ReviewAlzheimer's research & therapy2013
Protein quality control by Rer1p in the early secretory pathway: from mechanism to implication in Alzheimer's disease.
Review in Alzheimer's research & therapy, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed, 5 citations in OpenAlex.
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
γ-Secretase-mediated production of amyloid β from the amyloid precursor protein is recognized as a central player in the neuropathogenesis of Alzheimer's disease (AD). One of the most peculiar features of this enzymatic activity is the fact that it targets transmembrane domains of mostly type I integral membrane proteins and thus manages to proteolyse peptide bonds within the hydrophobic lipid bilayers. In addition, γ-secretase does not exert its activity solely towards amyloid precursor protein, but to an increasing number of membrane proteins, including Notch, cadherins, syndecans, and so on. Because of the requirement of intramembrane proteolysis for a plethora of signaling pathways and cellular processes during embryonic development and organ physiology, this enzyme has drawn a lot of attention in the past 20 years. γ-Secretase is a multimeric transmembrane complex consisting of the catalytic presenilin, nicastrin, presenilin enhancer 2 (PEN2) and anterior-pharynx defective-1 (APH1) subunits. Proper assembly into functional complexes requires quality control mechanisms associated with the early biosynthetic compartments and allows mature complexes to transit to distal compartments where its activity is required. We previously identified Retrieval to ER protein 1 (Rer1p) as the first negative regulator of the stepwise assembly of γ-secretase during endoplasmic reticulum-to-Golgi transport. We review here the state of the art on how Rer1p regulates complex assembly, particularly γ-secretase, and evaluate the therapeutic potential of such regulatory processes in the context of AD.
Identifiers
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.