Conformational changes and disease — serpins, prions and Alzheimer's
- 1 December 1998
- journal article
- review article
- Published by Elsevier in Current Opinion in Structural Biology
- Vol. 8 (6), 799-809
- https://doi.org/10.1016/s0959-440x(98)80101-2
Abstract
No abstract availableKeywords
This publication has 55 references indexed in Scilit:
- Implications for function and therapy of a 2.9 å structure of binary-complexed antithrombinJournal of Molecular Biology, 1998
- Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III moduleJournal of Molecular Biology, 1998
- Wild-type α1-antitrypsin is in the canonical inhibitory conformationJournal of Molecular Biology, 1998
- Perlecan Binds to the β‐Amyloid Proteins (Aβ) of Alzheimer's Disease, Accelerates Aβ Fibril Formation, and Maintains Aβ Fibril StabilityJournal of Neurochemistry, 1997
- Common core structure of amyloid fibrils by synchrotron X-ray diffraction 1 1Edited by F. E. CohenJournal of Molecular Biology, 1997
- Conformational diseaseThe Lancet, 1997
- Biological implications of a 3 å structure of dimeric antithrombinStructure, 1994
- Structural basis of latency in plasminogen activator inhibitor-1Nature, 1992
- Amyloid Deposits and AmyloidosisNew England Journal of Medicine, 1980
- Amyloid Deposits and AmyloidosisNew England Journal of Medicine, 1980