Mutations can cause light chains to be too stable or too unstable to form amyloid fibrils.
about
Differential recruitment efficacy of patient-derived amyloidogenic and myeloma light chain proteins by synthetic fibrils-A metric for predicting amyloid propensity.Recruitment of Light Chains by Homologous and Heterologous Fibrils Shows Distinctive Kinetic and Conformational Specificity.Differences in Protein Concentration Dependence for Nucleation and Elongation in Light Chain Amyloid Formation.Aggregation of Full-length Immunoglobulin Light Chains from Systemic Light Chain Amyloidosis (AL) Patients Is Remodeled by Epigallocatechin-3-gallate.Effect of amino acid mutations on the conformational dynamics of amyloidogenic immunoglobulin light-chains: A combined NMR and in silico study.Concurrent structural and biophysical traits link with immunoglobulin light chains amyloid propensity.sw ApoMb Amyloid Aggregation under Nondenaturing Conditions: The Role of Native Structure Stability.Convergent mechanisms favor fast amyloid formation in two lambda 6a Ig light chain mutants.
P2860
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P2860
Mutations can cause light chains to be too stable or too unstable to form amyloid fibrils.
description
2015 nî lūn-bûn
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2015年の論文
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2015年論文
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2015年論文
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2015年論文
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2015年論文
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2015年論文
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2015年论文
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2015年论文
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2015年论文
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name
Mutations can cause light chai ...... table to form amyloid fibrils.
@en
type
label
Mutations can cause light chai ...... table to form amyloid fibrils.
@en
prefLabel
Mutations can cause light chai ...... table to form amyloid fibrils.
@en
P2093
P2860
P356
P1433
P1476
Mutations can cause light chai ...... table to form amyloid fibrils.
@en
P2093
Jofre Güell-Bosch
Luis M Blancas-Mejía
Marina Ramirez-Alvarado
Marta Marin-Argany
P2860
P304
P356
10.1002/PRO.2790
P577
2015-08-24T00:00:00Z