Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro.
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Structural evidence for native state stabilization of a conformationally labile amyloidogenic transthyretin variant by fibrillogenesis inhibitorsNatural polyphenols inhibit different steps of the process of transthyretin (TTR) amyloid fibril formationThe 8 and 5 kDa fragments of plasma gelsolin form amyloid fibrils by a nucleated polymerization mechanism, while the 68 kDa fragment is not amyloidogenic3D domain swapping: a mechanism for oligomer assemblyMechanism 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 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 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 plasmaPotent Kinetic Stabilizers That Prevent Transthyretin-Mediated Cardiomyocyte ProteotoxicityCrystallographic 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 ConjugateTafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascadeStilbene Vinyl Sulfonamides as Fluorogenic Sensors of and Traceless Covalent Kinetic Stabilizers of Transthyretin That Prevent AmyloidogenesisProteolytic cleavage of Ser52Pro variant transthyretin triggers its amyloid fibrillogenesisStructural insights into the aggregation behavior of Murraya koenigii miraculin-like protein below pH 7.5Tertiary structure of an amyloid immunoglobulin light chain protein: a proposed model for amyloid fibril formationInhibiting transthyretin conformational changes that lead to amyloid fibril formationTertiary structures of amyloidogenic and non-amyloidogenic transthyretin variants: new model for amyloid fibril formationThe preaggregated state of an amyloidogenic protein: hydrostatic pressure converts native transthyretin into the amyloidogenic stateModulating self-assembly of amyloidogenic proteins as a therapeutic approach for neurodegenerative diseases: strategies and mechanismsRepurposing diflunisal for familial amyloid polyneuropathy: a randomized clinical trialThe role of cystatin C in cerebral amyloid angiopathy and stroke: cell biology and animal modelsBeyond genetic factors in familial amyloidotic polyneuropathy: protein glycation and the loss of fibrinogen's chaperone activityModifications 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 TetramerFunction of the Greek key connection analysed using circular permutants of superoxide dismutase.Serum transthyretin monomer in patients with familial amyloid polyneuropathy.Simulation of pH-dependent edge strand rearrangement in human beta-2 microglobulin.Fourier transform infrared spectroscopy provides a fingerprint for the tetramer and for the aggregates of transthyretin.Inhibition of the mechano-enzymatic amyloidogenesis of transthyretin: role of ligand affinity, binding cooperativity and occupancy of the inner channel.Differential expression of Cathepsin E in transthyretin amyloidosis: from neuropathology to the immune system.Formation of amyloid fibrils in vitro from partially unfolded intermediates of human gammaC-crystallin.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.Conformational Abs recognizing a generic amyloid fibril epitope.The protofilament structure of insulin amyloid fibrils.Synthesis and conformational analysis of bicyclic extended dipeptide surrogates.
P2860
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P2860
Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro.
description
1992 nî lūn-bûn
@nan
1992 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Partial denaturation of transt ...... oid fibril formation in vitro.
@ast
Partial denaturation of transt ...... oid fibril formation in vitro.
@en
Partial denaturation of transt ...... oid fibril formation in vitro.
@nl
type
label
Partial denaturation of transt ...... oid fibril formation in vitro.
@ast
Partial denaturation of transt ...... oid fibril formation in vitro.
@en
Partial denaturation of transt ...... oid fibril formation in vitro.
@nl
prefLabel
Partial denaturation of transt ...... oid fibril formation in vitro.
@ast
Partial denaturation of transt ...... oid fibril formation in vitro.
@en
Partial denaturation of transt ...... oid fibril formation in vitro.
@nl
P356
P1433
P1476
Partial denaturation of transt ...... oid fibril formation in vitro.
@en
P2093
P304
P356
10.1021/BI00151A036
P407
P577
1992-09-01T00:00:00Z