β2-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro
- 1 October 2001
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 313 (3) , 559-571
- https://doi.org/10.1006/jmbi.2001.5071
Abstract
No abstract availableKeywords
This publication has 51 references indexed in Scilit:
- Ultrastructural Organization of Amyloid Fibrils byAtomic Force MicroscopyBiophysical Journal, 2000
- The protofilament substructure of amyloid fibrils11Edited by F. E. CohenJournal of Molecular Biology, 2000
- Monitoring the assembly of Ig light-chain amyloid fibrils by atomic force microscopyProceedings of the National Academy of Sciences, 1999
- Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packingThe EMBO Journal, 1999
- Watching amyloid fibrils grow by time-lapse atomic force microscopy 1 1Edited by W. BaumeisterJournal of Molecular Biology, 1999
- Polymorphic Fibrillar Assembly of Human AmylinJournal of Structural Biology, 1997
- Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helixStructure, 1996
- Thioflavine T interaction with amyloid β-sheet structuresAmyloid, 1995
- AMYLOIDOSISAnnual Review of Biochemistry, 1992
- ON THE BINDING OF CONGO RED BY AMYLOIDJournal of Histochemistry & Cytochemistry, 1962