Evidence map›Paper›PMID 21176768›Full record

ReviewArchives of biochemistry and biophysics2011

Tyrosine hydroxylase and regulation of dopamine synthesis.

S Colette Daubner, Tiffany Le, Shanzhi Wang

Open access · greenAbstract readReview
In one paragraph

Review in Archives of biochemistry and biophysics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 526 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
526citing papers in PubMed, 2 pooled it
7.3field-weighted citation impact, top 2% 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

526 citing papers in PubMed, 2 syntheses or guidelines pooled it, 1,028 citations in OpenAlex.

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466 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 1 country.

S Colette DaubnerDepartment of Biological Sciences, St. Mary's University, San Antonio, TX 78228, USA. sdaubner@stmarytx.edu
Tiffany Le
Shanzhi Wang
St. Mary's University, Texas · USTexas A&M University · US

Funding

NEUROTRANSMITTER BIOSYNTHESISR01GM047291 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI FITZPATRICK, PAUL F. · 1992 to 2011
$3.2M
NIGMS NIH HHS R01 GM047291
6 · The paper itself

Abstract

Tyrosine hydroxylase is the rate-limiting enzyme of catecholamine biosynthesis; it uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to DOPA. Its amino terminal 150 amino acids comprise a domain whose structure is involved in regulating the enzyme's activity. Modes of regulation include phosphorylation by multiple kinases at four different serine residues, and dephosphorylation by two phosphatases. The enzyme is inhibited in feedback fashion by the catecholamine neurotransmitters. Dopamine binds to TyrH competitively with tetrahydrobiopterin, and interacts with the R domain. TyrH activity is modulated by protein-protein interactions with enzymes in the same pathway or the tetrahydrobiopterin pathway, structural proteins considered to be chaperones that mediate the neuron's oxidative state, and the protein that transfers dopamine into secretory vesicles. TyrH is modified in the presence of NO, resulting in nitration of tyrosine residues and the glutathionylation of cysteine residues.

Indexed as

Amino Acid SequenceAnimalsDopamineHumansMolecular Sequence DataNitratesProtein Structure, TertiarySulfhydryl CompoundsTyrosine 3-MonooxygenaseDopamineNitratesSulfhydryl CompoundsTyrosine 3-Monooxygenase

Identifiers

PMID21176768
PMCPMC3065393
OpenAlexW2103493168

What OpenQuestion holds

Textmetadata
LicenceTDM
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.