X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation.
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Structural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrilsCharacteristics of Tau and Its Ligands in PET ImagingThe Beta-amyloid protein of Alzheimer's disease: communication breakdown by modifying the neuronal cytoskeletonDesigned protein tetramer zipped together with a hydrophobic Alzheimer homology: A structural clue to amyloid assemblyTowards a Pharmacophore for AmyloidMolecular basis for amyloid- polymorphismTau StructuresA primer of amyloid nomenclatureAlzheimer's disease: paired helical filaments and cytomembranesPhase diagrams describing fibrillization by polyalanine peptides.Stability and structure of oligomers of the Alzheimer peptide Abeta16-22: from the dimer to the 32-merSpontaneous fibril formation by polyalanines; discontinuous molecular dynamics simulationsOrientation of tyrosine side chain in neurotoxic Aβ differs in two different secondary structures of the peptideIsolation and chemical characterization of Alzheimer's disease paired helical filament cytoskeletons: differentiation from amyloid plaque core proteinSecondary Metabolites in Ramalina terebrata Detected by UHPLC/ESI/MS/MS and Identification of Parietin as Tau Protein Inhibitor3D structure of Alzheimer's amyloid-beta(1-42) fibrilsAtomic-resolution structure of a disease-relevant Aβ(1-42) amyloid fibril.Aggregation of Aß(25-35) on DOPC and DOPC/DHA bilayers: an atomic force microscopy studyBiophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.Structural classification of toxic amyloid oligomersToxic fibrillar oligomers of amyloid-β have cross-β structure.Synthesis and secondary structural studies of penta(acetyl-Hmb)A beta(1-40).Anthraquinones inhibit tau aggregation and dissolve Alzheimer's paired helical filaments in vitro and in cells.Bacterial inclusion bodies contain amyloid-like structureFormation and growth of oligomers: a Monte Carlo study of an amyloid tau fragmentMechanisms of enzymatic degradation of amyloid Beta microfibrils generating nanofilaments and nanospheres related to cytotoxicity.Confocal fluorescence detected linear dichroism imaging of isolated human amyloid fibrils. Role of supercoiling.Effect of metals on kinetic pathways of amyloid-β aggregationOxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filamentsAmyloid-beta aggregation: selective inhibition of aggregation in mixtures of amyloid with different chain lengths.Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopyHollow core of Alzheimer's Abeta42 amyloid observed by cryoEM is relevant at physiological pH.pH-dependent structural transitions of Alzheimer amyloid peptides.Structure of beta-crystallite assemblies formed by Alzheimer beta-amyloid protein analogues: analysis by x-ray diffraction.Amino acid sequence in constitutionally isomeric tetrapeptide amphiphiles dictates architecture of one-dimensional nanostructures.Amyloid structure: conformational diversity and consequences.Amyloid-beta peptide assembly: a critical step in fibrillogenesis and membrane disruption.Amyloid peptide Aβ40 inhibits aggregation of Aβ42: evidence from molecular dynamics simulations.Synthetic peptide homologous to beta protein from Alzheimer disease forms amyloid-like fibrils in vitroStructure of core domain of fibril-forming PHF/Tau fragments.
P2860
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P2860
X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation.
description
1986 nî lūn-bûn
@nan
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
1986年论文
@zh
1986年论文
@zh-cn
name
X-ray diffraction from intrane ...... cates cross-beta conformation.
@ast
X-ray diffraction from intrane ...... cates cross-beta conformation.
@en
type
label
X-ray diffraction from intrane ...... cates cross-beta conformation.
@ast
X-ray diffraction from intrane ...... cates cross-beta conformation.
@en
prefLabel
X-ray diffraction from intrane ...... cates cross-beta conformation.
@ast
X-ray diffraction from intrane ...... cates cross-beta conformation.
@en
P2093
P2860
P356
P1476
X-ray diffraction from intrane ...... cates cross-beta conformation.
@en
P2093
D A Kirschner
D J Selkoe
P2860
P304
P356
10.1073/PNAS.83.2.503
P407
P577
1986-01-01T00:00:00Z