Evidence map›Paper›PMID 42819270›Full record

ArticleJACS Au2026

Development of a Polypeptide-Based Platform to Construct Antibody-Drug Conjugates with High Potency.

Ruyao Tang, Fusheng Guo, Jinyi Bai, Xiaoguang Lei

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in JACS Au, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

4 authors.

Ruyao TangBeijing National Laboratory for Molecular Sciences, Key Laboratory of Bioorganic Chemistry of the Ministry of Education, College of Chemistry and Molecular Engineering, New Cornerstone Science Laboratory, Peking University, Beijing 100871, People's Republic of China.
Fusheng GuoBeijing National Laboratory for Molecular Sciences, Key Laboratory of Bioorganic Chemistry of the Ministry of Education, College of Chemistry and Molecular Engineering, New Cornerstone Science Laboratory, Peking University, Beijing 100871, People's Republic of China.
Jinyi BaiBeijing National Laboratory for Molecular Sciences, Key Laboratory of Bioorganic Chemistry of the Ministry of Education, College of Chemistry and Molecular Engineering, New Cornerstone Science Laboratory, Peking University, Beijing 100871, People's Republic of China.
Xiaoguang LeiBeijing National Laboratory for Molecular Sciences, Key Laboratory of Bioorganic Chemistry of the Ministry of Education, College of Chemistry and Molecular Engineering, New Cornerstone Science Laboratory, Peking University, Beijing 100871, People's Republic of China.ORCID https://orcid.org/0000-0002-0380-8035

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antibody-drug conjugates (ADCs) represent an emerging pharmaceutical category that leverages antibodies to facilitate drug delivery to target cells. A key challenge for ADCs is increasing the drug-antibody ratio (DAR) to improve efficacy without compromising their properties, such as pharmacokinetics. Here, we present a novel polypeptide-based platform that substantially increases the DAR of antibody-payload ADCs while minimally compromising the ADCs' inherent characteristics. A polypeptide-based antibody-drug conjugate lead (polypeptide ADC

Indexed as

antibody-drug conjugatesanticancer drugshigh DARmultivalent conjugationPolypeptide-based platform

Identifiers

PMID42819270
PMCPMC13625539

What OpenQuestion holds

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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.