Evidence map›Paper›PMID 10575013›Full record

ArticleThe Journal of biological chemistry1999

Fetal Alz-50 clone 1, a novel zinc finger protein, binds a specific DNA sequence and acts as a transcriptional regulator.

K L Jordan-Sciutto, J M Dragich, J L Rhodes, R Bowser

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 1999. 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
0.5field-weighted citation impact, top 40% 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, 31 citations in OpenAlex.

  1. Article
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  5. The Chromatin Remodeling Protein Bptf Promotes Posterior Neuroectodermal Fate by Enhancing Smad2-Activated wnt8a Expression.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
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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

4 authors at 1 institution in 1 country.

K L Jordan-SciuttoDepartment of Pathology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261, USA.
J M Dragich
J L Rhodes
R Bowser
University of Pittsburgh · US

Funding

TREATMENT OF DEPRESSION IN ALZHEIMER'S DISEASEP50AG005133 · NIA · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BELLE, STEVEN H. · 1985 to 2019
$43.0M
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 AG05133NIA NIH HHS AG13208NIA NIH HHS P50 AG005133NINDS NIH HHS F32 NS010572NINDS NIH HHS NS10572
6 · The paper itself

Abstract

Fetal Alz-50 clone 1 (FAC1) is a novel, developmentally regulated gene that exhibits changes in protein expression and subcellular localization during neuronal development and neurodegeneration. To understand the functional implications of altered subcellular localization, we have established a normal cellular function of FAC1. The FAC1 amino acid sequence contains regional homology to transcriptional regulators. Using the polymerase chain reaction-assisted binding site selection assay, we have identified a DNA sequence recognized by recombinant FAC1. Mutation of any 2 adjacent base pairs in the identified binding site dramatically reduced the binding preference of FAC1, demonstrating that the binding is specific for the identified site. Nuclear extracts from neural and non-neural cell lines contained a DNA-binding activity with similar specificity and nucleotide requirements as the recombinant FAC1 protein. This DNA-binding activity can be attributed to FAC1 since it is dependent upon the presence of FAC1 and behaves identically on a nondenaturing polyacrylamide gel as transiently transfected FAC1. In NIH3T3 cells, luciferase reporter plasmids containing the identified binding site (CACAACAC) were repressed by cotransfected FAC1 whether the binding site was proximal or distal to the transcription initiation site. This study indicates that FAC1 is a DNA-binding protein that functions as a transcription factor when localized to the nucleus.

Indexed as

DNA-Binding ProteinsGenes, RegulatorTranscription Factors3T3 CellsAnimalsAntigensAntigens, NuclearBase SequenceBinding SitesBromodomain Containing ProteinsCOS CellsHumansImmunoblottingMiceMolecular Sequence DataNerve Tissue ProteinsAlzheimer's disease antigenAntigensAntigens, NuclearBromodomain Containing ProteinsDNA-Binding Proteinsfetal Alzheimer antigenNerve Tissue ProteinsRecombinant ProteinsTranscription Factors

Identifiers

PMID10575013
PMCPMC3670955
OpenAlexW2028224086

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.