Evidence map›Paper›PMID 36479973›Full record

ArticleeLife2022

Human Dectin-1 is

Shojiro Haji, Taiki Ito, Carla Guenther, Miyako Nakano, Takashi Shimizu, Daiki Mori, Yasunori Chiba, Masato Tanaka, Sushil K Mishra, Janet A Willment and 3 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. Review
  3. Secondary Sites of the C-type Lectin-Like Fold.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024
    Review
  4. Review
  5. 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

13 authors at 7 institutions in 3 countries.

Shojiro HajiDepartment of Molecular Immunology, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.ORCID 0000-0003-3651-2836
Taiki ItoDepartment of Molecular Immunology, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.ORCID 0000-0002-1408-7288
Carla GuentherDepartment of Molecular Immunology, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.ORCID 0000-0001-7915-1028
Miyako NakanoGraduate School of Integrated Sciences for Life, Hiroshima University, Hiroshima, Japan.
Takashi ShimizuDepartment of Molecular Immunology, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.
Daiki MoriDepartment of Molecular Immunology, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.
Yasunori ChibaCellular and Molecular Biotechnology Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Japan.
Masato TanakaLaboratory of Immune Regulation School of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Japan.
Sushil K MishraThe Glycoscience Group, National University of Ireland, Galway, Galway, Ireland.ORCID 0000-0002-3080-9754
Janet A WillmentMedical Research Council Centre for Medical Mycology, University of Exeter, Exeter, United Kingdom.ORCID 0000-0002-7040-0857
Gordon D BrownMedical Research Council Centre for Medical Mycology, University of Exeter, Exeter, United Kingdom.
Masamichi NagaeDepartment of Molecular Immunology, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.ORCID 0000-0002-5470-3807
Sho YamasakiDepartment of Molecular Immunology, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.ORCID 0000-0002-5184-6917
The University of Osaka · JPUniversity of Exeter · GBHiroshima University · JPKyushu University · JPNational Institute of Advanced Industrial Science and Technology · JPOllscoil na Gaillimhe – University of Galway · IETokyo University of Pharmacy and Life Sciences · JP

Funding

Tracking Glycosylation State with Fluorinated Glycosides ProbesP20GM130460 · NIGMS · UNIVERSITY OF MISSISSIPPI · PI Joshua S Sharp · 2020 to 2026
$17.9M
Medical Research Council MR/N006364/1Medical Research Council MR/N006364/2Medical Research Council MR/V033417/1Wellcome Trust 102705/Z/13/Z
6 · The paper itself

Abstract

C-type lectin receptors (CLRs) elicit immune responses upon recognition of glycoconjugates present on pathogens and self-components. While Dectin-1 is the best-characterized CLR recognizing β-glucan on pathogens, the endogenous targets of Dectin-1 are not fully understood. Herein, we report that human Dectin-1 is a ligand for CLEC-2, another CLR expressed on platelets. Biochemical analyses revealed that Dectin-1 is a mucin-like protein as its stalk region is highly

Indexed as

Blood PlateletsLectins, C-TypeAnimalsDectin-1GlycosylationHumansLigandsMiceCLEC-2 protein, mouseDectin-1Lectins, C-TypeLigandsC-type lectin receptorglycosylationhumanimmunologyinflammationmousepattern recognition receptorplatelet

Identifiers

PMID36479973
PMCPMC9788829
OpenAlexW4310937810

What OpenQuestion holds

Textmetadata
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.