The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid.
about
Deficiency of disulfide bonds facilitating fibrillogenesis of endostatinCharacterization of the native and fibrillar conformation of the human Nalpha-acetyltransferase ARD1A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitroMechanism 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 prognosisCrystal structure of monomeric human -2-microglobulin reveals clues to its amyloidogenic propertiesHuman-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 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 CytotoxicityNovel 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 ConjugateStilbene Vinyl Sulfonamides as Fluorogenic Sensors of and Traceless Covalent Kinetic Stabilizers of Transthyretin That Prevent AmyloidogenesisInhibiting transthyretin conformational changes that lead to amyloid fibril formationTertiary structures of amyloidogenic and non-amyloidogenic transthyretin variants: new model for amyloid fibril formationFast-folding proteins under stressThe preaggregated state of an amyloidogenic protein: hydrostatic pressure converts native transthyretin into the amyloidogenic stateThe Hofmeister effect on amyloid formation using yeast prion proteinRole of the single disulphide bond of beta(2)-microglobulin in amyloidosis in vitroExperimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrilsUV-light exposed prion protein fails to form amyloid fibrilsThe 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 SpecificityAmyloid-like fibril formation in an all beta-barrel protein. Partially structured intermediate state(s) is a precursor for fibril formation.Amyloid fibril formation by an SH3 domain.Transthyretin variants with improved inhibition of β-amyloid aggregation.Serum transthyretin monomer in patients with familial amyloid polyneuropathy.Identification of S-sulfonation and S-thiolation of a novel transthyretin Phe33Cys variant from a patient diagnosed with familial transthyretin amyloidosisFourier transform infrared spectroscopy provides a fingerprint for the tetramer and for the aggregates of transthyretin.Effect of simulated air dive and decompression sickness on the plasma proteome of rats.Potentially amyloidogenic conformational intermediates populate the unfolding landscape of transthyretin: insights from molecular dynamics simulations.Gene expression profile in hereditary transthyretin amyloidosis: differences in targeted and source organsIdentifying the amylome, proteins capable of forming amyloid-like fibrilsLarge proteins have a great tendency to aggregate but a low propensity to form amyloid fibrilsSupport for the multigenic hypothesis of amyloidosis: the binding stoichiometry of retinol-binding protein, vitamin A, and thyroid hormone influences transthyretin amyloidogenicity in vitro.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.Genistein, a natural product from soy, is a potent inhibitor of transthyretin amyloidosisAssembly and kinetic folding pathways of a tetrameric beta-sheet complex: molecular dynamics simulations on simplified off-lattice protein modelsDetection and characterization of aggregates, prefibrillar amyloidogenic oligomers, and protofibrils using fluorescence spectroscopy.
P2860
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P2860
The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid.
description
1996 nî lūn-bûn
@nan
1996 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
The acid-mediated denaturation ...... an self-assemble into amyloid.
@ast
The acid-mediated denaturation ...... an self-assemble into amyloid.
@en
The acid-mediated denaturation ...... an self-assemble into amyloid.
@nl
type
label
The acid-mediated denaturation ...... an self-assemble into amyloid.
@ast
The acid-mediated denaturation ...... an self-assemble into amyloid.
@en
The acid-mediated denaturation ...... an self-assemble into amyloid.
@nl
prefLabel
The acid-mediated denaturation ...... an self-assemble into amyloid.
@ast
The acid-mediated denaturation ...... an self-assemble into amyloid.
@en
The acid-mediated denaturation ...... an self-assemble into amyloid.
@nl
P2093
P356
P1433
P1476
The acid-mediated denaturation ...... an self-assemble into amyloid.
@en
P2093
P304
P356
10.1021/BI952501G
P407
P577
1996-05-01T00:00:00Z