Evidence map›Paper›PMID 30833330›Full record

ArticleThe Journal of biological chemistry2019

Receptor-destroying enzyme (RDE) from

Tatsuya Yamazaki, Masanori Inui, Keiko Hiemori, Susumu Tomono, Makoto Itoh, Isao Ichimonji, Akina Nakashima, Hidekazu Takagi, Mrityunjoy Biswas, Kumi Izawa and 5 more

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2019. 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
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

3 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. Article
  3. 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

15 authors at 4 institutions in 2 countries.

Tatsuya YamazakiFrom the Department of Microbiology and Immunology, Aichi Medical University School of Medicine, 1-1 Yazakokarimata, Nagakute, Aichi 480-1195.
Masanori InuiFrom the Department of Microbiology and Immunology, Aichi Medical University School of Medicine, 1-1 Yazakokarimata, Nagakute, Aichi 480-1195.
Keiko Hiemorithe Biotechnology Research Institute for Drug Discovery, National Institute of Advanced Industrial Science and Technology, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568.
Susumu TomonoFrom the Department of Microbiology and Immunology, Aichi Medical University School of Medicine, 1-1 Yazakokarimata, Nagakute, Aichi 480-1195.
Makoto ItohFrom the Department of Microbiology and Immunology, Aichi Medical University School of Medicine, 1-1 Yazakokarimata, Nagakute, Aichi 480-1195.
Isao IchimonjiFrom the Department of Microbiology and Immunology, Aichi Medical University School of Medicine, 1-1 Yazakokarimata, Nagakute, Aichi 480-1195.
Akina NakashimaFrom the Department of Microbiology and Immunology, Aichi Medical University School of Medicine, 1-1 Yazakokarimata, Nagakute, Aichi 480-1195.
Hidekazu TakagiFrom the Department of Microbiology and Immunology, Aichi Medical University School of Medicine, 1-1 Yazakokarimata, Nagakute, Aichi 480-1195.
Mrityunjoy BiswasFrom the Department of Microbiology and Immunology, Aichi Medical University School of Medicine, 1-1 Yazakokarimata, Nagakute, Aichi 480-1195.
Kumi Izawathe Atopy Research Center, Juntendo University Graduate School of Medicine, 2-1-1 Hongo, Bunkyo-ku, Tokyo 113-8421.
Jiro Kitaurathe Atopy Research Center, Juntendo University Graduate School of Medicine, 2-1-1 Hongo, Bunkyo-ku, Tokyo 113-8421.
Teruko Imaithe Graduate School of Pharmaceutical Sciences, Kumamoto University, 5-1 Oe-Honmachi, Kumamoto 862-0973, and.
Nobuo SugiuraFrom the Department of Microbiology and Immunology, Aichi Medical University School of Medicine, 1-1 Yazakokarimata, Nagakute, Aichi 480-1195.
Hiroaki Tatenothe Biotechnology Research Institute for Drug Discovery, National Institute of Advanced Industrial Science and Technology, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568.ORCID 0000-0003-3006-1659
Sachiko Akashi-TakamuraFrom the Department of Microbiology and Immunology, Aichi Medical University School of Medicine, 1-1 Yazakokarimata, Nagakute, Aichi 480-1195, sachiko@aichi-med-u.ac.jp.ORCID 0000-0003-4890-3172
Aichi Medical University · JPJuntendo University · JPNational Institute of Advanced Industrial Science and Technology · JPKumamoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

IgE plays a key role in allergies by binding to allergens and then sensitizing mast cells through the Fc receptor, resulting in the secretion of proinflammatory mediators. Therefore, IgE is a major target for managing allergies. Previous studies have reported that oligomannose on IgE can be a potential target to inhibit allergic responses. However, enzymes that can modulate IgE activity are not yet known. Here, we found that the commercial receptor-destroying enzyme (RDE) (II) from

Indexed as

AnaphylaxisAnimalsBinding SitesBone Marrow CellsEnzymesImmunoglobulin EImmunoglobulin GMast CellsMicePolysaccharidesProtease InhibitorsProtein ConformationTrypsinVibrio choleraeEnzymesImmunoglobulin EImmunoglobulin Gpoly-N-acetyllactosaminePolysaccharidesProtease InhibitorsTrypsinallergyanaphylaxisautoimmune disorderglycansimmune responseimmunoglobulin E (IgE)inflammationmast celloligomannoseVibrio cholerae

Identifiers

PMID30833330
PMCPMC6497938
OpenAlexW2920252492

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.