D18G transthyretin is monomeric, aggregation prone, and not detectable in plasma and cerebrospinal fluid: a prescription for central nervous system amyloidosis?
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Tissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue cultureSequence determinants of protein aggregation: tools to increase protein solubility.Mechanism of Action and Clinical Application of Tafamidis in Hereditary Transthyretin AmyloidosisToward 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 †Amyloidogenic 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 CytotoxicityEndoplasmic reticulum quality control and systemic amyloid disease: Impacting protein stability from the inside outAmyloidogenic propensity of a natural variant of human apolipoprotein A-I: stability and interaction with ligandsExpression, purification, and in vitro cysteine-10 modification of native sequence recombinant human transthyretinBiochemical characteristics of variant transthyretins causing hereditary leptomeningeal amyloidosis.Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival.Fourier transform infrared spectroscopy provides a fingerprint for the tetramer and for the aggregates of transthyretin.Uptake of aggregating transthyretin by fat body in a Drosophila model for TTR-associated amyloidosis.Recent progress in the understanding and treatment of transthyretin 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.ATF6 activation reduces the secretion and extracellular aggregation of destabilized variants of an amyloidogenic protein.The modulation of transthyretin tetramer stability by cysteine 10 adducts and the drug diflunisal. Direct analysis by fluorescence-detected analytical ultracentrifugationUnfolded protein response-induced ERdj3 secretion links ER stress to extracellular proteostasis.Synthesis and evaluation of transthyretin amyloidosis inhibitors containing carborane pharmacophores.Lys-315 at the Interfaces of Diagonal Subunits of δ-Crystallin Plays a Critical Role in the Reversibility of Folding and Subunit Assembly.Enhanced Aromatic Sequons Increase Oligosaccharyltransferase Glycosylation Efficiency and Glycan Homogeneity.Inhibition of human transthyretin aggregation by non-steroidal anti-inflammatory compounds: a structural and thermodynamic analysisTransthyretin as both a sensor and a scavenger of β-amyloid oligomersA current pharmacologic agent versus the promise of next generation therapeutics to ameliorate protein misfolding and/or aggregation diseases.Stress-independent activation of XBP1s and/or ATF6 reveals three functionally diverse ER proteostasis environmentsQuantification of the thermodynamically linked quaternary and tertiary structural stabilities of transthyretin and its disease-associated variants: the relationship between stability and amyloidosis.Studies on bacterial inclusion bodies.The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug.Gelsolin amyloidosis: genetics, biochemistry, pathology and possible strategies for therapeutic intervention.Semi-quantitative models for identifying potent and selective transthyretin amyloidogenesis inhibitors.Endoplasmic reticulum quality control regulates the fate of transthyretin variants in the cell.Transthyretin Binding Heterogeneity and Anti-amyloidogenic Activity of Natural Polyphenols and Their MetabolitesPathological, biochemical, and biophysical characteristics of the transthyretin variant Y114H (p.Y134H) explain its very mild clinical phenotype.The Endoplasmic Reticulum-associated Degradation of Transthyretin Variants Is Negatively Regulated by BiP in Mammalian Cells.Partitioning conformational intermediates between competing refolding and aggregation pathways: insights into transthyretin amyloid disease.Aged vervet monkeys developing transthyretin amyloidosis with the human disease-causing Ile122 allele: a valid pathological model of the human disease.CSP-1103 (CHF5074) stabilizes human transthyretin in healthy human subjects.Pathogenesis of transthyretin amyloidosis.
P2860
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P2860
D18G transthyretin is monomeric, aggregation prone, and not detectable in plasma and cerebrospinal fluid: a prescription for central nervous system amyloidosis?
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
D18G transthyretin is monomeri ...... al nervous system amyloidosis?
@ast
D18G transthyretin is monomeri ...... al nervous system amyloidosis?
@en
D18G transthyretin is monomeri ...... al nervous system amyloidosis?
@nl
type
label
D18G transthyretin is monomeri ...... al nervous system amyloidosis?
@ast
D18G transthyretin is monomeri ...... al nervous system amyloidosis?
@en
D18G transthyretin is monomeri ...... al nervous system amyloidosis?
@nl
prefLabel
D18G transthyretin is monomeri ...... al nervous system amyloidosis?
@ast
D18G transthyretin is monomeri ...... al nervous system amyloidosis?
@en
D18G transthyretin is monomeri ...... al nervous system amyloidosis?
@nl
P2093
P50
P356
P1433
P1476
D18G transthyretin is monomeri ...... al nervous system amyloidosis?
@en
P2093
Amareth Lim
Ferenc Garzuly
Joleen T White
Klaus Altland
Per Hammarström
Yoshiki Sekijima
P304
P356
10.1021/BI027319B
P407
P577
2003-06-01T00:00:00Z