ArticleProceedings of the National Academy of Sciences of the United States of America1997
Cell surface expression of the Alzheimer disease-related presenilin proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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.
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Who cites it
18 citing papers in PubMed, 63 citations in OpenAlex.
- Article
- Review: cell cycle aberrations and neurodegeneration.Neuropathology and applied neurobiology · 2010Review
- Benchmarking B-cell epitope prediction for the design of peptide-based vaccines: problems and prospects.Journal of biomedicine & biotechnology · 2010Review
- Assessment of pluripotency and multilineage differentiation potential of NTERA-2 cells as a model for studying human embryonic stem cells.Cell proliferation · 2006Article
- The presenilins turned inside out: implications for their structures and functions.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- The discrepancy between presenilin subcellular localization and gamma-secretase processing of amyloid precursor protein.The Journal of cell biology · 2001Article
- Presenilin-1 mutations reduce cytoskeletal association, deregulate neurite growth, and potentiate neuronal dystrophy and tau phosphorylation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2001Article
- Mice lacking both presenilin genes exhibit early embryonic patterning defects.Genes & development · 1999Article
- Presenilin 1 controls gamma-secretase processing of amyloid precursor protein in pre-golgi compartments of hippocampal neurons.The Journal of cell biology · 1999Article
- Drosophila presenilin is required for neuronal differentiation and affects notch subcellular localization and signaling.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999Article
- Endogenous presenilin 1 redistributes to the surface of lamellipodia upon adhesion of Jurkat cells to a collagen matrix.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- A myristoylated calcium-binding protein that preferentially interacts with the Alzheimer's disease presenilin 2 protein.The Journal of cell biology · 1999Article
- Presenilins: structural aspects and posttranslational events.Molecular neurobiology · 1999Review
- The role of cell cycle-mediated events in Alzheimer's disease.International journal of experimental pathology · 1999Review
- Additional evidence for an eight-transmembrane-domain topology for Caenorhabditis elegans and human presenilins.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- On the spurious endoproteolytic processing of the presenilin proteins in cultured cells and tissues.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- The seven-transmembrane spanning topography of the Alzheimer disease-related presenilin proteins in the plasma membranes of cultured cells.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Neurons bearing presenilins: weapons for defense or suicide?Journal of cellular and molecular medicineArticle
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The presenilin proteins PS-1 and PS-2 are crucially involved in Alzheimer disease (AD), but their molecular functions are not known. They are integral membrane proteins, but whether they can be expressed at the surface of cells has been in dispute. Here we show by immunofluorescence experiments, using anti-peptide antibodies specific for either PS-1 or PS-2, that live cultured DAMI cells and differentiated human NT2N neuronal cells are specifically immunolabeled for their endogenous as well as transfected presenilins, although the cells cannot be immunolabeled for their intracellular tubulin, unless they are first fixed and permeabilized. These and other results establish that portions of the presenilins are indeed expressed at the surfaces of these cells. These findings support our previous proposal that the presenilins on the surface of a cell engage in intercellular interactions with the beta-amyloid precursor protein on the surface of a neighboring cell, as a critical step in the molecular and cellular mechanisms that lead to AD.
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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.