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:

A chemoenzymatic strategy for site-selective functionalization of native peptides and proteins
Anna Fryszkowska, Chihui An, Oscar Alvizo, et al.
Science (2022) Vol. 376, Iss. 6599, pp. 1321-1327
Closed Access | Times Cited: 35

Showing 1-25 of 35 citing articles:

From nature to industry: Harnessing enzymes for biocatalysis
Rebecca Buller, Stefan Lutz, Romas J. Kazlauskas, et al.
Science (2023) Vol. 382, Iss. 6673
Open Access | Times Cited: 168

Engineering protein-based therapeutics through structural and chemical design
Sasha B. Ebrahimi, Devleena Samanta
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 119

The Evolving Nature of Biocatalysis in Pharmaceutical Research and Development
Scott P. France, Russell D. Lewis, Carlos A. Martínez
JACS Au (2023) Vol. 3, Iss. 3, pp. 715-735
Open Access | Times Cited: 69

Biocatalytic amide bond formation
Max Lubberink, William Finnigan, Sabine L. Flitsch
Green Chemistry (2023) Vol. 25, Iss. 8, pp. 2958-2970
Open Access | Times Cited: 41

Enzymatic Bioconjugation: A Perspective from the Pharmaceutical Industry
Aaron Debon, Elina Siirola, Radka Šnajdrová
JACS Au (2023) Vol. 3, Iss. 5, pp. 1267-1283
Open Access | Times Cited: 26

Non-Native Site-Selective Enzyme Catalysis
Dibyendu Mondal, Harrison M. Snodgrass, Christian A. Gomez, et al.
Chemical Reviews (2023) Vol. 123, Iss. 16, pp. 10381-10431
Open Access | Times Cited: 22

Accelerated enzyme engineering by machine-learning guided cell-free expression
Grant M. Landwehr, Jonathan W. Bogart, Carol Magalhaes, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access

Cascades of Evolved Enzymes for the Synthesis of Complex Molecules
Katrin Rosenthal, Uwe T. Bornscheuer, Stephan Lütz
Angewandte Chemie International Edition (2022) Vol. 61, Iss. 39
Open Access | Times Cited: 28

Promiscuous acyltransferases for ester and amide synthesis in aqueous solution
Benjamin Baumert, Hannes Meinert, Clemens Cziegler, et al.
Catalysis Today (2024) Vol. 442, pp. 114925-114925
Open Access | Times Cited: 4

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: 3

Biocatalysis in Drug Design: Engineered Reductive Aminases (RedAms) Are Used to Access Chiral Building Blocks with Multiple Stereocenters
Arnau Rué Casamajo, Yuqi Yu, Christian Schnepel, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 40, pp. 22041-22046
Open Access | Times Cited: 9

Accelerated enzyme engineering by machine-learning guided cell-free expression
Grant M. Landwehr, Jonathan W. Bogart, Carol Magalhaes, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 2

Catalyzing the future: recent advances in chemical synthesis using enzymes
Julia C. Reisenbauer, Kathleen M. Sicinski, Frances H. Arnold
Current Opinion in Chemical Biology (2024) Vol. 83, pp. 102536-102536
Closed Access | Times Cited: 2

Single‐Shot Solid‐Phase Synthesis of Full‐Length H2 Relaxin Disulfide Surrogates
Rui Zhao, Pan Shi, Ji‐bin Cui, et al.
Angewandte Chemie International Edition (2022) Vol. 62, Iss. 6
Closed Access | Times Cited: 13

Insulin–Dendrimer Nanocomplex for Multi‐Day Glucose‐Responsive Therapy in Mice and Swine
Sijie Xian, Yuanhui Xiang, Dongping Liu, et al.
Advanced Materials (2023) Vol. 36, Iss. 5
Closed Access | Times Cited: 7

Efficient production of peptidylglycine α-hydroxylating monooxygenase in yeast for protein C-terminal functionalization
Tong Zhu, Xuanshuo Zhang, Ruifeng Li, et al.
International Journal of Biological Macromolecules (2024) Vol. 263, pp. 130443-130443
Closed Access | Times Cited: 1

Penicillin G acylase-responsive near-infrared fluorescent probe: Unravelling biofilm regulation and combating bacterial infections
Yang Liu, Leilei Zhang, Kaixuan Liu, et al.
Chinese Chemical Letters (2024) Vol. 35, Iss. 11, pp. 109759-109759
Closed Access | Times Cited: 1

Unraveling dynamic protein structures by two-dimensional infrared spectra with a pretrained machine learning model
Fan Wu, Yan Huang, Guokun Yang, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 27
Open Access | Times Cited: 1

Chromophore-Assisted Light Inactivation for Protein Degradation and Its Application in Biomedicine
Lvjia Zhou, Jintong Na, Xiyu Liu, et al.
Bioengineering (2024) Vol. 11, Iss. 7, pp. 651-651
Open Access

An open source in silico workflow to assist in the design of fusion proteins
Christophe J. Lalaurie, Chengqi Zhang, Shiming Liu, et al.
Computational Biology and Chemistry (2024) Vol. 113, pp. 108209-108209
Open Access

Repurposing Amide Bond-Forming Enzymes for Non-native Protein Modification
Tong Zhu, Bian Wu
ACS Catalysis (2024) Vol. 14, Iss. 21, pp. 15811-15826
Closed Access

Ancestral Sequence Reconstruction to Enable Biocatalytic Synthesis of Azaphilones
Chang-Hwa Chiang, Ye Wang, Azam Hussain, et al.
Journal of the American Chemical Society (2024) Vol. 146, Iss. 44, pp. 30194-30203
Closed Access

Recent Advances in Peptide Drug Discovery: Novel Strategies and Targeted Protein Degradation
Katarina Vrbnjak, Raj Nayan Sewduth
Pharmaceutics (2024) Vol. 16, Iss. 11, pp. 1486-1486
Open Access

Selective N-terminal modification of peptides and proteins using acyl phosphates
Laura Rodríguez Pérez, Thomas A. King, William Finnigan, et al.
(2023)
Open Access | Times Cited: 1

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