3D structure of Alzheimer's amyloid-β(1–42) fibrils

By Thorsten Lührs, C. Ritter, M. Adrian, Dominique Riek-Loher, B. Bohrmann, H. Döbeli, D. Schubert, Roland Riek. 2005

1,866 citations recorded by the source corpus.

Subfields: Molecular Biology, Physiology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/21f5247e8d040f2523c8aea0479a128db264cbaf

Citations in the corpus

• Structural conversion of neurotoxic amyloid-β(1–42) oligomers to fibrils (2010, neutral): “Our model differs from the one proposed by Lührs et al. 14 with respect to the specific side-chain packing arrangement within the β -turn- β unit.”
• Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. (2017, neutral): “…number a Colvin et al. 2016 ssNMR Bertini et al. 2011 ssNMR Paravastu et al. 2008 ssNMR Petkova et al. 2006 ssNMR Kheterpal et al. 2006 H/D exchange Lührs et al. 2005 H/D + ssNMR Török et al. 2002 EPR –2.0 –1.5 –1.0 –0.5 0.0 0.5 1.0 1.5 0 20 40 60 80 100 A gg re ga ti on p ro pe ns it…”