Evidence map›Paper›PMID 33964321›Full record

ReviewMolecular and cellular endocrinology2021

Cryo-EM: A new dawn in thyroid biology.

Francesca Coscia, Ajda Taler-Verčič

Open access · hybridAbstract readReview
In one paragraph

Review in Molecular and cellular endocrinology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Impact of Therapeutic Ultrasound on Metabolic Hormone Release From Thyroid Gland.Journal of ultrasound in medicine : official journal of the American Institute of Ultrasound in Medicine · 2026
    Article
  2. Article
  3. Review
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 2 institutions in 3 countries.

Francesca CosciaMRC Laboratory of Molecular Biology, Cambridge, CB2 0QH, UK; Human Technopole, Via Cristina Belgioioso 171, 20157, Milano, Italy. Electronic address: fcoscia@mrc-lmb.cam.ac.uk.
Ajda Taler-VerčičUniversity of Ljubljana, Faculty of Medicine, Institute of Biochemistry and Molecular Genetics, Vrazov Trg 2, 1000, Ljubljana, Slovenia.
MRC Laboratory of Molecular Biology · GBUniversity of Ljubljana · SI

Funding

Medical Research Council MC_U105184326Medical Research Council U105184326Wellcome Trust 202754/Z/16/ZWellcome Trust 203149
6 · The paper itself

Abstract

The thyroid gland accumulates the rare dietary element iodine and incorporates it into iodinated thyroid hormones, utilising several tightly regulated reactions and molecular mechanisms. Thyroid hormones are essential in vertebrates and play a central role in many biological processes, such as development, thermogenesis and growth. The control of these functions is exerted through the binding of hormones to nuclear thyroid hormone receptors that rule the transcription of numerous metabolic genes. Over the last 50 years, thyroid biology has been studied extensively at the cellular and organismal levels, revealing its multiple clinical implications, yet, a complete molecular understanding is still lacking. This includes the atomic structures of crucial pathway components that would be needed to elucidate molecular mechanisms. Here we review the currently known protein structures involved in thyroid hormone synthesis, regulation, transport, and actions. We also highlight targets for future investigations that will significantly benefit from recent advances in macromolecular structure determination by electron cryo-microscopy (cryo-EM). As an example, we demonstrate how cryo-EM was crucial to obtain the structure of the large thyroid hormone precursor protein, thyroglobulin. We discuss modern cryo-EM compared to other structure determination methods and how an integrated structural and cell biological approach will help filling the molecular knowledge gap in our understanding of thyroid hormone metabolism. Together with clinical, cellular and high-throughput 'omics' studies, atomic structures of thyroid components will provide an important framework to map disease mutations and to interpret and predict thyroid phenotypes.

Indexed as

Cryoelectron MicroscopyCrystallography, X-RayHumansProtein ConformationThyroglobulinThyroid GlandTG protein, humanThyroglobulinCryo-EMElectron microscopyIodineStructural biologyThyroglobulinThyroid hormones

Identifiers

PMID33964321
PMCPMC8316605
OpenAlexW3159509032

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.