Mutations can cause light chains to be too stable or too unstable to form amyloid fibrils
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Title
Mutations can cause light chains to be too stable or too unstable to form amyloid fibrils
Authors
Keywords
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Journal
PROTEIN SCIENCE
Volume 24, Issue 11, Pages 1829-1840
Publisher
Wiley
Online
2015-08-24
DOI
10.1002/pro.2790
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- Kinetic Control in Protein Folding for Light Chain Amyloidosis and the Differential Effects of Somatic Mutations
- (2013) Luis.M. Blancas-Mejía et al. JOURNAL OF MOLECULAR BIOLOGY
- Elongation of the C-terminal domain of an anti-amyloid β single-chain variable fragment increases its thermodynamic stability and decreases its aggregation tendency
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- (2012) Ara Celi DiCostanzo et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- An anti-Aβ (amyloid β) single-chain variable fragment prevents amyloid fibril formation and cytotoxicity by withdrawing Aβ oligomers from the amyloid pathway
- (2011) Marta Marín-Argany et al. BIOCHEMICAL JOURNAL
- Structural Evolution of Iowa Mutant β-Amyloid Fibrils from Polymorphic to Homogeneous States under Repeated Seeded Growth
- (2011) Wei Qiang et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Light Chain Amyloidosis – Current Findings and Future Prospects
- (2009) Elizabeth Baden et al. CURRENT PROTEIN & PEPTIDE SCIENCE
- Structural Alterations within Native Amyloidogenic Immunoglobulin Light Chains
- (2009) Edward G. Randles et al. JOURNAL OF MOLECULAR BIOLOGY
- Mutations in Specific Structural Regions of Immunoglobulin Light Chains Are Associated with Free Light Chain Levels in Patients with AL Amyloidosis
- (2009) Tanya L. Poshusta et al. PLoS One
- Salts enhance both protein stability and amyloid formation of an immunoglobulin light chain
- (2008) Laura A. Sikkink et al. BIOPHYSICAL CHEMISTRY
- Altered Dimer Interface Decreases Stability in an Amyloidogenic Protein
- (2008) Elizabeth M. Baden et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Structural Insights into the Role of Mutations in Amyloidogenesis
- (2008) Elizabeth M. Baden et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Amyloid formation by globular proteins under native conditions
- (2008) Fabrizio Chiti et al. Nature Chemical Biology
- Potential roles of abundant extracellular chaperones in the control of amyloid formation and toxicity
- (2007) Mark R. Wilson et al. Molecular BioSystems
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