Solution structure of amyloid beta-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is?
about
An atomic model for the pleated beta-sheet structure of abeta amyloid protofilamentsStructures of human insulin-degrading enzyme reveal a new substrate recognition mechanismAmyloid 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 peptideAlzheimer's disease--a panorama glimpseDimer formation enhances structural differences between amyloid β-protein (1-40) and (1-42): an explicit-solvent molecular dynamics studyA Redox-Active, Compact Molecule for Cross-Linking Amyloidogenic Peptides into Nontoxic, Off-Pathway Aggregates: In Vitro and In Vivo Efficacy and Molecular Mechanisms.Solution structure of the Alzheimer amyloid beta-peptide (1-42) in an apolar microenvironment. Similarity with a virus fusion domainDynamic -Helix Structure of Micelle-bound Human AmylinThree-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 248−286Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environmentIn silico analysis of the apolipoprotein E and the amyloid beta peptide interaction: misfolding induced by frustration of the salt bridge networkModels of membrane-bound Alzheimer's Abeta peptide assembliesBeta-barrel models of soluble amyloid beta oligomers and annular protofibrils.Investigation of the effect of erythrosine B on amyloid beta peptide using molecular modeling.Strategies for dealing with conformational sampling in structural calculations of flexible or kinked transmembrane peptides.Maximally asymmetric transbilayer distribution of anionic lipids alters the structure and interaction with lipids of an amyloidogenic protein dimer bound to the membrane surfaceSwitch region for pathogenic structural change in conformational disease and its predictionData supporting beta-amyloid dimer structural transitions and protein-lipid interactions on asymmetric lipid bilayer surfaces using MD simulations on experimentally derived NMR protein structures.Spatial 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.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).Cholesterol is an important factor affecting the membrane insertion of beta-amyloid peptide (A beta 1-40), which may potentially inhibit the fibril formation.Measuring translational diffusion coefficients of peptides and proteins by PFG-NMR using band-selective RF pulses.The Dependence of Amyloid-β Dynamics on Protein Force Fields and Water Models.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.CSF amyloid-beta-peptides in Alzheimer's disease, dementia with Lewy bodies and Parkinson's disease dementiaHow cholesterol constrains glycolipid conformation for optimal recognition of Alzheimer's beta amyloid peptide (Abeta1-40).The amyloidogenic SEVI precursor, PAP248-286, is highly unfolded in solution despite an underlying helical tendency.Unfolding of the amyloid β-peptide central helix: mechanistic insights from molecular dynamics simulations.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Conformational transition of amyloid beta-peptide.The intramembrane cleavage site of the amyloid precursor protein depends on the length of its transmembrane domain.A molecular dynamics study of the early stages of amyloid-beta(1-42) oligomerization: the role of lipid membranes.Molecular insights into amyloid regulation by membrane cholesterol and sphingolipids: common mechanisms in neurodegenerative diseasesEffects of ligands on unfolding of the amyloid β-peptide central helix: mechanistic insights from molecular dynamics simulations.Positive evolutionary selection of an HD motif on Alzheimer precursor protein orthologues suggests a functional role.Protein aggregation/folding: the role of deterministic singularities of sequence hydrophobicity as determined by nonlinear signal analysis of acylphosphatase and Abeta(1-40)
P2860
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P2860
Solution structure of amyloid beta-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is?
description
1998 nî lūn-bûn
@nan
1998 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Solution structure of amyloid ...... g domain where we think it is?
@ast
Solution structure of amyloid ...... g domain where we think it is?
@en
Solution structure of amyloid ...... g domain where we think it is?
@nl
type
label
Solution structure of amyloid ...... g domain where we think it is?
@ast
Solution structure of amyloid ...... g domain where we think it is?
@en
Solution structure of amyloid ...... g domain where we think it is?
@nl
prefLabel
Solution structure of amyloid ...... g domain where we think it is?
@ast
Solution structure of amyloid ...... g domain where we think it is?
@en
Solution structure of amyloid ...... g domain where we think it is?
@nl
P2093
P3181
P356
P1433
P1476
Solution structure of amyloid ...... g domain where we think it is?
@en
P2093
P304
11064-11077
P3181
P356
10.1021/BI972979F
P407
P577
1998-08-01T00:00:00Z