Evidence map›Paper›PMID 35280700›Full record

ArticleNuclear receptor research2020

Mislocalization of Cancer-associated Thyroid Hormone Receptor Mutants.

Michael S Salomon, S Harshini Malapati, Jerry O' Dwyer, Carolina Lopez Silva, Cheyenne C Williams, Michelle C Barbeau, Delbert Yip, Paige Punzalan, Veronica L Nagle, Shantá D Hinton and 2 more

Open access · greenAbstract read
In one paragraph

Article in Nuclear receptor research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.1field-weighted citation impact, top 52% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. 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

12 authors at 1 institution in 1 country.

Michael S SalomonDepartment of Biology, William & Mary, 540 Landrum Drive, ISC 3035, Williamsburg, VA, 23185, USA.
S Harshini MalapatiDepartment of Biology, William & Mary, 540 Landrum Drive, ISC 3035, Williamsburg, VA, 23185, USA.
Jerry O' DwyerDepartment of Biology, William & Mary, 540 Landrum Drive, ISC 3035, Williamsburg, VA, 23185, USA.
Carolina Lopez SilvaDepartment of Biology, William & Mary, 540 Landrum Drive, ISC 3035, Williamsburg, VA, 23185, USA.
Cheyenne C WilliamsDepartment of Biology, William & Mary, 540 Landrum Drive, ISC 3035, Williamsburg, VA, 23185, USA.
Michelle C BarbeauDepartment of Biology, William & Mary, 540 Landrum Drive, ISC 3035, Williamsburg, VA, 23185, USA.
Delbert YipDepartment of Biology, William & Mary, 540 Landrum Drive, ISC 3035, Williamsburg, VA, 23185, USA.
Paige PunzalanDepartment of Biology, William & Mary, 540 Landrum Drive, ISC 3035, Williamsburg, VA, 23185, USA.
Veronica L NagleDepartment of Biology, William & Mary, 540 Landrum Drive, ISC 3035, Williamsburg, VA, 23185, USA.
Shantá D HintonDepartment of Biology, William & Mary, 540 Landrum Drive, ISC 3035, Williamsburg, VA, 23185, USA.
Vincent R RoggeroDepartment of Biology, William & Mary, 540 Landrum Drive, ISC 3035, Williamsburg, VA, 23185, USA.
Lizabeth A AllisonDepartment of Biology, William & Mary, 540 Landrum Drive, ISC 3035, Williamsburg, VA, 23185, USA.
William & Mary · US

Funding

Thyroid Hormone Receptor Mislocalization and PathogenesisR15DK058028 · NIDDK · COLLEGE OF WILLIAM AND MARY · PI ALLISON, LIZABETH A · 2001 to 2022
$1.9M
NIDDK NIH HHS R15 DK058028
6 · The paper itself

Abstract

The thyroid hormone receptor (TR) is essential for the proper regulation of metabolism and development, as it regulates gene expression in response to thyroid hormone. Nuclear localization signals (NLSs) and nuclear export signals (NESs) allow for TR transport into and out of the nucleus, respectively. Previous research suggests that nuclear import, nuclear retention, and nuclear export of TR are associated with modulation of gene expression, the alteration of which can contribute to various diseases. Here, we examined the impact of cancer-associated mutations on TR localization patterns as a way of analyzing key structural components of TR and to further explore the correlation between TR trafficking, misfolding, and disease. Through mammalian cell transfection of expression plasmids for green fluorescent protein (GFP) and mCherry-tagged TRα1 and quantitative fluorescence microscopy, we examined particular groups of TRα1 mutations that were observed in patients with hepatocellular carcinoma, renal cell carcinoma, and thyroid cancer, and are associated with NLSs and NESs of TRα1. We also investigated structural alterations of the mutants by

Indexed as

aggresomecancernuclear exportnuclear importThyroid hormone receptor α

Identifiers

PMID35280700
PMCPMC8909557
OpenAlexW4287944374

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.