Evidence map›Paper›PMID 9770640›Full record

ReviewJournal of molecular neuroscience : MN1998

Advances in the molecular characterization of tryptophan hydroxylase.

S M Mockus, K E Vrana

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of molecular neuroscience : MN, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.3field-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

26 citing papers in PubMed, 95 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Protective Role of Melatonin and Its Metabolites in Skin Aging.International journal of molecular sciences · 2022
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Local melatoninergic system as the protector of skin integrity.International journal of molecular sciences · 2014
    Review
  15. Article
  16. Boosting serotonin in the brain: is it time to revamp the treatment of depression?Journal of psychopharmacology (Oxford, England) · 2012
    Article
  17. Review
  18. Review
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

S M MockusProgram in Neuroscience, Wake Forest University School of Medicine, Winston-Salem, NC 27157-1083, USA.
K E Vrana
Wake Forest University · US

Funding

MOLECULAR CHARACTERIZATION OF TYROSINE HYDEOXYLASER01GM038931 · NIGMS · WEST VIRGINIA UNIVERSITY · PI VRANA, KENT E · 1991 to 2010
$2.0M
NIAAA NIH HHS T32-AA0756NIGMS NIH HHS GM-38931
6 · The paper itself

Abstract

The neurotransmitter serotonin has been implicated in numerous physiological functions and pathophysiological disorders. The hydroxylation of the aromatic amino acid tryptophan is rate-limiting in the synthesis of serotonin. Tryptophan hydroxylase (TPH), as the rate-limiting enzyme, determines the concentrations of serotonin in vivo. Relative serotonin concentrations are clearly important in neural transmission, but serotonin has also been reported to function as a local antioxidant. Identification of the mechanisms regulating TPH activity has been hindered by its low levels in tissues and the instability of the enzyme. Several TPH expression systems have been developed to circumvent these problems. In addition, eukaryotic expressions systems are currently being developed and represent a new avenue of research for identifying TPH regulatory mechanisms. Recombinant DNA technology has enabled the synthesis of TPH deletions, chimeras, and point mutations that have served as tools for identifying structural and functional domains within TPH. Notably, the experiments have proven long-held hypotheses that TPH is organized into N-terminal regulatory and C-terminal catalytic domains, that serine-58 is a site for PKA-mediated phosphorylation, and that a C-terminal leucine zipper is involved in formation of the tetrameric holoenzyme. Several new findings have also emerged regarding regulation of TPH activity by posttranslational phosphorylation, kinetic inhibition, and covalent modification. Inhibition of TPH by L-DOPA may have implications for depression in Parkinson's disease (PD) patients. In addition, TPH inactivation by nitric oxide may be involved in amphetamine-induced toxicity. These regulatory concepts, in conjunction with new systems for studying TPH activity, are the focus of this article.

Indexed as

Catalytic DomainCell LineEnzyme ActivationEnzyme RepressionEnzyme StabilityHumansPhosphorylationRecombinant ProteinsTryptophan HydroxylaseRecombinant ProteinsTryptophan Hydroxylase

Identifiers

PMID9770640
OpenAlexW2071863426

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.