Altered Dimer Interface Decreases Stability in an Amyloidogenic Protein
Open Access
- 1 June 2008
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 283 (23) , 15853-15860
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- The effects of sodium sulfate, glycosaminoglycans, and Congo red on the structure, stability, and amyloid formation of an immunoglobulin light‐chain proteinProtein Science, 2006
- (CAG)n-hairpin DNA binds to Msh2–Msh3 and changes properties of mismatch recognitionNature Structural & Molecular Biology, 2005
- Coot: model-building tools for molecular graphicsActa Crystallographica Section D Structural Biology, 2004
- Therapeutic approaches to protein-misfolding diseasesNature, 2003
- Three-dimensional structure of an immunoglobulin light-chain dimer with amyloidogenic propertiesActa Crystallographica Section D Structural Biology, 2002
- Use of TLS parameters to model anisotropic displacements in macromolecular refinementActa Crystallographica Section D Structural Biology, 2001
- Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9 1 1Edited by A. R. FershtJournal of Molecular Biology, 1999
- Extended Analysis of AL-Amyloid Protein from Abdominal Wall Subcutaneous Fat Biopsy: Kappa IV Immunoglobulin Light ChainBiochemical and Biophysical Research Communications, 1998
- Refinement of Macromolecular Structures by the Maximum-Likelihood MethodActa Crystallographica Section D Structural Biology, 1997
- [20] Processing of X-ray diffraction data collected in oscillation mode1997