Evidence map›Paper›PMID 32424043›Full record

ArticleThe Journal of biological chemistry2020

Molecular mechanism of the recognition of bacterially cleaved immunoglobulin by the immune regulatory receptor LILRA2.

Rika Yamazaki, Atsushi Furukawa, Kouyuki Hirayasu, Kohei Yumoto, Hideo Fukuhara, Hisashi Arase, Katsumi Maenaka

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.3field-weighted citation impact, top 14% 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

9 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. LILRB4, an immune checkpoint on myeloid cells.Blood science (Baltimore, Md.) · 2022
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. 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

7 authors at 3 institutions in 1 country.

Rika YamazakiLaboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.ORCID 0000-0002-9550-0758
Atsushi FurukawaLaboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan maenaka@pharm.hokudai.ac.jp afuru@pharm.hokudai.ac.jp.ORCID 0000-0003-1281-2252
Kouyuki HirayasuWPI Immunology Frontier Research Center, Osaka University, Suita, Osaka, Japan.
Kohei YumotoLaboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Hideo FukuharaCenter for Research and Education on Drug Discovery, Hokkaido University, Sapporo, Japan.
Hisashi AraseWPI Immunology Frontier Research Center, Osaka University, Suita, Osaka, Japan.
Katsumi MaenakaLaboratory of Biomolecular Science, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan maenaka@pharm.hokudai.ac.jp afuru@pharm.hokudai.ac.jp.ORCID 0000-0002-5459-521X
Hokkaido University · JPKanazawa University · JPThe University of Osaka · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human leukocyte immunoglobulin-like receptors (LILRs) typically regulate immune activation by binding to the human leukocyte antigen class I molecules. LILRA2, a member of the LILR family, was recently reported to bind to other unique ligands, the bacterially degraded Igs (N-truncated Igs), for the activation of immune cells. Therefore, LILRA2 is currently attracting significant attention as a novel innate immune receptor. However, the detailed recognition mechanisms required for this interaction remain unclear. In this study, using several biophysical techniques, we uncovered the molecular mechanism of N-truncated Ig recognition by LILRA2. Surface plasmon resonance analysis disclosed that LILRA2 specifically binds to N-truncated Ig with weak affinity (

Indexed as

BacteriaHumansImmunoglobulin Fab FragmentsMicroscopy, Atomic ForceReceptors, ImmunologicSurface Plasmon ResonanceImmunoglobulin Fab FragmentsLILRA2 protein, humanReceptors, Immunologicatomic force microscopy (AFM)bacterially cleaved immunoglobulincell surface receptorimmune regulationimmune regulatory receptorimmunoglobulin G (IgG)immunologyleukocyte immunoglobulin-like receptor (LILR)LILRA2protein-protein interactionsurface plasmon resonance (SPR)

Identifiers

PMID32424043
PMCPMC7363141
OpenAlexW3026328925

What OpenQuestion holds

Textmetadata
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.