Mutations in specific structural regions of immunoglobulin light chains are associated with free light chain levels in patients with AL amyloidosis.
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Amyloid formation in light chain amyloidosisA Single Mutation Promotes Amyloidogenicity through a Highly Promiscuous Dimer InterfaceUtility of Doppler myocardial imaging, cardiac biomarkers, and clonal immunoglobulin genes to assess left ventricular performance and stratify risk following peripheral blood stem cell transplantation in patients with systemic light chain amyloidosiUsing simple artificial intelligence methods for predicting amyloidogenesis in antibodiesSite-directed mutagenesis reveals regions implicated in the stability and fiber formation of human λ3r light chainsStability engineering of anti-EGFR scFv antibodies by rational design of a lambda-to-kappa swap of the VL framework using a structure-guided approachCurrent perspectives on cardiac amyloidosis.Effect of single point mutations in a form of systemic amyloidosis.Assessment of renal response with urinary exosomes in patients with AL amyloidosis: A proof of concept.Thermal stability threshold for amyloid formation in light chain amyloidosis.Systemic amyloidoses.Emerging Advances in the Management of Cardiac Amyloidosis.Mutations can cause light chains to be too stable or too unstable to form amyloid fibrils.Effect of amino acid mutations on the conformational dynamics of amyloidogenic immunoglobulin light-chains: A combined NMR and in silico study.Cytotoxicity of amyloidogenic immunoglobulin light chains in cell culture.A residue-specific shift in stability and amyloidogenicity of antibody variable domains.Epigallocatechin-3-gallate preferentially induces aggregation of amyloidogenic immunoglobulin light chains.Screening and differential diagnosis of renal light chain-associated diseases.Structure and energetic basis of overrepresented λ light chain in systemic light chain amyloidosis patients.Mechanisms of recognition of amyloid-β (Aβ) monomer, oligomer, and fibril by homologous antibodies.Kinetic stability and sequence/structure studies of urine-derived Bence-Jones proteins from multiple myeloma and light chain amyloidosis patients.
P2860
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P2860
Mutations in specific structural regions of immunoglobulin light chains are associated with free light chain levels in patients with AL amyloidosis.
description
2009 nî lūn-bûn
@nan
2009 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Mutations in specific structur ...... patients with AL amyloidosis.
@ast
Mutations in specific structur ...... patients with AL amyloidosis.
@en
type
label
Mutations in specific structur ...... patients with AL amyloidosis.
@ast
Mutations in specific structur ...... patients with AL amyloidosis.
@en
prefLabel
Mutations in specific structur ...... patients with AL amyloidosis.
@ast
Mutations in specific structur ...... patients with AL amyloidosis.
@en
P2093
P2860
P1433
P1476
Mutations in specific structur ...... patients with AL amyloidosis.
@en
P2093
Laura A Sikkink
Marina Ramirez-Alvarado
Raynell J Clark
Tanya L Poshusta
P2860
P356
10.1371/JOURNAL.PONE.0005169
P407
P577
2009-04-13T00:00:00Z