Domain Stability in Immunoglobulin Light Chain Deposition Disorders
References (178)
- et al.
Biochim. Biophys. Acta
(1991) - et al.
Biochim. Biophys. Acta
(1996) - et al.
Structure
(1996) - et al.
Neurosci. Lett.
(1996) Hermat./Oncol. Clin. North Am.
(1992)- et al.
Folding Des.
(1996) - et al.
J. Biol. Chem.
(1993) - et al.
Blood
(1992) - et al.
Biochem. Biophys. Res. Commun.
(1988) - et al.
Mol. Immunol
(1986)
Trends Biotechnol.
Biochem. Biophys. Res. Commun.
J. Biol. Chem.
Kidney Int.
J. Biol. Chem.
Chem. Biol.
J. Mol. Biol.
Biophys J.
J. Biol. Chem.
Cell
J. Biol. Chem.
Curr Opin. Struct. Biol.
Mol Immunol.
Biopolymers
Verhandl. Deutsch. Path. Gesellsch.
Biochem. J.
Proc. Natl. Acad. Sci. USA
Protein Sci.
“Introduction to Protein Structure”
Biotechnology
Ann. Int. Med.
Proc. Natl. Acad. Sci. USA
Manuscript submitted.
Biochemistry
Int. J. Dermatol.
Biochemistry
Science
“Proteins: Structures and Molecular Properties”
Protein Sci.
Scand.J. Immunol.
J. Histochem. Cytochem.
Eur. J. Biochem.
Proc. Natl. Acad. Sci. USA
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A Stable Mutant Predisposes Antibody Domains to Amyloid Formation through Specific Non-Native Interactions
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2015, Journal of Biological ChemistryKinetic control in protein folding for light chain amyloidosis and the differential effects of somatic mutations
2014, Journal of Molecular BiologyCitation Excerpt :Numerous experimental reports have implicated thermodynamic stability as one of the major modulators of light chain amyloidogenicity. Studies using light chain proteins from AL amyloidosis patients [4–12] have shown that mutations (somatic and otherwise destabilizing) that reduce thermodynamic stability make the proteins more prone to form amyloid fibrils. Based on these reports, an empirical rule has been proposed that amyloidogenic light chains are less thermodynamically stable than their non-amyloidogenic counterparts [10,13,14].
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