Evidence map›Paper›PMID 30886871›Full record

ReviewJournal of immunology research2019

Immunoglobulin Gamma-Like Therapeutic Bispecific Antibody Formats for Tumor Therapy.

Shixue Chen, Lingling Li, Fan Zhang, Yu Wang, Yi Hu, Lei Zhao

Open access · goldAbstract readReview
In one paragraph

Review in Journal of immunology research, 2019. 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
1.5field-weighted citation impact, top 18% 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, 15 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Therapeutic Antibodies: An Overview.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  6. Review
  7. Article
  8. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Shixue ChenNational Clinical Research Center for Normal Aging and Geriatric & Department of Oncology & Institute of Geriatric & The Key Lab of Normal Aging and Geriatric, The Second Medical Centre, PLA General Hospital, Beijing, China.
Lingling LiNational Clinical Research Center for Normal Aging and Geriatric & Department of Oncology & Institute of Geriatric & The Key Lab of Normal Aging and Geriatric, The Second Medical Centre, PLA General Hospital, Beijing, China.
Fan ZhangNational Clinical Research Center for Normal Aging and Geriatric & Department of Oncology & Institute of Geriatric & The Key Lab of Normal Aging and Geriatric, The Second Medical Centre, PLA General Hospital, Beijing, China.
Yu WangNational Clinical Research Center for Normal Aging and Geriatric & Department of Oncology & Institute of Geriatric & The Key Lab of Normal Aging and Geriatric, The Second Medical Centre, PLA General Hospital, Beijing, China.
Yi HuNational Clinical Research Center for Normal Aging and Geriatric & Department of Oncology & Institute of Geriatric & The Key Lab of Normal Aging and Geriatric, The Second Medical Centre, PLA General Hospital, Beijing, China.ORCID 0000-0001-9319-5692
Lei ZhaoNational Clinical Research Center for Normal Aging and Geriatric & Department of Oncology & Institute of Geriatric & The Key Lab of Normal Aging and Geriatric, The Second Medical Centre, PLA General Hospital, Beijing, China.ORCID 0000-0002-5884-2708
Chinese PLA General Hospital · CNNankai University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bispecific antibodies (BsAbs) are a sort of dual functional proteins with specific binding to two distinct targets, which have become a focus of interest in antibody engineering and drug development research and have a promising future for wide applications in cancer immunotherapy and autoimmune disease. The key of clinical application and commercial-scale manufacturing of BsAbs is the amenability to assembly and purification of desired heterodimers. Advances in genetic engineering technology had resulted in the development of diverse BsAbs. Multiple recombinant strategies have been used to solve the mispairing problem between light and heavy chains, as well as to enforce accurate dimerization of heterologous heavy chains. There are 23 platforms available to generate 62 BsAbs which can be further divided into IgG-like ones and fragment-based ones, and more than 50 molecules are undergoing clinical trials currently. BsAbs with IgG-like architecture exhibit superior advantages in structure (similar to natural antibodies), pharmacokinetics, half-life, FcR-mediated function, and biological activity. This review considers various IgG-like BsAb generation approaches, summarizes the clinical applications of promising new BsAbs, and describes the mechanism of BsAbs in tumor therapy.

Indexed as

AnimalsAntibodies, BispecificDimerizationGenetic EngineeringHumansImmunoglobulin GImmunoglobulin Heavy ChainsImmunoglobulin Light ChainsImmunotherapyNeoplasmsAntibodies, BispecificImmunoglobulin GImmunoglobulin Heavy ChainsImmunoglobulin Light Chains

Identifiers

PMID30886871
PMCPMC6388348
OpenAlexW2911912536

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.