Mutational analysis of the ability of resveratrol to inhibit amyloid formation by islet amyloid polypeptide: critical evaluation of the importance of aromatic-inhibitor and histidine-inhibitor interactions

Mutational analysis of the ability of resveratrol to inhibit amyloid formation by islet amyloid polypeptide: critical evaluation of the importance of aromatic-inhibitor and histidine-inhibitor interactions

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Q35027146

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Inhibition of IAPP Aggregation and Toxicity by Natural Products and Derivatives Implications of aromatic-aromatic interactions: From protein structures to peptide models Bridging Type 2 Diabetes and Alzheimer's Disease: Assembling the Puzzle Pieces in the Quest for the Molecules With Therapeutic and Preventive Potential Stabilizing Off-pathway Oligomers by Polyphenol Nanoassemblies for IAPP Aggregation Inhibition Pancreatic β-Cell Membrane Fluidity and Toxicity Induced by Human Islet Amyloid Polypeptide Species.Natural product-based amyloid inhibitors.Role of resveratrol in the management of insulin resistance and related conditions: Mechanism of action.β-Hairpin mimics containing a piperidine-pyrrolidine scaffold modulate the β-amyloid aggregation process preserving the monomer species.An in vivo platform for identifying inhibitors of protein aggregation.Inhibition of Insulin Amyloid Fibrillation by a Novel Amphipathic Heptapeptide: MECHANISTIC DETAILS STUDIED BY SPECTROSCOPY IN COMBINATION WITH MICROSCOPY Inhibition of hIAPP Amyloid Aggregation and Pancreatic β-Cell Toxicity by OH-Terminated PAMAM Dendrimer.

P2860

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P2860

Mutational analysis of the ability of resveratrol to inhibit amyloid formation by islet amyloid polypeptide: critical evaluation of the importance of aromatic-inhibitor and histidine-inhibitor interactions

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http://www.wikidata.org/entity/Q35027146

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2015 nî lūn-bûn

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2015 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի հունվարին հրատարակված գիտական հոդված

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2015年の論文

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2015年学术文章

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2015年学术文章

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2015年学术文章

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2015年学术文章

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2015年学术文章

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2015年學術文章

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name

Mutational analysis of the abi ...... stidine-inhibitor interactions

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Mutational analysis of the abi ...... stidine-inhibitor interactions

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Mutational analysis of the abi ...... stidine-inhibitor interactions

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label

Mutational analysis of the abi ...... stidine-inhibitor interactions

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Mutational analysis of the abi ...... stidine-inhibitor interactions

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Mutational analysis of the abi ...... stidine-inhibitor interactions

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Mutational analysis of the abi ...... stidine-inhibitor interactions

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Mutational analysis of the abi ...... stidine-inhibitor interactions

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Mutational analysis of the abi ...... stidine-inhibitor interactions

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2-s2.0-84921836834

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P1433

Biochemistry

P1476

Mutational analysis of the abi ...... stidine-inhibitor interactions

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P2093

Amy G Wong

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P2860

The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds

Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis

Atomic structure of the cross-β spine of islet amyloid polypeptide (amylin)

Structure of trans -Resveratrol in Complex with the Cardiac Regulatory Protein Troponin C

Inhibition of amyloid fibril formation by polyphenols: structural similarity and aromatic interactions as a common inhibition mechanism

The binding of thioflavin-T to amyloid fibrils: localisation and implications.

The aggregation potential of human amylin determines its cytotoxicity towards islet beta-cells.

Islet amyloid: a long-recognized but underappreciated pathological feature of type 2 diabetes.

Islet amyloid deposition limits the viability of human islet grafts but not porcine islet grafts.

EGCG remodels mature alpha-synuclein and amyloid-beta fibrils and reduces cellular toxicity.

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666-676

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scholarly article

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10.1021/BI501016R

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English

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1029950972

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2011192333

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