Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity. - Wikidata - awgldk - TriplyDB

Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity.

Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity.

http://www.wikidata.org/entity/Q34443897

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Tissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture Mechanism of Action and Clinical Application of Tafamidis in Hereditary Transthyretin Amyloidosis Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis Natural history and therapy of TTR-cardiac amyloidosis: emerging disease-modifying therapies from organ transplantation to stabilizer and silencer drugs The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology Human-murine transthyretin heterotetramers are kinetically stable and non-amyloidogenic. A lesson in the generation of transgenic models of diseases involving oligomeric proteins Altered Dimer Interface Decreases Stability in an Amyloidogenic Protein Iodine Atoms: A New Molecular Feature for the Design of Potent Transthyretin Fibrillogenesis Inhibitors 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 ANALYSES A Substructure Combination Strategy To Create Potent and Selective Transthyretin Kinetic Stabilizers That Prevent Amyloidogenesis and Cytotoxicity Aromatic Sulfonyl Fluorides Covalently Kinetically Stabilize Transthyretin to Prevent Amyloidogenesis while Affording a Fluorescent Conjugate AG10 inhibits amyloidogenesis and cellular toxicity of the familial amyloid cardiomyopathy-associated V122I transthyretin Tafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascade Bifunctional coumarin derivatives that inhibit transthyretin amyloidogenesis and serve as fluorescent transthyretin folding sensors Stilbene Vinyl Sulfonamides as Fluorogenic Sensors of and Traceless Covalent Kinetic Stabilizers of Transthyretin That Prevent Amyloidogenesis Is the prevalent human prion protein 129M/V mutation a living fossil from a Paleolithic panzootic superprion pandemic?Intrinsic fibrillation of fast-acting insulin analogs.Sequence determinants of amyloid fibril formation Simulation of pH-dependent edge strand rearrangement in human beta-2 microglobulin.Safety and efficacy of long-term diflunisal administration in hereditary transthyretin (ATTR) amyloidosis.Model discrimination and mechanistic interpretation of kinetic data in protein aggregation studies.Fourier transform infrared spectroscopy provides a fingerprint for the tetramer and for the aggregates of transthyretin.Potentially amyloidogenic conformational intermediates populate the unfolding landscape of transthyretin: insights from molecular dynamics simulations.A possible role for miRNA silencing in disease phenotype variation in Swedish transthyretin V30M carriers.Tafamidis for transthyretin familial amyloid polyneuropathy: a randomized, controlled trial Characterization of the interaction of β-amyloid with transthyretin monomers and tetramers.Detection and characterization of aggregates, prefibrillar amyloidogenic oligomers, and protofibrils using fluorescence spectroscopy.Identification and characterization of Aβ peptide interactors in Alzheimer's disease by structural approaches.Initial conformational changes of human transthyretin under partially denaturing conditions Quantification of quaternary structure stability in aggregation-prone proteins under physiological conditions: the transthyretin case.Recent progress in the understanding and treatment of transthyretin amyloidosis.An overview of drugs currently under investigation for the treatment of transthyretin-related hereditary amyloidosis.Sulfated glycosaminoglycans accelerate transthyretin amyloidogenesis by quaternary structural conversion 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.Prevention of amyloid-like aggregation as a driving force of protein evolution.Amyloidogenic and non-amyloidogenic transthyretin variants interact differently with human cardiomyocytes: insights into early events of non-fibrillar tissue damage.Structure-based analysis of A19D, a variant of transthyretin involved in familial amyloid cardiomyopathy.Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro.

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P2860

Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity.

http://www.wikidata.org/entity/Q34443897

description

2002 nî lūn-bûn

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2002 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2002 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2002年の論文

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年學術文章

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name

Sequence-dependent denaturatio ...... in amyloid disease diversity.

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Sequence-dependent denaturatio ...... in amyloid disease diversity.

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Sequence-dependent denaturatio ...... in amyloid disease diversity.

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type

label

Sequence-dependent denaturatio ...... in amyloid disease diversity.

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Sequence-dependent denaturatio ...... in amyloid disease diversity.

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Sequence-dependent denaturatio ...... in amyloid disease diversity.

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prefLabel

Sequence-dependent denaturatio ...... in amyloid disease diversity.

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Sequence-dependent denaturatio ...... in amyloid disease diversity.

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Sequence-dependent denaturatio ...... in amyloid disease diversity.

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Sequence-dependent denaturatio ...... in amyloid disease diversity.

@en

P2093

Amy R Hurshman

http://www.w3.org/2001/XMLSchema#string

Evan T Powers

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Per Hammarström

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Xin Jiang

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P2860

Fibril in senile systemic amyloidosis is derived from normal transthyretin

Transthyretin stability as a key factor in amyloidogenesis: X-ray analysis at atomic resolution

An engineered transthyretin monomer that is nonamyloidogenic, unless it is partially denatured

Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

Protein misfolding, evolution and disease

Detection of two partially structured species in the folding process of the amyloidogenic protein beta 2-microglobulin.

Geographical distribution of TTR met30 carriers in northern Sweden: discrepancy between carrier frequency and prevalence rate.

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.

Trans-suppression of misfolding in an amyloid disease.

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16427-16432

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scholarly article

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10.1073/PNAS.202495199

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P478

99 Suppl 4

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Jeffery W. Kelly

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2002-09-25T00:00:00Z

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11104847

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12351683

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139904

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