Inhibiting transthyretin amyloid fibril formation via protein stabilization.
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New Class of Inhibitors of Amyloid-beta Fibril Formation. IMPLICATIONS FOR THE MECHANISM OF PATHOGENESIS IN ALZHEIMER'S DISEASEBinding of epigallocatechin-3-gallate to transthyretin modulates its amyloidogenicityMechanism of Action and Clinical Application of Tafamidis in Hereditary Transthyretin AmyloidosisAssessing the causes and consequences of co-polymerization in amyloid formationChemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosisHuman-murine transthyretin heterotetramers are kinetically stable and non-amyloidogenic. A lesson in the generation of transgenic models of diseases involving oligomeric proteinsIodine Atoms: A New Molecular Feature for the Design of Potent Transthyretin Fibrillogenesis InhibitorsToward 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 CytotoxicityChemoselective small molecules that covalently modify one lysine in a non-enzyme protein in plasmaCrystallographic Study of Novel Transthyretin Ligands Exhibiting Negative-Cooperativity between Two Thyroxine Binding SitesInhibiting transthyretin conformational changes that lead to amyloid fibril formationBeyond genetic factors in familial amyloidotic polyneuropathy: protein glycation and the loss of fibrinogen's chaperone activityRational design of small-molecule stabilizers of spermine synthase dimer by virtual screening and free energy-based approachThe flavonoid luteolin, but not luteolin-7-O-glucoside, prevents a transthyretin mediated toxic responseModifications of the 7-Hydroxyl Group of the Transthyretin Ligand Luteolin Provide Mechanistic Insights into Its Binding Properties and High Plasma SpecificityTetrabromobisphenol A Is an Efficient Stabilizer of the Transthyretin TetramerA quasi-spontaneous amyloid route in a DNA binding gene regulatory domain: The papillomavirus HPV16 E2 protein.Biologic and genetic characterization of the novel amyloidogenic lambda light chain-secreting human cell lines, ALMC-1 and ALMC-2.A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea.Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methodsDesigned Trpzip-3 β-Hairpin Inhibits Amyloid Formation in Two Different Amyloid SystemsAmyloid diseases: abnormal protein aggregation in neurodegenerationDiverse clinical compounds alter the quaternary structure and inhibit the activity of an essential enzymeSmall-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation.Support for the multigenic hypothesis of amyloidosis: the binding stoichiometry of retinol-binding protein, vitamin A, and thyroid hormone influences transthyretin amyloidogenicity in vitro.Formation of amyloid fibers by monomeric light chain variable domains.Recent progress in the understanding and treatment of transthyretin amyloidosis.Stability of the transthyretin molecule as a key factor in the interaction with a-beta peptide--relevance in Alzheimer's disease.A competition assay to identify amyloidogenesis inhibitors by monitoring the fluorescence emitted by the covalent attachment of a stilbene derivative to transthyretin.Orally administered diflunisal stabilizes transthyretin against dissociation required for amyloidogenesis.Therapeutic strategies for human amyloid diseases.The modulation of transthyretin tetramer stability by cysteine 10 adducts and the drug diflunisal. Direct analysis by fluorescence-detected analytical ultracentrifugationProtein aggregation in disease: a role for folding intermediates forming specific multimeric interactions.Cooperative stabilization of transthyretin by clusterin and diflunisal.Intrinsically disordered and aggregation prone regions underlie β-aggregation in S100 proteins.Immunological approaches as therapy for Alzheimer's disease.The systemic amyloidoses: clearer understanding of the molecular mechanisms offers hope for more effective therapies.Synthesis and evaluation of transthyretin amyloidosis inhibitors containing carborane pharmacophores.Mouse senile amyloid deposition is suppressed by adenovirus-mediated overexpression of amyloid-resistant apolipoprotein A-II
P2860
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P2860
Inhibiting transthyretin amyloid fibril formation via protein stabilization.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on December 1996
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Inhibiting transthyretin amyloid fibril formation via protein stabilization.
@en
Inhibiting transthyretin amyloid fibril formation via protein stabilization.
@nl
type
label
Inhibiting transthyretin amyloid fibril formation via protein stabilization.
@en
Inhibiting transthyretin amyloid fibril formation via protein stabilization.
@nl
prefLabel
Inhibiting transthyretin amyloid fibril formation via protein stabilization.
@en
Inhibiting transthyretin amyloid fibril formation via protein stabilization.
@nl
P2093
P2860
P356
P1476
Inhibiting transthyretin amyloid fibril formation via protein stabilization.
@en
P2093
P2860
P304
15051-15056
P356
10.1073/PNAS.93.26.15051
P407
P577
1996-12-01T00:00:00Z