Evidence map›Paper›PMID 30287791›Full record

ArticleInternational journal of molecular sciences2018

Identification of a Novel PPAR-γ Agonist through a Scaffold Tuning Approach.

Hyo Jin Gim, Yong-Sung Choi, Hua Li, Yoon-Jung Kim, Jae-Ha Ryu, Raok Jeon

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed, 1 pooled it
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

10 citing papers in PubMed, 1 synthesis or guideline pooled it, 17 citations in OpenAlex.

  1. Pooled it
  2. Design,ACS omega · 2026
    Article
  3. Article
  4. PreliminaryLife (Basel, Switzerland) · 2026
    Article
  5. Evaluation of 3',4'-Di-Biomolecules · 2026
    Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. 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

6 authors at 1 institution in 1 country.

Hyo Jin GimResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Sookmyung Women's University, Cheongpa-ro 47-gil 100, Yongsan-gu, Seoul 04310, Korea. hjgim83@gmail.com.
Yong-Sung ChoiResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Sookmyung Women's University, Cheongpa-ro 47-gil 100, Yongsan-gu, Seoul 04310, Korea. uriys2@gmail.com.
Hua LiResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Sookmyung Women's University, Cheongpa-ro 47-gil 100, Yongsan-gu, Seoul 04310, Korea. cooldog227@hotmail.com.
Yoon-Jung KimResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Sookmyung Women's University, Cheongpa-ro 47-gil 100, Yongsan-gu, Seoul 04310, Korea. yoonjungkim73@gmail.com.
Jae-Ha RyuResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Sookmyung Women's University, Cheongpa-ro 47-gil 100, Yongsan-gu, Seoul 04310, Korea. ryuha@sookmyung.ac.kr.
Raok JeonResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Sookmyung Women's University, Cheongpa-ro 47-gil 100, Yongsan-gu, Seoul 04310, Korea. rjeon@sookmyung.ac.kr.
Sookmyung Women's University · KR

Funding

National Research Foundation of Korea (NRF) 2014R1A2A1A11052761National Research Foundation of Korea (NRF) No. 2011-0030074National Research Foundation of Korea (NRF) NRF-2016R1A6A3A11932164National Research Foundation of Korea (NRF) NRF-2017R1A6A3A11034603
6 · The paper itself

Abstract

Peroxisome proliferator-activated receptors (PPARs) are important targets in metabolic diseases including obesity, metabolic syndrome, diabetes, and non-alcoholic fatty liver disease. Recently, they have been highlighted as attractive targets for the treatment of cardiovascular diseases and chronic myeloid leukemia. The PPAR agonist structure is consists of a polar head, a hydrophobic tail, and a linker. Each part interacts with PPARs through hydrogen bonds or hydrophobic interactions to stabilize target protein conformation, thus increasing its activity. Acidic head is essential for PPAR agonist activity. The aromatic linker plays an important role in making hydrophobic interactions with PPAR as well as adjusting the head-to-tail distance and conformation of the whole molecule. By tuning the scaffold of compound, the whole molecule could fit into the ligand-binding domain to achieve proper binding mode. We modified indol-3-ylacetic acid scaffold to (indol-1-ylmethyl)benzoic acid, whereas 2,4-dichloroanilide was fixed as the hydrophobic tail. We designed, synthesized, and assayed the in vitro activity of novel indole compounds with (indol-1-ylmethyl)benzoic acid scaffold. Compound

Indexed as

Quantitative Structure-Activity RelationshipAnimalsBenzoatesCell LineChlorocebus aethiopsIndolesMolecular Docking SimulationPPAR gammaProtein BindingBenzoatesIndolesPPAR gammaagonistindolePPARscaffoldtuning

Identifiers

PMID30287791
PMCPMC6213020
OpenAlexW2894986372

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.