The Tetrameric Protein Transthyretin Dissociates to a Non-native Monomer in Solution
Open Access
- 1 November 1999
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 274 (46) , 32943-32949
- https://doi.org/10.1074/jbc.274.46.32943
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- The Crystal Structure of Amyloidogenic Leu55→ Pro Transthyretin Variant Reveals a Possible Pathway for Transthyretin Polymerization into Amyloid FibrilsJournal of Biological Chemistry, 1998
- Thyroxine binding to transthyretin Met 119Endocrine, 1997
- The Acid-Mediated Denaturation Pathway of Transthyretin Yields a Conformational Intermediate That Can Self-Assemble into AmyloidBiochemistry, 1996
- Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitroBiochemistry, 1992
- Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbonsProteins-Structure Function and Bioinformatics, 1991
- Normal transthyretin and synthetic transthyretin fragments from amyloid-like fibrils in vitroBiochemical and Biophysical Research Communications, 1991
- Production of recombinant human transthyretin with biological activities toward the understanding of the molecular basis of familial amyloidotic polyneuropathy (FAP)Biochemistry, 1991
- A sensitive assay of transthyretin (prealbumin) in human cerebrospinal fluid in nanogram amounts by ELISAClinica Chimica Acta; International Journal of Clinical Chemistry, 1991
- Amyloid fibril protein in familial amyloidotic polyneuropathy, Portuguese type. Definition of molecular abnormality in transthyretin (prealbumin).Journal of Clinical Investigation, 1984
- Structure of prealbumin: Secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 ÅJournal of Molecular Biology, 1978