Evidence map›Paper›PMID 18815314›Full record

ReviewEndocrine reviews2008

Cellular and molecular basis of deiodinase-regulated thyroid hormone signaling.

Balázs Gereben, Ann Marie Zavacki, Scott Ribich, Brian W Kim, Stephen A Huang, Warner S Simonides, Anikó Zeöld, Antonio C Bianco

Open access · bronzeAbstract readReview
In one paragraph

Review in Endocrine reviews, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 348 papers, 6 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
348citing papers in PubMed, 6 pooled it
23.5field-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

348 citing papers in PubMed, 6 syntheses or guidelines pooled it, 864 citations in OpenAlex.

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288 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

8 authors at 6 institutions in 3 countries.

Balázs GerebenLaboratory of Endocrine Neurobiology, Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, Hungary.
Ann Marie Zavacki
Scott Ribich
Brian W Kim
Stephen A Huang
Warner S Simonides
Anikó Zeöld
Antonio C Bianco
Brigham and Women's Hospital · USHungarian Academy of Sciences · HUAmsterdam UMC Location Vrije Universiteit Amsterdam · NLBoston Children's Hospital · USHarvard University · USUniversity of Miami · US

Funding

SELENODEIODINAS PROCESSING BY THE PROTEASOME SYSTEMR01DK058538 · NIDDK · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI BIANCO, ANTONIO C, GEREBEN, BALÁZS · 2001 to 2024
$6.0M
Thyroid-adrenergic synergism and adaptive thermogenesisR01DK065055 · NIDDK · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI BIANCO, ANTONIO C · 2005 to 2021
$4.4M
Role of Deiodinases in Thyroid Hormone HomeostasisR01DK076117 · NIDDK · BRIGHAM AND WOMEN'S HOSPITAL · PI ZAVACKI, ANN M · 2006 to 2010
$1.5M
Regulation of the human Dio3 geneR01DK076099 · NIDDK · BOSTON CHILDREN'S HOSPITAL · PI HUANG, STEPHEN A · 2007 to 2010
$1.2M
Physiologic Role of Type 2 Deiodinase in Skeletal MuscleK08DK064643 · NIDDK · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI KIM, BRIAN W · 2005 to 2009
$670k
Selenodeidinase Processing by the Proteasome SystemR56DK058538 · NIDDK · UNIVERSITY OF CHICAGO · PI BIANCO, ANTONIO C · 2019 to 2019
$203k
The Role of Type 2 Deiodinase (D2) in AdipogenesisF32DK078476 · NIDDK · BRIGHAM AND WOMEN'S HOSPITAL · PI RIBICH, SCOTT · 2008 to 2008
$26k
NIDDK NIH HHS DK064643NIDDK NIH HHS DK076099NIDDK NIH HHS DK078476NIDDK NIH HHS DK58538NIDDK NIH HHS DK65055NIDDK NIH HHS DK76117NIDDK NIH HHS DK78560NIDDK NIH HHS F32 DK078476NIDDK NIH HHS K08 DK064643NIDDK NIH HHS R01 DK058538NIDDK NIH HHS R01 DK065055NIDDK NIH HHS R01 DK076099NIDDK NIH HHS R01 DK076117NIDDK NIH HHS R56 DK058538
6 · The paper itself

Abstract

The iodothyronine deiodinases initiate or terminate thyroid hormone action and therefore are critical for the biological effects mediated by thyroid hormone. Over the years, research has focused on their role in preserving serum levels of the biologically active molecule T(3) during iodine deficiency. More recently, a fascinating new role of these enzymes has been unveiled. The activating deiodinase (D2) and the inactivating deiodinase (D3) can locally increase or decrease thyroid hormone signaling in a tissue- and temporal-specific fashion, independent of changes in thyroid hormone serum concentrations. This mechanism is particularly relevant because deiodinase expression can be modulated by a wide variety of endogenous signaling molecules such as sonic hedgehog, nuclear factor-kappaB, growth factors, bile acids, hypoxia-inducible factor-1alpha, as well as a growing number of xenobiotic substances. In light of these findings, it seems clear that deiodinases play a much broader role than once thought, with great ramifications for the control of thyroid hormone signaling during vertebrate development and metamorphosis, as well as injury response, tissue repair, hypothalamic function, and energy homeostasis in adults.

Indexed as

AnimalsHumansIodide PeroxidaseSignal TransductionThyroid DiseasesThyroid GlandThyroxineTriiodothyronineIodide PeroxidaseThyroxineTriiodothyronine

Identifiers

PMID18815314
PMCPMC2647704
OpenAlexW2100049277

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.