Review: TTR Amyloidosis—Structural Features Leading to Protein Aggregation and Their Implications on Therapeutic Strategies
- 1 June 2000
- journal article
- review article
- Published by Elsevier in Journal of Structural Biology
- Vol. 130 (2-3) , 290-299
- https://doi.org/10.1006/jsbi.2000.4273
Abstract
No abstract availableKeywords
This publication has 57 references indexed in Scilit:
- Potential treatment of transthyretin-type amyloidoses by sulfiteneurogenetics, 1999
- Electrically neutral microheterogeneity of human plasma transthyretin (prealbumin) detected by isoelectric focusing in urea gradientsElectrophoresis, 1999
- Comparative Stability and Clearance of [Met30]Transthyretin and [Met119]TransthyretinEuropean Journal of Biochemistry, 1997
- Thyroxine binding to transthyretin Met 119Endocrine, 1997
- Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helixStructure, 1996
- ‘In vitro’ amyloid fibril formation from transthyretin: the influence of ions and the amyloidogenicity of TTR variantsBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 1996
- Human plasma transthyretin (TTR) is composed of many different molecular species with modifiable stabilityNeuromuscular Disorders, 1996
- Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 ÅJournal of Molecular Biology, 1978
- Structure of human plasma prealbumin at 2.5 A resolutionJournal of Molecular Biology, 1974
- A PECULIAR FORM OF PERIPHERAL NEUROPATHYBrain, 1952