Evidence map›Paper›PMID 40140132›Full record

ArticleBulletin of experimental biology and medicine2025

Comparison of the Effects of Tetrahydrobiopterine, L-Tryptophan, and Iron Ions on the Thermal Stability of Wild Type and P447R Mutant Tryptophan Hydroxylase 2.

P D Komleva, R Deeb, E I Terentieva, A V Kulikov

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in Bulletin of experimental biology and medicine, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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.

P D KomlevaFederal Research Center Institute of Cytology and Genetics, Siberian Branch of Russian Academy of Sciences, Novosibirsk, Russia.
R DeebFederal Research Center Institute of Cytology and Genetics, Siberian Branch of Russian Academy of Sciences, Novosibirsk, Russia.
E I TerentievaFederal Research Center Institute of Cytology and Genetics, Siberian Branch of Russian Academy of Sciences, Novosibirsk, Russia.
A V KulikovFederal Research Center Institute of Cytology and Genetics, Siberian Branch of Russian Academy of Sciences, Novosibirsk, Russia. v_kulikov@bionet.nsc.ru.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The enzyme tryptophan hydroxylase 2 (TPH2) hydroxylates L-tryptophan to L-5-hydroxytryptophan (5-HTP) in the presence of tetrahydrobiopterin (BH

Indexed as

BiopterinsIronTryptophanTryptophan Hydroxylase5-HydroxytryptophanAnimalsEnzyme StabilityMiceMice, Inbred BALB CMice, Inbred C57BLMutationSerotonin5-HydroxytryptophanBiopterinsIronsapropterinSerotoninTph2 protein, mouseTryptophanTryptophan Hydroxylaseiron ionsL-tryptophantetrahydrobiopterinethermal stabilitytryptophan hydroxylase 2

Identifiers

PMID40140132

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.