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Neurotrophic and neurotoxic effects of amyloid beta protein: reversal by tachykinin neuropeptides.
The amyloid beta protein could function as a neurotrophic factor for differentiating neurons, but at high concentrations in mature neurons, as in Alzheimer's disease, could cause neuronal degeneration.
On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants.
- A. Lomakin, D. S. Chung, G. Benedek, D. Kirschner, D. Teplow
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 6 February 1996
The approach provides a powerful means for the quantitative assay of A beta fibrillogenesis and found that the surfactant n-dodecylhexaoxyethylene glycol monoether (C12E6) slowed nucleation and elongation of fibrils in a concentration-dependent manner.
Constitutively Active Akt Induces Enhanced Myelination in the CNS
In vivo, constitutively active Akt enhances CNS myelination but not PNSMyelination and has no impact developmentally on oligodendrocyte number.
X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation.
The cross-beta conformation of PHF and amyloid fibers that the authors have found from x-ray diffraction is in contrast to the predominant alpha-helical coiled-coil conformed of the neurofilaments with which they share epitopes and from which they have been postulated to derive.
Mice deficient for the myelin-associated glycoprotein show subtle abnormalities in myelin.
Observations suggest that MAG participates in the formation of the periaxonal cytoplasmic collar of oligodendrocytes and in the recognition between oligodendedrocyte processes and axons.
Structural analysis of Alzheimer's beta(1-40) amyloid: protofilament assembly of tubular fibrils.
Kinetic theory of fibrillogenesis of amyloid β-protein
It is suggested that the method of QLS in combination with this theory can serve as a powerful tool for understanding the molecular factors that control Aβ plaque formation.
pH-dependent structural transitions of Alzheimer amyloid peptides.
Compact myelin exists in the absence of basic protein in the shiverer mutant mouse
The shiverer mouse is unique in showing a striking alteration in myelin protein composition that does not significantly affect the gross morphology and lamellar organisation of the myelin sheath, and this results question the proposed role of basic proteins15–19 in Myelin as ‘structural cement’.
The Formation of Straight and Twisted Filaments from Short Tau Peptides*
Results suggest that the core of PHF6 is localized at VYK, and the interaction between small amphiphilic segments of tau may initiate nucleation and lead to filaments displaying paired helical filament morphology.