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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:

Pervasive cooperative mutational effects on multiple catalytic enzyme traits emerge via long-range conformational dynamics
Carlos G. Acevedo‐Rocha, Aitao Li, Lorenzo D’Amore, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 96

Showing 1-25 of 96 citing articles:

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: 90
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: 69
Opportunities and Challenges for Machine Learning-Assisted Enzyme Engineering
Jason Yang, Francesca-Zhoufan Li, Frances H. Arnold
ACS Central Science (2024) Vol. 10, Iss. 2, pp. 226-241
Open Access | Times Cited: 67
Noteworthy Consensus Effects of D/E Residues in Umami Peptides Used for Designing the Novel Umami Peptides
Zhiyong Cui, Hengli Meng, Tianxing Zhou, et al.
Journal of Agricultural and Food Chemistry (2024) Vol. 72, Iss. 5, pp. 2789-2800
Closed Access | Times Cited: 18
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: 18
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: 71
Making Enzymes Suitable for Organic Chemistry by Rational Protein Design
Manfred T. Reetz
ChemBioChem (2022) Vol. 23, Iss. 14
Open Access | Times Cited: 51
Flexibility Regulation of Loops Surrounding the Tunnel Entrance in Cytochrome P450 Enhanced Substrate Access Substantially
Zhongyu Li, Shuaiqi Meng, Kaili Nie, et al.
ACS Catalysis (2022) Vol. 12, Iss. 20, pp. 12800-12808
Closed Access | Times Cited: 51
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: 44
A Chemoenzymatic Strategy for the Synthesis of Steroid Drugs Enabled by P450 Monooxygenase-Mediated Steroidal Core Modification
Yaqin Peng, Chenghua Gao, Zili Zhang, et al.
ACS Catalysis (2022) Vol. 12, Iss. 5, pp. 2907-2914
Closed Access | Times Cited: 42
Reshaping Substrate-Binding Pocket of Leucine Dehydrogenase for Bidirectionally Accessing Structurally Diverse Substrates
Tao Wu, Yinmiao Wang, Ningxin Zhang, et al.
ACS Catalysis (2022) Vol. 13, Iss. 1, pp. 158-168
Closed Access | Times Cited: 39
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: 39
Using Computational Chemistry To Reveal Nature’s Blueprints for Single-Site Catalysis of C–H Activation
Aditya Nandy, Husain Adamji, David W. Kastner, et al.
ACS Catalysis (2022) Vol. 12, Iss. 15, pp. 9281-9306
Closed Access | Times Cited: 38
Accurate Prediction of Enzyme Thermostabilization with Rosetta Using AlphaFold Ensembles
Francesca Peccati, Sara Alunno-Rufini, Gonzalo Jiménez‐Osés
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 3, pp. 898-909
Open Access | Times Cited: 29
Computational-Aided Engineering of a Selective Unspecific Peroxygenase toward Enantiodivergent β-Ionone Hydroxylation
Judith Münch, Jordi Soler Soler, Nicole Hünecke, et al.
ACS Catalysis (2023) Vol. 13, Iss. 13, pp. 8963-8972
Open Access | Times Cited: 23
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: 15
Choose Your Own Adventure: A Comprehensive Database of Reactions Catalyzed by Cytochrome P450 BM3 Variants
Douglas J. Fansher, Jonathan N. Besna, Ali Fendri, et al.
ACS Catalysis (2024) Vol. 14, Iss. 8, pp. 5560-5592
Open Access | Times Cited: 14
Simplification of Corticosteroids Biosynthetic Pathway by Engineering P450BM3
Qihang Chen, Zikai Chao, Ke Wang, et al.
ACS Catalysis (2024) Vol. 14, Iss. 6, pp. 4117-4129
Closed Access | Times Cited: 13
Computer-aided understanding and engineering of enzymatic selectivity
Lunjie Wu, Lei Qin, Yao Nie, et al.
Biotechnology Advances (2021) Vol. 54, pp. 107793-107793
Closed Access | Times Cited: 53
Exploiting enzyme evolution for computational protein design
Gaspar Pinto, Marina Corbella, Andrey O. Demkiv, et al.
Trends in Biochemical Sciences (2021) Vol. 47, Iss. 5, pp. 375-389
Open Access | Times Cited: 41
Reversing the Enantioselectivity of Enzymatic Carbene N−H Insertion Through Mechanism‐Guided Protein Engineering**
Carla Calvó‐Tusell, Zhen Liu, Kai Chen, et al.
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 35
Open Access | Times Cited: 19
MD simulations indicate Omicron P132H of SARS-CoV-2 Mpro is a potential allosteric mutant involved in modulating the dynamics of catalytic site entry loop
Zahoor Ahmad Bhat, Mohd Muzammil Khan, Ayyub Rehman, et al.
International Journal of Biological Macromolecules (2024) Vol. 262, pp. 130077-130077
Closed Access | Times Cited: 7
How can we discover developable antibody-based biotherapeutics?
Joschka Bauer, Nandhini Rajagopal, Priyanka Gupta, et al.
Frontiers in Molecular Biosciences (2023) Vol. 10
Open Access | Times Cited: 16
DNA Framework–Programmed Nanoscale Enzyme Assemblies
Nan Cao, Ruiyan Guo, Ping Song, et al.
Nano Letters (2024) Vol. 24, Iss. 15, pp. 4682-4690
Closed Access | Times Cited: 5
Witnessing the Birth of Directed Evolution of Stereoselective Enzymes as Catalysts in Organic Chemistry
Manfred T. Reetz
Advanced Synthesis & Catalysis (2022) Vol. 364, Iss. 19, pp. 3326-3335
Open Access | Times Cited: 19
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