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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:

Directed Evolution of Protein Catalysts
Cathleen Zeymer, Donald Hilvert
Annual Review of Biochemistry (2018) Vol. 87, Iss. 1, pp. 131-157
Open Access | Times Cited: 407

Showing 26-50 of 407 citing articles:

Site-Selective Protein Modification: From Functionalized Proteins to Functional Biomaterials
Jared A. Shadish, Cole A. DeForest
Matter (2020) Vol. 2, Iss. 1, pp. 50-77
Closed Access | Times Cited: 129
Enzyme engineering: Reshaping the biocatalytic functions
Misha Ali, Hassan Mubarak Ishqi, Qayyum Husain
Biotechnology and Bioengineering (2020) Vol. 117, Iss. 6, pp. 1877-1894
Closed Access | Times Cited: 129
Computational Design of Stable and Soluble Biocatalysts
Miloš Musil, Hannes Konegger, Jiří Hon, et al.
ACS Catalysis (2018) Vol. 9, Iss. 2, pp. 1033-1054
Open Access | Times Cited: 125
Bacteria as genetically programmable producers of bioactive natural products
Joachim J. Hug, Daniel Krug, Rolf Müller
Nature Reviews Chemistry (2020) Vol. 4, Iss. 4, pp. 172-193
Open Access | Times Cited: 125
A machine learning approach for reliable prediction of amino acid interactions and its application in the directed evolution of enantioselective enzymes
Frédéric Cadet, Nicolas Fontaine, Guangyue Li, et al.
Scientific Reports (2018) Vol. 8, Iss. 1
Open Access | Times Cited: 124
Directed Evolution of Artificial Metalloenzymes: A Universal Means to Tune the Selectivity of Transition Metal Catalysts?
Manfred T. Reetz
Accounts of Chemical Research (2019) Vol. 52, Iss. 2, pp. 336-344
Closed Access | Times Cited: 111
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
Retrosynthetic design of metabolic pathways to chemicals not found in nature
Geng-Min Lin, Robert Warden‐Rothman, Christopher A. Voigt
Current Opinion in Systems Biology (2019) Vol. 14, pp. 82-107
Open Access | Times Cited: 111
Harnessing Conformational Plasticity to Generate Designer Enzymes
Rory Crean, Jasmine M. Gardner, Shina Caroline Lynn Kamerlin
Journal of the American Chemical Society (2020) Vol. 142, Iss. 26, pp. 11324-11342
Open Access | Times Cited: 111
Upgrading aminoacyl-tRNA synthetases for genetic code expansion
Oscar Vargas‐Rodriguez, Anastasia Sevostyanova, Dieter Söll, et al.
Current Opinion in Chemical Biology (2018) Vol. 46, pp. 115-122
Open Access | Times Cited: 106
The power and accessibility of high-throughput methods for catalysis research
C. Liana Allen, David C. Leitch, M. Anson, et al.
Nature Catalysis (2019) Vol. 2, Iss. 1, pp. 2-4
Closed Access | Times Cited: 105
A global analysis of function and conservation of catalytic residues in enzymes
António J. M. Ribeiro, Jonathan D. Tyzack, Neera Borkakoti, et al.
Journal of Biological Chemistry (2019) Vol. 295, Iss. 2, pp. 314-324
Open Access | Times Cited: 105
Design of novel enzyme biocatalysts for industrial bioprocess: Harnessing the power of protein engineering, high throughput screening and synthetic biology
Aravind Madhavan, K. B. Arun, Parameswaran Binod, et al.
Bioresource Technology (2020) Vol. 325, pp. 124617-124617
Closed Access | Times Cited: 105
Fluorescence-Activated Droplet Sorting for Single-Cell Directed Evolution
Derek Vallejo, Ali Nikoomanzar, Brian M. Paegel, et al.
ACS Synthetic Biology (2019) Vol. 8, Iss. 6, pp. 1430-1440
Open Access | Times Cited: 99
Biotechnological relevance of the lipase A from Candida antarctica
Rodolpho R. C. Monteiro, José J. Virgen-Ortíz, Ángel Berenguer‐Murcia, et al.
Catalysis Today (2020) Vol. 362, pp. 141-154
Open Access | Times Cited: 98
Looking Back: A Short History of the Discovery of Enzymes and How They Became Powerful Chemical Tools
Christian M. Heckmann, Francesca Paradisi
ChemCatChem (2020) Vol. 12, Iss. 24, pp. 6082-6102
Open Access | Times Cited: 94
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: 92
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: 92
Recent Advances in Biocatalysis with Chemical Modification and Expanded Amino Acid Alphabet
Amol D. Pagar, Mahesh D. Patil, Dillon T. Flood, et al.
Chemical Reviews (2021) Vol. 121, Iss. 10, pp. 6173-6245
Closed Access | Times Cited: 91
Microfluidics for Biotechnology: Bridging Gaps to Foster Microfluidic Applications
Vera Ortseifen, Martina Viefhues, Lutz Wobbe, et al.
Frontiers in Bioengineering and Biotechnology (2020) Vol. 8
Open Access | Times Cited: 89
Directed Evolution of a Designer Enzyme Featuring an Unnatural Catalytic Amino Acid
Clemens Mayer, Christopher Dulson, Eswar R. Reddem, et al.
Angewandte Chemie International Edition (2018) Vol. 58, Iss. 7, pp. 2083-2087
Open Access | Times Cited: 84
Artificial cysteine-lipases with high activity and altered catalytic mechanism created by laboratory evolution
Yixin Cen, Warispreet Singh, M Arkin, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 83
Biocatalysis as Useful Tool in Asymmetric Synthesis: An Assessment of Recently Granted Patents (2014–2019)
Pablo de María, Gonzalo de Gonzalo, Andrés R. Alcántara
Catalysts (2019) Vol. 9, Iss. 10, pp. 802-802
Open Access | Times Cited: 82
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: 79
Near-perfect control of the regioselective glucosylation enabled by rational design of glycosyltransferases
Jiao Li, Ge Qu, Na Shang, et al.
Green Synthesis and Catalysis (2021) Vol. 2, Iss. 1, pp. 45-53
Open Access | Times Cited: 75

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