Positioning of the Alzheimer Abeta(1-40) peptide in SDS micelles using NMR and paramagnetic probes.
about
Structures of rat and human islet amyloid polypeptide IAPP(1-19) in micelles by NMR spectroscopySolution NMR studies on the orientation of membrane-bound peptides and proteins by paramagnetic probesDynamic -Helix Structure of Micelle-bound Human AmylinThree-Dimensional Structure and Orientation of Rat Islet Amyloid Polypeptide Protein in a Membrane Environment by Solution NMR SpectroscopySolution Structure and Phospholipid Interactions of the Isolated Voltage-Sensor Domain from KvAPResidues within a lipid-associated segment of the PECAM-1 cytoplasmic domain are susceptible to inducible, sequential phosphorylationInteraction between amyloid beta peptide and an aggregation blocker peptide mimicking islet amyloid polypeptideStructural Model of the Bilitranslocase Transmembrane Domain Supported by NMR and FRET DataAlpha-helix targeting reduces amyloid-beta peptide toxicity.Spatial structure of heptapeptide Aβ(16-22) (beta-amyloid Aβ(1-40) active fragment) in solution and in complex with a biological membrane model.Membrane-Induced Folding of the Plant Stress Dehydrin Lti30.Unfolding of the amyloid β-peptide central helix: mechanistic insights from molecular dynamics simulations.Differences between amyloid-β aggregation in solution and on the membrane: insights into elucidation of the mechanistic details of Alzheimer's disease.Effects of ligands on unfolding of the amyloid β-peptide central helix: mechanistic insights from molecular dynamics simulations.Design of small molecules that target metal-A{beta} species and regulate metal-induced A{beta} aggregation and neurotoxicity.Spectroscopic Characterization of Intermolecular Interaction of Amyloid β Promoted on GM1 Micelles.Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation.Membrane-Induced Dichotomous Conformation of Amyloid β with the Disordered N-Terminal Segment Followed by the Stable C-Terminal β Structure.Specific Binding of Cu(II) Ions to Amyloid-Beta Peptides Bound to Aggregation-Inhibiting Molecules or SDS Micelles Creates Complexes that Generate Radical Oxygen Species.Is the Conformational Ensemble of Alzheimer's Aβ10-40 Peptide Force Field Dependent?Structural studies of the transmembrane C-terminal domain of the amyloid precursor protein (APP): does APP function as a cholesterol sensor?Exploring the reactivity of flavonoid compounds with metal-associated amyloid-β species.Prion protein-detergent micelle interactions studied by NMR in solution.Studying the structure and dynamics of biomolecules by using soluble paramagnetic probesBiophysical studies of the amyloid β-peptide: interactions with metal ions and small molecules.The hairpin conformation of the amyloid β peptide is an important structural motif along the aggregation pathway.Cellular polyamines promote amyloid-beta (Aβ) peptide fibrillation and modulate the aggregation pathways.Development of bifunctional stilbene derivatives for targeting and modulating metal-amyloid-β species.Phosphorylation Interferes with Maturation of Amyloid-β Fibrillar Structure in the N Terminus.Small molecule modulators of copper-induced Abeta aggregationInfluence of residue 22 on the folding, aggregation profile, and toxicity of the Alzheimer's amyloid beta peptide.N-terminal engineering of amyloid-β-binding Affibody molecules yields improved chemical synthesis and higher binding affinity.Membrane Interaction of the Glycosyltransferase WaaG.Interaction of PiB-derivative metal complexes with beta-amyloid peptides: selective recognition of the aggregated forms.Negatively charged lipid membranes promote a disorder-order transition in the Yersinia YscU protein.Membrane-Accelerated Amyloid-β Aggregation and Formation of Cross-β Sheets.Formation of dynamic soluble surfactant-induced amyloid β peptide aggregation intermediatesInterdomain flexibility in full-length matrix metalloproteinase-1 (MMP-1).Interaction of the amyloid β peptide with sodium dodecyl sulfate as a membrane-mimicking detergent.Designed fluorescent probes reveal interactions between amyloid-beta(1-40) peptides and GM1 gangliosides in micelles and lipid vesicles.
P2860
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P2860
Positioning of the Alzheimer Abeta(1-40) peptide in SDS micelles using NMR and paramagnetic probes.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh
2007年學術文章
@zh-hant
name
Positioning of the Alzheimer Abeta
@nl
Positioning of the Alzheimer A ...... g NMR and paramagnetic probes.
@en
type
label
Positioning of the Alzheimer Abeta
@nl
Positioning of the Alzheimer A ...... g NMR and paramagnetic probes.
@en
prefLabel
Positioning of the Alzheimer Abeta
@nl
Positioning of the Alzheimer A ...... g NMR and paramagnetic probes.
@en
P50
P1476
Positioning of the Alzheimer A ...... g NMR and paramagnetic probes.
@en
P2093
Peter Damberg
P2888
P356
10.1007/S10858-007-9176-4
P577
2007-07-27T00:00:00Z