Evidence map›Paper›PMID 38464469›Full record

ArticleBiomaterials research2024

Novel Estrogen Receptor Dimerization BRET-Based Biosensors for Screening Estrogenic Endocrine-Disrupting Chemicals.

Gyuho Choi, Hyunkoo Kang, Jung-Soo Suh, Haksoo Lee, Kiseok Han, Gaeun Yoo, Hyejin Jo, Yeong Min Shin, Tae-Jin Kim, BuHyun Youn

Abstract read
In one paragraph

Article in Biomaterials research, 2024. 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
–field-weighted citation impact
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.

  1. 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

10 authors.

Gyuho ChoiDepartment of Integrated Biological Science, Pusan National University, Busan 46241, Republic of Korea.
Hyunkoo KangDepartment of Integrated Biological Science, Pusan National University, Busan 46241, Republic of Korea.
Jung-Soo SuhDepartment of Integrated Biological Science, Pusan National University, Busan 46241, Republic of Korea.
Haksoo LeeDepartment of Integrated Biological Science, Pusan National University, Busan 46241, Republic of Korea.
Kiseok HanDepartment of Integrated Biological Science, Pusan National University, Busan 46241, Republic of Korea.
Gaeun YooDepartment of Integrated Biological Science, Pusan National University, Busan 46241, Republic of Korea.
Hyejin JoFood Safety Risk Assessment Division, National Institute of Food and Drug Safety Evaluation, Ministry of Food and Drug Safety, Cheongju 28159, Republic of Korea.
Yeong Min ShinFood Safety Risk Assessment Division, National Institute of Food and Drug Safety Evaluation, Ministry of Food and Drug Safety, Cheongju 28159, Republic of Korea.
Tae-Jin KimDepartment of Integrated Biological Science, Pusan National University, Busan 46241, Republic of Korea.
BuHyun YounDepartment of Integrated Biological Science, Pusan National University, Busan 46241, Republic of Korea.ORCID https://orcid.org/0000-0002-8010-519X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The increasing prevalence of endocrine-disrupting chemicals (EDCs) in our environment is a growing concern, with numerous studies highlighting their adverse effects on the human endocrine system. Among the EDCs, estrogenic endocrine-disrupting chemicals (eEDCs) are exogenous compounds that perturb estrogenic hormone function by interfering with estrogen receptor (ER) homo (α/α, β/β) or hetero (α/β) dimerization. To date, a comprehensive screening approach for eEDCs affecting all ER dimer forms in live cells is lacking. Here, we developed ER dimerization-detecting biosensors (ERDDBs), based on bioluminescence resonance energy transfer, for dimerization detection and rapid eEDC identification. To enhance the performance of these biosensors, we determined optimal donor and acceptor locations using computational analysis. Additionally, employing HaloTag as the acceptor and incorporating the P2A peptide as a linker yielded the highest sensitivity among the prototypes. We also established stable cell lines to screen potential ER dimerization inducers among estrogen analogs (EAs). The EAs were categorized through cross-comparison of ER dimer responses, utilizing EC values derived from a standard curve established with 17β-estradiol. We successfully classified 26 of 72 EAs, identifying which ER dimerization types they induce. Overall, our study underscores the effectiveness of the optimized ERDDB for detecting ER dimerization and its applicability in screening and identifying eEDCs.

Identifiers

PMID38464469
PMCPMC10923609

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.