By C. L. Masters, K. Beyreuther (auth.), C. L. Masters M.D., K. Beyreuther Ph.D., M. Trillet Prof., Y. Christen Ph.D. (eds.)
This publication summarizes the final ten years' examine on Alzheimer's ailment. Genetic mutations within the gene which codes for amyloid precursor protein (APP) have now been proven to reason Alzheimer's sickness in a few households. different genetic loci at the moment are being stumbled on which relate to Alzheimer's affliction in a few households. knowing the conventional constitution and serve as of the APP gene product will ultimately supply avenues for constructing particular healing innovations unique on the amyloid deposition within the Alzheimer's disorder mind. medications which could inhibit or dissolve the amyloid, have an effect on the synthesis and proteolysis of APP, or which control the job of the APP gene all carry the promise of ultimately yielding a good therapy for Alzheimer's ailment.
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Additional info for Amyloid Protein Precursor in Development, Aging and Alzheimer's Disease (Research and Perspectives in Alzheimer's Disease)
Together with the green birefringence of polarized light after Congo red staining, these results prove an antiparalle1 f3-pleated sheet as the main 26 C. Hilbich et al. structural feature of f3A4 pep tides in the solid state. This finding has also been confirmed by low resolution X-ray analysis of filaments prepared from a peptide 1-42 (Fraser et al. 1991). The secondary structure of solubilized f3A4 pep tides was determined by circular dichroism (CD) spectroscopy. When solubilized in distilled water, peptide 10-43 contains an amount of 80% f3-sheet, 10% turn (of type I) and 10% random coil conformations.
The analysis of f3A4 partial sequences and analogues leads us to propose a structural model of a f3A4 monomer within an aggregate (Fig. 4). A central f3-turn formed by residues 26 to 29 is flanked by two f3-pleated sheet regions of approximately equal length. Residues 1 to 9 protrude from this hairpin-like structure. In the direction of the long axis of filaments, aggregation is due to the formation of antiparallel f3-sheets. The hydrogen bonds are arranged parallel to the filament axis, forming a cross-f3 conformation.
Nature 363: 83-85 Rubin GM (1988) Drosophila melanogaster as an experimental organism. Science 240: 1453-1459 Rudnicki MA, Braun T, Hinuma S, Jaenisch R (1992) Inactivation of MyoD in mice leads to up-regulation of the myogenic HLH gene Myf5 and results in apparently normal muscle development. Cell 71: 383-390 Saitoh T, Sundsmo M, Roch J-M, Kimura N, Cole G, Schubert D, OltersdorfT, Schenk DB (1989) Secreted form of amyloid II protein precursor is involved in the growth regulation of fibroblasts.