Evidence map›Paper›PMID 25423174›Full record

ArticleBioscience reports2014

Analysis of mRNA recognition by human thymidylate synthase.

Nicholas D Brunn, Sergey M Dibrov, Melody B Kao, Majid Ghassemian, Thomas Hermann

Open access · goldAbstract read
In one paragraph

Article in Bioscience reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.0field-weighted citation impact, top 22% 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

16 citing papers in PubMed, 24 citations in OpenAlex.

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  6. Detection of a G-Quadruplex as a Regulatory Element inInternational journal of molecular sciences · 2020
    Article
  7. The polymorphism of rs11614913 T/T in pri-American journal of translational research · 2020
    Article
  8. Article
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  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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.

Nicholas D Brunn*Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093, U.S.A.
Sergey M Dibrov*Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093, U.S.A.
Melody B Kao*Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093, U.S.A.
Majid Ghassemian*Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093, U.S.A.
Thomas Hermann*Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093, U.S.A.
University of California San Diego · US

Funding

VIRAL MALIGNANCYP30CA023100 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DIANE M SIMEONE · 1985 to 2026
$124.9M
Chemotherapy targeting human thymidylate synthase messenger RNAR01CA132753 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HERMANN, THOMAS C · 2009 to 2013
$1.6M
NCI NIH HHS CA132753NCI NIH HHS P30 CA023100
6 · The paper itself

Abstract

Expression of hTS (human thymidylate synthase), a key enzyme in thymidine biosynthesis, is regulated on the translational level through a feedback mechanism that is rarely found in eukaryotes. At low substrate concentrations, the ligand-free enzyme binds to its own mRNA and stabilizes a hairpin structure that sequesters the start codon. When in complex with dUMP (2'-deoxyuridine-5'-monophosphate) and a THF (tetrahydrofolate) cofactor, the enzyme adopts a conformation that is unable to bind and repress expression of mRNA. Here, we have used a combination of X-ray crystallography, RNA mutagenesis and site-specific cross-linking studies to investigate the molecular recognition of TS mRNA by the hTS enzyme. The interacting mRNA region was narrowed to the start codon and immediately flanking sequences. In the hTS enzyme, a helix-loop-helix domain on the protein surface was identified as the putative RNA-binding site.

Indexed as

Nucleic Acid ConformationProtein Structure, TertiaryBase SequenceBinding SitesCodon, InitiatorCrystallography, X-RayElectrophoresis, Polyacrylamide GelGene Expression RegulationHumansMass SpectrometryModels, MolecularMutagenesisNucleotide MotifsProtein BindingRNA, MessengerThymidylate SynthaseCodon, InitiatorRNA, MessengerThymidylate Synthase

Identifiers

PMID25423174
PMCPMC4274661
OpenAlexW2325164520

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.