Evidence map›Paper›PMID 9437013›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience1998

Interaction of presenilins with the filamin family of actin-binding proteins.

W Zhang, S W Han, D W McKeel, A Goate, J Y Wu

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed, 1 pooled it
10.9field-weighted citation impact, top 1% 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

33 citing papers in PubMed, 1 synthesis or guideline pooled it, 123 citations in OpenAlex.

  1. Pooled it
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  10. Review
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  15. Article
  16. Filamin B deficiency in mice results in skeletal malformations and impaired microvascular development.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  17. Article
  18. Genetic malformations of cortical development.Experimental brain research · 2006
    Review
  19. Review
  20. 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

5 authors at 1 institution in 1 country.

W ZhangDepartment of Pediatrics and Molecular Biology and Pharmacology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
S W Han
D W McKeel
A Goate
J Y Wu
Washington University in St. Louis · US

Funding

WASHINGTON UNIVERSITY ALZHEIMERS DISEASE RESEARCH CENTERP50AG005681 · NIA · WASHINGTON UNIVERSITY · PI MORRIS, JOHN · 1985 to 2019
$52.1M
Pre-mRNA Splicing Defects and Retinal DegenerationR01EY014576 · NEI · VANDERBILT UNIVERSITY · PI WU, JANE Y · 2004 to 2008
$1.8M
Slit Signaling in Breast CancerR01CA114197 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI WU, JANE Y · 2006 to 2010
$1.3M
Alternative splicing regulation of caspase-2 geneR01GM070967 · NIGMS · VANDERBILT UNIVERSITY · PI WU, JANE Y · 2005 to 2008
$939k
CORTICOSTEROID RECEPTORS AND NEURONAL VIABILITYF32AG005861 · NIA · UNIVERSITY OF KENTUCKY · PI SIPE, KIMBERLY J · 1999 to 1999
–
NCI NIH HHS R01 CA114197NEI NIH HHS R01 EY014576NIA NIH HHS AG00634NIA NIH HHS AG05681NIA NIH HHS AG-05861NIA NIH HHS F32 AG005861NIA NIH HHS P50 AG005681NIGMS NIH HHS R01 GM070967
6 · The paper itself

Abstract

Mutations in presenilin genes PS1 and PS2 account for approximately 50% of early-onset familial Alzheimer's disease (FAD). The PS1 and PS2 genes encode highly homologous transmembrane proteins related to the Caenorhabditis elegans sel-12 and spe-4 gene products. A hydrophilic loop region facing the cytoplasmic compartment is likely to be functionally important because at least 14 mutations in FAD patients have been identified in this region. We report here that the loop regions of PS1 and PS2 interact with nonmuscle filamin (actin-binding protein 280, ABP280) and a structurally related protein (filamin homolog 1, Fh1). Overexpression of PS1 appears to modify the distribution of ABP280 and Fh1 proteins in cultured cells. A monoclonal antibody recognizing ABP280 and Fh1 binds to blood vessels, astrocytes, neurofibrillary tangles, neuropil threads, and dystrophic neurites in the AD brain. Detection of ABP280/Fh1 proteins in these structures suggests that these presenilin-interacting proteins may be involved in the development of AD and that interactions between presenilins and ABP280/Fh1 may be functionally significant. The ABP280 gene is located on the human X chromosome, whereas the newly identified Fh1 gene maps to human chromosome 3. These results provide a new basis for understanding the function of presenilin proteins and further implicate cytoskeletal elements in AD pathogenesis.

Indexed as

AgedAged, 80 and overAlzheimer DiseaseAnimalsAntibodies, MonoclonalBrain ChemistryCarrier ProteinsChromosome MappingChromosomes, Human, Pair 3Contractile ProteinsCOS CellsCytoskeletonFemaleFilaminsHumansMaleAntibodies, MonoclonalCarrier ProteinsContractile ProteinsFilaminsFLNC protein, humanMembrane ProteinsMicrofilament ProteinsPresenilin-1Presenilin-2PSEN1 protein, humanPSEN2 protein, human

Identifiers

PMID9437013
PMCPMC2042137
OpenAlexW1499973238

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.