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• W2050500331 startingPage "1560" @default.
• W2050500331 abstract "Abstract We performed an analysis of mutation patterns in all 10 hydrophobic regions (HRs) of presenilin‐1 (PS‐1) and PS‐2 using a recent database of Alzheimer's disease (AD) mutations. The linear patterns were confirmed and extended to areas spanning as many as three faces of a given HR. The complementary areas of residues free of AD mutations were identified based on the location of non‐pathogenic polymorphisms and PS‐1 versus PS‐2 amino acid discordances. Taking into account the location of areas of AD mutations and mutation‐free areas/regions, we proposed a preliminary model of PS‐1 structure using a general stick‐out‐mutation rule. To build a molecular structure of PS‐1 and preserve features of the preliminary model, we used bacteriorhodopsin template in homology/comparative modelling. Two molecular models were built differing in the location of C‐terminal fragment helices. The models properly distinguish residues belonging to AD‐affected sites and non‐pathogenic areas, and may be used for classification purposes. They also comply with experimental results, such as differences in accessibility of the catalytic residues in uncleaved PS‐1, and binding of PEN‐2 by the PS‐1 NF motif." @default.
• W2050500331 created "2016-06-24" @default.
• W2050500331 creator A5001609547 @default.
• W2050500331 creator A5054011421 @default.
• W2050500331 creator A5087383129 @default.
• W2050500331 date "2006-07-05" @default.
• W2050500331 modified "2023-10-16" @default.
• W2050500331 title "Linear patterns of Alzheimer's disease mutations along α-helices of presenilins as a tool for PS-1 model construction" @default.
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• W2050500331 doi "https://doi.org/10.1111/j.1471-4159.2006.03983.x" @default.
• W2050500331 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16923167" @default.
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