Evidence map›Paper›PMID 38077981›Full record

ArticleRSC advances2023

Synthesis and evaluation of tirbanibulin derivatives: a detailed exploration of the structure-activity relationship for anticancer activity.

Jaebeom Park, Minji Kang, Ahyoung Lim, Kyung-Jin Cho, Chong Hak Chae, Byumseok Koh, Hongjun Jeon

Open access · goldAbstract read
In one paragraph

Article in RSC advances, 2023. 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
0.4field-weighted citation impact, top 40% 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, 3 citations in OpenAlex.

  1. Article
  2. 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

7 authors at 2 institutions in 1 country.

Jaebeom ParkTherapeutics & Biotechnology Division, Korea Research Institute of Chemical Technology Daejeon 34114 Republic of Korea bkoh@krict.re.kr hjeon@krict.re.kr.
Minji KangTherapeutics & Biotechnology Division, Korea Research Institute of Chemical Technology Daejeon 34114 Republic of Korea bkoh@krict.re.kr hjeon@krict.re.kr.
Ahyoung LimTherapeutics & Biotechnology Division, Korea Research Institute of Chemical Technology Daejeon 34114 Republic of Korea bkoh@krict.re.kr hjeon@krict.re.kr.
Kyung-Jin ChoTherapeutics & Biotechnology Division, Korea Research Institute of Chemical Technology Daejeon 34114 Republic of Korea bkoh@krict.re.kr hjeon@krict.re.kr.
Chong Hak ChaeTherapeutics & Biotechnology Division, Korea Research Institute of Chemical Technology Daejeon 34114 Republic of Korea bkoh@krict.re.kr hjeon@krict.re.kr.
Byumseok KohTherapeutics & Biotechnology Division, Korea Research Institute of Chemical Technology Daejeon 34114 Republic of Korea bkoh@krict.re.kr hjeon@krict.re.kr.ORCID https://orcid.org/0000-0002-1106-1891
Hongjun JeonTherapeutics & Biotechnology Division, Korea Research Institute of Chemical Technology Daejeon 34114 Republic of Korea bkoh@krict.re.kr hjeon@krict.re.kr.ORCID https://orcid.org/0000-0001-5153-5118
Korea Research Institute of Chemical Technology · KRChungbuk National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tirbanibulin, an FDA-approved microtubule-targeting agent (MTA) introduced in 2020, represents a pioneering treatment for precancerous actinic keratosis. Despite its failure to gain approval as an anticancer agent due to insufficient efficacy, there remains potential value in extending its application into malignancy treatment through tirbanibulin-based derivatives. Tirbanibulin possesses a distinctive dual mechanism of action involving microtubule and Src inhibition, distinguishing it from other MTAs. In spite of its unique profile, exploration of tirbanibulin's structure-activity relationship (SAR) and the development of its derivatives are significantly limited in the current literature. This study addresses this gap by synthesizing various tirbanibulin derivatives and exploring their SAR through modifications in the core amide motif and the eastern benzylamine part. Our results underscore the critical role of the pyridinyl acetamide core structure for optimal cellular potency, with favorable tolerance observed for modifications at the

Identifiers

PMID38077981
PMCPMC10698511
OpenAlexW4389392860

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.