Evidence map›Paper›PMID 15379550›Full record

ArticleBiochemistry2004

Fetal Alz-50 clone 1 interacts with the human orthologue of the Kelch-like Ech-associated protein.

Gordon D Strachan, Kathleen L Morgan, Linda L Otis, John Caltagarone, Aryn Gittis, Robert Bowser, Kelly L Jordan-Sciutto

Abstract read
In one paragraph

Article in Biochemistry, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

15 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Beyond repression of Nrf2: An update on Keap1.Free radical biology & medicine · 2020
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
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  15. 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

7 authors at 2 institutions in 1 country.

Gordon D StrachanDepartment of Pathology, University of Pennsylvania, 4010 Locust Street, Philadelphia, Pennsylvania 19104-6030, USA.
Kathleen L Morgan
Linda L Otis
John Caltagarone
Aryn Gittis
Robert Bowser
Kelly L Jordan-Sciutto
University of Pennsylvania · USUniversity of Pittsburgh Medical Center · US

Funding

ROLE OF CELL CYCLE PROTEINS IN HIV ENCEPHALITISR01NS041202 · NINDS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI JORDAN-SCIUTTO, KELLY L · 2001 to 2015
$4.5M
NOVEL ANTIGEN IN DEVELOPING BRAIN AND ALZHEIMERS DISEASER01NS042902 · NINDS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BOWSER, ROBERT P · 2001 to 2004
$1.3M
NOVEL ANTIGEN IN DEVELOPING BRAIN AND ALZHEIMERS DISEASER29AG013208 · NIA · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BOWSER, ROBERT P · 1995 to 2000
$113k
MOLECULAR MECHANISMS OF BRAIN DEVELOPMENT AND DISEASEF32NS010572 · NINDS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI JORDAN-SCIUTTO, KELLY L · 1997 to 1998
–
NIA NIH HHS AG13208NINDS NIH HHS F32 NS010572NINDS NIH HHS NS10572NINDS NIH HHS NS41202NINDS NIH HHS NS42902NINDS NIH HHS R01 NS041202NINDS NIH HHS R01 NS042902
6 · The paper itself

Abstract

The fetal Alz-50 reactive clone 1 (FAC1) protein exhibits altered expression and subcellular localization during neuronal development and neurodegenerative diseases such as Alzheimer's disease. Using the yeast two-hybrid screen, the human orthologue of Keap1 (hKeap1) was identified as a FAC1 interacting protein. Keap1 is an important regulator of the oxidative stress response pathway through its interaction with the Nrf family of transcription factors. An interaction between full-length FAC1 and hKeap1 proteins has been demonstrated, and the FAC1 binding domain of hKeap1 has been identified as the Kelch repeats. In addition, FAC1 colocalizes with endogenous Keap1 within the cytoplasm of PT67 cells. Exogenously introduced eGFP:hKeap1 fusion protein redistributed FAC1 to colocalize with eGFP:hKeap1 in perinuclear, spherical structures. The interaction between FAC1 and hKeap1 is reduced by competition with the Nrf2 protein. However, competition by Nrf2 for hKeap1 is reduced by diethylmaleate (DEM), a known disrupter of the Nrf2:Keap1 interaction. DEM does not affect the ability of FAC1 to bind hKeap1 in our assay. These results suggest that hKeap1 regulates FAC1 in addition to its known role in control of Nrf2. Furthermore, the observed competition between FAC1 and Nrf2 for binding hKeap1 indicates that the interplay between these three proteins has important implications for neuronal response to oxidative stress.

Indexed as

ActinsAmino Acid MotifsAnimalsAntigens, NuclearBinding, CompetitiveBromodomain Containing ProteinsCell LineCytoplasmDNA-Binding ProteinsFibroblastsGene Expression RegulationHumansIntracellular Signaling Peptides and ProteinsKelch-Like ECH-Associated Protein 1MaleatesMiceActinsAntigens, NuclearBromodomain Containing Proteinsdiethyl maleateDNA-Binding Proteinsfetal Alzheimer antigenIntracellular Signaling Peptides and ProteinsKEAP1 protein, humanKelch-Like ECH-Associated Protein 1MaleatesNerve Tissue ProteinsNFE2L2 protein, humanNfe2l2 protein, mouseNF-E2-Related Factor 2ProteinsTrans-ActivatorsTranscription Factors

Identifiers

PMID15379550
PMCPMC3670950
OpenAlexW2062417683

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.