Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis.
about
Rationally designed turn promoting mutation in the amyloid-β peptide sequence stabilizes oligomers in solutionThe 3D profile method for identifying fibril-forming segments of proteinsStructure of the cross-beta spine of amyloid-like fibrilsDe novo proteins from designed combinatorial librariesThe Alzheimer's peptides Abeta40 and 42 adopt distinct conformations in water: a combined MD / NMR studyPrediction of "hot spots" of aggregation in disease-linked polypeptidesTransient dynamics of Aβ contribute to toxicity in Alzheimer's diseaseStructural Conversion of Aβ17-42 Peptides from Disordered Oligomers to U-Shape Protofilaments via Multiple Kinetic PathwaysOxidative stress in Alzheimer's and Parkinson's diseases: insights from the yeast Saccharomyces cerevisiaeNeuroserpin binds Abeta and is a neuroprotective component of amyloid plaques in Alzheimer diseaseExperimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrilsSolid-state NMR as a probe of amyloid structureCharacterization of amyloid structures at the molecular level by solid state nuclear magnetic resonance spectroscopyAβ peptide fibrillar architectures controlled by conformational constraints of the monomerMapping the structure of amyloid nucleation precursors by protein engineering kinetic analysis.Monoclonal antibodies against Aβ42 fibrils distinguish multiple aggregation state polymorphisms in vitro and in Alzheimer disease brain.Molecular architecture of Aβ fibrils grown in cerebrospinal fluid solution and in a cell culture model of Aβ plaque formation.Structural polymorphism of Alzheimer Abeta and other amyloid fibrilsCotranslational incorporation of a structurally diverse series of proline analogues in an Escherichia coli expression system.Effect of the amyloid β hairpin's structure on the handedness of helices formed by its aggregates.Microscopic analysis of protein oxidative damage: effect of carbonylation on structure, dynamics, and aggregability of villin headpieceKinetic study of beta-amyloid residue accessibility using reductive alkylation and mass spectrometry.Structural differences between Abeta(1-40) intermediate oligomers and fibrils elucidated by proteolytic fragmentation and hydrogen/deuterium exchange.Simultaneous monitoring of peptide aggregate distributions, structure, and kinetics using amide hydrogen exchange: application to Abeta(1-40) fibrillogenesisStructural properties of Abeta protofibrils stabilized by a small molecule.Polymorphic fibril formation by residues 10-40 of the Alzheimer's beta-amyloid peptide.Flexibility and Solvation of Amyloid-β Hydrophobic CoreParallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p.Modulation of Abeta42 low-n oligomerization using a novel yeast reporter systemAGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides.Stereochemical criteria for prediction of the effects of proline mutations on protein stability.The turn formation at positions 22 and 23 in the 42-mer amyloid beta peptide: the emerging role in the pathogenesis of Alzheimer's disease.Point mutations in Aβ result in the formation of distinct polymorphic aggregates in the presence of lipid bilayers.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Development and validation of a yeast high-throughput screen for inhibitors of Aβ₄₂ oligomerization.Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs.The critical role of the central hydrophobic core (residues 71-77) of amyloid-forming αA66-80 peptide in α-crystallin aggregation: a systematic proline replacement study.Characterization of the interaction of β-amyloid with transthyretin monomers and tetramers.Amyloid structure: conformational diversity and consequences.Simulation of the β- to α-sheet transition results in a twisted sheet for antiparallel and an α-nanotube for parallel strands: implications for amyloid formation.
P2860
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P2860
Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh-hant
name
Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis.
@en
Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis.
@nl
type
label
Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis.
@en
Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis.
@nl
prefLabel
Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis.
@en
Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis.
@nl
P2093
P1476
Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis.
@en
P2093
Angela D Williams
Erik Portelius
Indu Kheterpal
Jun-tao Guo
Ronald Wetzel
P304
P356
10.1016/J.JMB.2003.11.008
P407
P577
2004-01-01T00:00:00Z