An engineered transthyretin monomer that is nonamyloidogenic, unless it is partially denatured
about
Tissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue cultureChemical 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 proteinsAmyloidogenic Potential of Transthyretin Variants: INSIGHTS FROM STRUCTURAL AND COMPUTATIONAL ANALYSESA 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 plasmaNovel Zn2+-binding Sites in Human Transthyretin: IMPLICATIONS FOR AMYLOIDOGENESIS AND RETINOL-BINDING PROTEIN RECOGNITIONAromatic Sulfonyl Fluorides Covalently Kinetically Stabilize Transthyretin to Prevent Amyloidogenesis while Affording a Fluorescent ConjugateBifunctional 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 fibrillogenesisTransthyretin variants with improved inhibition of β-amyloid aggregation.Fourier transform infrared spectroscopy provides a fingerprint for the tetramer and for the aggregates of transthyretin.Transthyretin-derived peptides as β-amyloid inhibitors.Progress in transthyretin fibrillogenesis research strengthens the amyloid hypothesis.The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis.Characterization of the interaction of β-amyloid with transthyretin monomers and tetramers.A stilbene that binds selectively to transthyretin in cells and remains dark until it undergoes a chemoselective reaction to create a bright blue fluorescent conjugate.Initial conformational changes of human transthyretin under partially denaturing conditionsQuantification of quaternary structure stability in aggregation-prone proteins under physiological conditions: the transthyretin case.Recent progress in the understanding and treatment of transthyretin amyloidosis.Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity.Curcumin could reduce the monomer of TTR with Tyr114Cys mutation via autophagy in cell model of familial amyloid polyneuropathy.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.ATF6 activation reduces the secretion and extracellular aggregation of destabilized variants of an amyloidogenic protein.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.Unfolded protein response-induced ERdj3 secretion links ER stress to extracellular proteostasis.Cooperative stabilization of transthyretin by clusterin and diflunisal.Structure-based analysis of A19D, a variant of transthyretin involved in familial amyloid cardiomyopathy.Mechanisms of transthyretin cardiomyocyte toxicity inhibition by resveratrol analogs.The H2A-H2B dimeric kinetic intermediate is stabilized by widespread hydrophobic burial with few fully native interactions.A New Folding Kinetic Mechanism for Human Transthyretin and the Influence of the Amyloidogenic V30M Mutation.Targeting protein aggregation for the treatment of degenerative diseasesUncovering the Mechanism of Aggregation of Human Transthyretin.Identification of beta-amyloid-binding sites on transthyretin.Contributions of hydrophobic domain interface interactions to the folding and stability of human gammaD-crystallin.Repositioning tolcapone as a potent inhibitor of transthyretin amyloidogenesis and associated cellular toxicity.
P2860
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P2860
An engineered transthyretin monomer that is nonamyloidogenic, unless it is partially denatured
description
2001 nî lūn-bûn
@nan
2001 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի սեպտեմբերին 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
An engineered transthyretin mo ...... less it is partially denatured
@ast
An engineered transthyretin mo ...... less it is partially denatured
@en
An engineered transthyretin mo ...... less it is partially denatured
@nl
type
label
An engineered transthyretin mo ...... less it is partially denatured
@ast
An engineered transthyretin mo ...... less it is partially denatured
@en
An engineered transthyretin mo ...... less it is partially denatured
@nl
prefLabel
An engineered transthyretin mo ...... less it is partially denatured
@ast
An engineered transthyretin mo ...... less it is partially denatured
@en
An engineered transthyretin mo ...... less it is partially denatured
@nl
P2093
P3181
P356
P1433
P1476
An engineered transthyretin mo ...... less it is partially denatured
@en
P2093
H M Petrassi
J C Sacchettini
P304
11442-11452
P3181
P356
10.1021/BI011194D
P407
P577
2001-09-01T00:00:00Z