Evidence map›Paper›PMID 38032124›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2024

Affinity-Directed Site-Specific Protein Labeling and Its Application to Antibody-Drug Conjugates.

Sooin Kim, Sanggil Kim, Sangji Kim, Namkyoung Kim, Sang Won Lee, Hanbin Yi, Seungeun Lee, Taebo Sim, Yongseok Kwon, Hyun Soo Lee

Open access · goldAbstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

13 citing papers in PubMed, 15 citations in OpenAlex.

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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 3 institutions in 1 country.

Sooin KimDepartment of Chemistry, Sogang University, 35 Baekbeom-ro, Mapo-gu, Seoul, 04107, Republic of Korea.
Sanggil KimNew Drug Development Center, Osong Medical Innovation Foundation, 123 Osongsaengmyeong-ro, Heungdeok-gu, Cheongju, Chungbuk, 28160, Republic of Korea.
Sangji KimSchool of Pharmacy, Sungkyunkwan University, 2066 Seobu-ro, Jangan-gu, Suwon, 16419, Republic of Korea.
Namkyoung KimDepartment of Biomedical Sciences, Graduate School of Medical Science, Brain Korea 21 Project, Yonsei University College of Medicine, 50 Yonsei-ro, Seodaemun-gu, Seoul, 03722, Republic of Korea.
Sang Won LeeDepartment of Chemistry, Sogang University, 35 Baekbeom-ro, Mapo-gu, Seoul, 04107, Republic of Korea.
Hanbin YiDepartment of Chemistry, Sogang University, 35 Baekbeom-ro, Mapo-gu, Seoul, 04107, Republic of Korea.
Seungeun LeeDepartment of Chemistry, Sogang University, 35 Baekbeom-ro, Mapo-gu, Seoul, 04107, Republic of Korea.
Taebo SimDepartment of Biomedical Sciences, Graduate School of Medical Science, Brain Korea 21 Project, Yonsei University College of Medicine, 50 Yonsei-ro, Seodaemun-gu, Seoul, 03722, Republic of Korea.
Yongseok KwonSchool of Pharmacy, Sungkyunkwan University, 2066 Seobu-ro, Jangan-gu, Suwon, 16419, Republic of Korea.
Hyun Soo LeeDepartment of Chemistry, Sogang University, 35 Baekbeom-ro, Mapo-gu, Seoul, 04107, Republic of Korea.ORCID 0000-0002-1981-0391
Sogang University · KRYonsei University · KRSungkyunkwan University · KR

Funding

Advanced Bio-interface Core Research FacilityBasic Science Research Program in Korea 2018R1A6A1A03024940Basic Science Research Program in Korea 2021R1A2C3011992Basic Science Research Program in Korea 2022M3E5F2017857Basic Science Research Program in Korea NRF-2022R1A2C1006402
6 · The paper itself

Abstract

Chemically modified proteins have diverse applications; however, conventional chemo-selective methods often yield heterogeneously labeled products. To address this limitation, site-specific protein labeling holds significant potential, driving extensive research in this area. Nevertheless, site-specific modification of native proteins remains challenging owing to the complexity of their functional groups. Therefore, a method for site-selective labeling of intact proteins is aimed to design. In this study, a novel approach to traceless affinity-directed intact protein labeling is established, which leverages small binding proteins and genetic code expansion technology. By applying this method, a site-specific antibody labeling with a drug, which leads to the production of highly effective antibody-drug conjugates specifically targeting breast cancer cell lines is achieved. This approach enables traceless conjugation of intact target proteins, which is a critical advantage in pharmaceutical applications. Furthermore, small helical binding proteins can be easily engineered for various target proteins, thereby expanding their potential applications in diverse fields. This innovative approach represents a significant advancement in site-specific modification of native proteins, including antibodies. It also bears immense potential for facilitating the development of therapeutic agents for various diseases.

Indexed as

ImmunoconjugatesAntibodiesProteinsAntibodiesImmunoconjugatesProteinsantibody-drug conjugatesbioorthogonal chemistrygenetic code expansionnative protein labelingsmall helical binding protein

Identifiers

PMID38032124
PMCPMC10811483
OpenAlexW4389178838

What OpenQuestion holds

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LicenceCC BY
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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.