Evidence map›Paper›PMID 40245052›Full record

ArticleJournal of the American Chemical Society2025

NMR-Based Rational Drug Design of G:G Mismatch DNA Binding Ligand Trapping Transient Complex via Disruption of a Key Allosteric Interaction.

Shuhei Sakurabayashi, Kyoko Furuita, Takeshi Yamada, Noriaki Sugiura, Makoto Nomura, Takanori Nakane, Akihiro Kawamoto, Genji Kurisu, Yohei Miyanoiri, Toshimichi Fujiwara and 2 more

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Shuhei SakurabayashiDepartment of Regulatory Bioorganic Chemistry, The Institute of Scientific and Industrial Research (SANKEN), Osaka University, 8-1 Mihogaoka, Osaka, Ibaraki 567-0047, Japan.ORCID 0000-0001-6561-2356
Kyoko FuruitaInstitute for Protein Research, Osaka University, 3-2 Yamadaoka, Osaka, Suita 565-0871, Japan.
Takeshi YamadaDepartment of Regulatory Bioorganic Chemistry, The Institute of Scientific and Industrial Research (SANKEN), Osaka University, 8-1 Mihogaoka, Osaka, Ibaraki 567-0047, Japan.ORCID 0000-0003-3275-415X
Noriaki SugiuraDepartment of Regulatory Bioorganic Chemistry, The Institute of Scientific and Industrial Research (SANKEN), Osaka University, 8-1 Mihogaoka, Osaka, Ibaraki 567-0047, Japan.
Makoto NomuraGraduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.
Takanori NakaneInstitute for Protein Research, Osaka University, 3-2 Yamadaoka, Osaka, Suita 565-0871, Japan.
Akihiro KawamotoInstitute for Protein Research, Osaka University, 3-2 Yamadaoka, Osaka, Suita 565-0871, Japan.
Genji KurisuInstitute for Protein Research, Osaka University, 3-2 Yamadaoka, Osaka, Suita 565-0871, Japan.
Yohei MiyanoiriInstitute for Protein Research, Osaka University, 3-2 Yamadaoka, Osaka, Suita 565-0871, Japan.ORCID 0000-0001-6889-5160
Toshimichi FujiwaraInstitute for Protein Research, Osaka University, 3-2 Yamadaoka, Osaka, Suita 565-0871, Japan.ORCID 0000-0001-7739-3525
Kazuhiko NakataniDepartment of Regulatory Bioorganic Chemistry, The Institute of Scientific and Industrial Research (SANKEN), Osaka University, 8-1 Mihogaoka, Osaka, Ibaraki 567-0047, Japan.ORCID 0000-0002-1705-5265
Chojiro KojimaInstitute for Protein Research, Osaka University, 3-2 Yamadaoka, Osaka, Suita 565-0871, Japan.ORCID 0000-0003-2723-8249

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small molecules that bind to mismatched DNA have been applied in various fields, including nanotechnology, bioimaging, and therapeutics. However, the intrinsic dynamic nature of mismatched DNA complicates the prediction of structural changes upon ligand binding, hindering rational ligand design. In this study, NMR was used for structure-based drug design, with a focus on the G:G mismatch binder

Indexed as

Base Pair MismatchDNADrug DesignAllosteric SiteKineticsLigandsNuclear Magnetic Resonance, BiomolecularThermodynamicsDNALigands

Identifiers

PMID40245052
PMCPMC12046557

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Registered trials

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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.