Evidence map›Paper›PMID 19729063›Full record

ArticleThe Journal of steroid biochemistry and molecular biology2009

Differential effects of TR ligands on hormone dissociation rates: evidence for multiple ligand entry/exit pathways.

Suzana T Cunha Lima, Ngoc-Ha Nguyen, Marie Togashi, James W Apriletti, Phuong Nguyen, Igor Polikarpov, Thomas S Scanlan, John D Baxter, Paul Webb

Open access · greenAbstract read
In one paragraph

Article in The Journal of steroid biochemistry and molecular biology, 2009. 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
0.2field-weighted citation impact, top 37% 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, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

9 authors at 6 institutions in 2 countries.

Suzana T Cunha LimaDepartment of General Biology, Biology Institute, Federal University of Bahia, Campus of Ondina, Salvador, BA, Brazil.
Ngoc-Ha Nguyen
Marie Togashi
James W Apriletti
Phuong Nguyen
Igor Polikarpov
Thomas S Scanlan
John D Baxter
Paul Webb
University of California, San Francisco · USHouston Methodist · USOregon Health & Science University · USUniversidade de Brasília · BRUniversidade de São Paulo · BRUniversidade Federal da Bahia · BR

Funding

Thyroid Hormone ActionR01DK052798 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SCANLAN, THOMAS STERLING · 1997 to 2020
$5.7M
THYROID HORMONE RECEPTORR01DK041842 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WEBB, PAUL · 1989 to 2011
$2.8M
MUTATION ANALYSIS OF THYROID RECEPTOR FUNCTIONR01DK051281 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BAXTER, JOHN D · 1996 to 2009
$2.6M
Thyroid Hormone ActionR56DK052798 · NIDDK · OREGON HEALTH & SCIENCE UNIVERSITY · PI SCANLAN, THOMAS STERLING · 2009 to 2021
$581k
NIDDK NIH HHS DK41482NIDDK NIH HHS DK51281NIDDK NIH HHS DK52798NIDDK NIH HHS R01 DK041842NIDDK NIH HHS R01 DK051281NIDDK NIH HHS R56 DK052798
6 · The paper itself

Abstract

Some nuclear receptor (NR) ligands promote dissociation of radiolabeled bound hormone from the buried ligand binding cavity (LBC) more rapidly than excess unlabeled hormone itself. This result was interpreted to mean that challenger ligands bind allosteric sites on the LBD to induce hormone dissociation, and recent findings indicate that ligands bind weakly to multiple sites on the LBD surface. Here, we show that a large fraction of thyroid hormone receptor (TR) ligands promote rapid dissociation (T(1/2)<2h) of radiolabeled T(3) vs. T(3) (T(1/2) approximately 5-7h). We cannot discern relationships between this effect and ligand size, activity or affinity for TRbeta. One ligand, GC-24, binds the TR LBC and (weakly) to the TRbeta-LBD surface that mediates dimer/heterodimer interaction, but we cannot link this interaction to rapid T(3) dissociation. Instead, several lines of evidence suggest that the challenger ligand must interact with the buried LBC to promote rapid T(3) release. Since previous molecular dynamics simulations suggest that TR ligands leave the LBC by several routes, we propose that a subset of challenger ligands binds and stabilizes a partially unfolded intermediate state of TR that arises during T(3) release and that this effect enhances hormone dissociation.

Indexed as

DimerizationKineticsLigandsReceptors, Thyroid HormoneThyroid HormonesLigandsReceptors, Thyroid HormoneThyroid Hormones

Identifiers

PMID19729063
PMCPMC2784034
OpenAlexW2066179420

What OpenQuestion holds

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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.