Supramolecular Structure in Full-Length Alzheimer's β-Amyloid Fibrils: Evidence for a Parallel β-Sheet Organization from Solid-State Nuclear Magnetic Resonance

By J. Balbach, A. Petkova, N. Oyler, O. Antzutkin, D. Gordon, S. Meredith, R. Tycko. 2002

259 citations recorded by the source corpus.

Subfields: Nuclear and High Energy Physics, Physiology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/fdd4c012b084162f634ee4e73245bd3a96a917a2

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Nuclear and High Energy Physics

1. R. Tycko
2. A. Paravastu
3. Richard Leapman
4. Wai-Ming Yau

In Physiology

1. Wai-Ming Yau
2. A. Paravastu
3. Richard Leapman
4. R. Tycko
5. C. Glabe
6. Christopher M. Dobson
7. Fabrizio Chiti

In Spectroscopy

1. Wai-Ming Yau
2. R. Tycko
3. A. Paravastu
4. Richard Leapman

Citations in the corpus

• Common mechanisms of amyloid oligomer pathogenesis in degenerative disease. (2006, background): “[6] Balbach JJ, Petkova AT, Oyler NA, Antzutkin ON, Gordon”
• Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils. (2006, methodology): “Residues 1-8 are omitted, as these residues are known to be structurally disordered from solid state NMR linewidth data (10, 11), measurements of intermolecular 13C-13C dipole-dipole couplings (37, 38), hydrogen exchange data (26, 27), and proteolysis data (61, 62).”
• Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils (2008, background): “These data show that the -strands of A 1–40 form 2 in-register parallel -sheets, as previously observed for other A 1–40 fibrils (4, 21, 22) and for amyloid fibrils formed by other polypeptides (13, 23–26).”
• Structural conversion of neurotoxic amyloid-β(1–42) oligomers to fibrils (2010, unknown): “, and there are two largely hydrophobic β-strand segments within the fibrils that have a parallel and in-register orientatio”