Fibril in senile systemic amyloidosis is derived from normal transthyretin
about
The 8 and 5 kDa fragments of plasma gelsolin form amyloid fibrils by a nucleated polymerization mechanism, while the 68 kDa fragment is not amyloidogenicBinding of perlecan to transthyretin in vitroAmyloid heart disease. New frontiers and insights in pathophysiology, diagnosis, and management.Chemical 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 †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 plasmaPotent 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 cascadeX-ray crystal structure and activity of fluorenyl-based compounds as transthyretin fibrillogenesis inhibitorsStructural evidence for asymmetric ligand binding to transthyretinSynthesis and structural analysis of halogen substituted fibril formation inhibitors of Human Transthyretin (TTR)Evolving landscape in the management of transthyretin amyloidosisBeyond genetic factors in familial amyloidotic polyneuropathy: protein glycation and the loss of fibrinogen's chaperone activityThe proteome response to amyloid protein expression in vivoTransthyretin Amyloidosis: Chaperone Concentration Changes and Increased Proteolysis in the Pathway to DiseaseTetrabromobisphenol A Is an Efficient Stabilizer of the Transthyretin TetramerIs the prevalent human prion protein 129M/V mutation a living fossil from a Paleolithic panzootic superprion pandemic?Expression, purification, and in vitro cysteine-10 modification of native sequence recombinant human transthyretinThe sour side of neurodegenerative disorders: the effects of protein glycation.Is Transthyretin a Regulator of Ubc9 SUMOylation?Transthyretin variants with improved inhibition of β-amyloid aggregation.A transthyretin mutation (Tyr78Phe) associated with peripheral neuropathy, carpal tunnel syndrome and skin amyloidosis.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.Identification and quantitative analysis of human transthyretin variants in human serum by Fourier transform ion-cyclotron resonance mass spectrometry.Amyloidosis and the respiratory tractBeta arcades: recurring motifs in naturally occurring and disease-related amyloid fibrilsThe V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis.Pathologic changes and glucose homeostasis according to expression of human islet amyloid polypeptide in type 2 diabetic patientsThe relative amounts of plasma transthyretin forms in familial transthyretin amyloidosis: a quantitative analysis by Fourier transform ion-cyclotron resonance mass spectrometry.Genistein, a natural product from soy, is a potent inhibitor of transthyretin amyloidosisCharacterization of the interaction of β-amyloid with transthyretin monomers and tetramers.Detection and characterization of aggregates, prefibrillar amyloidogenic oligomers, and protofibrils using fluorescence spectroscopy.
P2860
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P2860
Fibril in senile systemic amyloidosis is derived from normal transthyretin
description
1990 nî lūn-bûn
@nan
1990 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
Fibril in senile systemic amyloidosis is derived from normal transthyretin
@ast
Fibril in senile systemic amyloidosis is derived from normal transthyretin
@en
Fibril in senile systemic amyloidosis is derived from normal transthyretin
@nl
type
label
Fibril in senile systemic amyloidosis is derived from normal transthyretin
@ast
Fibril in senile systemic amyloidosis is derived from normal transthyretin
@en
Fibril in senile systemic amyloidosis is derived from normal transthyretin
@nl
prefLabel
Fibril in senile systemic amyloidosis is derived from normal transthyretin
@ast
Fibril in senile systemic amyloidosis is derived from normal transthyretin
@en
Fibril in senile systemic amyloidosis is derived from normal transthyretin
@nl
P2093
P2860
P3181
P356
P1476
Fibril in senile systemic amyloidosis is derived from normal transthyretin
@en
P2093
B Johansson
G G Cornwell
P Westermark
P2860
P304
P3181
P356
10.1073/PNAS.87.7.2843
P407
P577
1990-04-01T00:00:00Z