The Crystal Structure of Amyloidogenic Leu55→ Pro Transthyretin Variant Reveals a Possible Pathway for Transthyretin Polymerization into Amyloid Fibrils
Open Access
- 1 September 1998
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 273 (38) , 24715-24722
- https://doi.org/10.1074/jbc.273.38.24715
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Structure-dependent, competitive interaction of hydroxy-polychlorobiphenyls, -dibenzo-p-dioxins and -dibenzofurans with human transthyretinPublished by Elsevier ,2002
- Structure of the Val122Ile Variant Transthyretin – a Cardiomyopathic MutantActa Crystallographica Section D-Biological Crystallography, 1996
- Crystallization and preliminary X-ray diffraction studies of Leu55Pro variant transthyretinActa Crystallographica Section D-Biological Crystallography, 1996
- Structural changes in transthyretin produced by the Ile 84 Ser mutation which result in decreased affinity for retinol-binding proteinAmyloid, 1996
- Structure of a complex of two plasma proteins: transthyretin and retinol-binding proteinScience, 1995
- Transthyretin mutations in health and diseaseHuman Mutation, 1995
- AMoRe: an automated package for molecular replacementActa Crystallographica Section A Foundations of Crystallography, 1994
- Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 ÅJournal of Molecular Biology, 1978
- Metabolism of the Vitamin A Transporting Protein ComplexEuropean Journal of Clinical Investigation, 1973
- A PECULIAR FORM OF PERIPHERAL NEUROPATHYBrain, 1952