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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:

Protein engineering: the potential of remote mutations
Matthew Wilding, Nansook Hong, Matthew A. Spence, et al.
Biochemical Society Transactions (2019) Vol. 47, Iss. 2, pp. 701-711
Open Access | Times Cited: 86

Showing 1-25 of 86 citing articles:

The Role of Conformational Dynamics and Allostery in Modulating Protein Evolution
Paul Campitelli, Tushar Modi, Sudhir Kumar, et al.
Annual Review of Biophysics (2020) Vol. 49, Iss. 1, pp. 267-288
Open Access | Times Cited: 155
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: 81
Complete Depolymerization of PET Wastes by an Evolved PET Hydrolase from Directed Evolution
Lixia Shi, Pi Liu, Zijian Tan, et al.
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 14
Closed Access | Times Cited: 81
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: 52
Evolution of new enzymes by gene duplication and divergence
Shelley D. Copley
FEBS Journal (2020) Vol. 287, Iss. 7, pp. 1262-1283
Open Access | Times Cited: 117
Hinge-shift mechanism as a protein design principle for the evolution of β-lactamases from substrate promiscuity to specificity
Tushar Modi, Valeria A. Risso, Sergio Martı́nez-Rodrı́guez, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 61
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: 51
Engineering Enzyme Properties for Improved Biocatalytic Processes in Batch and Continuous Flow
Raquel Abdallah da Rocha, Robert Speight, Colin Scott
Organic Process Research & Development (2022) Vol. 26, Iss. 7, pp. 1914-1924
Open Access | Times Cited: 45
Temporal and spatial resolution of distal protein motions that activate hydrogen tunneling in soybean lipoxygenase
Jan Paulo T. Zaragoza, Adam R. Offenbacher, Shenshen Hu, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 10
Open Access | Times Cited: 30
Designed active-site library reveals thousands of functional GFP variants
Jonathan J. Weinstein, Carlos Martí‐Gómez, Rosalie Lipsh‐Sokolik, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 25
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: 69
A mechanistic view of enzyme evolution
Gloria Yang, C.M. Miton, Nobuhiko Tokuriki
Protein Science (2020) Vol. 29, Iss. 8, pp. 1724-1747
Open Access | Times Cited: 67
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: 64
Ancestral sequence reconstruction produces thermally stable enzymes with mesophilic enzyme-like catalytic properties
Ryutaro Furukawa, Wakako Toma, Koji Yamazaki, et al.
Scientific Reports (2020) Vol. 10, Iss. 1
Open Access | Times Cited: 57
A beginner's guide to molecular dynamics simulations and the identification of cross-correlation networks for enzyme engineering
Haoran Yu, Paul A. Dalby
Methods in enzymology on CD-ROM/Methods in enzymology (2020), pp. 15-49
Closed Access | Times Cited: 51
Enhancing computational enzyme design by a maximum entropy strategy
Wen Jun Xie, Mojgan Asadi, Arieh Warshel
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 7
Open Access | Times Cited: 34
Dynamic coupling of residues within proteins as a mechanistic foundation of many enigmatic pathogenic missense variants
Nicholas J. Ose, Brandon M. Butler, Avishek Kumar, et al.
PLoS Computational Biology (2022) Vol. 18, Iss. 4, pp. e1010006-e1010006
Open Access | Times Cited: 29
Perspectives on improving crop Rubisco by directed evolution
Matteo Gionfriddo, Timothy Rhodes, Spencer M. Whitney
Seminars in Cell and Developmental Biology (2023) Vol. 155, pp. 37-47
Closed Access | Times Cited: 19
Addressing epistasis in the design of protein function
Rosalie Lipsh‐Sokolik, Sarel J. Fleishman
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 34
Open Access | Times Cited: 7
Electric Fields Are a Key Determinant of Carbapenemase Activity in Class A β-Lactamases
Hira Jabeen, Michael Beer, James Spencer, et al.
ACS Catalysis (2024) Vol. 14, Iss. 9, pp. 7166-7172
Open Access | Times Cited: 6
Tailoring Tryptophan Synthase TrpB for Selective Quaternary Carbon Bond Formation
Markus Dick, Nicholas S. Sarai, Michael W. Martynowycz, et al.
Journal of the American Chemical Society (2019) Vol. 141, Iss. 50, pp. 19817-19822
Open Access | Times Cited: 52
Practically useful protein-design methods combining phylogenetic and atomistic calculations
Jonathan J. Weinstein, Olga Khersonsky, Sarel J. Fleishman
Current Opinion in Structural Biology (2020) Vol. 63, pp. 58-64
Open Access | Times Cited: 43
Substitutions at Nonconserved Rheostat Positions Modulate Function by Rewiring Long-Range, Dynamic Interactions
Paul Campitelli, Liskin Swint‐Kruse, S. Banu Ozkan
Molecular Biology and Evolution (2020) Vol. 38, Iss. 1, pp. 201-214
Open Access | Times Cited: 41
Nature-inspired Enzyme engineering and sustainable catalysis: biochemical clues from the world of plants and extremophiles
Anwesha Chatterjee, Sonakshi Puri, Pankaj Kumar Sharma, et al.
Frontiers in Bioengineering and Biotechnology (2023) Vol. 11
Open Access | Times Cited: 15
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: 39
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