Evidence map›Paper›PMID 32368617›Full record

ArticleMolecular therapy oncolytics2020

Polymorphic Region-Specific Antibody for Evaluation of Affinity-Associated Profile of Chimeric Antigen Receptor.

Chungyong Han, Beom K Choi, Seon-Hee Kim, Su-Jung Sim, Seongeun Han, Bomi Park, Yohei Tsuchiya, Masaki Takahashi, Young H Kim, Hyeon-Seok Eom and 3 more

Open access · goldAbstract read
In one paragraph

Article in Molecular therapy oncolytics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.1field-weighted citation impact, top 57% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. 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

13 authors at 4 institutions in 3 countries.

Chungyong HanDivision of Tumor Immunology, Research Institute, National Cancer Center, Goyang, Republic of Korea.
Beom K ChoiBiomedicine Production Branch, Research Institute, National Cancer Center, Goyang, Republic of Korea.
Seon-Hee KimDivision of Tumor Immunology, Research Institute, National Cancer Center, Goyang, Republic of Korea.
Su-Jung SimDivision of Tumor Immunology, Research Institute, National Cancer Center, Goyang, Republic of Korea.
Seongeun HanDivision of Tumor Immunology, Research Institute, National Cancer Center, Goyang, Republic of Korea.
Bomi ParkBiomedicine Production Branch, Research Institute, National Cancer Center, Goyang, Republic of Korea.
Yohei TsuchiyaInterdisciplinary Graduate School of Science and Engineering, Tokyo Institute of Technology, Yokohama, Japan.
Masaki TakahashiGraduate School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
Young H KimBiomedicine Production Branch, Research Institute, National Cancer Center, Goyang, Republic of Korea.
Hyeon-Seok EomCenter for Hematologic Malignancy, Hospital, National Cancer Center, Goyang, Republic of Korea.
Tetsuya KitaguchiLaboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan.
Hiroshi UedaLaboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan.
Byoung S KwonDivision of Tumor Immunology, Research Institute, National Cancer Center, Goyang, Republic of Korea.
National Cancer Center · KRLife Science Institute · JPTokyo Institute of Technology · JPTulane University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antibody applications in cancer immunotherapy involve diverse strategies, some of which redirect T cell-mediated immunity via engineered antibodies. Affinity is a trait that is crucial for these strategies, as optimal affinity reduces unwanted side effects while retaining therapeutic function. Antibody-antigen pairs possessing a broad affinity range are required to define optimal affinity and to investigate the affinity-associated functional profiles of T cell-engaging strategies such as bispecific antibodies and chimeric antigen receptor-engineered T cells. Here, we demonstrate the unique binding characteristic of the developed antibody clone MVR, which exhibits robust binding to B-lymphoid cell lines. Intriguingly, MVR specifically recognizes the highly polymorphic human leukocyte antigen (HLA)-DR complex and exhibits varying affinities that are dependent upon the

Indexed as

activation-induced cell deathaffinityantibodychimeric antigen receptorHLA-DRpolyfunctionalitypolymorphismT cell

Identifiers

PMID32368617
PMCPMC7191539
OpenAlexW3016990044

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.