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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:

Predicting protein stability and solubility changes upon mutations: data perspective
Stanislav Mazurenko
ChemCatChem (2020) Vol. 12, Iss. 22, pp. 5590-5598
Open Access | Times Cited: 31

Showing 1-25 of 31 citing articles:

Recent trends in biocatalysis
Dong Yi, Thomas Bayer, Christoffel P. S. Badenhorst, et al.
Chemical Society Reviews (2021) Vol. 50, Iss. 14, pp. 8003-8049
Open Access | Times Cited: 264
Machine Learning-Guided Protein Engineering
Petr Kouba, Pavel Kohout, Faraneh Haddadi, et al.
ACS Catalysis (2023) Vol. 13, Iss. 21, pp. 13863-13895
Open Access | Times Cited: 65
Transfer learning to leverage larger datasets for improved prediction of protein stability changes
Henry Dieckhaus, Michael Brocidiacono, Nicholas Z. Randolph, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 6
Open Access | Times Cited: 34
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
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
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
Modern Approaches to Protein Constructions: A Comprehensive Review of Computational Tools and Databases for De Novo Protein Design and Engineering
Md. Mojnu Mia, Habiba Sultana, Md. Al Amin, et al.
Engineering Reports (2025) Vol. 7, Iss. 2
Open Access
Web-based tools for computational enzyme design
Sérgio M. Marques, Joan Planas-Iglesias, Jiřı́ Damborský
Current Opinion in Structural Biology (2021) Vol. 69, pp. 19-34
Open Access | Times Cited: 50
Assessing the performance of computational predictors for estimating protein stability changes upon missense mutations
Shahid Iqbal, Fuyi Li, Tatsuya Akutsu, et al.
Briefings in Bioinformatics (2021) Vol. 22, Iss. 6
Closed Access | Times Cited: 45
Recent Advances in β-Glucosidase Sequence and Structure Engineering: A Brief Review
Bei Ouyang, Guoping Wang, Nian Zhang, et al.
Molecules (2023) Vol. 28, Iss. 13, pp. 4990-4990
Open Access | Times Cited: 18
Transfer learning to leverage larger datasets for improved prediction of protein stability changes
Henry Dieckhaus, Michael Brocidiacono, Nicholas Z. Randolph, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 13
In-depth analysis of biocatalysts by microfluidics: An emerging source of data for machine learning
Michal Vasina, David Kovář, Jiřı́ Damborský, et al.
Biotechnology Advances (2023) Vol. 66, pp. 108171-108171
Closed Access | Times Cited: 12
TISIGNER.com: web services for improving recombinant protein production
Bikash Kumar Bhandari, Chun Shen Lim, Paul P. Gardner
Nucleic Acids Research (2021) Vol. 49, Iss. W1, pp. W654-W661
Open Access | Times Cited: 27
SCONES: Self-Consistent Neural Network for Protein Stability Prediction Upon Mutation
Yashas B. L. Samaga, Shampa Raghunathan, U. Deva Priyakumar
The Journal of Physical Chemistry B (2021) Vol. 125, Iss. 38, pp. 10657-10671
Closed Access | Times Cited: 25
Data set and fitting dependencies when estimating protein mutant stability: Toward simple, balanced, and interpretable models
Kristoffer T. Bæk, Kasper P. Kepp
Journal of Computational Chemistry (2022) Vol. 43, Iss. 8, pp. 504-518
Open Access | Times Cited: 17
The role of data imbalance bias in the prediction of protein stability change upon mutation
Jianwen Fang
PLoS ONE (2023) Vol. 18, Iss. 3, pp. e0283727-e0283727
Open Access | Times Cited: 8
Revolutionizing biocatalysis: A review on innovative design and applications of enzyme-immobilized microfluidic devices
Pravin D. Patil, Niharika Gargate, Khushi Dongarsane, et al.
International Journal of Biological Macromolecules (2024), pp. 136193-136193
Closed Access | Times Cited: 2
Curse and Blessing of Non‐Proteinogenic Parts in Computational Enzyme Engineering
Kerlen T. Korbeld, Maximilian J. L. J. Fürst
ChemBioChem (2023) Vol. 24, Iss. 12
Open Access | Times Cited: 6
Decoding the intricate network of molecular interactions of a hyperstable engineered biocatalyst
Klára Marková, Klaudia Chmelova, Sérgio M. Marques, et al.
Chemical Science (2020) Vol. 11, Iss. 41, pp. 11162-11178
Open Access | Times Cited: 18
Data Analytics for Catalysis Predictions: Are We Ready Yet?
Difan Zhang, Brett A. Smith, Haiyi Wu, et al.
ACS Catalysis (2024) Vol. 14, Iss. 10, pp. 8073-8086
Closed Access | Times Cited: 1
Exploring the Effect of Enhanced Sampling on Protein Stability Prediction
Daniel Markthaler, Maximilian Fleck, Bartosz Stankiewicz, et al.
Journal of Chemical Theory and Computation (2022) Vol. 18, Iss. 4, pp. 2569-2583
Closed Access | Times Cited: 9
Target‐template relationships in protein structure prediction and their effect on the accuracy of thermostability calculations
Muyun Lihan, Dmitry Lupyan, Daniel P. Oehme
Protein Science (2022) Vol. 32, Iss. 2
Open Access | Times Cited: 8
Development of an Ontology for Biocatalysis
Marian J. Menke, Alexander S. Behr, Katrin Rosenthal, et al.
Chemie Ingenieur Technik (2022) Vol. 94, Iss. 11, pp. 1827-1835
Open Access | Times Cited: 5
Introducing glutamic acid residues to acyl-ACP reductase to enhance alka(e)ne production in Escherichia coli: computer-aided design and subsequent experimental validation
Jiahu Han, Takuya Matsumoto, Ryosuke Yamada, et al.
Biochemical and Biophysical Research Communications (2024) Vol. 745, pp. 151237-151237
Closed Access
Web-based Tools for Computational Enzyme Design
Sérgio M. Marques, Joan Planas-Iglesias, Jiřı́ Damborský
(2020)
Open Access | Times Cited: 4
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