Formation of amyloid-like fibrils by self-association of a partially unfolded fibronectin type III module
- 10 July 1998
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 280 (2), 245-258
- https://doi.org/10.1006/jmbi.1998.1863
Abstract
No abstract availableKeywords
This publication has 45 references indexed in Scilit:
- The conformational equilibrium of human growth hormoneJournal of Molecular Biology, 1998
- A comparison of the folding kinetics and thermodynamics of two homologous fibronectin type III modulesJournal of Molecular Biology, 1997
- A novel role for the integrin-binding III-10 module in fibronectin matrix assembly.The Journal of cell biology, 1996
- Reversible Association of the Equilibrium Unfolding Intermediate of λ Cro RepressorJournal of Molecular Biology, 1996
- Examination of the Structure of the Transthyretin Amyloid Fibril by Image Reconstruction from Electron MicrographsJournal of Molecular Biology, 1995
- Assembly of fibronectin into extracellular matrixCurrent Opinion in Structural Biology, 1993
- Domain structure and domain-domain interactions in the carboxy-terminal heparin binding region of fibronectinJournal of Molecular Biology, 1992
- Domain structure and interactions of the type I and type II modules in the gelatin-binding region of fibronectin: All six modules are independently foldedJournal of Molecular Biology, 1991
- Inhibition of binding of fibronectin to matrix assembly sites by anti-integrin (alpha 5 beta 1) antibodies.The Journal of cell biology, 1990
- Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroismJournal of Molecular Biology, 1980