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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:

Utility of B-Factors in Protein Science: Interpreting Rigidity, Flexibility, and Internal Motion and Engineering Thermostability
Zhoutong Sun, Qian Liu, Ge Qu, et al.
Chemical Reviews (2019) Vol. 119, Iss. 3, pp. 1626-1665
Closed Access | Times Cited: 421

Showing 1-25 of 421 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
The Crucial Role of Methodology Development in Directed Evolution of Selective Enzymes
Ge Qu, Aitao Li, Carlos G. Acevedo‐Rocha, et al.
Angewandte Chemie International Edition (2019) Vol. 59, Iss. 32, pp. 13204-13231
Closed Access | Times Cited: 386
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
Advances in ultrahigh-throughput screening for directed enzyme evolution
Ulrich Markel, Khalil Essani, Volkan Besirlioglu, et al.
Chemical Society Reviews (2019) Vol. 49, Iss. 1, pp. 233-262
Closed Access | Times Cited: 212
Protein X-ray Crystallography and Drug Discovery
Laurent Maveyraud, Lionel Mourey
Molecules (2020) Vol. 25, Iss. 5, pp. 1030-1030
Open Access | Times Cited: 186
Stereodivergent Protein Engineering of a Lipase To Access All Possible Stereoisomers of Chiral Esters with Two Stereocenters
Jian Xu, Yixin Cen, Warispreet Singh, et al.
Journal of the American Chemical Society (2019) Vol. 141, Iss. 19, pp. 7934-7945
Open Access | Times Cited: 141
Thermal stability enhancement: Fundamental concepts of protein engineering strategies to manipulate the flexible structure
Mahdie Rahban, Samaneh Zolghadri, Najmeh Salehi, et al.
International Journal of Biological Macromolecules (2022) Vol. 214, pp. 642-654
Closed Access | Times Cited: 69
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
AlphaFold2 Can Predict Single-Mutation Effects
J. Michael McBride, Konstantin Polev, Amirbek Abdirasulov, et al.
Physical Review Letters (2023) Vol. 131, Iss. 21
Open Access | Times Cited: 39
Automated in vivo enzyme engineering accelerates biocatalyst optimization
Enrico Orsi, Lennart Schada von Borzyskowski, Stephan Noack, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 18
Enhancing efficiency of protein language models with minimal wet-lab data through few-shot learning
Ziyi Zhou, Liang Zhang, Yuanxi Yu, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 16
Machine learning-guided co-optimization of fitness and diversity facilitates combinatorial library design in enzyme engineering
Kerr Ding, M. A. Chin, Yunlong Zhao, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 13
MISATO: machine learning dataset of protein–ligand complexes for structure-based drug discovery
Till Siebenmorgen, Filipe Menezes, Sabrina Benassou, et al.
Nature Computational Science (2024) Vol. 4, Iss. 5, pp. 367-378
Open Access | Times Cited: 12
Can Machine Learning Revolutionize Directed Evolution of Selective Enzymes?
Guangyue Li, Yijie Dong, Manfred T. Reetz
Advanced Synthesis & Catalysis (2019) Vol. 361, Iss. 11, pp. 2377-2386
Open Access | Times Cited: 111
Light‐Driven Kinetic Resolution of α‐Functionalized Carboxylic Acids Enabled by an Engineered Fatty Acid Photodecarboxylase
Jian Xu, Yujing Hu, Jiajie Fan, et al.
Angewandte Chemie International Edition (2019) Vol. 58, Iss. 25, pp. 8474-8478
Closed Access | Times Cited: 90
Unlocking the Stereoselectivity and Substrate Acceptance of Enzymes: Proline‐Induced Loop Engineering Test
Ge Qu, Yuexin Bi, Beibei Liu, et al.
Angewandte Chemie International Edition (2021) Vol. 61, Iss. 1
Closed Access | Times Cited: 64
Overview of strategies for developing high thermostability industrial enzymes: Discovery, mechanism, modification and challenges
Hao Wu, Qiuming Chen, Wenli Zhang, et al.
Critical Reviews in Food Science and Nutrition (2021) Vol. 63, Iss. 14, pp. 2057-2073
Closed Access | Times Cited: 57
Hot spots-making directed evolution easier
Haoran Yu, Shuang Ma, Yiwen Li, et al.
Biotechnology Advances (2022) Vol. 56, pp. 107926-107926
Open Access | Times Cited: 56
Protein design via deep learning
Wenze Ding, Kenta Nakai, Haipeng Gong
Briefings in Bioinformatics (2022) Vol. 23, Iss. 3
Open Access | Times Cited: 56
Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance
Haiyang Cui, Lobna Eltoukhy, Lingling Zhang, et al.
Angewandte Chemie International Edition (2021) Vol. 60, Iss. 20, pp. 11448-11456
Open Access | Times Cited: 54
Effects of cryo-EM cooling on structural ensembles
Lars V. Bock, Helmut Grubmüller
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 54
Mass Spectrometry Methods for Measuring Protein Stability
Daniel D. Vallejo, Carolina Rojas Ramírez, Kristine F. Parson, et al.
Chemical Reviews (2022) Vol. 122, Iss. 8, pp. 7690-7719
Open Access | Times Cited: 53
Engineering functional thermostable proteins using ancestral sequence reconstruction
Raine E. S. Thomson, Saskya E. Carrera-Pacheco, Elizabeth M. J. Gillam
Journal of Biological Chemistry (2022) Vol. 298, Iss. 10, pp. 102435-102435
Open Access | Times Cited: 48
Genome interpretation using in silico predictors of variant impact
Panagiotis Katsonis, Kevin Wilhelm, Amanda M. Williams, et al.
Human Genetics (2022) Vol. 141, Iss. 10, pp. 1549-1577
Open Access | Times Cited: 47
Enhancement of the degradation capacity of IsPETase for PET plastic degradation by protein engineering
Yidi Liu, Zhanzhi Liu, Zhiyong Guo, et al.
The Science of The Total Environment (2022) Vol. 834, pp. 154947-154947
Closed Access | Times Cited: 46
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