β2-Microglobulin H31Y Variant 3D Structure Highlights the Protein Natural Propensity Towards Intermolecular Aggregation
- 23 January 2004
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 335 (4) , 1051-1064
- https://doi.org/10.1016/j.jmb.2003.11.040
Abstract
No abstract availableKeywords
This publication has 45 references indexed in Scilit:
- The role of disulfide bond in the amyloidogenic state of β2‐microglobulin studied by heteronuclear NMRProtein Science, 2002
- Crystal structure of monomeric human β-2-microglobulin reveals clues to its amyloidogenic propertiesProceedings of the National Academy of Sciences, 2002
- The solution structure of human β2‐microglobulin reveals the prodromes of its amyloid transitionProtein Science, 2002
- The Intrachain Disulfide Bond of 2-Microglobulin Is Not Essential for the Immunoglobulin Fold at Neutral pH, but Is Essential for Amyloid Fibril Formation at Acidic pHThe Journal of Biochemistry, 2002
- Role of the single disulphide bond of β2‐microglobulin in amyloidosis in vitroProtein Science, 2001
- β 2‐microglobulin can be refolded into a native state from ex vivo amyloid fibrilsEuropean Journal of Biochemistry, 1998
- Beta-2-Microglobulin-Associated AmyloidosisNephron, 1996
- Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolutionJournal of Molecular Biology, 1991
- Three-dimensional structure of beta 2-microglobulin.Proceedings of the National Academy of Sciences, 1985
- A new form of amyloid protein associated with chronic hemodialysis was identified as β2-microglobulinBiochemical and Biophysical Research Communications, 1985