Evidence map›Paper›PMID 39268708›Full record

ArticleActa crystallographica. Section D, Structural biology2024

Microcrystal electron diffraction structure of Toll-like receptor 2 TIR-domain-nucleated MyD88 TIR-domain higher-order assembly.

Y Li, L C Pacoste, W Gu, S J Thygesen, K J Stacey, T Ve, B Kobe, H Xu, J D Nanson

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Review
  3. Structural basis for TIR domain-mediated innate immune signaling by Toll-like receptor adaptors TRIF and TRAM.Proceedings of the National Academy of Sciences of the United States of America · 2025
    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

9 authors.

Y LiInstitute of Molecular Bioscience, The University of Queensland, Brisbane, Queensland 4072, Australia.ORCID 0000-0001-8317-824X
L C PacosteDepartment of Materials and Environmental Chemistry, Stockholm University, Frescativägen 8, 114 18 Stockholm, Sweden.ORCID 0009-0005-6090-8736
W GuSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland 4072, Australia.ORCID 0000-0002-1185-3557
S J ThygesenSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland 4072, Australia.ORCID 0000-0002-7512-4097
K J StaceySchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland 4072, Australia.ORCID 0000-0002-3992-7802
T VeInstitute for Glycomics, Griffith University, Southport, Queensland 4215, Australia.ORCID 0000-0002-0113-1905
B KobeSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland 4072, Australia.ORCID 0000-0001-9413-9166
H XuDepartment of Materials and Environmental Chemistry, Stockholm University, Frescativägen 8, 114 18 Stockholm, Sweden.ORCID 0000-0002-8271-3906
J D NansonSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland 4072, Australia.ORCID 0000-0003-1306-1948

Funding

Australian Research Council FL180100109Australian Research Council FL200100572Knut och Alice Wallenbergs Stiftelse 2018.0237National Health and Medical Research Council 1107804National Health and Medical Research Council 1160570National Health and Medical Research Council 1196590National Health and Medical Research Council 2025931Vetenskapsrådet 2019-00815
6 · The paper itself

Abstract

Eukaryotic TIR (Toll/interleukin-1 receptor protein) domains signal via TIR-TIR interactions, either by self-association or by interaction with other TIR domains. In mammals, TIR domains are found in Toll-like receptors (TLRs) and cytoplasmic adaptor proteins involved in pro-inflammatory signaling. Previous work revealed that the MAL TIR domain (MAL

Indexed as

Myeloid Differentiation Factor 88Toll-Like Receptor 2Crystallography, X-RayHumansModels, MolecularProtein DomainsProtein MultimerizationReceptors, Interleukin-1Toll-Like Receptor 1Toll-Like Receptor 6MYD88 protein, humanMyeloid Differentiation Factor 88Receptors, Interleukin-1TLR1 protein, humanTLR2 protein, humanToll-Like Receptor 1Toll-Like Receptor 2Toll-Like Receptor 6higher-order assembliesMicroEDMyD88signalosomesTIR domainsToll/interleukin-1 receptor proteinToll-like receptors

Identifiers

PMID39268708
PMCPMC11394124

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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.