)
A high-angle neutron fibre diffraction study of the hydration of deuterated A-DNA.Biophysical chemistry, 69 1
D. Kirschner, C. Abraham, D. Selkoe (1986)
X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation.Proceedings of the National Academy of Sciences of the United States of America, 83 2
V. Forsyth, R. Greenall, R. Hussain, A. Mahendrasingam, C. Nave, W. Pigram, W. Fuller (1986)
X-ray high-angle fibre diffraction studies of nucleic acid structure using the Daresbury Synchrotron Radiation Source.Biochemical Society transactions, 14 3
M. Blakeley, F. Ruiz, R. Cachau, I. Hazemann, F. Meilleur, A. Mitschler, S. Ginell, P. Afonine, O. Ventura, A. Cousido-Siah, M. Haertlein, A. Joachimiak, D. Myles, A. Podjarny (2008)
Quantum model of catalysis based on a mobile proton revealed by subatomic x-ray and neutron diffraction studies of h-aldose reductaseProceedings of the National Academy of Sciences, 105
C. Sachse, M. Fändrich, N. Grigorieff (2008)
Paired β-sheet structure of an Aβ(1-40) amyloid fibril revealed by electron microscopyProceedings of the National Academy of Sciences, 105
Emmanouil Kasotakis, E. Mossou, Lihi Adler‐Abramovich, E. Mitchell, V. Forsyth, E. Gazit, A. Mitraki (2009)
Design of metal‐binding sites onto self‐assembled peptide fibrilsPeptide Science, 92
(2002)
Cryst
Swetha Vijayakrishnan, S. Kelly, Robert Gilbert, P. Callow, D. Bhella, T. Forsyth, J. Lindsay, O. Byron (2010)
Solution Structure and Characterisation of the Human Pyruvate Dehydrogenase Complex Core AssemblyJournal of Molecular Biology, 399
A. Kovalevsky, L. Hanson, S. Fisher, M. Mustyakimov, S. Mason, V. Forsyth, M. Blakeley, D. Keen, T. Wagner, H. Carrell, A. Katz, J. Glusker, P. Langan, P. Langan (2010)
Metal ion roles and the movement of hydrogen during reaction catalyzed by D-xylose isomerase: a joint x-ray and neutron diffraction study.Structure, 18 6
(2000)
Biochim
K. Gardner, A. English, V. Forsyth (2004)
New insights into the structure of poly(p-phenylene terephthalamide) from neutron fiber diffraction studiesMacromolecules, 37
M. Blakeley, P. Langan, N. Niimura, A. Podjarny (2008)
Neutron crystallography: opportunities, challenges, and limitations.Current opinion in structural biology, 18 5
S. Teixeira, J. Ankner, M. Bellissent-Funel, R. Bewley, M. Blakeley, L. Coates, R. Dahint, R. Dalgliesh, N. Dencher, J. Dhont, P. Fischer, V. Forsyth, G. Fragneto, B. Frick, T. Geue, R. Gilles, T. Gutberlet, M. Haertlein, T. Hauß, W. Häussler, W. Heller, K. Herwig, O. Holderer, F. Jurányi, R. Kampmann, R. Knott, J. Kohlbrecher, S. Kreuger, P. Langan, R. Lechner, G. Lynn, C. Majkrzak, R. May, F. Meilleur, Y. Mo, K. Mortensen, D. Myles, F. Natali, C. Neylon, N. Niimura, J. Ollivier, A. Ostermann, J. Peters, J. Pieper, A. Rühm, D. Schwahn, K. Shibata, A. Soper, T. Straessle, U-I Suzuki, I. Tanaka, M. Tehei, P. Timmins, N. Torikai, T. Unruh, V. Urban, R. Vavrin, K. Weiss, G. Zaccai (2008)
New sources and instrumentation for neutrons in biology.Chemical physics, 345 2-3
The first neutron fibre diffraction studies of an amyloid system are presented. The techniques used to prepare the large samples needed are described, as well as the procedures used to isotopically replace H2O in the sample by D2O. The results demonstrate the feasibility of this type of approach for the pursuit of novel structural analyses that will strongly complement X‐ray fibre diffraction studies and probe aspects of amyloid structure that to date have remained obscure. The approach is demonstrated using an amyloid form of the peptide NSGAITIG, but is equally applicable for the study of other systems such as Alzheimer's Aβ peptide.
Acta Crystallographica Section F – Wiley
Published: Mar 1, 2011
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