Evidence map›Paper›PMID 24153409›Full record

ArticleMolecular bioSystems2014

Iodotyrosine deiodinase: a unique flavoprotein present in organisms of diverse phyla.

Abhishek Phatarphekar, Jennifer M Buss, Steven E Rokita

Open access · hybridAbstract read
In one paragraph

Article in Molecular bioSystems, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

22 citing papers in PubMed, 35 citations in OpenAlex.

  1. Substrate for Thyroid Hormone Synthesis: Biochemistry, Evolution, and Physiology.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Review
  2. Article
  3. Article
  4. Misregulation of bromotyrosine compromises fertility in maleProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Cross-species applicability of an adverse outcome pathway network for thyroid hormone system disruption.Toxicological sciences : an official journal of the Society of Toxicology · 2023
    Review
  6. Article
  7. Article
  8. Article
  9. Redox control of iodotyrosine deiodinase.Protein science : a publication of the Protein Society · 2019
    Article
  10. Evaluating Iodide Recycling Inhibition as a Novel Molecular Initiating Event for Thyroid Axis Disruption in Amphibians.Toxicological sciences : an official journal of the Society of Toxicology · 2018
    Article
  11. The importance of a halotyrosine dehalogenase forThe Journal of biological chemistry · 2018
    Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Functional analysis of iodotyrosine deiodinase from drosophila melanogaster.Protein science : a publication of the Protein Society · 2016
    Article
  18. Article
  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

3 authors at 2 institutions in 1 country.

Abhishek PhatarphekarDepartment of Chemistry, Johns Hopkins University, 3400 N. Charles St., Baltimore, MD 21218, USA. rokita@jhu.edu.
Jennifer M Buss
Steven E Rokita
Johns Hopkins University · USUniversity of Maryland, College Park · US

Funding

The Chemistry-Biology Interface Program at Johns Hopkins UniversityT32GM080189 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI ROKITA, STEVEN E · 2008 to 2022
$3.5M
Reductive Dehalogenation in Mammals by Iodotyrosine DeiodinaseR01DK084186 · NIDDK · UNIV OF MARYLAND, COLLEGE PARK · PI ROKITA, STEVEN E · 2009 to 2012
$1.3M
NIDDK NIH HHS R01 DK084186NIGMS NIH HHS T32 GM080189
6 · The paper itself

Abstract

Iodide is required for thyroid hormone synthesis in mammals and other vertebrates. The role of both iodide and iodinated tyrosine derivatives is currently unknown in lower organisms, yet the presence of a key enzyme in iodide conservation, iodotyrosine deiodinase (IYD), is suggested by genomic data from a wide range of multicellular organisms as well as some bacteria. A representative set of these genes has now been expressed, and the resulting enzymes all catalyze reductive deiodination of diiodotyrosine with kcat/Km values within a single order of magnitude. This implies a physiological presence of iodotyrosines (or related halotyrosines) and a physiological role for their turnover. At least for Metazoa, IYD should provide a new marker for tracing the evolutionary development of iodinated amino acids as regulatory signals through the tree of life.

Indexed as

AnimalsCatalytic DomainDiiodotyrosineEvolution, MolecularGene Expression Regulation, EnzymologicHalogenationIodide PeroxidaseIodidesMiceProtein ConformationThyroid HormonesTyrosineDiiodotyrosineIodide PeroxidaseIodidesThyroid HormonesTyrosine

Identifiers

PMID24153409
PMCPMC3858845
OpenAlexW2071450491

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.