Conformation and fibrillogenesis of Alzheimer A beta peptides with selected substitution of charged residues.
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Aβ42-oligomer Interacting Peptide (AIP) neutralizes toxic amyloid-β42 species and protects synaptic structure and function.Site-specific identification of non-beta-strand conformations in Alzheimer's beta-amyloid fibrils by solid-state NMRMultiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrilsEffect of the amyloid β hairpin's structure on the handedness of helices formed by its aggregates.Concentration effect on the aggregation of a self-assembling oligopeptide.Amyloid fibers are water-filled nanotubes.A nucleated assembly mechanism of Alzheimer paired helical filaments.In silico theoretical molecular modeling for Alzheimer's disease: the nicotine-curcumin paradigm in neuroprotection and neurotherapy.In situ characterization of beta-amyloid in Alzheimer's diseased tissue by synchrotron Fourier transform infrared microspectroscopyPolymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.Stabilities and conformations of Alzheimer's beta -amyloid peptide oligomers (Abeta 16-22, Abeta 16-35, and Abeta 10-35): Sequence effects.Allosteric stabilization of the amyloid-β peptide hairpin by the fluctuating N-terminal.Influence of the physiochemical properties of superparamagnetic iron oxide nanoparticles on amyloid β protein fibrillation in solution.Propagating structure of Alzheimer's beta-amyloid(10-35) is parallel beta-sheet with residues in exact registerThe impact of ataxin-1-like histidine insertions on polyglutamine aggregationAnalytical methods and formulation factors to enhance protein stability in solution.Micelle formation by a fragment of human islet amyloid polypeptide.The toxicity in vitro of beta-amyloid protein.Amyloid β-peptide 25-35 self-assembly and its inhibition: a model undecapeptide system to gain atomistic and secondary structure details of the Alzheimer's disease process and treatment.Solvent effects on self-assembly of beta-amyloid peptideThe conformation of Alzheimer's beta peptide determines the rate of amyloid formation and its resistance to proteolysis.Structure, stability, and aggregation of paired helical filaments from tau protein and FTDP-17 mutants probed by tryptophan scanning mutagenesis.Effect of electrostatic interaction on fibril formation of human calcitonin as studied by high resolution solid state 13C NMR.Charge substitution shows that repulsive electrostatic interactions impede the oligomerization of Alzheimer amyloid peptides.Contact regions in the dimer of Alzheimer beta-amyloid domain [1-28] studied by mass spectrometry.Structural and kinetic features of amyloid beta-protein fibrillogenesis.The diversity and utility of amyloid fibrils formed by short amyloidogenic peptides.Molecular simulation of the primary and secondary structures of the Abeta(1-42)-peptide of Alzheimer's disease.Histidine residues underlie Congo red binding to A beta analogs.Characterisation of the Structure and Oligomerisation of Islet Amyloid Polypeptides (IAPP): A Review of Molecular Dynamics Simulation Studies
P2860
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P2860
Conformation and fibrillogenesis of Alzheimer A beta peptides with selected substitution of charged residues.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Conformation and fibrillogenes ...... stitution of charged residues.
@en
Conformation and fibrillogenes ...... stitution of charged residues.
@nl
type
label
Conformation and fibrillogenes ...... stitution of charged residues.
@en
Conformation and fibrillogenes ...... stitution of charged residues.
@nl
prefLabel
Conformation and fibrillogenes ...... stitution of charged residues.
@en
Conformation and fibrillogenes ...... stitution of charged residues.
@nl
P2093
P356
P1476
Conformation and fibrillogenes ...... bstitution of charged residues
@en
P2093
P356
10.1006/JMBI.1994.1704
P407
P577
1994-11-01T00:00:00Z