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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:

NMR-guided directed evolution
Sagar Bhattacharya, Eleonora Margheritis, Katsuya Takahashi, et al.
Nature (2022) Vol. 610, Iss. 7931, pp. 389-393
Open Access | Times Cited: 39

Showing 1-25 of 39 citing articles:

Engineered enzymes for the synthesis of pharmaceuticals and other high-value products
Manfred T. Reetz, Ge Qu, Zhoutong Sun
Nature Synthesis (2024) Vol. 3, Iss. 1, pp. 19-32
Closed Access | Times Cited: 58
Learning from Protein Engineering by Deconvolution of Multi‐Mutational Variants
Frank Hollmann, Joaquin Sanchis, Manfred T. Reetz
Angewandte Chemie International Edition (2024) Vol. 63, Iss. 36
Open Access | Times Cited: 11
Enzyme engineering for biocatalysis
Caroline E. Paul, Ulf Hanefeld, Frank Hollmann, et al.
Molecular Catalysis (2024) Vol. 555, pp. 113874-113874
Open Access | Times Cited: 9
Efficient searches in protein sequence space through AI-driven iterative learning
Ignacio Suarez-Martin, Valeria A. Risso, Rocío Romero-Záliz, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Closed Access
Exploring and Learning the Universe of Protein Allostery Using Artificial Intelligence Augmented Biophysical and Computational Approaches
Steve Agajanian, Mohammed Alshahrani, Fang Bai, et al.
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 5, pp. 1413-1428
Closed Access | Times Cited: 19
Structure-based investigation of a DNA aptamer targeting PTK7 reveals an intricate 3D fold guiding functional optimization
Axin He, Liqi Wan, Yuchao Zhang, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 29
Open Access | Times Cited: 5
Rational enzyme design by reducing the number of hotspots and library size
Zongmin Qin, Bo Yuan, Ge Qu, et al.
Chemical Communications (2024) Vol. 60, Iss. 76, pp. 10451-10463
Closed Access | Times Cited: 4
Protein Representations: Encoding Biological Information for Machine Learning in Biocatalysis
David Harding-Larsen, Jonathan Funk, Niklas Gesmar Madsen, et al.
(2024)
Open Access | Times Cited: 3
Advances in aldo-keto reductases immobilization for biocatalytic synthesis of chiral alcohol
Wen Zhang, Zi-Qing Shao, Zhi‐Xiu Wang, et al.
International Journal of Biological Macromolecules (2024) Vol. 274, pp. 133264-133264
Closed Access | Times Cited: 3
N-terminal truncation (N-) and directional proton transfer in an old yellow enzyme enables tunable efficient producing (R)- or (S)-citronellal
Jie Zhang, Yueshu Li, Hui Gao, et al.
International Journal of Biological Macromolecules (2024) Vol. 262, pp. 130129-130129
Closed Access | Times Cited: 3
Creating new-to-nature carbon fixation: A guide
Helena Schulz-Mirbach, Beau Dronsella, Hai He, et al.
Metabolic Engineering (2023) Vol. 82, pp. 12-28
Closed Access | Times Cited: 9
Protein representations: Encoding biological information for machine learning in biocatalysis
David Harding-Larsen, Jonathan Funk, Niklas Gesmar Madsen, et al.
Biotechnology Advances (2024) Vol. 77, pp. 108459-108459
Closed Access | Times Cited: 2
Second-Shell Residues Contribute to Catalysis by Predominately Preorganizing the Apo State in PafA
Jiahua Deng, Qiang Cui
Journal of the American Chemical Society (2023) Vol. 145, Iss. 20, pp. 11333-11347
Closed Access | Times Cited: 7
Understanding Protein Functions in the Biological Context
Tianwen Wang, Wei Zhang
Protein and Peptide Letters (2023) Vol. 30, Iss. 6, pp. 449-458
Closed Access | Times Cited: 6
Multiple Functions of Compatible Solute Ectoine and Strategies for Constructing Overproducers for Biobased Production
Wei Zhang, Kun Liu, Fang Kong, et al.
Molecular Biotechnology (2023) Vol. 66, Iss. 8, pp. 1772-1785
Closed Access | Times Cited: 5
Biomolecular NMR in the AI-assisted structural biology era: Old tricks and new opportunities
Theodoros K. Karamanos, Stephen Matthews
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (2023) Vol. 1872, Iss. 2, pp. 140949-140949
Open Access | Times Cited: 5
Fishing for Catalysis: Experimental Approaches to Narrowing Search Space in Directed Evolution of Enzymes
Liam R. Marshall, Sagar Bhattacharya, Ivan V. Korendovych
JACS Au (2023) Vol. 3, Iss. 9, pp. 2402-2412
Open Access | Times Cited: 5
Hotspot Wizard‐informed engineering of a hyperthermophilic β‐glucosidase for enhanced enzyme activity at low temperatures
Mehmet Emre Erkanli, Khalid El‐Halabi, Ted Keunsil Kang, et al.
Biotechnology and Bioengineering (2024) Vol. 121, Iss. 7, pp. 2079-2090
Closed Access | Times Cited: 1
Protection of Catalytic Cofactors by Polypeptides as a Driver for the Emergence of Primordial Enzymes
Luis I. Gutierrez-Rus, Gloria Gamiz-Arco, J.A. Gavira, et al.
Molecular Biology and Evolution (2023) Vol. 40, Iss. 6
Open Access | Times Cited: 4
Rational design of an artificial ethylbenzene hydroxylase using a molecular dynamics simulation to enhance enantioselectivity
Koji Oohora, Yoshiyuki Kagawa, Takako Nishiura, et al.
Chemistry Letters (2023) Vol. 53, Iss. 2
Open Access | Times Cited: 3
Efficient Base-Catalyzed Kemp Elimination in an Engineered Ancestral Enzyme
Luis I. Gutierrez-Rus, Miguel Alcalde, Valeria A. Risso, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 16, pp. 8934-8934
Open Access | Times Cited: 6
Engineering of a P450-based Kemp eliminase with a new mechanism
Aitao Li, Qian Wang, Xitong Song, et al.
CHINESE JOURNAL OF CATALYSIS (CHINESE VERSION) (2023) Vol. 47, pp. 191-199
Open Access | Times Cited: 2
Allostery at a protein-protein interface harboring an intermolecular dynamic network
Sara Medina Gomez, Suresh K. Vasa, Rasmus Linser
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Binding versus Catalysis in <em>De Novo</em> Enzyme Design<strong> </strong>
José M. Sánchez‐Ruiz
(2024)
Open Access
Lernen aus Protein‐Engineering durch Dekonvolution von Multi‐Mutationalen Enzymvarianten**
Frank Hollmann, Joaquin Sanchis, Manfred T. Reetz
Angewandte Chemie (2024) Vol. 136, Iss. 36
Open Access
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