Evidence map›Paper›PMID 36968530›Full record

ArticleACS central science2023

Modular Chemical Construction of IgG-like Mono- and Bispecific Synthetic Antibodies (SynAbs).

Fabien Thoreau, Peter A Szijj, Michelle K Greene, Léa N C Rochet, Ioanna A Thanasi, Jaine K Blayney, Antoine Maruani, James R Baker, Christopher J Scott, Vijay Chudasama

Open access · diamondFull text read
In one paragraph

Article in ACS central science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

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  8. Antibody-Nanoparticle Conjugates in Therapy: Combining the Best of Two Worlds.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Review
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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 2 institutions in 1 country.

Fabien ThoreauDepartment of Chemistry, University College London, 20 Gordon Street, London WC1H 0AJ, U.K.ORCID https://orcid.org/0000-0003-1092-4170
Peter A SzijjDepartment of Chemistry, University College London, 20 Gordon Street, London WC1H 0AJ, U.K.ORCID https://orcid.org/0000-0002-2944-2676
Michelle K GreenePatrick G Johnston Centre for Cancer Research, School of Medicine, Dentistry and Biomedical Sciences, Queen's University Belfast, Belfast BT9 7AEU.K.
Léa N C RochetDepartment of Chemistry, University College London, 20 Gordon Street, London WC1H 0AJ, U.K.
Ioanna A ThanasiDepartment of Chemistry, University College London, 20 Gordon Street, London WC1H 0AJ, U.K.
Jaine K BlayneyPatrick G Johnston Centre for Cancer Research, School of Medicine, Dentistry and Biomedical Sciences, Queen's University Belfast, Belfast BT9 7AEU.K.
Antoine MaruaniDepartment of Chemistry, University College London, 20 Gordon Street, London WC1H 0AJ, U.K.
James R BakerDepartment of Chemistry, University College London, 20 Gordon Street, London WC1H 0AJ, U.K.ORCID https://orcid.org/0000-0002-7223-2279
Christopher J ScottPatrick G Johnston Centre for Cancer Research, School of Medicine, Dentistry and Biomedical Sciences, Queen's University Belfast, Belfast BT9 7AEU.K.
Vijay ChudasamaDepartment of Chemistry, University College London, 20 Gordon Street, London WC1H 0AJ, U.K.ORCID https://orcid.org/0000-0002-8876-3285
University College London · GBQueen's University Belfast · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

In recent years there has been rising interest in the field of protein-protein conjugation, especially related to bispecific antibodies (bsAbs) and their therapeutic applications. These constructs contain two paratopes capable of binding two distinct epitopes on target molecules and are thus able to perform complex biological functions (mechanisms of action) not available to monospecific mAbs. Traditionally these bsAbs have been constructed through protein engineering, but recently chemical methods for their construction have started to (re)emerge. While these have been shown to offer increased modularity, speed, and for some methods even the inherent capacity for further functionalization (e.g., with small molecule cargo), most of these approaches lacked the ability to include a fragment crystallizable (Fc) modality. The Fc component of IgG antibodies offers effector function and increased half-life. Here we report a first-in-class disulfide rebridging and click-chemistry-based method for the generation of Fc-containing, IgG-like mono- and bispecific antibodies. These are in the Fc

Identifiers

PMID36968530
PMCPMC10037451
OpenAlexW4321435487

What OpenQuestion holds

Textfull text, public
LicenceCC BY
measurements read12
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.