Evidence map›Paper›PMID 10727395›Full record

ReviewThe Biochemical journal2000

Tetrahydrobiopterin biosynthesis, regeneration and functions.

B Thöny, G Auerbach, N Blau

Open access · bronzeAbstract readReview
In one paragraph

Review in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 334 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
334citing papers in PubMed, 2 pooled it
13.1field-weighted citation impact, top 1% 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

334 citing papers in PubMed, 2 syntheses or guidelines pooled it, 849 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. No effect of acute tetrahydrobiopterin (BHJournal of applied physiology (Bethesda, Md. : 1985) · 2022
    Trial
  4. Genome-integrated engineering ofSynthetic and systems biotechnology · 2027
    Article
  5. Engineering a heme-dependent tryptophan hydroxylase pathway inSynthetic and systems biotechnology · 2026
    Article
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274 more citing papers are in PubMed but not listed here.

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 2 institutions in 2 countries.

B ThönyDivision of Clinical Chemistry, University Children's Hospital, Steinwiesstrasse 75, 8032 Zurich, Switzerland.
G Auerbach
N Blau
University Children's Hospital Zurich · CHMax Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tetrahydrobiopterin (BH(4)) cofactor is essential for various processes, and is present in probably every cell or tissue of higher organisms. BH(4) is required for various enzyme activities, and for less defined functions at the cellular level. The pathway for the de novo biosynthesis of BH(4) from GTP involves GTP cyclohydrolase I, 6-pyruvoyl-tetrahydropterin synthase and sepiapterin reductase. Cofactor regeneration requires pterin-4a-carbinolamine dehydratase and dihydropteridine reductase. Based on gene cloning, recombinant expression, mutagenesis studies, structural analysis of crystals and NMR studies, reaction mechanisms for the biosynthetic and recycling enzymes were proposed. With regard to the regulation of cofactor biosynthesis, the major controlling point is GTP cyclohydrolase I, the expression of which may be under the control of cytokine induction. In the liver at least, activity is inhibited by BH(4), but stimulated by phenylalanine through the GTP cyclohydrolase I feedback regulatory protein. The enzymes that depend on BH(4) are the phenylalanine, tyrosine and tryptophan hydroxylases, the latter two being the rate-limiting enzymes for catecholamine and 5-hydroxytryptamine (serotonin) biosynthesis, all NO synthase isoforms and the glyceryl-ether mono-oxygenase. On a cellular level, BH(4) has been found to be a growth or proliferation factor for Crithidia fasciculata, haemopoietic cells and various mammalian cell lines. In the nervous system, BH(4) is a self-protecting factor for NO, or a general neuroprotecting factor via the NO synthase pathway, and has neurotransmitter-releasing function. With regard to human disease, BH(4) deficiency due to autosomal recessive mutations in all enzymes (except sepiapterin reductase) have been described as a cause of hyperphenylalaninaemia. Furthermore, several neurological diseases, including Dopa-responsive dystonia, but also Alzheimer's disease, Parkinson's disease, autism and depression, have been suggested to be a consequence of restricted cofactor availability.

Indexed as

Alcohol OxidoreductasesAmino Acid SequenceAnimalsAntioxidantsBiopterinsGTP CyclohydrolaseHumansMiceModels, MolecularMolecular Sequence DataMolecular StructurePhosphorus-Oxygen LyasesProtein ConformationRatsSequence Alignment6-pyruvoyltetrahydropterin synthaseAlcohol OxidoreductasesAntioxidantsBiopterinsGTP CyclohydrolasePhosphorus-Oxygen Lyasessapropterinsepiapterin reductase

Identifiers

PMID10727395
PMCPMC1220924
OpenAlexW2128399345

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.