Evidence map›Paper›PMID 41997963›Full record

ArticleNature communications2026

Structural Mechanism of Receptor-Triggered MyD88 Oligomeric Assembly in Innate Immune Signaling.

Kazuki Kasai, Kayo Imamura, Masatoshi Uno, Shiho Nukui, Naotaka Sekiyama, Tomoko Miyata, Fumiaki Makino, Ryusei Yamada, Yoshiki Takahashi, Noriyuki Kodera and 5 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2026. 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
–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

2 citing papers in PubMed.

  1. Review
  2. 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

15 authors.

Kazuki KasaiDepartment of Biophysics, Graduate School of Science, Kyoto University, Kitashirakawa Oiwake-cho, Sakyo-ku, Kyoto, Japan.ORCID http://orcid.org/0000-0002-1803-4036
Kayo ImamuraDepartment of Biophysics, Graduate School of Science, Kyoto University, Kitashirakawa Oiwake-cho, Sakyo-ku, Kyoto, Japan.
Masatoshi UnoDepartment of Biophysics, Graduate School of Science, Kyoto University, Kitashirakawa Oiwake-cho, Sakyo-ku, Kyoto, Japan.
Shiho NukuiDepartment of Biophysics, Graduate School of Science, Kyoto University, Kitashirakawa Oiwake-cho, Sakyo-ku, Kyoto, Japan.
Naotaka SekiyamaDepartment of Biophysics, Graduate School of Science, Kyoto University, Kitashirakawa Oiwake-cho, Sakyo-ku, Kyoto, Japan.ORCID http://orcid.org/0000-0003-4537-6565
Tomoko MiyataGraduate School of Frontier Biosciences, The University of Osaka, 1-3 Yamadaoka, Suita, Osaka, Japan.
Fumiaki MakinoGraduate School of Frontier Biosciences, The University of Osaka, 1-3 Yamadaoka, Suita, Osaka, Japan.
Ryusei YamadaGraduate School of Natural Science and Technology, Kanazawa University, Kakuma-cho, Kanazawa, Ishikawa, Japan.
Yoshiki TakahashiGraduate School of Natural Science and Technology, Kanazawa University, Kakuma-cho, Kanazawa, Ishikawa, Japan.
Noriyuki KoderaWPI Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-cho, Kanazawa, Ishikawa, Japan.ORCID http://orcid.org/0000-0003-4880-8423
Keiichi NambaGraduate School of Frontier Biosciences, The University of Osaka, 1-3 Yamadaoka, Suita, Osaka, Japan.ORCID http://orcid.org/0000-0003-2911-5875
Hidenori OhnishiDepartment of Pediatrics, Graduate School of Medicine, Gifu University, 1-1 Yanagido, Gifu, Japan.
Akihiro NaritaDepartment of Biological Science, Graduate School of Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, Japan.ORCID http://orcid.org/0000-0003-1504-9352
Hiroki KonnoGraduate School of Natural Science and Technology, Kanazawa University, Kakuma-cho, Kanazawa, Ishikawa, Japan.
Hidehito TochioDepartment of Biophysics, Graduate School of Science, Kyoto University, Kitashirakawa Oiwake-cho, Sakyo-ku, Kyoto, Japan. tochio@mb.biophys.kyoto-u.ac.jp.ORCID http://orcid.org/0000-0003-3843-3330

Funding

MEXT | Japan Science and Technology Agency (JST) JPMJCR1762MEXT | Japan Science and Technology Agency (JST) JPMJCR23I5MEXT | Japan Society for the Promotion of Science (JSPS) 23H02421
6 · The paper itself

Abstract

MyD88 plays a pivotal role in Toll-like receptor (TLR) and interleukin-1 family signaling through its oligomerization upon receptor activation, leading to downstream protein recruitment. The Toll/interleukin-1 receptor domain of MyD88 (TIR

Indexed as

Immunity, InnateMyeloid Differentiation Factor 88Receptors, Interleukin-1Signal TransductionAnimalsCryoelectron MicroscopyHumansMicroscopy, Atomic ForceProtein BindingProtein MultimerizationToll-Like ReceptorsMYD88 protein, humanMyeloid Differentiation Factor 88Receptors, Interleukin-1Toll-Like Receptors

Identifiers

PMID41997963
PMCPMC13276377

What OpenQuestion holds

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LicenceCC BY
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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.