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:

Computational Design of Stable and Soluble Biocatalysts
Miloš Musil, Hannes Konegger, Jiří Hon, et al.
ACS Catalysis (2018) Vol. 9, Iss. 2, pp. 1033-1054
Open Access | Times Cited: 125

Showing 1-25 of 125 citing articles:

Computational Redesign of a PETase for Plastic Biodegradation under Ambient Condition by the GRAPE Strategy
Yinglu Cui, Yanchun Chen, Xinyue Liu, et al.
ACS Catalysis (2021) Vol. 11, Iss. 3, pp. 1340-1350
Closed Access | Times Cited: 399

Machine Learning in Enzyme Engineering
Stanislav Mazurenko, Zbyněk Prokop, Jiřı́ Damborský
ACS Catalysis (2019) Vol. 10, Iss. 2, pp. 1210-1223
Open Access | Times Cited: 328

Power of Biocatalysis for Organic Synthesis
Christoph K. Winkler, Joerg H. Schrittwieser, Wolfgang Kroutil
ACS Central Science (2021) Vol. 7, Iss. 1, pp. 55-71
Open Access | Times Cited: 266

Machine learning-enabled retrobiosynthesis of molecules
Tianhao Yu, Aashutosh Girish Boob, Michael Volk, et al.
Nature Catalysis (2023) Vol. 6, Iss. 2, pp. 137-151
Closed Access | Times Cited: 61

Role of distal sites in enzyme engineering
Jie Gu, Yan Xu, Yao Nie
Biotechnology Advances (2023) Vol. 63, pp. 108094-108094
Closed Access | Times Cited: 43

SoluProt: prediction of soluble protein expression inEscherichia coli
Jiří Hon, Martin Marusiak, Tomáš Martínek, et al.
Bioinformatics (2020) Vol. 37, Iss. 1, pp. 23-28
Open Access | Times Cited: 120

Catalytic Asymmetric Hydroalkoxylation of C–C Multiple Bonds
Jennifer L. Kennemur, Rajat Maji, Manuel J. Scharf, et al.
Chemical Reviews (2021) Vol. 121, Iss. 24, pp. 14649-14681
Open Access | Times Cited: 91

FireProtDB: database of manually curated protein stability data
Jan Štourač, Juraj Dúbrava, Miloš Musil, et al.
Nucleic Acids Research (2020) Vol. 49, Iss. D1, pp. D319-D324
Open Access | Times Cited: 90

EnzymeMiner: automated mining of soluble enzymes with diverse structures, catalytic properties and stabilities
Jiří Hon, Simeon Borko, Jan Štourač, et al.
Nucleic Acids Research (2020) Vol. 48, Iss. W1, pp. W104-W109
Open Access | Times Cited: 74

Computer-Aided Targeted Mutagenesis of Thermoclostridium caenicola d-Allulose 3-Epimerase for Improved Thermostability
Jiajun Chen, Chen Ding, Qiuming Chen, et al.
Journal of Agricultural and Food Chemistry (2022) Vol. 70, Iss. 6, pp. 1943-1951
Closed Access | Times Cited: 45

Computational enzyme redesign: large jumps in function
Yinglu Cui, Jinyuan Sun, Bian Wu
Trends in Chemistry (2022) Vol. 4, Iss. 5, pp. 409-419
Closed Access | Times Cited: 36

Counteraction of stability-activity trade-off of Nattokinase through flexible region shifting
Jie Luo, Chenshuo Song, Wenjing Cui, et al.
Food Chemistry (2023) Vol. 423, pp. 136241-136241
Closed Access | Times Cited: 30

Accelerating Biocatalysis Discovery with Machine Learning: A Paradigm Shift in Enzyme Engineering, Discovery, and Design
Braun Markus, Gruber Christian C, Krassnigg Andreas, et al.
ACS Catalysis (2023) Vol. 13, Iss. 21, pp. 14454-14469
Open Access | Times Cited: 29

Advancing Enzyme’s Stability and Catalytic Efficiency through Synergy of Force-Field Calculations, Evolutionary Analysis, and Machine Learning
Antonín Kunka, Sérgio M. Marques, Martin Havlasek, et al.
ACS Catalysis (2023) Vol. 13, Iss. 19, pp. 12506-12518
Open Access | Times Cited: 25

FireProt 2.0: web-based platform for the fully automated design of thermostable proteins
Miloš Musil, Andrej Jezik, Jana Horackova, et al.
Briefings in Bioinformatics (2023) Vol. 25, Iss. 1
Open Access | Times Cited: 22

Protein Engineering with Lightweight Graph Denoising Neural Networks
Bingxin Zhou, Lirong Zheng, Banghao Wu, et al.
Journal of Chemical Information and Modeling (2024) Vol. 64, Iss. 9, pp. 3650-3661
Open Access | Times Cited: 8

Unlocking the potential of enzyme engineering via rational computational design strategies
Lei Zhou, Chunmeng Tao, Xiaolin Shen, et al.
Biotechnology Advances (2024) Vol. 73, pp. 108376-108376
Closed Access | Times Cited: 7

Computational Enzyme Redesign Enhances Tolerance to Denaturants for Peptide C-Terminal Amidation
Tong Zhu, Jinyuan Sun, Hua Pang, et al.
JACS Au (2024) Vol. 4, Iss. 2, pp. 788-797
Open Access | Times Cited: 6

Biocatalytic enzymes in food packaging, biomedical, and biotechnological applications: A comprehensive review
Palanisamy Vasudhevan, Ruoyu Zhang, Hui Ma, et al.
International Journal of Biological Macromolecules (2025), pp. 140069-140069
Closed Access

A Practical Guide to Computational Tools for Engineering Biocatalytic Properties
Aitor Vega, Antoni Planas, Xevi Biarnés
International Journal of Molecular Sciences (2025) Vol. 26, Iss. 3, pp. 980-980
Open Access

Robust ω-Transaminases by Computational Stabilization of the Subunit Interface
Qinglong Meng, Nikolas Capra, Cyntia M. Palacio, et al.
ACS Catalysis (2020) Vol. 10, Iss. 5, pp. 2915-2928
Open Access | Times Cited: 66

One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates
Sara Arana‐Peña, Diego Carballares, Ángel Berenguer‐Murcia, et al.
Catalysts (2020) Vol. 10, Iss. 6, pp. 605-605
Open Access | Times Cited: 66

Evaluating Protein Engineering Thermostability Prediction Tools Using an Independently Generated Dataset
Peishan Huang, Simon K. S. Chu, Henrique N. Frizzo, et al.
ACS Omega (2020) Vol. 5, Iss. 12, pp. 6487-6493
Open Access | Times Cited: 62

Recent advances in user-friendly computational tools to engineer protein function
Carlos Eduardo Sequeiros-Borja, Bartłomiej Surpeta, Jan Brezovský
Briefings in Bioinformatics (2020) Vol. 22, Iss. 3
Open Access | Times Cited: 60

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