Trapping of palindromic ligands within native transthyretin prevents amyloid formation - Wikidata - awgldk - TriplyDB

Trapping of palindromic ligands within native transthyretin prevents amyloid formation

Trapping of palindromic ligands within native transthyretin prevents amyloid formation

http://www.wikidata.org/entity/Q27665687

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Aromatic Sulfonyl Fluorides Covalently Kinetically Stabilize Transthyretin to Prevent Amyloidogenesis while Affording a Fluorescent Conjugate Tafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascade Proteolytic cleavage of Ser52Pro variant transthyretin triggers its amyloid fibrillogenesis Systemic amyloidosis: lessons from β2-microglobulin.Inhibition of the mechano-enzymatic amyloidogenesis of transthyretin: role of ligand affinity, binding cooperativity and occupancy of the inner channel.Binding site asymmetry in human transthyretin: insights from a joint neutron and X-ray crystallographic analysis using perdeuterated protein Bifunctional crosslinking ligands for transthyretin A novel mechano-enzymatic cleavage mechanism underlies transthyretin amyloidogenesis.Updates in cardiac amyloidosis: a review.Statistical discovery of site inter-dependencies in sub-molecular hierarchical protein structuring Substoichiometric inhibition of transthyretin misfolding by immune-targeting sparsely populated misfolding intermediates: a potential diagnostic and therapeutic for TTR amyloidoses.Protein folding and aggregation into amyloid: the interference by natural phenolic compounds Disorder transitions and conformational diversity cooperatively modulate biological function in proteins.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.Oleuropein aglycone and polyphenols from olive mill waste water ameliorate cognitive deficits and neuropathology.Preliminary neutron crystallographic study of human transthyretin Transthyretin Binding Heterogeneity and Anti-amyloidogenic Activity of Natural Polyphenols and Their Metabolites Emerging therapeutic targets currently under investigation for the treatment of systemic amyloidosis.Stabilization of protein-protein interactions in drug discovery.Multivalent helix mimetics for PPI-inhibition.Ion mobility coupled to native mass spectrometry as a relevant tool to investigate extremely small ligand-induced conformational changes.

P2860

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P2860

Trapping of palindromic ligands within native transthyretin prevents amyloid formation

http://www.wikidata.org/entity/Q27665687

description

2010 nî lūn-bûn

@nan

2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Trapping of palindromic ligands within native transthyretin prevents amyloid formation

@ast

Trapping of palindromic ligands within native transthyretin prevents amyloid formation

@en

Trapping of palindromic ligands within native transthyretin prevents amyloid formation

@nl

type

label

Trapping of palindromic ligands within native transthyretin prevents amyloid formation

@ast

Trapping of palindromic ligands within native transthyretin prevents amyloid formation

@en

Trapping of palindromic ligands within native transthyretin prevents amyloid formation

@nl

prefLabel

Trapping of palindromic ligands within native transthyretin prevents amyloid formation

@ast

Trapping of palindromic ligands within native transthyretin prevents amyloid formation

@en

Trapping of palindromic ligands within native transthyretin prevents amyloid formation

@nl

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PNAS.1008255107

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

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Trapping of palindromic ligands within native transthyretin prevents amyloid formation

@en

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Alexander J A Cobb

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Angus J Morrison

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Glenys A Tennent

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Graham W Taylor

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Jane Mitchell

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Margaret G McCammon

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Martin D Smith

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Palma P Mangione

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Raj Gill

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Stéphanie Deroo

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P2860

Synthesis and characterization of potent bivalent amyloidosis inhibitors that bind prior to transthyretin tetramerization

Diflunisal analogues stabilize the native state of transthyretin. Potent inhibition of amyloidogenesis

Biochemical and structural evaluation of highly selective 2-arylbenzoxazole-based transthyretin amyloidogenesis inhibitors

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

Coot: model-building tools for molecular graphics

Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling

Refinement of macromolecular structures by the maximum-likelihood method

The integration of macromolecular diffraction data

Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis

Targeting C-reactive protein for the treatment of cardiovascular disease.

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20483-20488

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scholarly article

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10.1073/PNAS.1008255107

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47

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107

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Timothy D Warner

Simon Erik Kolstoe

Carol V. Robinson

Anthony G Coyne

Stephen P. Wood

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2010-11-08T00:00:00Z

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47717906

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21059958

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