Comparing the folding free-energy landscapes of Abeta42 variants with different aggregation properties.
about
β-hairpin-mediated formation of structurally distinct multimers of neurotoxic prion peptidesDimer formation enhances structural differences between amyloid β-protein (1-40) and (1-42): an explicit-solvent molecular dynamics studyAmyloid-β protofibrils: size, morphology and synaptotoxicity of an engineered mimicAmyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineeringAmyloid peptide Aβ40 inhibits aggregation of Aβ42: evidence from molecular dynamics simulations.Conformational and aggregation properties of the 1-93 fragment of apolipoprotein A-I.Comparative studies of disordered proteins with similar sequences: application to Aβ40 and Aβ42Alzheimer's protective A2T mutation changes the conformational landscape of the Aβ₁₋₄₂ monomer differently than does the A2V mutation.A Monte Carlo Study of the Early Steps of Functional Amyloid FormationDynamics of metastable β-hairpin structures in the folding nucleus of amyloid β-protein.Role of β-hairpin formation in aggregation: the self-assembly of the amyloid-β(25-35) peptide.Turn nucleation perturbs amyloid β self-assembly and cytotoxicity.Aβ monomers transiently sample oligomer and fibril-like configurations: ensemble characterization using a combined MD/NMR approachArginine and disordered amyloid-β peptide structures: molecular level insights into the toxicity in Alzheimer's diseaseOn the subject of rigor in the study of amyloid β-protein assembly.Structure of ring-shaped Aβ₄₂ oligomers determined by conformational selection.Identification of small-molecule binding pockets in the soluble monomeric form of the Aβ42 peptide.Emergence of Alternative Structures in Amyloid Beta 1-42 Monomeric Landscape by N-terminal Hexapeptide Amyloid Inhibitors.Atomic and dynamic insights into the beneficial effect of the 1,4-naphthoquinon-2-yl-L-tryptophan inhibitor on Alzheimer's Aβ1-42 dimer in terms of aggregation and toxicity.Mechanical resistance in unstructured proteins.Effect of the English familial disease mutation (H6R) on the monomers and dimers of Aβ40 and Aβ42Effect of the Tottori familial disease mutation (D7N) on the monomers and dimers of Aβ40 and Aβ42.
P2860
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P2860
Comparing the folding free-energy landscapes of Abeta42 variants with different aggregation properties.
description
2010 nî lūn-bûn
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2010年の論文
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
@zh-hans
2010年学术文章
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2010年學術文章
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name
Comparing the folding free-ene ...... ferent aggregation properties.
@en
Comparing the folding free-ene ...... ferent aggregation properties.
@nl
type
label
Comparing the folding free-ene ...... ferent aggregation properties.
@en
Comparing the folding free-ene ...... ferent aggregation properties.
@nl
prefLabel
Comparing the folding free-ene ...... ferent aggregation properties.
@en
Comparing the folding free-ene ...... ferent aggregation properties.
@nl
P50
P356
P1433
P1476
Comparing the folding free-ene ...... ferent aggregation properties.
@en
P2093
Iskra Staneva
P304
P356
10.1002/PROT.22775
P407
P577
2010-09-01T00:00:00Z