Evidence map›Paper›PMID 33335727›Full record

ArticleBiomedical reports2021

TLR4/MD-2 is a receptor for extracellular nucleophosmin 1.

Kota Nakatomi, Hikari Ueno, Yuto Ishikawa, Ronny Christiadi Salim, Yuki Mori, Issey Kanemoto, Salunya Tancharoen, Kiyoshi Kikuchi, Naoki Miura, Taketo Omori and 6 more

Open access · diamondAbstract read
In one paragraph

Article in Biomedical reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.3field-weighted citation impact, top 42% 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

8 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Review
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  4. Salvimulticanol from3 Biotech · 2024
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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

16 authors at 4 institutions in 2 countries.

Kota NakatomiDepartment of Biomedical Engineering, Osaka Institute of Technology, Osaka 535-8585, Japan.
Hikari UenoDepartment of Biomedical Engineering, Osaka Institute of Technology, Osaka 535-8585, Japan.
Yuto IshikawaDepartment of Biomedical Engineering, Osaka Institute of Technology, Osaka 535-8585, Japan.
Ronny Christiadi SalimDepartment of Biomedical Engineering, Osaka Institute of Technology, Osaka 535-8585, Japan.
Yuki MoriDepartment of Biomedical Engineering, Osaka Institute of Technology, Osaka 535-8585, Japan.
Issey KanemotoDepartment of Biomedical Engineering, Osaka Institute of Technology, Osaka 535-8585, Japan.
Salunya TancharoenDepartment of Biomedical Engineering, Osaka Institute of Technology, Osaka 535-8585, Japan.
Kiyoshi KikuchiDepartment of Pharmacology, Faculty of Dentistry, Mahidol University, Bangkok 10400, Thailand.
Naoki MiuraVeterinary Teaching Hospital, Joint Faculty of Veterinary Medicine, Kagoshima University, Kagoshima 890-8580, Japan.
Taketo OmoriDepartment of Biomedical Engineering, Osaka Institute of Technology, Osaka 535-8585, Japan.
Emiko Okuda-AshitakaDepartment of Biomedical Engineering, Osaka Institute of Technology, Osaka 535-8585, Japan.
Kiyoshi MatsumuraDepartment of Biomedical Engineering, Osaka Institute of Technology, Osaka 535-8585, Japan.
Hitoshi ImaizumiDepartment of Anesthesiology and Intensive Care Medicine, Tokyo Medical University, School of Medicine, Tokyo 160-0023, Japan.
Yoshihiro MotomiyaSuiyukai Clinic, Kashihara, Nara 634-0007, Japan.
Ikuro MaruyamaDepartment of Biomedical Engineering, Osaka Institute of Technology, Osaka 535-8585, Japan.
Ko-Ichi KawaharaDepartment of Biomedical Engineering, Osaka Institute of Technology, Osaka 535-8585, Japan.
Osaka Institute of Technology · JPKagoshima University · JPMahidol University · THTokyo Medical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nucleophosmin 1 (NPM1) primarily localizes to the nucleus and is passively released into the extracellular milieu by necrotic or damaged cells, or is secreted by monocytes and macrophages. Extracellular NPM1 acts as a potent inflammatory stimulator by promoting cytokine production [e.g., tumor necrosis factor-α (TNF-α)], which suggests that NPM1 acts as a damage-associated molecular pattern. However, the receptor of NPM1 is unknown. Evidence indicates that DAMPs, which include high mobility group box 1 and histones, may bind Toll-like receptors (TLRs). In the present study, it was shown that NPM1 signaling was mediated via the TLR4 pathway, which suggests that TLR4 is an NPM1 receptor. TLR4 binds myeloid differentiation protein-2 (MD-2), which is essential for intracellular signaling. Furthermore, the TLR4 antagonist, LPS-

Indexed as

damage-associated molecular patternsmyeloid differentiation protein-2nucleophosmin 1sepsisToll-like receptor 4

Identifiers

PMID33335727
PMCPMC7739869
OpenAlexW3108239808

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.