Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria.
about
Myelin membrane assembly is driven by a phase transition of myelin basic proteins into a cohesive protein meshworkAn additional substrate binding site in a bacterial phenylalanine hydroxylaseBioorthogonal cyclization-mediated in situ self-assembly of small-molecule probes for imaging caspase activity in vivoMitochondria 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 dynamicsAligning 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 phenylketonuriaSupramolecular 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 PhenylketonuriaThe interactions of phenylalanines in β-sheet-like structures from molecular orbital calculations using density functional theory (DFT), MP2, and CCSD(T) methodsPhenylalanine 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 assembliesExploring 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.
P2860
Q27317306-62AE753C-025D-4307-9DD1-3B0A1FF19801Q27679109-D48FDE9C-33F4-4F43-AE3B-D7438930F97FQ30578692-19107CF9-9A43-419E-94F5-1035980053F8Q33822486-BE1927CB-DDDB-447F-AD6E-7FD32EDACECEQ34118100-FDE6E3BE-6AA4-4609-94B4-ACF0F42E73AFQ34355767-5BA1BDD5-4415-464F-BC0F-761D1501BA66Q35002394-66760271-E034-4D27-8460-DE1207CB98BDQ35359482-D2FB073B-D39F-4D62-A2A9-DF72286192E0Q35757446-8200D608-0023-4028-A870-9587418B281FQ36221601-9593F743-9894-4EC5-9649-137A6130E5B9Q36344367-4F8403BF-EF8B-4124-874D-24ACEF3F6A2EQ36846193-2CA39D5C-76F1-4AD9-8608-9FBAE273EAFEQ37008866-5A35693C-0F68-43FC-9AC0-B0E5B6243049Q38086186-6DFAA1D4-757B-4678-A5EF-EC13479BEC91Q38237547-E158873D-606D-4112-9794-24E87121F814Q38246910-4C670F8D-379A-4F27-B7F3-157D78CE45A7Q38747376-334DF553-0D9A-4F46-A1AD-EF71BA9DDC74Q38871578-8BE5D2DC-EFA5-483B-9EE7-F5DD2F0CCF0AQ38917334-38200196-7F06-4CDD-AB34-096D83365E06Q39322110-25A532B7-F524-46DA-BBC0-2F6B16577E95Q41329671-283658FA-0AE2-4AF2-8124-39D9A53169BCQ41882919-5446F0F6-E782-4870-A01C-A9A6E93B7D95Q41997204-E51B7189-CDB8-41B9-A124-98246A4A8677Q42619969-74AB4422-F6E4-4D34-8AA6-64B462B228D5Q42757401-DE19648E-5012-4881-A2C1-565849A3F8F8Q46609347-2C4A9C82-08CD-42C6-9A43-239CD94F0928Q46651347-799EEC0C-5895-44F3-8AEA-EE19A97F36EDQ47150857-BEE30341-D431-4961-9441-0B42B62F4D0AQ47591502-E86A29F2-70B5-4A27-AB31-1502DAF9C459Q48172417-C23F53FF-EEE0-44A5-A1D9-F1564B596762Q48314753-3BD876B2-4704-4154-8F89-D37134C54EA5Q48692890-16C8B61C-62B7-4994-A49B-8F2E806D9732Q48855121-BB7C3E39-C209-49CF-8137-C5E254D38D06Q50196463-E358772D-282B-4953-BB02-B94AE8FF2621Q50238179-C5046B48-E180-4D25-872E-3DF833897EB2Q51311781-8E3A01CF-D550-42C0-A234-F994F2FADBCDQ51638385-5C541B38-D3D0-46C8-9435-F8DB20F047C1Q51814713-0E24E521-A278-471B-AF5C-F753664F4F1CQ51814865-BADD6EC3-B15A-42CB-B975-5A13AA291F29Q52362136-4154A8CB-5A7C-48AF-9700-D96C02D35A38
P2860
Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria.
description
2012 nî lūn-bûn
@nan
2012 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
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
P2093
P2860
P356
P1476
Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria.
@en
P2093
Amedeo Caflisch
Andrea Magno
Dan Frenkel
Dorit Trudler
Ehud Gazit
Lihi Adler-Abramovich
Lilach Vaks
Ohad Carny
P2860
P2888
P304
P356
10.1038/NCHEMBIO.1002
P577
2012-06-17T00:00:00Z
P6179
1041319030