Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease
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An atomic model for the pleated beta-sheet structure of abeta amyloid protofilamentsStructures of human insulin-degrading enzyme reveal a new substrate recognition mechanismA capillary electrophoresis method for evaluation of Abeta proteolysis in vitroAmyloid beta-protein monomer folding: free-energy surfaces reveal alloform-specific differencesAlzheimer's disease--a panorama glimpseStructure of human immunodeficiency virus type 1 Vpr(34-51) peptide in micelle containing aqueous solutionSolution structure of the Alzheimer amyloid beta-peptide (1-42) in an apolar microenvironment. Similarity with a virus fusion domainStructural studies of the tethered N-terminus of the Alzheimer's disease amyloid-β peptideCrystal structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assemblyThe alpha-to-beta conformational transition of Alzheimer's Abeta-(1-42) peptide in aqueous media is reversible: a step by step conformational analysis suggests the location of beta conformation seedingMultiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrilsStructural Analysis and Aggregation Propensity of Pyroglutamate Aβ(3-40) in Aqueous TrifluoroethanolSpatial structure of heptapeptide Aβ(16-22) (beta-amyloid Aβ(1-40) active fragment) in solution and in complex with a biological membrane model.Comparison of the structures of beta amyloid peptide (25-35) and substance P in trifluoroethanol/water solution.Cholesterol is an important factor affecting the membrane insertion of beta-amyloid peptide (A beta 1-40), which may potentially inhibit the fibril formation.Mirror-image phage display: aiming at the mirror.Simulation study on the disordered state of an Alzheimer's beta amyloid peptide Abeta(12 36) in water consisting of random-structural, beta-structural, and helical clusters.Structure and dynamics of the Abeta(21-30) peptide from the interplay of NMR experiments and molecular simulations.Structural changes of region 1-16 of the Alzheimer disease amyloid beta-peptide upon zinc binding and in vitro aging.Conformational transition of amyloid beta-peptide.Positive evolutionary selection of an HD motif on Alzheimer precursor protein orthologues suggests a functional role.Structural analysis of Alzheimer's beta(1-40) amyloid: protofilament assembly of tubular fibrils.Amyloid-beta peptide assembly: a critical step in fibrillogenesis and membrane disruption.Solvent and mutation effects on the nucleation of amyloid beta-protein foldingMechanism of fiber assembly: treatment of Aβ peptide aggregation with a coarse-grained united-residue force field.Amyloid peptide Aβ40 inhibits aggregation of Aβ42: evidence from molecular dynamics simulations.Dominance of misfolded intermediates in the dynamics of α-helix foldingFrom Alzheimer to Huntington: why is a structural understanding so difficult?Modeling amyloid-beta as homogeneous dodecamers and in complex with cellular prion protein.Interplay of histidine residues of the Alzheimer's disease Aβ peptide governs its Zn-induced oligomerization.A synchrotron-based hydroxyl radical footprinting analysis of amyloid fibrils and prefibrillar intermediates with residue-specific resolution.How ionic strength affects the conformational behavior of human and rat beta amyloids--a computational studyAmyloid beta-degrading cryptidases: insulin degrading enzyme, presequence peptidase, and neprilysin.Nuclear translocation uncovers the amyloid peptide Aβ42 as a regulator of gene transcription.A study of the α-helical intermediate preceding the aggregation of the amino-terminal fragment of the β amyloid peptide (Aβ(1-28))Membrane-Induced Dichotomous Conformation of Amyloid β with the Disordered N-Terminal Segment Followed by the Stable C-Terminal β Structure.Monomeric Amyloid Beta Peptide in Hexafluoroisopropanol Detected by Small Angle Neutron ScatteringFolding a protein with equal probability of being helix or hairpin.Linking folding with aggregation in Alzheimer's beta-amyloid peptidesThe inverted free energy landscape of an intrinsically disordered peptide by simulations and experiments.
P2860
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P2860
Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease
description
1995 nî lūn-bûn
@nan
1995 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease
@ast
Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease
@en
Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease
@nl
type
label
Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease
@ast
Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease
@en
Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease
@nl
prefLabel
Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease
@ast
Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease
@en
Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease
@nl
P2093
P2860
P50
P1433
P1476
Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease
@en
P2093
P2860
P356
10.1111/J.1432-1033.1995.293_1.X
P407
P577
1995-10-01T00:00:00Z