Mutations can cause light chains to be too stable or too unstable to form amyloid fibrils

scientific article published on 24 August 2015

Mutations can cause light chains to be too stable or too unstable to form amyloid fibrils is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1002/PRO.2790
P932PMC publication ID4622216
P698PubMed publication ID26300552
P5875ResearchGate publication ID281226792

P50authorSandra VillegasQ37370937
P2093author name stringMarina Ramirez-Alvarado
Marta Marin-Argany
Luis M Blancas-Mejía
Jofre Güell-Bosch
P2860cites workThe paradox between m values and deltaCp's for denaturation of ribonuclease T1 with disulfide bonds intact and brokenQ42847124
Structural basis of light chain amyloidogenicity: comparison of the thermodynamic properties, fibrillogenic potential and tertiary structural features of four Vlambda6 proteins.Q44959095
Alanine scanning mutagenesis of Abeta(1-40) amyloid fibril stabilityQ46942788
Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T1.Q52487321
Thermodynamic instability of human lambda 6 light chains: correlation with fibrillogenicityQ73101377
Thermodynamic modulation of light chain amyloid fibril formationQ73357534
Protein thermal stability, hydrogen bonds, and ion pairsQ73497866
Tyrosine, phenylalanine, and disulfide contributions to the circular dichroism of proteins: circular dichroism spectra of wild-type and mutant bovine pancreatic trypsin inhibitorQ78140340
A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitroQ24672760
The contribution of polar group burial to protein stability is strongly context-dependentQ27641427
Altered Dimer Interface Decreases Stability in an Amyloidogenic ProteinQ27650295
Structural Insights into the Role of Mutations in AmyloidogenesisQ27651956
Structural Alterations within Native Amyloidogenic Immunoglobulin Light ChainsQ27654651
Kinetic Control in Protein Folding for Light Chain Amyloidosis and the Differential Effects of Somatic MutationsQ27680456
Protein misfolding, functional amyloid, and human diseaseQ28131732
Both the environment and somatic mutations govern the aggregation pathway of pathogenic immunoglobulin light chainQ28204331
Determination and analysis of urea and guanidine hydrochloride denaturation curvesQ29616644
Salts enhance both protein stability and amyloid formation of an immunoglobulin light chainQ30368702
Mechanism of thioflavin T binding to amyloid fibrils.Q31001970
Mutations in specific structural regions of immunoglobulin light chains are associated with free light chain levels in patients with AL amyloidosisQ33429992
Detection and characterization of aggregates, prefibrillar amyloidogenic oligomers, and protofibrils using fluorescence spectroscopyQ34190708
Formation of amyloid fibers by monomeric light chain variable domainsQ34283400
Structural evolution of Iowa mutant β-amyloid fibrils from polymorphic to homogeneous states under repeated seeded growthQ34694664
Amyloid formation by globular proteins under native conditionsQ34905853
The molecular basis for the chemical denaturation of proteins by ureaQ34982168
Differential effects on light chain amyloid formation depend on mutations and type of glycosaminoglycansQ35103966
A role for destabilizing amino acid replacements in light-chain amyloidosisQ35458844
Tyrosine residues mediate fibril formation in a dynamic light chain dimer interfaceQ36201752
Hsp70 and antifibrillogenic peptides promote degradation and inhibit intracellular aggregation of amyloidogenic light chainsQ36375810
Engineered turns of a recombinant antibody improve its in vivo foldingQ36706337
Potential roles of abundant extracellular chaperones in the control of amyloid formation and toxicity.Q37030603
Thermal stability threshold for amyloid formation in light chain amyloidosisQ37375492
Light chain amyloidosis - current findings and future prospectsQ37502618
Systemic amyloidosesQ38085664
An anti-Aβ (amyloid β) single-chain variable fragment prevents amyloid fibril formation and cytotoxicity by withdrawing Aβ oligomers from the amyloid pathwayQ39557102
Mutations and off-pathway aggregation of proteinsQ40534798
Steady-state and time-resolved Thioflavin-T fluorescence can report on morphological differences in amyloid fibrils formed by Aβ(1-40) and Aβ(1-42).Q41466652
The effects of sodium sulfate, glycosaminoglycans, and Congo red on the structure, stability, and amyloid formation of an immunoglobulin light-chain proteinQ41814354
Elongation of the C-terminal domain of an anti-amyloid β single-chain variable fragment increases its thermodynamic stability and decreases its aggregation tendencyQ42846245
P433issue11
P304page(s)1829-1840
P577publication date2015-08-24
P1433published inProtein ScienceQ7251445
P1476titleMutations can cause light chains to be too stable or too unstable to form amyloid fibrils
P478volume24

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cites work (P2860)
Q39056446Aggregation of Full-length Immunoglobulin Light Chains from Systemic Light Chain Amyloidosis (AL) Patients Is Remodeled by Epigallocatechin-3-gallate
Q47140242Concurrent structural and biophysical traits link with immunoglobulin light chains amyloid propensity
Q48137977Convergent mechanisms favor fast amyloid formation in two lambda 6a Ig light chain mutants.
Q39027744Differences in Protein Concentration Dependence for Nucleation and Elongation in Light Chain Amyloid Formation
Q36325334Differential recruitment efficacy of patient-derived amyloidogenic and myeloma light chain proteins by synthetic fibrils-A metric for predicting amyloid propensity
Q41606174Effect of amino acid mutations on the conformational dynamics of amyloidogenic immunoglobulin light-chains: A combined NMR and in silico study.
Q37141705Recruitment of Light Chains by Homologous and Heterologous Fibrils Shows Distinctive Kinetic and Conformational Specificity
Q47847903sw ApoMb Amyloid Aggregation under Nondenaturing Conditions: The Role of Native Structure Stability

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