The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug.
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Structural evidence for native state stabilization of a conformationally labile amyloidogenic transthyretin variant by fibrillogenesis inhibitorsMechanism of Action and Clinical Application of Tafamidis in Hereditary Transthyretin AmyloidosisFunctional Amyloid Signaling via the Inflammasome, Necrosome, and Signalosome: New Therapeutic Targets in Heart FailureMechanisms of islet amyloidosis toxicity in type 2 diabetesExpanding proteostasis by membrane trafficking networksSelf-propagation of pathogenic protein aggregates in neurodegenerative diseasesProtein homeostasis as a therapeutic target for diseases of protein conformationExpanding the number of 'druggable' targets: non-enzymes and protein-protein interactionsNatural history and therapy of TTR-cardiac amyloidosis: emerging disease-modifying therapies from organ transplantation to stabilizer and silencer drugsAromatic Sulfonyl Fluorides Covalently Kinetically Stabilize Transthyretin to Prevent Amyloidogenesis while Affording a Fluorescent ConjugateStilbene Vinyl Sulfonamides as Fluorogenic Sensors of and Traceless Covalent Kinetic Stabilizers of Transthyretin That Prevent AmyloidogenesisStructural evidence for asymmetric ligand binding to transthyretinFirst European consensus for diagnosis, management, and treatment of transthyretin familial amyloid polyneuropathySpreading of pathology in neurodegenerative diseases: a focus on human studiesEndoplasmic reticulum quality control and systemic amyloid disease: Impacting protein stability from the inside outModifications of the 7-Hydroxyl Group of the Transthyretin Ligand Luteolin Provide Mechanistic Insights into Its Binding Properties and High Plasma SpecificityIdentification of fibrillogenic regions in human triosephosphate isomerase.Biology and genetics of prions causing neurodegenerationCataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.Using pharmacological chaperones to restore proteostasisA chaperone trap contributes to the onset of cystic fibrosis.FAP neuropathy and emerging treatments.An overview of drugs currently under investigation for the treatment of transthyretin-related hereditary amyloidosis.Noncerebral Amyloidoses: Aspects on Seeding, Cross-Seeding, and Transmission.A consensus method for the prediction of 'aggregation-prone' peptides in globular proteins.ATF6 activation reduces the secretion and extracellular aggregation of destabilized variants of an amyloidogenic protein.Recent advances in transthyretin amyloidosis therapyTransthyretin is a key regulator of myoblast differentiation.Irreversible denaturation of maltodextrin glucosidase studied by differential scanning calorimetry, circular dichroism, and turbidity measurementsCooperative stabilization of transthyretin by clusterin and diflunisal.Intrinsically disordered and aggregation prone regions underlie β-aggregation in S100 proteins.Cardiac amyloidosis in a heart transplant patient - A case report and retrospective analysis of amyloidosis evolution.Structure-based analysis of A19D, a variant of transthyretin involved in familial amyloid cardiomyopathy.In vivo detection of nerve injury in familial amyloid polyneuropathy by magnetic resonance neurography.A multi-pathway perspective on protein aggregation: implications for control of the rate and extent of amyloid formation.Structure-Based Small Molecule Modulation of a Pre-Amyloid State: Pharmacological Enhancement of IAPP Membrane-Binding and Toxicity.Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiationAn Enzyme from Aristolochia indica Destabilizes Fibrin-β Amyloid Co-Aggregate: Implication in Cerebrovascular Diseases.Transthyretin deposition in articular cartilage: a novel mechanism in the pathogenesis of osteoarthritis.Personalized medicine approach for optimizing the dose of tafamidis to potentially ameliorate wild-type transthyretin amyloidosis (cardiomyopathy).
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P2860
The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug.
description
article científic
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article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
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artigo científico
@pt-br
artikel ilmiah
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artikull shkencor
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artículo científico
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name
The transthyretin amyloidoses: ...... gulatory-agency-approved drug.
@en
The transthyretin amyloidoses: ...... gulatory-agency-approved drug.
@nl
type
label
The transthyretin amyloidoses: ...... gulatory-agency-approved drug.
@en
The transthyretin amyloidoses: ...... gulatory-agency-approved drug.
@nl
prefLabel
The transthyretin amyloidoses: ...... gulatory-agency-approved drug.
@en
The transthyretin amyloidoses: ...... gulatory-agency-approved drug.
@nl
P2093
P2860
P1476
The transthyretin amyloidoses: ...... gulatory-agency-approved drug.
@en
P2093
Colleen Fearns
Stephen Connelly
Steven M Johnson
P2860
P304
P356
10.1016/J.JMB.2011.12.060
P407
P577
2012-01-05T00:00:00Z