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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:

Rewriting the Genetic Code
Takahito Mukai, Marc J. Lajoie, Markus Englert, et al.
Annual Review of Microbiology (2017) Vol. 71, Iss. 1, pp. 557-577
Open Access | Times Cited: 151

Showing 1-25 of 151 citing articles:

A semi-synthetic organism that stores and retrieves increased genetic information
Yorke Zhang, Jerod L. Ptacin, Emil C. Fischer, et al.
Nature (2017) Vol. 551, Iss. 7682, pp. 644-647
Open Access | Times Cited: 312
Aminoacyl-tRNA synthetases
Miguel A. Rubio, Michael Ibba
RNA (2020) Vol. 26, Iss. 8, pp. 910-936
Open Access | Times Cited: 307
Codon usage bias
Sujatha Thankeswaran Parvathy, V. Udayasuriyan, V. P. Bhadana
Molecular Biology Reports (2021) Vol. 49, Iss. 1, pp. 539-565
Open Access | Times Cited: 270
Achieving Controlled Biomolecule–Biomaterial Conjugation
Christopher D. Spicer, E. Thomas Pashuck, Molly M. Stevens
Chemical Reviews (2018) Vol. 118, Iss. 16, pp. 7702-7743
Open Access | Times Cited: 194
Upgrading aminoacyl-tRNA synthetases for genetic code expansion
Oscar Vargas‐Rodriguez, Anastasia Sevostyanova, Dieter Söll, et al.
Current Opinion in Chemical Biology (2018) Vol. 46, pp. 115-122
Open Access | Times Cited: 106
Mutually Orthogonal Nonsense-Suppression Systems and Conjugation Chemistries for Precise Protein Labeling at up to Three Distinct Sites
James S. Italia, Partha Sarathi Addy, Sarah B. Erickson, et al.
Journal of the American Chemical Society (2019) Vol. 141, Iss. 15, pp. 6204-6212
Open Access | Times Cited: 95
Expanding the limits of the second genetic code with ribozymes
Joongoo Lee, Kenneth E. Schwieter, Andrew M. Watkins, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 89
Artificial Metalloenzyme Design with Unnatural Amino Acids and Non-Native Cofactors
Yang Yu, Cheng Hu, Lin Xia, et al.
ACS Catalysis (2018) Vol. 8, Iss. 3, pp. 1851-1863
Closed Access | Times Cited: 88
Site-Specific Labeling of Proteins Using Unnatural Amino Acids.
Kyung Jin Lee, Deokhee Kang, Hee-Sung Park
PubMed (2019) Vol. 42, Iss. 5, pp. 386-396
Closed Access | Times Cited: 79
De novo metalloprotein design
Matthew J. Chalkley, Samuel I. Mann, William F. DeGrado
Nature Reviews Chemistry (2021) Vol. 6, Iss. 1, pp. 31-50
Open Access | Times Cited: 79
Functional analysis of protein post‐translational modifications using genetic codon expansion
Tao Peng, Tandrila Das, Ke Ding, et al.
Protein Science (2023) Vol. 32, Iss. 4
Open Access | Times Cited: 24
Evolution of Pyrrolysyl-tRNA Synthetase: From Methanogenesis to Genetic Code Expansion
Nikolaj G. Koch, Nediljko Budiša
Chemical Reviews (2024) Vol. 124, Iss. 16, pp. 9580-9608
Open Access | Times Cited: 11
Orthogonal Translation for Site-Specific Installation of Post-translational Modifications
Qinglei Gan, Chenguang Fan
Chemical Reviews (2024) Vol. 124, Iss. 5, pp. 2805-2838
Closed Access | Times Cited: 10
Cracking the Code: Reprogramming the Genetic Script in Prokaryotes and Eukaryotes to Harness the Power of Noncanonical Amino Acids
Cosimo Jann, Sabrina Giofrè, Rajanya Bhattacharjee, et al.
Chemical Reviews (2024) Vol. 124, Iss. 18, pp. 10281-10362
Closed Access | Times Cited: 9
Pyrrolysine Aminoacyl-tRNA Synthetase as a Tool for Expanding the Genetic Code
Anastasia Dakhnevich, Alisa Kazakova, Danila Iliushin, et al.
International Journal of Molecular Sciences (2025) Vol. 26, Iss. 2, pp. 539-539
Open Access
An expanded phylogenomic analysis of Heterolobosea reveals the deep relationships, non-canonical genetic codes, and cryptic flagellate stages in the group
Tomáš Pánek, Alexander K. Tice, Pierre Corre, et al.
Molecular Phylogenetics and Evolution (2025), pp. 108289-108289
Closed Access
Engineering of Silkworm Tyrosyl-tRNA Synthetase Variants to Create Halogenated Silk Fiber with Improved Thermal Stability
Hidetoshi Teramoto, Y. Amano, Katsura Kojima, et al.
Biomacromolecules (2025)
Closed Access
Therapeutic applications of genetic code expansion
Yujia Huang, Tao Liu
Synthetic and Systems Biotechnology (2018) Vol. 3, Iss. 3, pp. 150-158
Open Access | Times Cited: 67
Engineered ribosomes with tethered subunits for expanding biological function
Erik D. Carlson, Anne E. d’Aquino, Do Soon Kim, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 64
Resurrecting the Bacterial Tyrosyl-tRNA Synthetase/tRNA Pair for Expanding the Genetic Code of Both E. coli and Eukaryotes
James S. Italia, Christopher Latour, Chester J. J. Wrobel, et al.
Cell chemical biology (2018) Vol. 25, Iss. 10, pp. 1304-1312.e5
Open Access | Times Cited: 60
Evolution of plant mutagenesis tools: a shifting paradigm from random to targeted genome editing
Rahul Mahadev Shelake, Dibyajyoti Pramanik, Jae‐Yean Kim
Plant Biotechnology Reports (2019) Vol. 13, Iss. 5, pp. 423-445
Closed Access | Times Cited: 57
Transgene Biocontainment Strategies for Molecular Farming
Michael Clark, Maciej Maselko
Frontiers in Plant Science (2020) Vol. 11
Open Access | Times Cited: 57
Synthetic Genomes
Weimin Zhang, Leslie A. Mitchell, Joel S. Bader, et al.
Annual Review of Biochemistry (2020) Vol. 89, Iss. 1, pp. 77-101
Closed Access | Times Cited: 56
Synthetic Biological Circuits within an Orthogonal Central Dogma
Alan Costello, Ahmed H. Badran
Trends in biotechnology (2020) Vol. 39, Iss. 1, pp. 59-71
Open Access | Times Cited: 55
Multiplex suppression of four quadruplet codons via tRNA directed evolution
Erika A. DeBenedictis, Gavriela D. Carver, Christina Z. Chung, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 45
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