Evidence map›Paper›PMID 24590690›Full record

ReviewMetabolic brain disease2014

Thiamine triphosphate: a ubiquitous molecule in search of a physiological role.

Lucien Bettendorff, Bernard Lakaye, Gregory Kohn, Pierre Wins

Abstract readReview
PubMed Publisher
In one paragraph

Review in Metabolic brain disease, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

14 citing papers in PubMed, 58 citations in OpenAlex.

  1. Trial
  2. Trial
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. The importance of thiamine (vitamin BThe Journal of biological chemistry · 2020
    Review
  10. Article
  11. Role of the Synthetic B1 Vitamin Sulbutiamine on Health.Journal of nutrition and metabolism · 2020
    Review
  12. Review
  13. Dietary reference values for thiamin.EFSA journal. European Food Safety Authority · 2016
    Article
  14. 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

4 authors at 1 institution in 1 country.

Lucien BettendorffGIGA-Neurosciences, University of Liège, Avenue de l'Hôpital, 1, 4000, Liège, Belgium, L.Bettendorff@ulg.ac.be.
Bernard Lakaye
Gregory Kohn
Pierre Wins
University of Liège · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thiamine triphosphate (ThTP) was discovered over 60 years ago and it was long thought to be a specifically neuroactive compound. Its presence in most cell types, from bacteria to mammals, would suggest a more general role but this remains undefined. In contrast to thiamine diphosphate (ThDP), ThTP is not a coenzyme. In E. coli cells, ThTP is transiently produced in response to amino acid starvation, while in mammalian cells, it is constitutively produced at a low rate. Though it was long thought that ThTP was synthesized by a ThDP:ATP phosphotransferase, more recent studies indicate that it can be synthesized by two different enzymes: (1) adenylate kinase 1 in the cytosol and (2) FoF1-ATP synthase in brain mitochondria. Both mechanisms are conserved from bacteria to mammals. Thus ThTP synthesis does not seem to require a specific enzyme. In contrast, its hydrolysis is catalyzed, at least in mammalian tissues, by a very specific cytosolic thiamine triphosphatase (ThTPase), controlling the steady-state cellular concentration of ThTP. In some tissues where adenylate kinase activity is high and ThTPase is absent, ThTP accumulates, reaching ≥ 70% of total thiamine, with no obvious physiological consequences. In some animal tissues, ThTP was able to phosphorylate proteins, and activate a high-conductance anion channel in vitro. These observations raise the possibility that ThTP is part of a still uncharacterized cellular signaling pathway. On the other hand, its synthesis by a chemiosmotic mechanism in mitochondria and respiring bacteria might suggest a role in cellular energetics.

Indexed as

Adenosine TriphosphateAdenylate KinaseAmino AcidsAnimalsBrainCytosolForecastingHumansLeigh DiseaseMitochondriaModels, BiologicalModels, NeurologicalOrgan SpecificityPhosphorylationProtein Processing, Post-TranslationalProton-Translocating ATPasesAdenosine TriphosphateAdenylate Kinaseadenylate kinase 1Amino AcidsProton-Translocating ATPasesThiamine TriphosphateThiamin-Triphosphatase

Identifiers

PMID24590690
OpenAlexW2137978958

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.