Solution structures of micelle-bound amyloid beta-(1-40) and beta-(1-42) peptides of Alzheimer's disease.
about
The Alzheimer's amyloid β-peptide (Aβ) binds a specific DNA Aβ-interacting domain (AβID) in the APP, BACE1, and APOE promoters in a sequence-specific manner: characterizing a new regulatory motifAmyloid beta-protein monomer folding: free-energy surfaces reveal alloform-specific differencesStabilization of neurotoxic soluble beta-sheet-rich conformations of the Alzheimer's disease amyloid-beta peptideMechanisms of amyloid formation revealed by solution NMRTransient dynamics of Aβ contribute to toxicity in Alzheimer's diseaseSolution structure of the Alzheimer amyloid beta-peptide (1-42) in an apolar microenvironment. Similarity with a virus fusion domainThree-Dimensional Structure and Orientation of Rat Islet Amyloid Polypeptide Protein in a Membrane Environment by Solution NMR SpectroscopyNMR Structure in a Membrane Environment Reveals Putative Amyloidogenic Regions of the SEVI Precursor Peptide PAP 248−286Structural studies of the tethered N-terminus of the Alzheimer's disease amyloid-β peptideMultiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrilsStructure and dynamics of parallel beta-sheets, hydrophobic core, and loops in Alzheimer's A beta fibrilsStructural Analysis and Aggregation Propensity of Pyroglutamate Aβ(3-40) in Aqueous TrifluoroethanolDirect detection of transient alpha-helical states in islet amyloid polypeptideAβ42 assembles into specific β-barrel pore-forming oligomers in membrane-mimicking environments.Models of membrane-bound Alzheimer's Abeta peptide assembliesProbing the origins of increased activity of the E22Q "Dutch" mutant Alzheimer's beta-amyloid peptide.NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, A beta(1-40)(ox) and A beta(1-42)(ox).Sodium dodecyl sulfate monomers induce XAO peptide polyproline II to α-helix transition.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.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Conformational transition of amyloid beta-peptide.Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopyDisordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs.NBD-labeled phospholipid accelerates apolipoprotein C-II amyloid fibril formation but is not incorporated into mature fibrils.Resolving the paradox for protein aggregation diseases: NMR structure and dynamics of the membrane-embedded P56S-MSP causing ALS imply a common mechanism for aggregation-prone proteins to attack membranesSolvent 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.Design of small molecules that target metal-A{beta} species and regulate metal-induced A{beta} aggregation and neurotoxicity.From Alzheimer to Huntington: why is a structural understanding so difficult?Interplay of histidine residues of the Alzheimer's disease Aβ peptide governs its Zn-induced oligomerization.A study of the α-helical intermediate preceding the aggregation of the amino-terminal fragment of the β amyloid peptide (Aβ(1-28))Investigating how peptide length and a pathogenic mutation modify the structural ensemble of amyloid beta monomer.Interpeptide interactions induce helix to strand structural transition in Abeta peptidesLinking folding with aggregation in Alzheimer's beta-amyloid peptidesSpecific Binding of Cu(II) Ions to Amyloid-Beta Peptides Bound to Aggregation-Inhibiting Molecules or SDS Micelles Creates Complexes that Generate Radical Oxygen Species.Molecular interactions in the formation and deposition of beta2-microglobulin-related amyloid fibrils.Pyroglutamate-Modified Amyloid-β(3-42) Shows α-Helical Intermediates before Amyloid Formation.Synergistic effects of high fat feeding and apolipoprotein E deletion on enterocytic amyloid-beta abundance.
P2860
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P2860
Solution structures of micelle-bound amyloid beta-(1-40) and beta-(1-42) peptides of Alzheimer's disease.
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Solution structures of micelle ...... ptides of Alzheimer's disease.
@ast
Solution structures of micelle ...... ptides of Alzheimer's disease.
@en
type
label
Solution structures of micelle ...... ptides of Alzheimer's disease.
@ast
Solution structures of micelle ...... ptides of Alzheimer's disease.
@en
prefLabel
Solution structures of micelle ...... ptides of Alzheimer's disease.
@ast
Solution structures of micelle ...... ptides of Alzheimer's disease.
@en
P2093
P356
P1476
Solution structures of micelle ...... ptides of Alzheimer's disease.
@en
P2093
P304
P356
10.1006/JMBI.1998.2348
P407
P577
1999-01-01T00:00:00Z