Evidence map›Paper›PMID 37249578›Full record

ArticleeLife2023

Noncovalent antibody catenation on a target surface greatly increases the antigen-binding avidity.

Jinyeop Song, Bo-Seong Jeong, Seong-Woo Kim, Seong-Bin Im, Seonghoon Kim, Chih-Jen Lai, Wonki Cho, Jae U Jung, Myung-Ju Ahn, Byung-Ha Oh

Open access · goldAbstract read
In one paragraph

Article in eLife, 2023. 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
0.5field-weighted citation impact, top 35% 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

10 authors at 3 institutions in 2 countries.

Jinyeop Song *Department of Physics, Korea Advanced Institute of Science and Technology, Daejeon, Republic of Korea.ORCID 0000-0002-4113-5185
Bo-Seong Jeong *Department of Biological Sciences, KAIST Institute for the Biocentury, Korea Advanced Institute of Science and Technology, Daejeon, Republic of Korea.ORCID 0000-0003-0629-6722
Seong-Woo KimDepartment of Biological Sciences, KAIST Institute for the Biocentury, Korea Advanced Institute of Science and Technology, Daejeon, Republic of Korea.ORCID 0000-0002-4374-2093
Seong-Bin ImDepartment of Biological Sciences, KAIST Institute for the Biocentury, Korea Advanced Institute of Science and Technology, Daejeon, Republic of Korea.ORCID 0000-0003-1488-6386
Seonghoon KimDepartment of Biological Sciences, KAIST Institute for the Biocentury, Korea Advanced Institute of Science and Technology, Daejeon, Republic of Korea.
Chih-Jen LaiCancer Biology Department, Infection Biology Program, and Global Center for Pathogen and Human Health Research, Lerner Research Institute, Cleveland Clinic, Cleveland, United States.
Wonki ChoDepartment of Biological Sciences, KAIST Institute for the Biocentury, Korea Advanced Institute of Science and Technology, Daejeon, Republic of Korea.
Jae U JungCancer Biology Department, Infection Biology Program, and Global Center for Pathogen and Human Health Research, Lerner Research Institute, Cleveland Clinic, Cleveland, United States.
Myung-Ju AhnDepartment of Medicine, Samsung Medical Center, Sungkyunkwan University School of Medicine, Seoul, Republic of Korea.
Byung-Ha OhDepartment of Biological Sciences, KAIST Institute for the Biocentury, Korea Advanced Institute of Science and Technology, Daejeon, Republic of Korea.ORCID 0000-0002-6437-8470
Korea Advanced Institute of Science and Technology · KRCleveland Clinic Lerner College of Medicine · USSamsung Medical Center · KR

Funding

Tickborne SFTS Virus Vaccine DevelopmentR01AI152190 · NIAID · CLEVELAND CLINIC LERNER COM-CWRU · PI JUNG, JAE U · 2020 to 2024
$2.9M
NIAID NIH HHS R01 AI152190
6 · The paper itself

Abstract

Immunoglobulin G (IgG) antibodies are widely used for diagnosis and therapy. Given the unique dimeric structure of IgG, we hypothesized that, by genetically fusing a homodimeric protein (catenator) to the C-terminus of IgG, reversible catenation of antibody molecules could be induced on a surface where target antigen molecules are abundant, and that it could be an effective way to greatly enhance the antigen-binding avidity. A thermodynamic simulation showed that quite low homodimerization affinity of a catenator,

Indexed as

AntigensImmunoglobulin GAntibody AffinityAntigensImmunoglobulin Gantibody applicationantibody catenationavidity enhancementcomputational biologyhumanIgG antibodymolecular biophysicsnew technologystructural biologysystems biologyviruses

Identifiers

PMID37249578
PMCPMC10229114
OpenAlexW4378745489

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.