The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions.
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Tissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue cultureCharacterization of the native and fibrillar conformation of the human Nalpha-acetyltransferase ARD1Toward 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 †A 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 RECOGNITIONCrystallographic 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 ConjugateA mathematical model of the kinetics of beta-amyloid fibril growth from the denatured stateSolution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domainAltered aggregation properties of mutant gamma-crystallins cause inherited cataractAmyloid-like fibril formation in an all beta-barrel protein involves the formation of partially structured intermediate(s).Serum transthyretin monomer in patients with familial amyloid polyneuropathy.Support for the multigenic hypothesis of amyloidosis: the binding stoichiometry of retinol-binding protein, vitamin A, and thyroid hormone influences transthyretin amyloidogenicity in vitro.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 amyloidosisDetection and characterization of aggregates, prefibrillar amyloidogenic oligomers, and protofibrils using fluorescence spectroscopy.Cataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone.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.Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity.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.TRPM8 and Nav1.8 sodium channels are required for transthyretin-induced calcium influx in growth cones of small-diameter TrkA-positive sensory neurons.The modulation of transthyretin tetramer stability by cysteine 10 adducts and the drug diflunisal. Direct analysis by fluorescence-detected analytical ultracentrifugationTargeting protein aggregation for the treatment of degenerative diseasesComputational On-Chip Imaging of Nanoparticles and Biomolecules using Ultraviolet Light.Identification of beta-amyloid-binding sites on transthyretin.The human serpin proteinase inhibitor-9 self-associates at physiological temperatures.Why is Leu55-->Pro55 transthyretin variant the most amyloidogenic: insights from molecular dynamics simulations of transthyretin monomersRepositioning tolcapone as a potent inhibitor of transthyretin amyloidogenesis and associated cellular toxicity.Localized structural fluctuations promote amyloidogenic conformations in transthyretin.A current pharmacologic agent versus the promise of next generation therapeutics to ameliorate protein misfolding and/or aggregation diseases.Quantification of the thermodynamically linked quaternary and tertiary structural stabilities of transthyretin and its disease-associated variants: the relationship between stability and amyloidosis.Induced pluripotent stem cell modeling of multisystemic, hereditary transthyretin amyloidosis.Quantification of transthyretin kinetic stability in human plasma using subunit exchange.The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug.Statistical mechanical treatments of protein amyloid formation.Capture of a dimeric intermediate during transthyretin amyloid formation.The importance of a gatekeeper residue on the aggregation of transthyretin: implications for transthyretin-related amyloidoses
P2860
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P2860
The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
1999年论文
@zh
1999年论文
@zh-cn
name
The most pathogenic transthyre ...... nder physiological conditions.
@en
type
label
The most pathogenic transthyre ...... nder physiological conditions.
@en
prefLabel
The most pathogenic transthyre ...... nder physiological conditions.
@en
P2093
P356
P1433
P1476
The most pathogenic transthyre ...... nder physiological conditions.
@en
P2093
P304
13560-13573
P356
10.1021/BI991021C
P407
P577
1999-10-01T00:00:00Z