Evidence map›Paper›PMID 12810950›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

Human acetyl-CoA carboxylase 1 gene: presence of three promoters and heterogeneity at the 5'-untranslated mRNA region.

Jianqiang Mao, Subrahmanyam S Chirala, Salih J Wakil

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. 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
1.6field-weighted citation impact, top 17% 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, 59 citations in OpenAlex.

  1. Review
  2. Acetyl-CoA Carboxylases and Diseases.Frontiers in oncology · 2022
    Review
  3. Article
  4. Article
  5. Article
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  7. Article
  8. Article
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  11. Article
  12. Review
  13. Article
  14. Article
  15. Mutant mice lacking acetyl-CoA carboxylase 1 are embryonically lethal.Proceedings of the National Academy of Sciences of the United States of America · 2005
    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.

Jianqiang MaoVerna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030.
Subrahmanyam S Chirala
Salih J Wakil
Baylor College of Medicine · US

Funding

Role of the Acetyl-CoA Carboxylases in Energy MetabolismR01GM063115 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI WAKIL, SALIH JAWAD · 2002 to 2011
$3.2M
NIGMS NIH HHS GM-63115NIGMS NIH HHS R01 GM063115
6 · The paper itself

Abstract

Acetyl-CoA carboxylase 1 (ACC1) catalyzes the formation of malonyl-CoA, the C2 donor for de novo synthesis of long-chain fatty acids. We have identified 64 exons, including 7 alternatively spliced minor exons (1A, 1B, 1C, 3, 5A', 5A, and 5B) in human ACC1 gene ( approximately 330 kb). The gene is regulated by three promoters (PI, PII, and PIII), which are located upstream of exons 1, 2, and 5A, respectively. PI is a constitutive promoter and has no homology with the PI sequences of other mammalian ACC1. PII is regulated by various hormones. PIII is expressed in a tissue-specific manner. The presence of several alternatively spliced exons does not alter the translation of the 265-kDa ACC1 protein starting from an ATG present in exon 5. Translation of PIII transcripts from exon 5A generates a 259-kDa isoform in which the N-terminal 75 aa of 265-kDa ACC1 are replaced with a new sequence of 17 aa. Interestingly, the inclusion of exon 5B between 5A and 6 in PIII transcripts would yield a third 257-kDa isoform, which is translated from an ATG in exon 6. However, the presence of exon 5B in PI and PII transcripts leads to an in-frame stop codon that results in an ACC1-related 77-aa peptide. The presence of alternatively spliced exons and three isoforms of ACC1 could contribute to overall ACC1 activity either by influencing the mRNA stability and translational efficiency or by increasing the stability and specific activity of the ACC1 protein, respectively.

Indexed as

5' Untranslated RegionsPromoter Regions, GeneticAcetyl-CoA CarboxylaseAlternative SplicingBase SequenceCell LineCholesterolCloning, MolecularDNA, ComplementaryExonsGene DeletionGenes, ReporterHumansModels, GeneticMolecular Sequence DataPlasmids5' Untranslated RegionsAcetyl-CoA CarboxylaseCholesterolDNA, ComplementaryProtein IsoformsRNA, MessengerTriiodothyronine

Identifiers

PMID12810950
PMCPMC164618
OpenAlexW2163216733

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.