ArticleThe FEBS journal2025
A phosphoserine phosphatase variant present in the brain of Alzheimer's disease patients favors nuclear mistargeting.
Article in The FEBS journal, 2025. 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.
- Evolution-guided yeast complementation reveals functional differences in human PSPH variants.FEBS open bio · 2026Article
- Post-translational regulation of human D-3-phosphoglycerate dehydrogenase in Alzheimer's disease.Protein science : a publication of the Protein Society · 2026Article
- Detection and functional assessment of D-amino acids as potential biomarkers in neurological disorders.Molecular biology reports · 2025Review
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11 authors.
Funding
Abstract
Phosphoserine phosphatase (PSP) catalyzes the dephosphorylation of 3-phosphoserine, which is the final step in the de novo biosynthesis of l-serine (l-Ser) via the phosphorylated pathway in human astrocytes. Individuals who are homozygous or compound heterozygous for functionally defective PSP variants exhibit reduced cerebrospinal fluid l-Ser levels and severe neurological symptoms. In the present study, single nucleotide polymorphisms in PSP were identified in hippocampal samples from Alzheimer's disease (AD) patients. Two single nucleotide polymorphisms, likely forming a haplotype (chr7:56088825 T>A and chr7:56088811 T>C, encoding R27S and D32G PSP variants, respectively), were detected exclusively in AD patients (three females and one male). Biochemical characterization of the recombinant R27S/D32G PSP enzyme revealed a slight decrease in thermostability, a 38-fold reduction in catalytic efficiency and a two-fold increase in IC
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