Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions. - Wikidata - wikimedia - TriplyDB

Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions.

Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions.

http://www.wikidata.org/entity/Q30502077

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Disrupting self-assembly and toxicity of amyloidogenic protein oligomers by "molecular tweezers" - from the test tube to animal models Inhibition of IAPP Aggregation and Toxicity by Natural Products and Derivatives On the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP Peptides Engineering amyloid-like assemblies from unstructured peptides via site-specific lipid conjugation Polymorphism of β2-microglobulin amyloid fibrils manifested by ultrasonication-enhanced fibril formation in trifluoroethanol Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation.A desolvation model for trifluoroethanol-induced aggregation of enhanced green fluorescent protein.Amyloidogenic Mutation Promotes Fibril Formation of the N-terminal Apolipoprotein A-I on Lipid Membranes.Dual role of an N-terminal amyloidogenic mutation in apolipoprotein A-I: destabilization of helix bundle and enhancement of fibril formation.Aggregation of Chameleon Peptides: Implications of α-Helicity in Fibril Formation Structure, folding dynamics, and amyloidogenesis of D76N β2-microglobulin: roles of shear flow, hydrophobic surfaces, and α-crystallin.Mechanistic Contributions of Biological Cofactors in Islet Amyloid Polypeptide Amyloidogenesis.The A53T mutation is key in defining the differences in the aggregation kinetics of human and mouse α-synuclein.Salvianolic acid B inhibits the amyloid formation of human islet amyloid polypeptide and protects pancreatic beta-cells against cytotoxicity.Aspirin, diabetes, and amyloid: re-examination of the inhibition of amyloid formation by aspirin and ketoprofen Over-Expressed Pathogenic miRNAs in Alzheimer's Disease (AD) and Prion Disease (PrD) Drive Deficits in TREM2-Mediated Aβ42 Peptide Clearance.Design and study of lipopeptide inhibitors on preventing aggregation of human islet amyloid polypeptide residues 11-20.Membrane-mediated amyloid deposition of human islet amyloid polypeptide.Site-specific detection of protein secondary structure using 2D IR dihedral indexing: a proposed assembly mechanism of oligomeric hIAPP.Copper(ii) and zinc(ii) dependent effects on Aβ42 aggregation: a CD, Th-T and SFM study

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P2860

Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions.

http://www.wikidata.org/entity/Q30502077

description

2011 nî lūn-bûn

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2011 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2011 թվականի մայիսին հրատարակված գիտական հոդված

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2011年の論文

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2011年学术文章

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2011年学术文章

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2011年学术文章

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2011年学术文章

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2011年学术文章

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2011年學術文章

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name

Hexafluoroisopropanol induces ...... nd electrostatic interactions.

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Hexafluoroisopropanol induces ...... nd electrostatic interactions.

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Hexafluoroisopropanol induces ...... nd electrostatic interactions.

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Journal of Biological Chemistry

P1476

Hexafluoroisopropanol induces ...... nd electrostatic interactions.

@en

P2093

Hisashi Yagi

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

Kazumasa Sakurai

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Kotaro Yanagi

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Mizue Ashizaki

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Young-Ho Lee

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Yuji Goto

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P2860

Structure of the cross-beta spine of amyloid-like fibrils

Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells

Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients

Medin: an integral fragment of aortic smooth muscle cell-produced lactadherin forms the most common human amyloid

Atomic structures of amyloid cross-beta spines reveal varied steric zippers

Protein misfolding, functional amyloid, and human disease

Protein folding and misfolding

Ultrasonication-dependent production and breakdown lead to minimum-sized amyloid fibrils.

Laser-induced propagation and destruction of amyloid beta fibrils.

Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion.

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10.1074/JBC.M111.226688

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