Evidence map›Paper›PMID 20306493›Full record

ArticleProtein science : a publication of the Protein Society2010

Dimer-monomer equilibrium of human thymidylate synthase monitored by fluorescence resonance energy transfer.

Filippo Genovese, Stefania Ferrari, Giambattista Guaitoli, Monica Caselli, M Paola Costi, Glauco Ponterini

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2010. 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
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Crystal structure of the active form of native human thymidylate synthase in the absence of bound substrates.Acta crystallographica. Section F, Structural biology communications · 2017
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. EmrE dimerization depends on membrane environment.Biochimica et biophysica acta · 2014
    Article
  13. Neglected role of cAMP receptor protein monomer.Molecular biology reports · 2012
    Article
  14. Protein-protein interface-binding peptides inhibit the cancer therapy target human thymidylate synthase.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  15. Review
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

6 authors.

Filippo GenoveseDipartimento di Scienze Farmaceutiche, Università di Modena e Reggio Emilia, 41100 Modena, Italy.
Stefania Ferrari
Giambattista Guaitoli
Monica Caselli
M Paola Costi
Glauco Ponterini

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An ad hoc bioconjugation/fluorescence resonance energy transfer (FRET) assay has been designed to spectroscopically monitor the quaternary state of human thymidylate synthase dimeric protein. The approach enables the chemoselective engineering of allosteric residues while preserving the native protein functions through reversible masking of residues within the catalytic site, and is therefore suitable for activity/oligomerization dual assay screenings. It is applied to tag the two subunits of human thymidylate synthase at cysteines 43 and 43' with an excitation energy donor/acceptor pair. The dimer-monomer equilibrium of the enzyme is then characterized through steady-state fluorescence determination of the intersubunit resonance energy transfer efficiency.

Indexed as

Allosteric SiteCatalytic DomainFluorescence Resonance Energy TransferHumansKineticsModels, MolecularProtein MultimerizationThymidylate SynthaseThymidylate Synthase

Identifiers

PMID20306493
PMCPMC2868244

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.