A molecular model of Alzheimer amyloid beta-peptide fibril formation. - Wikidata - wikimedia - TriplyDB

A molecular model of Alzheimer amyloid beta-peptide fibril formation.

A molecular model of Alzheimer amyloid beta-peptide fibril formation.

http://www.wikidata.org/entity/Q33859393

about

Acceleration of alpha-synuclein aggregation by homologous peptides Identification of an amyloid fibril forming peptide comprising residues 46-59 of apolipoprotein A-I The 3D profile method for identifying fibril-forming segments of proteins A Fibril-Like Assembly of Oligomers of a Peptide Derived from β-Amyloid Molecular Structure of Aggregated Amyloid-β: Insights from Solid-State Nuclear Magnetic Resonance Molecular structure of monomorphic peptide fibrils within a kinetically trapped hydrogel network Ultrastructural organization of amyloid fibrils by atomic force microscopy.Supramolecular structure in full-length Alzheimer's beta-amyloid fibrils: evidence for a parallel beta-sheet organization from solid-state nuclear magnetic resonance.Site-specific identification of non-beta-strand conformations in Alzheimer's beta-amyloid fibrils by solid-state NMR A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils Solid-state NMR as a probe of amyloid structure Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrils Stability and structure of oligomers of the Alzheimer peptide Abeta16-22: from the dimer to the 32-mer Protein misfolding and aggregation in Alzheimer's disease and type 2 diabetes mellitus Drug Development in Conformational Diseases: A Novel Family of Chemical Chaperones that Bind and Stabilise Several Polymorphic Amyloid Structures Asynchronous evolutionary origins of Aβ and BACE1 Amyloid-like fibril formation in an all beta-barrel protein involves the formation of partially structured intermediate(s).Sequence determinants of amyloid fibril formation Inhibition of fibril formation of Abeta by guanidiniocarbonyl pyrrole receptors.Insight into the structure of amyloid fibrils from the analysis of globular proteins.Prediction of amyloidogenic and disordered regions in protein chains The turn formation at positions 22 and 23 in the 42-mer amyloid beta peptide: the emerging role in the pathogenesis of Alzheimer's disease.Impact on the replacement of Phe by Trp in a short fragment of Aβ amyloid peptide on the formation of fibrils.Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.Confocal microscopy for the analysis of siRNA delivery by polymeric nanoparticles.The circularization of amyloid fibrils formed by apolipoprotein C-II.Fibril-forming motifs are essential and sufficient for the fibrillization of human Tau.Folding/unfolding/refolding of proteins: present methodologies in comparison with capillary zone electrophoresis.Free energy landscapes for amyloidogenic tetrapeptides dimerization.Surface effects mediate self-assembly of amyloid-β peptides.Protein fragments: functional and structural roles of their coevolution networks.A novel retro-inverso peptide inhibitor reduces amyloid deposition, oxidation and inflammation and stimulates neurogenesis in the APPswe/PS1ΔE9 mouse model of Alzheimer's disease.Combining intracellular selection with protein-fragment complementation to derive Aβ interacting peptides.Role of amyloid peptides in vascular dysfunction and platelet dysregulation in Alzheimer's disease Intrinsic determinants of Aβ(12-24) pH-dependent self-assembly revealed by combined computational and experimental studies.Molecular alignment within beta-sheets in Abeta(14-23) fibrils: solid-state NMR experiments and theoretical predictions.A flexible nanoarray approach for the assembly and probing of molecular complexes.Structure-Based Peptide Design to Modulate Amyloid Beta Aggregation and Reduce Cytotoxicity Molecular dynamics simulations on the oligomer-formation process of the GNNQQNY peptide from yeast prion protein Sup35.

P2860

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P2860

A molecular model of Alzheimer amyloid beta-peptide fibril formation.

http://www.wikidata.org/entity/Q33859393

description

1999 nî lūn-bûn

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1999 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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1999 թվականի ապրիլին հրատարակված գիտական հոդված

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1999年の論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年论文

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name

A molecular model of Alzheimer amyloid beta-peptide fibril formation.

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A molecular model of Alzheimer amyloid beta-peptide fibril formation.

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type

label

A molecular model of Alzheimer amyloid beta-peptide fibril formation.

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A molecular model of Alzheimer amyloid beta-peptide fibril formation.

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prefLabel

A molecular model of Alzheimer amyloid beta-peptide fibril formation.

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A molecular model of Alzheimer amyloid beta-peptide fibril formation.

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A molecular model of Alzheimer amyloid beta-peptide fibril formation.

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Callaway DJ

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Hahne S

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12619-12625

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Alzheimer's disease