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OpenAlex Citation Counts

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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:

Tyrosine bioconjugation with hypervalent iodine
Nina Declas, John R. J. Maynard, Laure Menin, et al.
Chemical Science (2022) Vol. 13, Iss. 43, pp. 12808-12817
Open Access | Times Cited: 21

Showing 21 citing articles:

Recent Progress in Synthetic Applications of Hypervalent Iodine(III) Reagents
Akira Yoshimura, Viktor V. Zhdankin
Chemical Reviews (2024)
Open Access | Times Cited: 28
Recent developments in the cleavage, functionalization, and conjugation of proteins and peptides at tyrosine residues
Shengping Zhang, Luis M. De Leon Rodriguez, Freda F. Li, et al.
Chemical Science (2023) Vol. 14, Iss. 29, pp. 7782-7817
Open Access | Times Cited: 29
Nonperturbative Fluorogenic Labeling of Immunophilins Enables the Wash-free Detection of Immunosuppressants
Marco Bertolini, Lorena Mendive‐Tapia, Ouldouz Ghashghaei, et al.
ACS Central Science (2024) Vol. 10, Iss. 5, pp. 969-977
Open Access | Times Cited: 6
Peptide‐Hypervalent Iodine Reagent Chimeras: Enabling Peptide Functionalization and Macrocyclization**
Xingyu Liu, Xinjian Ji, Christian Heinis, et al.
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 33
Open Access | Times Cited: 12
Thermally Triggered Triazolinedione–Tyrosine Bioconjugation with Improved Chemo- and Site-Selectivity
Elias Denijs, Kamil Unal, Kevin Bevernaege, et al.
Journal of the American Chemical Society (2024) Vol. 146, Iss. 18, pp. 12672-12680
Closed Access | Times Cited: 4
Triazination/IEDDA Cascade Modular Strategy Installing Pyridines/Pyrimidines onto Tyrosine Enables Peptide Screening and Optimization
Quan Zuo, Xinyi Song, Jie Yan, et al.
Journal of the American Chemical Society (2025)
Closed Access
Research progress on chemical modifications of tyrosine residues in peptides and proteins
Wei Zeng, Jianyuan Xue, Haoxing Geng, et al.
Biotechnology and Bioengineering (2023) Vol. 121, Iss. 3, pp. 799-822
Closed Access | Times Cited: 10
Silver-Catalyzed Coupling of Ethynylbenziodoxolones with CO2 and Amines to Afford O-β-Oxoalkyl Carbamates
Wei Li, Yanhui Guo, Ziyang Li, et al.
Organic Letters (2024) Vol. 26, Iss. 22, pp. 4600-4605
Closed Access | Times Cited: 3
Post-synthetic Chemical Functionalization of Peptides
Stephanie A. Barros, Rosaura Padilla‐Salinas, Irini Abdiaj
Elsevier eBooks (2025)
Closed Access
Exploring Chemical Modifications of Aromatic Amino Acid Residues in Peptides
Bishwajit Paul, Modhu Sudan Maji, Susanta Bhunia, et al.
Synthesis (2023) Vol. 55, Iss. 22, pp. 3701-3724
Closed Access | Times Cited: 9
Electrochemical Bioconjugation of Tryptophan Residues: A Strategy for Peptide Modification
Chenggang Wan, Rong Sun, Wenjie Xia, et al.
Organic Letters (2024) Vol. 26, Iss. 26, pp. 5447-5452
Closed Access | Times Cited: 3
Recent Advances in Bioorthogonal Ligation and Bioconjugation
Florian M. Zielke, Floris P. J. T. Rutjes
Topics in Current Chemistry (2023) Vol. 381, Iss. 6
Open Access | Times Cited: 7
Toward a Traceless Tag for the Thiol‐Mediated Uptake of Proteins
John R. J. Maynard, Saidbakhrom Saidjalolov, Marie‐Claire Velluz, et al.
ChemistryEurope (2023) Vol. 1, Iss. 3
Open Access | Times Cited: 5
X‐Ray Visible Protein Scaffolds by Bulk Iodination
Carlos Flechas Becerra, Lady V. Barrios Silva, Ebtehal Ahmed, et al.
Advanced Science (2023) Vol. 11, Iss. 10
Open Access | Times Cited: 4
Three-component Friedel–Crafts-type difunctionalization of ynamides with (hetero)arenes and iodine(iii) electrophile
Jun Kikuchi, Toya Nagata, Shingo Ito, et al.
Organic Chemistry Frontiers (2024) Vol. 11, Iss. 11, pp. 3072-3079
Open Access | Times Cited: 1
Pd(I)-catalyzed ring-opening arylation of cyclopropyl-α-aminoamides: Access to α-ketoamide peptidomimetics
Yue Sun, Liming Yang, Yaohang Cheng, et al.
Chinese Chemical Letters (2023) Vol. 35, Iss. 6, pp. 109250-109250
Closed Access | Times Cited: 3
Disintegrate (DIN) Theory Enabling Precision Engineering of Proteins
Preeti Chauhan, V. Ragendu, Mohan Kumar, et al.
ACS Central Science (2023) Vol. 9, Iss. 2, pp. 137-150
Open Access | Times Cited: 2
Peptide‐Hypervalent Iodine Reagent Chimeras: Enabling Peptide Functionalization and Macrocyclization**
Xingyu Liu, Xinjian Ji, Christian Heinis, et al.
Angewandte Chemie (2023) Vol. 135, Iss. 33
Open Access | Times Cited: 2
Structure-reactivity analysis of novel hypervalent iodine reagents in S-vinylation of thiols
Sayad Doobary, Ester Maria Di Tommaso, Alexandru Postole, et al.
Frontiers in Chemistry (2024) Vol. 12
Open Access
Methodology of stable peptide based on propargylated sulfonium
Heng Li, Zhanfeng Hou, Yuena Wang, et al.
Biochemistry and Biophysics Reports (2023) Vol. 35, pp. 101508-101508
Open Access | Times Cited: 1
Stereoselective Approach to Multisubstituted Enolates from Unactivated Alkynes: Oxyalkylidenation of Alkynyl Ketone Enolates with Aldehydes
Shuma Sasaki, Jun Kikuchi, Shingo Ito, et al.
The Journal of Organic Chemistry (2023) Vol. 88, Iss. 19, pp. 14096-14104
Closed Access
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