Evidence map›Paper›PMID 41152269›Full record

ArticleNature communications2025

Structural and dynamic insights into the biased signaling mechanism of the human kappa opioid receptor.

Chiyo Suno-Ikeda, Ryo Nishikawa, Riko Suzuki, Shun Yokoi, Seiya Iwata, Tomoyo Takai, Takaya Ogura, Mika Hirose, Akihisa Tokuda, Risako Katamoto and 13 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Opioid Signaling in Multiple Sclerosis: Emerging Targets for Repair.International journal of molecular sciences · 2026
    Review
  3. Article
  4. 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

23 authors.

Chiyo Suno-Ikeda *Department of Medical Chemistry, Kansai Medical University, Hirakata, Japan.
Ryo Nishikawa *Department of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Nagoya, Japan.
Riko Suzuki *Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan.ORCID http://orcid.org/0000-0002-9465-3832
Shun YokoiDepartment of Physics, School of Science and Technology, Meiji University, Kawasaki, Kanagawa, Japan.ORCID http://orcid.org/0000-0003-2684-3420
Seiya IwataDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Nagoya, Japan.
Tomoyo TakaiDepartment of Medical Chemistry, Kansai Medical University, Hirakata, Japan.
Takaya OguraGraduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Miyagi, Japan.
Mika HiroseInstitute for Protein Research, Osaka University, Suita, Japan.
Akihisa TokudaInternational Institute for Integrative Sleep Medicine (WPI-IIIS), Tsukuba Institute for Advanced Research (TIAR), University of Tsukuba, Tsukuba, Ibaraki, Japan.
Risako KatamotoInternational Institute for Integrative Sleep Medicine (WPI-IIIS), Tsukuba Institute for Advanced Research (TIAR), University of Tsukuba, Tsukuba, Ibaraki, Japan.
Akitoshi InoueDepartment of Medical Chemistry, Kansai Medical University, Hirakata, Japan.
Eri AsaiDepartment of Medical Chemistry, Kansai Medical University, Hirakata, Japan.
Ryoji KiseGraduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan.ORCID http://orcid.org/0009-0000-6583-1719
Yukihiko SugitaHakubi Center for Advanced Research, Kyoto University, Kyoto, Japan.ORCID http://orcid.org/0000-0001-6861-4840
Takayuki KatoInstitute for Protein Research, Osaka University, Suita, Japan.ORCID http://orcid.org/0000-0002-8879-6685
Hiroshi NagaseInternational Institute for Integrative Sleep Medicine (WPI-IIIS), Tsukuba Institute for Advanced Research (TIAR), University of Tsukuba, Tsukuba, Ibaraki, Japan.ORCID http://orcid.org/0000-0003-0428-3979
Ayori MitsutakeDepartment of Physics, School of Science and Technology, Meiji University, Kawasaki, Kanagawa, Japan.ORCID http://orcid.org/0000-0002-4194-7255
Tsuyoshi SaitohInternational Institute for Integrative Sleep Medicine (WPI-IIIS), Tsukuba Institute for Advanced Research (TIAR), University of Tsukuba, Tsukuba, Ibaraki, Japan.ORCID http://orcid.org/0000-0001-6105-6292
Kota KatayamaDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Nagoya, Japan.ORCID http://orcid.org/0000-0001-8498-4374
Asuka InoueGraduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Japan.ORCID http://orcid.org/0000-0003-0805-4049
Hideki KandoriDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Nagoya, Japan.ORCID http://orcid.org/0000-0002-4922-1344
Takuya KobayashiDepartment of Medical Chemistry, Kansai Medical University, Hirakata, Japan. kobayatk@hirakata.kmu.ac.jp.ORCID http://orcid.org/0000-0001-6270-1353
Ryoji SunoDepartment of Medical Chemistry, Kansai Medical University, Hirakata, Japan. suno.ryo@kmu.ac.jp.ORCID http://orcid.org/0000-0003-2378-236X

Funding

MEXT | Japan Society for the Promotion of Science (JSPS) 19H03428MEXT | Japan Society for the Promotion of Science (JSPS) 21H05111MEXT | Japan Society for the Promotion of Science (JSPS) 24K02231
6 · The paper itself

Abstract

The κ-opioid receptor (KOR) is a member of the G protein-coupled receptor (GPCR) family, modulating cellular responses through transducers such as G proteins and β-arrestins. G-protein-biased KOR agonists aim to retain analgesic and antipruritic actions while limiting aversion and sedation. Aiming to inform G-biased KOR agonist design, we analyze signaling-relevant residues from structural and dynamic views. Here we show, using multiple complementary methods, shared residues that determine β-arrestin recruitment by nalfurafine and U-50,488H. Cryo-electron microscopy structures of the KOR-G

Indexed as

Analgesics, Non-NarcoticAntipruriticsbeta-ArrestinsReceptors, Opioid, kappa3,4-Dichloro-N-methyl-N-(2-(1-pyrrolidinyl)-cyclohexyl)-benzeneacetamide, (trans)-IsomerAmino Acid SequenceAnimalsBinding SitesCryoelectron MicroscopyDrug DesignGTP-Binding Protein alpha Subunits, Gi-GoHEK293 CellsHumansMolecular Dynamics SimulationMorphinansProtein Binding3,4-Dichloro-N-methyl-N-(2-(1-pyrrolidinyl)-cyclohexyl)-benzeneacetamide, (trans)-IsomerAnalgesics, Non-NarcoticAntipruriticsbeta-ArrestinsGTP-Binding Protein alpha Subunits, Gi-GoMorphinansReceptors, Opioid, kappaRecombinant ProteinsSpiro CompoundsTRK 820

Identifiers

PMID41152269
PMCPMC12569041

What OpenQuestion holds

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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 OpenQuestion graph.