ReviewMolecular neurobiology1999
Presenilins: structural aspects and posttranslational events.
Review in Molecular neurobiology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- Targeting γ-secretase triggers the selective enrichment of oligomeric APP-CTFs in brain extracellular vesicles from Alzheimer cell and mouse models.Translational neurodegeneration · 2019Article
- The mitochondrial permeability transition in neurologic disease.Neurochemistry international · 2007Review
- Unusual phenotypic alteration of beta amyloid precursor protein (betaAPP) maturation by a new Val-715 --> Met betaAPP-770 mutation responsible for probable early-onset Alzheimer's disease.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
Corrections and comments
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Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most of early-onset forms of Alzheimer's disease (AD) are caused by inherited mutations located on chromosomes 14 and 1, the gene products of which have been recently identified and referred to as presenilins 1 (PS1) and 2 (PS2), respectively. The first phenotypic alterations triggered by mutated PS were reported to be an increased production of the amyloid peptide (Abeta) and, more precisely, its 42 amino-acids long counterpart Abeta42. This overproduction is thought to be responsible for the genesis of the senile plaques that invade the cortical and subcortical areas of these AD-affected brains. The discovery of PSs has triggered numerous studies aimed at better understanding their normal physiology and the dysfunctions brought by the mutations that could explain, at least in part, the neurodegenerative process taking place in this syndrome. In this review, I will focus on the structural aspects of PS and on the various posttranscriptional events they undergo. I will also briefly discuss that current hypotheses concerning their normal functions and the influence of FAD-linked mutations.
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Registered trials
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