Prevention of transthyretin amyloid disease by changing protein misfolding energetics.
about
Tissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue cultureMolecular origin of polyglutamine aggregation in neurodegenerative diseases.Mechanism of Action and Clinical Application of Tafamidis in Hereditary Transthyretin AmyloidosisPharmacoperones: a new therapeutic approach for diseases caused by misfolded G protein-coupled receptorsExpanding the number of 'druggable' targets: non-enzymes and protein-protein interactionsChemical 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 proteinsToward Optimization of the Linker Substructure Common to Transthyretin Amyloidogenesis Inhibitors Using Biochemical and Structural Studies †Iodine 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 †Amyloidogenic Potential of Transthyretin Variants: INSIGHTS FROM STRUCTURAL AND COMPUTATIONAL ANALYSESNovel Transthyretin Amyloid Fibril Formation Inhibitors: Synthesis, Biological Evaluation, and X-Ray Structural AnalysisA 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 plasmaIdentification and structure of small-molecule stabilizers of 14-3-3 protein-protein interactionsPotent 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 cascadeBifunctional coumarin derivatives that inhibit transthyretin amyloidogenesis and serve as fluorescent transthyretin folding sensorsStilbene Vinyl Sulfonamides as Fluorogenic Sensors of and Traceless Covalent Kinetic Stabilizers of Transthyretin That Prevent AmyloidogenesisProteolytic cleavage of Ser52Pro variant transthyretin triggers its amyloid fibrillogenesisX-ray crystal structure and activity of fluorenyl-based compounds as transthyretin fibrillogenesis inhibitorsModulating self-assembly of amyloidogenic proteins as a therapeutic approach for neurodegenerative diseases: strategies and mechanismsRepurposing diflunisal for familial amyloid polyneuropathy: a randomized clinical trialModifications of the 7-Hydroxyl Group of the Transthyretin Ligand Luteolin Provide Mechanistic Insights into Its Binding Properties and High Plasma SpecificityIs the prevalent human prion protein 129M/V mutation a living fossil from a Paleolithic panzootic superprion pandemic?Structural and functional impact of cancer-related missense somatic mutations.Protein stability and in vivo concentration of missense mutations in phenylalanine hydroxylase.Proteolytic scanning calorimetry: a novel methodology that probes the fundamental features of protein kinetic stability.Pharmacological chaperone for α-crystallin partially restores transparency in cataract modelsA synergistic small-molecule combination directly eradicates diverse prion strain structuresAnthraquinones inhibit tau aggregation and dissolve Alzheimer's paired helical filaments in vitro and in cells.Safety and efficacy of long-term diflunisal administration in hereditary transthyretin (ATTR) amyloidosis.Identifying protein stabilizing ligands using GroEL.Tafamidis for transthyretin familial amyloid polyneuropathy: a randomized, controlled trialHighly anomalous energetics of protein cold denaturation linked to folding-unfolding kineticsGenistein, a natural product from soy, is a potent inhibitor of transthyretin amyloidosisEngineered disulfide bonds restore chaperone-like function of DJ-1 mutants linked to familial Parkinson's disease.Structure-based design of kinetic stabilizers that ameliorate the transthyretin amyloidoses
P2860
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P2860
Prevention of transthyretin amyloid disease by changing protein misfolding energetics.
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Prevention of transthyretin amyloid disease by changing protein misfolding energetics.
@ast
Prevention of transthyretin amyloid disease by changing protein misfolding energetics.
@en
Prevention of transthyretin amyloid disease by changing protein misfolding energetics.
@nl
type
label
Prevention of transthyretin amyloid disease by changing protein misfolding energetics.
@ast
Prevention of transthyretin amyloid disease by changing protein misfolding energetics.
@en
Prevention of transthyretin amyloid disease by changing protein misfolding energetics.
@nl
prefLabel
Prevention of transthyretin amyloid disease by changing protein misfolding energetics.
@ast
Prevention of transthyretin amyloid disease by changing protein misfolding energetics.
@en
Prevention of transthyretin amyloid disease by changing protein misfolding energetics.
@nl
P50
P356
P1433
P1476
Prevention of transthyretin amyloid disease by changing protein misfolding energetics
@en
P304
P356
10.1126/SCIENCE.1079589
P407
P577
2003-01-01T00:00:00Z