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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

Chemoselective and Site‐Selective Lysine‐Directed Lysine Modification Enables Single‐Site Labeling of Native Proteins
Srinivasa Rao Adusumalli, Dattatraya Gautam Rawale, Kalyani Thakur, et al.
Angewandte Chemie International Edition (2020) Vol. 59, Iss. 26, pp. 10332-10336
Closed Access | Times Cited: 69

Showing 1-25 of 69 citing articles:

Site-selective modification strategies in antibody–drug conjugates
Stephen J. Walsh, Jonathan D. Bargh, Friederike M. Dannheim, et al.
Chemical Society Reviews (2020) Vol. 50, Iss. 2, pp. 1305-1353
Open Access | Times Cited: 312
Spatial mapping of protein composition and tissue organization: a primer for multiplexed antibody-based imaging
John W. Hickey, Elizabeth K. Neumann, Andrea J. Radtke, et al.
Nature Methods (2021) Vol. 19, Iss. 3, pp. 284-295
Open Access | Times Cited: 250
The Chemistry Behind ADCs
Vesela Kostova, Patrice Désos, Jérôme-Benoît Starck, et al.
Pharmaceuticals (2021) Vol. 14, Iss. 5, pp. 442-442
Open Access | Times Cited: 83
Site-selective lysine conjugation methods and applications towards antibody–drug conjugates
Muhammed Haque, Nafsika Forte, James R. Baker
Chemical Communications (2021) Vol. 57, Iss. 82, pp. 10689-10702
Open Access | Times Cited: 66
Chemical modification of enzymes to improve biocatalytic performance
Pritam Giri, Amol D. Pagar, Mahesh D. Patil, et al.
Biotechnology Advances (2021) Vol. 53, pp. 107868-107868
Closed Access | Times Cited: 62
An overview of chemo- and site-selectivity aspects in the chemical conjugation of proteins
Charlotte Sornay, Valentine Vaur, Alain Wagner, et al.
Royal Society Open Science (2022) Vol. 9, Iss. 1
Open Access | Times Cited: 44
Development and Recent Advances in Lysine and N-Terminal Bioconjugation for Peptides and Proteins
Ajcharapan Tantipanjaporn, Man‐Kin Wong
Molecules (2023) Vol. 28, Iss. 3, pp. 1083-1083
Open Access | Times Cited: 29
A pyridinium-based strategy for lysine-selective protein modification and chemoproteomic profiling in live cells
Chuan Wan, Dongyan Yang, Chunli Song, et al.
Chemical Science (2024) Vol. 15, Iss. 14, pp. 5340-5348
Open Access | Times Cited: 11
Lipid-Directed Covalent Labeling of Plasma Membranes for Long-Term Imaging, Barcoding and Manipulation of Cells
Nathan Aknine, Rémi Pelletier, Andrey S. Klymchenko
JACS Au (2025) Vol. 5, Iss. 2, pp. 922-936
Open Access | Times Cited: 1
Morita–Baylis–Hillman Adduct Chemistry as a Tool for the Design of Lysine-Targeted Covalent Ligands
Marco Paolino, Giusy Tassone, Paolo Governa, et al.
ACS Medicinal Chemistry Letters (2025) Vol. 16, Iss. 3, pp. 397-405
Closed Access | Times Cited: 1
Chemical methods for modification of proteins
Neelesh C. Reddy, Mohan Kumar, Rajib Molla, et al.
Organic & Biomolecular Chemistry (2020) Vol. 18, Iss. 25, pp. 4669-4691
Closed Access | Times Cited: 63
Selective N-terminal modification of peptides and proteins: Recent progresses and applications
Hongfei Jiang, Wujun Chen, Jie Wang, et al.
Chinese Chemical Letters (2021) Vol. 33, Iss. 1, pp. 80-88
Closed Access | Times Cited: 48
A Traceless Site‐Specific Conjugation on Native Antibodies Enables Efficient One‐Step Payload Assembly
Yue Zeng, Wei Shi, Qian Dong, et al.
Angewandte Chemie International Edition (2022) Vol. 61, Iss. 36
Closed Access | Times Cited: 33
Chemical Conjugation to Less Targeted Proteinogenic Amino Acids
Nanna L. Kjærsgaard, Thorbjørn B. Nielsen, Kurt V. Gothelf
ChemBioChem (2022) Vol. 23, Iss. 19
Open Access | Times Cited: 32
Chemical modification of proteins – challenges and trends at the start of the 2020s
Niklas H. Fischer, Maria Teresa Oliveira, Frederik Diness
Biomaterials Science (2022) Vol. 11, Iss. 3, pp. 719-748
Closed Access | Times Cited: 32
Chemical technology principles for selective bioconjugation of proteins and antibodies
Preeti Chauhan, V. Ragendu, Mohan Kumar, et al.
Chemical Society Reviews (2023) Vol. 53, Iss. 1, pp. 380-449
Closed Access | Times Cited: 19
Non-symmetric stapling of native peptides
Fa‐Jie Chen, Wanzhen Lin, Fen‐Er Chen
Nature Reviews Chemistry (2024) Vol. 8, Iss. 5, pp. 304-318
Closed Access | Times Cited: 8
Protein Labeling and Crosslinking by Covalent Aptamers
Yaniv Tivon, Gianna Falcone, Alexander Deiters
Angewandte Chemie International Edition (2021) Vol. 60, Iss. 29, pp. 15899-15904
Open Access | Times Cited: 37
Precision Modification of Native Antibodies
Kuan‐Lin Wu, Chenfei Yu, Catherine Lee, et al.
Bioconjugate Chemistry (2021) Vol. 32, Iss. 9, pp. 1947-1959
Open Access | Times Cited: 36
Traceless cysteine-linchpin enables precision engineering of lysine in native proteins
Neelesh C. Reddy, Rajib Molla, Pralhad Namdev Joshi, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 26
Precision in protein chemical modification and total synthesis
Zhenquan Sun, Han Liu, Xuechen Li
Chem (2023) Vol. 10, Iss. 3, pp. 767-799
Closed Access | Times Cited: 15
Site-selective photocatalytic functionalization of peptides and proteins at selenocysteine
Luke J. Dowman, Sameer S. Kulkarni, Juan V. Alegre‐Requena, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 19
Recent progress of chemical methods for lysine site-selective modification of peptides and proteins
Jian Li, Jinjin Chen, Qi-Long Hu, et al.
Chinese Chemical Letters (2024), pp. 110126-110126
Closed Access | Times Cited: 4
Formation of mono- and dual-labelled antibody fragment conjugates via reversible site-selective disulfide modification and proximity induced lysine reactivity
Ioanna A. Thanasi, Nathalie Bouloc, Clíona McMahon, et al.
Chemical Science (2025)
Open Access
Linchpins empower promiscuous electrophiles to enable site-selective modification of histidine and aspartic acid in proteins
Dattatraya Gautam Rawale, Kalyani Thakur, Pranav Sreekumar, et al.
Chemical Science (2021) Vol. 12, Iss. 19, pp. 6732-6736
Open Access | Times Cited: 25
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