Evidence map›Paper›PMID 12628003›Full record

ArticleThe Biochemical journal2003

Characterization of the nutrient-sensing response unit in the human asparagine synthetase promoter.

Can Zhong, Chin Chen, Michael S Kilberg

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

20 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Asparagine synthetase: regulation by cell stress and involvement in tumor biology.American journal of physiology. Endocrinology and metabolism · 2013
    Review
  6. Article
  7. ATF4-dependent transcription mediates signaling of amino acid limitation.Trends in endocrinology and metabolism: TEM · 2009
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Asparagine synthetase chemotherapy.Annual review of biochemistry · 2006
    Review
  17. Article
  18. Article
  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

3 authors at 1 institution in 1 country.

Can ZhongDepartment of Biochemistry and Molecular Biology, University of Florida College of Medicine, Box 100245, Gainesville 32610-0245, USA.
Chin Chen
Michael S Kilberg
University of Florida · US

Funding

NUTRITIONAL CONTROL OF ASPARAGINE SYNTHETASER01DK052064 · NIDDK · UNIVERSITY OF FLORIDA · PI KILBERG, MICHAEL S. · 1997 to 2010
$3.4M
NIDDK NIH HHS DK-52064
6 · The paper itself

Abstract

Transcription from the human asparagine synthetase (A.S.) gene is increased in response to either amino acid (amino acid response) or glucose (endoplasmic reticulum stress response) deprivation. These two independent nutrient-sensing pathways converge on the same set of genomic cis -elements, referred to as nutrient sensing-response elements (NSREs) 1 and 2, within the A.S. promoter. The present report uses single-nucleotide mutagenesis to confirm that both NSRE-1 and NSRE-2 are absolutely required for gene activation and to identify the boundaries of each binding site. The core sequence of the NSRE-1 site is contained within nucleotides -68 to -60 and the NSRE-2 core sequence is within nucleotides -48 to -43. Through insertion or deletion of 5-10 nucleotides in the intervening sequence between NSRE-1 and NSRE-2, transient transfection studies with an A.S. promoter/reporter gene construct showed that the 11 bp distance between these two elements is critical. These results document that the optimal configuration is with both binding sites on the same side of the DNA helix, only one helical turn away from each other and the data provide support for the hypothesis that a larger multi-protein complex exists between the binding proteins for NSRE-1 and NSRE-2. The data also illustrate that the combination of NSRE-1 and NSRE-2, referred to as the nutrient-sensing response unit (NSRU), has enhancer activity in that it functions in an orientation- and position-independent manner, and conveys nutrient-dependent transcriptional control to a heterologous promoter.

Indexed as

Gene Expression Regulation, EnzymologicAspartate-Ammonia LigaseBase SequenceCarcinoma, HepatocellularEnzyme ActivationGenes, ReporterGlucoseHistidineHumansMolecular Sequence DataMutagenesis, Site-DirectedMutationPromoter Regions, GeneticRecombinant ProteinsResponse ElementsSequence DeletionAspartate-Ammonia LigaseGlucoseHistidineRecombinant ProteinsTranscription Factors

Identifiers

PMID12628003
PMCPMC1223424
OpenAlexW1973085898

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.