Evidence map›Paper›PMID 30774870›Full record

ArticleChemical science2019

A general approach for the site-selective modification of native proteins, enabling the generation of stable and functional antibody-drug conjugates.

Stephen J Walsh, Soleilmane Omarjee, Warren R J D Galloway, Terence T-L Kwan, Hannah F Sore, Jeremy S Parker, Marko Hyvönen, Jason S Carroll, David R Spring

Erratum issuedAbstract read
In one paragraph

Article in Chemical science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
–field-weighted citation impact
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

59 citing papers in PubMed.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Stephen J WalshDepartment of Chemistry , University of Cambridge , Cambridge , CB2 1EW , UK . Email: spring@ch.cam.ac.uk.ORCID 0000-0002-3164-1519
Soleilmane OmarjeeCancer Research UK Cambridge Institute , University of Cambridge , Cambridge , CB2 0RE , UK . Email: jason.carroll@cruk.cam.ac.uk.
Warren R J D GallowayDepartment of Chemistry , University of Cambridge , Cambridge , CB2 1EW , UK . Email: spring@ch.cam.ac.uk.
Terence T-L KwanDepartment of Chemistry , University of Cambridge , Cambridge , CB2 1EW , UK . Email: spring@ch.cam.ac.uk.
Hannah F SoreDepartment of Chemistry , University of Cambridge , Cambridge , CB2 1EW , UK . Email: spring@ch.cam.ac.uk.ORCID 0000-0002-6542-0394
Jeremy S ParkerEarly Chemical Development , Pharmaceutical Development , IMED Biotech Unit , AstraZeneca , Macclesfield , UK.ORCID 0000-0002-4758-3181
Marko HyvönenDepartment of Biochemistry , University of Cambridge , Cambridge , CB2 1GA , UK.ORCID 0000-0001-8683-4070
Jason S CarrollCancer Research UK Cambridge Institute , University of Cambridge , Cambridge , CB2 0RE , UK . Email: jason.carroll@cruk.cam.ac.uk.ORCID 0000-0003-3643-0080
David R SpringDepartment of Chemistry , University of Cambridge , Cambridge , CB2 1EW , UK . Email: spring@ch.cam.ac.uk.ORCID 0000-0001-7355-2824

Funding

Cancer Research UK 20411
6 · The paper itself

Abstract

Antibody-drug conjugates (ADCs) are a class of targeted therapeutics that utilize the specificity of antibodies to selectively deliver highly potent cytotoxins to target cells. Although recent years have witnessed significant interest in ADCs, problems remain with the standard linkage chemistries used for cytotoxin-antibody bioconjugation. These typically (1) generate unstable constructs, which may lead to premature cytotoxin release, (2) often give a wide variance in drug-antibody ratios (DAR) and (3) have poor control of attachment location on the antibody, resulting in a variable pharmacokinetic profile. Herein, we report a novel divinylpyrimidine (DVP) linker platform for selective bioconjugation

Identifiers

PMID30774870
PMCPMC6349026

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Registered trials

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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.