Evidence map›Paper›PMID 9275228›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

Cell surface expression of the Alzheimer disease-related presenilin proteins.

N N Dewji, S J Singer

Open access · greenAbstract read
In one paragraph

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.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
4.8field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Review: cell cycle aberrations and neurodegeneration.Neuropathology and applied neurobiology · 2010
    Review
  3. Review
  4. Article
  5. The presenilins turned inside out: implications for their structures and functions.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. 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 · 1999
    Article
  11. 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 · 1999
    Article
  12. Article
  13. Review
  14. The role of cell cycle-mediated events in Alzheimer's disease.International journal of experimental pathology · 1999
    Review
  15. 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 · 1998
    Article
  16. 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 · 1997
    Article
  17. Article
  18. Neurons bearing presenilins: weapons for defense or suicide?Journal of cellular and molecular medicine
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

N N DewjiDepartment of Medicine, University of California at San Diego, La Jolla, CA 92093, USA. ndewji@ucsd.edu
S J Singer
University of California, San Diego · US

Funding

NINDS NIH HHS 2RO1-NS27850
6 · The paper itself

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.

Indexed as

Alzheimer DiseaseAntibodiesCell LineCell MembraneHumansMembrane ProteinsNeuronsPresenilin-1Presenilin-2AntibodiesMembrane ProteinsPresenilin-1Presenilin-2PSEN1 protein, humanPSEN2 protein, human

Identifiers

PMID9275228
PMCPMC23298
OpenAlexW1996599959

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.