Evaluating the binding selectivity of transthyretin amyloid fibril inhibitors in blood plasma
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Natural polyphenols inhibit different steps of the process of transthyretin (TTR) amyloid fibril formationMechanism of Action and Clinical Application of Tafamidis in Hereditary Transthyretin AmyloidosisChemical 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 †Novel 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 plasmaTrapping of palindromic ligands within native transthyretin prevents amyloid formationCrystallographic Study of Novel Transthyretin Ligands Exhibiting Negative-Cooperativity between Two Thyroxine Binding SitesAromatic 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 sensorsFluorogenic small molecules requiring reaction with a specific protein to create a fluorescent conjugate for biological imaging-what we know and what we need to learnVKORC1 pharmacogenetics and pharmacoproteomics in patients on warfarin anticoagulant therapy: transthyretin precursor as a potential biomarkerTransthyretin Amyloidosis: Chaperone Concentration Changes and Increased Proteolysis in the Pathway to DiseaseImproving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methodsGenistein, a natural product from soy, is a potent inhibitor of transthyretin amyloidosisA stilbene that binds selectively to transthyretin in cells and remains dark until it undergoes a chemoselective reaction to create a bright blue fluorescent conjugate.An overview of drugs currently under investigation for the treatment of transthyretin-related hereditary amyloidosis.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.Mechanisms of transthyretin cardiomyocyte toxicity inhibition by resveratrol analogs.Analysis of striatal transcriptome in mice overexpressing human wild-type alpha-synuclein supports synaptic dysfunction and suggests mechanisms of neuroprotection for striatal neuronsBifunctional crosslinking ligands for transthyretinTargeting protein aggregation for the treatment of degenerative diseasesTransthyretin: A Transporter Protein Essential for Proliferation of Myoblast in the Myogenic Program.The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug.Semi-quantitative models for identifying potent and selective transthyretin amyloidogenesis inhibitors.Current and future treatment of amyloid diseases.Transthyretin interacts with the lysosome-associated membrane protein (LAMP-1) in circulationChaperonin-Based Biolayer Interferometry To Assess the Kinetic Stability of Metastable, Aggregation-Prone ProteinsSelective binding to transthyretin and tetramer stabilization in serum from patients with familial amyloidotic polyneuropathy by an iodinated diflunisal derivative.Synthesis and structural analysis of the N-terminal domain of the thyroid hormone-binding protein transthyretin.Native state stabilization by NSAIDs inhibits transthyretin amyloidogenesis from the most common familial disease variants.Optimization of an in vitro assay methodology for competitive binding of thyroidogenic xenobiotics with thyroxine on human transthyretin and albumin.Propagation of Fibrillar Structural Forms in Proteins Stopped by Naturally Occurring Short Polypeptide Chain Fragments.Understanding and Ameliorating the TTR Amyloidoses
P2860
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P2860
Evaluating the binding selectivity of transthyretin amyloid fibril inhibitors in blood plasma
description
2001 nî lūn-bûn
@nan
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
2001年论文
@zh
2001年论文
@zh-cn
name
Evaluating the binding selecti ...... ril inhibitors in blood plasma
@ast
Evaluating the binding selecti ...... ril inhibitors in blood plasma
@en
type
label
Evaluating the binding selecti ...... ril inhibitors in blood plasma
@ast
Evaluating the binding selecti ...... ril inhibitors in blood plasma
@en
prefLabel
Evaluating the binding selecti ...... ril inhibitors in blood plasma
@ast
Evaluating the binding selecti ...... ril inhibitors in blood plasma
@en
P2093
P2860
P356
P1476
Evaluating the binding selecti ...... ril inhibitors in blood plasma
@en
P2093
H E Purkey
M I Dorrell
P2860
P304
P356
10.1073/PNAS.091431798
P407
P577
2001-05-01T00:00:00Z