The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis.
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Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosisToward Optimization of the Linker Substructure Common to Transthyretin Amyloidogenesis Inhibitors Using Biochemical and Structural Studies †Toward Optimization of the Second Aryl Substructure Common to Transthyretin Amyloidogenesis Inhibitors Using Biochemical and Structural Studies †A Substructure Combination Strategy To Create Potent and Selective Transthyretin Kinetic Stabilizers That Prevent Amyloidogenesis and CytotoxicityPotent Kinetic Stabilizers That Prevent Transthyretin-Mediated Cardiomyocyte ProteotoxicityAromatic Sulfonyl Fluorides Covalently Kinetically Stabilize Transthyretin to Prevent Amyloidogenesis while Affording a Fluorescent ConjugateAG10 inhibits amyloidogenesis and cellular toxicity of the familial amyloid cardiomyopathy-associated V122I transthyretinTafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascadeTetrabromobisphenol A Is an Efficient Stabilizer of the Transthyretin TetramerPotentially amyloidogenic conformational intermediates populate the unfolding landscape of transthyretin: insights from molecular dynamics simulations.Significance of the amyloidogenic transthyretin Val 122 Ile allele in African Americans in the Arteriosclerosis Risk in Communities (ARIC) and Cardiovascular Health (CHS) Studies.Progress in transthyretin fibrillogenesis research strengthens the amyloid hypothesis.Cataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone.Quantification of quaternary structure stability in aggregation-prone proteins under physiological conditions: the transthyretin case.Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity.Sulfated glycosaminoglycans accelerate transthyretin amyloidogenesis by quaternary structural conversionA competition assay to identify amyloidogenesis inhibitors by monitoring the fluorescence emitted by the covalent attachment of a stilbene derivative to transthyretin.Therapeutic strategies for human amyloid diseases.Protein aggregation in disease: a role for folding intermediates forming specific multimeric interactions.Amyloidogenic and non-amyloidogenic transthyretin variants interact differently with human cardiomyocytes: insights into early events of non-fibrillar tissue damage.Cooperative stabilization of transthyretin by clusterin and diflunisal.The amyloidogenic V122I transthyretin variant in elderly black Americans.Uncovering the Mechanism of Aggregation of Human Transthyretin.Repositioning tolcapone as a potent inhibitor of transthyretin amyloidogenesis and associated cellular toxicity.Age-related oxidative modifications of transthyretin modulate its amyloidogenicitySubstoichiometric inhibition of transthyretin misfolding by immune-targeting sparsely populated misfolding intermediates: a potential diagnostic and therapeutic for TTR amyloidoses.Novel conformation-specific monoclonal antibodies against amyloidogenic forms of transthyretinA current pharmacologic agent versus the promise of next generation therapeutics to ameliorate protein misfolding and/or aggregation diseases.Quantification of the thermodynamically linked quaternary and tertiary structural stabilities of transthyretin and its disease-associated variants: the relationship between stability and amyloidosis.Comparison of cardiac amyloidosis due to wild-type and V122I transthyretin in older adults referred to an academic medical centerQuantification of transthyretin kinetic stability in human plasma using subunit exchange.The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug.Gelsolin amyloidosis: genetics, biochemistry, pathology and possible strategies for therapeutic intervention.Semi-quantitative models for identifying potent and selective transthyretin amyloidogenesis inhibitors.Transthyretin V122I (pV142I)* cardiac amyloidosis: an age-dependent autosomal dominant cardiomyopathy too common to be overlooked as a cause of significant heart disease in elderly African Americans.Prevalence of the amyloidogenic transthyretin (TTR) V122I allele in 14 333 African-Americans.Destabilizing mutations alter the hydrogen exchange mechanism in ribonuclease A.Partitioning conformational intermediates between competing refolding and aggregation pathways: insights into transthyretin amyloid disease.Stability and fibril formation properties of human and fish transthyretin, and of the Escherichia coli transthyretin-related protein.Aged vervet monkeys developing transthyretin amyloidosis with the human disease-causing Ile122 allele: a valid pathological model of the human disease.
P2860
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P2860
The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis.
description
2001 nî lūn-bûn
@nan
2001 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
The V122I cardiomyopathy varia ...... ng in accelerated amyloidosis.
@ast
The V122I cardiomyopathy varia ...... ng in accelerated amyloidosis.
@en
type
label
The V122I cardiomyopathy varia ...... ng in accelerated amyloidosis.
@ast
The V122I cardiomyopathy varia ...... ng in accelerated amyloidosis.
@en
prefLabel
The V122I cardiomyopathy varia ...... ng in accelerated amyloidosis.
@ast
The V122I cardiomyopathy varia ...... ng in accelerated amyloidosis.
@en
P2093
P2860
P356
P1476
The V122I cardiomyopathy varia ...... ng in accelerated amyloidosis.
@en
P2093
P2860
P304
14943-14948
P356
10.1073/PNAS.261419998
P407
P577
2001-12-01T00:00:00Z