Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria. - Wikidata - wikimedia - TriplyDB

Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria.

Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria.

http://www.wikidata.org/entity/Q34282165

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Myelin membrane assembly is driven by a phase transition of myelin basic proteins into a cohesive protein meshwork An additional substrate binding site in a bacterial phenylalanine hydroxylase Bioorthogonal cyclization-mediated in situ self-assembly of small-molecule probes for imaging caspase activity in vivo Mitochondria localization induced self-assembly of peptide amphiphiles for cellular dysfunction.The critical role of the central hydrophobic core (residues 71-77) of amyloid-forming αA66-80 peptide in α-crystallin aggregation: a systematic proline replacement study.Prion-like nanofibrils of small molecules (PriSM) selectively inhibit cancer cells by impeding cytoskeleton dynamics Aligning 3D nanofibrous networks from self-assembled phenylalanine nanofibers.A consistent force field parameter set for zwitterionic amino acid residues.pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils.Doxycycline hinders phenylalanine fibril assemblies revealing a potential novel therapeutic approach in phenylketonuria Supramolecular Amino Acid Based Hydrogels: Probing the Contribution of Additive Molecules using NMR Spectroscopy.A Specific Nutrient Combination Attenuates the Reduced Expression of PSD-95 in the Proximal Dendrites of Hippocampal Cell Body Layers in a Mouse Model of Phenylketonuria The interactions of phenylalanines in β-sheet-like structures from molecular orbital calculations using density functional theory (DFT), MP2, and CCSD(T) methods Phenylalanine hydroxylase: function, structure, and regulation.The physical properties of supramolecular peptide assemblies: from building block association to technological applications.Design of nanostructures based on aromatic peptide amphiphiles.Nanoparticles generated from a tryptophan derivative: physical characterization and anti-cancer drug delivery.Cross-interactions between the Alzheimer Disease Amyloid-β Peptide and Other Amyloid Proteins: A Further Aspect of the Amyloid Cascade Hypothesis.Peptide self-assembly: thermodynamics and kinetics.Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.Intrinsic property of phenylalanine to trigger protein aggregation and hemolysis has a direct relevance to phenylketonuria.Therapeutic implication of L-phenylalanine aggregation mechanism and its modulation by D-phenylalanine in phenylketonuria.Side-chain hydrophobicity and the stability of Aβ₁₆₋₂₂ aggregates.Extension of the generic amyloid hypothesis to nonproteinaceous metabolite assemblies Exploring the sequence-structure relationship for amyloid peptides.Spectral Transition in Bio-Inspired Self-Assembled Peptide Nucleic Acid Photonic Crystals.A 31-residue peptide induces aggregation of tau's microtubule-binding region in cells."Carboranyl-cysteine"-Synthesis, Structure and Self-Assembly Behavior of a Novel α-Amino Acid.Force field development and simulations of intrinsically disordered proteins.Seeding of proteins into amyloid structures by metabolite assemblies may clarify certain unexplained epidemiological associations.Covalent Tethering and Residues with Bulky Hydrophobic Side Chains Enable Self-Assembly of Distinct Amyloid Structures.Molecular co-assembly as a strategy for synergistic improvement of the mechanical properties of hydrogels.Synthetic minimalistic tryptophan zippers as a chiroptical switch.Halogen effects on the solid-state packing of phenylalanine derivatives and the resultant gelation properties.Metabolite amyloids: a new paradigm for inborn error of metabolism disorders.Sodium chloride's effect on self-assembly of diphenylalanine bilayer.End Capping Alters the Structural Characteristics and Mechanical Properties of Transthyretin (105-115) Amyloid Protofibrils.Circular Dichroism of Amino Acids: Following the Structural Formation of Phenylalanine.Speed of processing and executive functions in adults with phenylketonuria: Quick in finding the word, but not the ladybird.Tetrahydrobiopterin treatment reduces brain L-Phe but only partially improves serotonin in hyperphenylalaninemic ENU1/2 mice.

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P2860

Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria.

http://www.wikidata.org/entity/Q34282165

description

2012 nî lūn-bûn

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2012 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2012 թվականի հունիսին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria.

@ast

Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria.

@en

Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria.

@nl

type

label

Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria.

@ast

Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria.

@en

Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria.

@nl

prefLabel

Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria.

@ast

Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria.

@en

Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria.

@nl

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P1433

Nature Chemical Biology

P1476

Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria.

@en

P2093

Amedeo Caflisch

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

Andrea Magno

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

Dan Frenkel

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

Dorit Trudler

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

Ehud Gazit

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

Lihi Adler-Abramovich

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

Lilach Vaks

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

Ohad Carny

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

P2860

Clinical immunologic approaches for the treatment of Alzheimer's disease

CHARMM: the biomolecular simulation program

Protein misfolding, functional amyloid, and human disease

A specific amyloid-beta protein assembly in the brain impairs memory

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse

Molecular basis for amyloid fibril formation and stability.

Amyloid fibrillogenesis: themes and variations.

The neurochemistry of phenylketonuria.

A possible role for pi-stacking in the self-assembly of amyloid fibrils.

P2888

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701-706

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10.1038/NCHEMBIO.1002

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8

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8

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2012-06-17T00:00:00Z

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1041319030

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22706200

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P921

phenylketonuria