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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:

Machine-Learning-Guided Mutagenesis for Directed Evolution of Fluorescent Proteins
Yutaka Saitô, Misaki Oikawa, Hikaru Nakazawa, et al.
ACS Synthetic Biology (2018) Vol. 7, Iss. 9, pp. 2014-2022
Open Access | Times Cited: 142

Showing 26-50 of 142 citing articles:

Emerging Technologies for Biocatalysis in the Pharmaceutical Industry
Russell D. Lewis, Scott P. France, Carlos A. Martínez
ACS Catalysis (2023) Vol. 13, Iss. 8, pp. 5571-5577
Open Access | Times Cited: 24
Biophysics-based protein language models for protein engineering
Sam Gelman, Bryce Johnson, Chase R. Freschlin, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 9
Engineering of highly active and diverse nuclease enzymes by combining machine learning and ultra-high-throughput screening
Neil Thomas, David Belanger, Chenling Xu, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 8
Enhanced Sequence-Activity Mapping and Evolution of Artificial Metalloenzymes by Active Learning
Tobias Vornholt, Mojmír Mutný, Gregor W. Schmidt, et al.
ACS Central Science (2024) Vol. 10, Iss. 7, pp. 1357-1370
Open Access | Times Cited: 7
Machine learning-guided engineering of genetically encoded fluorescent calcium indicators
Sarah J. Wait, Marc Expòsit, Sophia Lin, et al.
Nature Computational Science (2024) Vol. 4, Iss. 3, pp. 224-236
Open Access | Times Cited: 6
Status of Biocatalysis in the Production of 2,5-Furandicarboxylic Acid
Derek Troiano, Valérie Orsat, Marie‐Josée Dumont
ACS Catalysis (2020) Vol. 10, Iss. 16, pp. 9145-9169
Closed Access | Times Cited: 60
Directed evolution for enzyme development in biocatalysis
Serena Gargiulo, Patrice Soumillion
Current Opinion in Chemical Biology (2020) Vol. 61, pp. 107-113
Closed Access | Times Cited: 53
Cluster learning-assisted directed evolution
Yuchi Qiu, Jian Hu, Guo‐Wei Wei
Nature Computational Science (2021) Vol. 1, Iss. 12, pp. 809-818
Open Access | Times Cited: 50
Genetically Encodable Fluorescent and Bioluminescent Biosensors Light Up Signaling Networks
Xin Zhou, Sohum Mehta, Jin Zhang
Trends in Biochemical Sciences (2020) Vol. 45, Iss. 10, pp. 889-905
Open Access | Times Cited: 49
Beyond natural: synthetic expansions of botanical form and function
Nicola J. Patron
New Phytologist (2020) Vol. 227, Iss. 2, pp. 295-310
Open Access | Times Cited: 48
Machine-Learning-Guided Library Design Cycle for Directed Evolution of Enzymes: The Effects of Training Data Composition on Sequence Space Exploration
Yutaka Saitô, Misaki Oikawa, Takumi Sato, et al.
ACS Catalysis (2021) Vol. 11, Iss. 23, pp. 14615-14624
Open Access | Times Cited: 46
Data-driven computational protein design
Vincent Frappier, Amy E. Keating
Current Opinion in Structural Biology (2021) Vol. 69, pp. 63-69
Open Access | Times Cited: 39
Learning protein fitness landscapes with deep mutational scanning data from multiple sources
Lin Chen, Zehong Zhang, Zhenghao Li, et al.
Cell Systems (2023) Vol. 14, Iss. 8, pp. 706-721.e5
Open Access | Times Cited: 19
Machine Learning: A Suitable Method for Biocatalysis
Pedro Sampaio, Pedro Fernandes
Catalysts (2023) Vol. 13, Iss. 6, pp. 961-961
Open Access | Times Cited: 15
Low-N protein engineering with data-efficient deep learning
Surojit Biswas, Grigory Khimulya, Ethan C. Alley, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 46
UMI-linked consensus sequencing enables phylogenetic analysis of directed evolution
Paul Jannis Zurek, Philipp Knyphausen, Katharina Neufeld, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 38
Improved Bst DNA Polymerase Variants Derived via a Machine Learning Approach
Inyup Paik, Phuoc H. T. Ngo, Raghav Shroff, et al.
Biochemistry (2021) Vol. 62, Iss. 2, pp. 410-418
Open Access | Times Cited: 35
The evolving art of creating genetic diversity: From directed evolution to synthetic biology
Andrew Currin, Steven J. Parker, Christopher Robinson, et al.
Biotechnology Advances (2021) Vol. 50, pp. 107762-107762
Open Access | Times Cited: 33
Inverse folding of protein complexes with a structure-informed language model enables unsupervised antibody evolution
Varun R. Shanker, Theodora U. J. Bruun, Brian Hie, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 13
Discrimination of psychrophilic enzymes using machine learning algorithms with amino acid composition descriptor
Ailan Huang, Fuping Lu, Fufeng Liu
Frontiers in Microbiology (2023) Vol. 14
Open Access | Times Cited: 12
Machine Learning for Protein Engineering
Kadina E. Johnston, Clara Fannjiang, Bruce J. Wittmann, et al.
Challenges and advances in computational chemistry and physics (2023), pp. 277-311
Closed Access | Times Cited: 11
Transforming drug development with synthetic biology and AI
Andrew Hill, Jane M. True, Charles H. Jones
Trends in biotechnology (2024) Vol. 42, Iss. 9, pp. 1072-1075
Open Access | Times Cited: 3
Functional Enhancement of Flavin-Containing Monooxygenase through Machine Learning Methodology
Takuma Matsushita, Shinji Kishimoto, Kodai Hara, et al.
ACS Catalysis (2024) Vol. 14, Iss. 9, pp. 6945-6951
Closed Access | Times Cited: 3
A new era in healthcare: The integration of artificial intelligence and microbial
Da-Liang Huo, Xiaogang Wang
Medicine in Novel Technology and Devices (2024) Vol. 23, pp. 100319-100319
Open Access | Times Cited: 3
Machine Learning Enables Selection of Epistatic Enzyme Mutants for Stability Against Unfolding and Detrimental Aggregation
Guangyue Li, Youcai Qin, Nicolas Fontaine, et al.
ChemBioChem (2020) Vol. 22, Iss. 5, pp. 904-914
Open Access | Times Cited: 31

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