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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:

Advanced database mining of efficient haloalkane dehalogenases by sequence and structure bioinformatics and microfluidics
Michal Vasina, Pavel Vaňáček, Jiří Hon, et al.
Chem Catalysis (2022) Vol. 2, Iss. 10, pp. 2704-2725
Open Access | Times Cited: 22

Showing 22 citing articles:

From nature to industry: Harnessing enzymes for biocatalysis
Rebecca Buller, Stefan Lutz, Romas J. Kazlauskas, et al.
Science (2023) Vol. 382, Iss. 6673
Open Access | Times Cited: 168
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: 65
Ultrahigh-Throughput Enzyme Engineering and Discovery in In Vitro Compartments
Maximilian Gantz, Stefanie Neun, Elliot J. Medcalf, et al.
Chemical Reviews (2023) Vol. 123, Iss. 9, pp. 5571-5611
Open Access | Times Cited: 46
Microbial Enzyme Biotechnology to Reach Plastic Waste Circularity: Current Status, Problems and Perspectives
Marco Orlando, Gianluca Molla, Pietro Castellani, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 4, pp. 3877-3877
Open Access | Times Cited: 41
Machine Learning and Deep Learning in Synthetic Biology: Key Architectures, Applications, and Challenges
Manoj Kumar Goshisht
ACS Omega (2024) Vol. 9, Iss. 9, pp. 9921-9945
Open Access | Times Cited: 20
Advancing Enzyme’s Stability and Catalytic Efficiency through Synergy of Force-Field Calculations, Evolutionary Analysis, and Machine Learning
Antonín Kunka, Sérgio M. Marques, Martin Havlasek, et al.
ACS Catalysis (2023) Vol. 13, Iss. 19, pp. 12506-12518
Open Access | Times Cited: 25
Computer vision meets microfluidics: a label-free method for high-throughput cell analysis
Shizheng Zhou, Bingbing Chen, Edgar S. Fu, et al.
Microsystems & Nanoengineering (2023) Vol. 9, Iss. 1
Open Access | Times Cited: 25
In-depth analysis of biocatalysts by microfluidics: An emerging source of data for machine learning
Michal Vasina, David Kovář, Jiřı́ Damborský, et al.
Biotechnology Advances (2023) Vol. 66, pp. 108171-108171
Closed Access | Times Cited: 12
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
Structure-Based Design of Small Imine Reductase Panels for Target Substrates
Yuqi Yu, Arnau Rué Casamajo, William Finnigan, et al.
ACS Catalysis (2023) Vol. 13, Iss. 18, pp. 12310-12321
Open Access | Times Cited: 9
Perspectives on flow biocatalysis: the engine propelling enzymatic reactions
Ana I. Benítez‐Mateos, Francesca Paradisi
Journal of Flow Chemistry (2023) Vol. 14, Iss. 1, pp. 211-218
Open Access | Times Cited: 8
Towards an active droplet-based microfluidic platform for programmable fluid handling
Xiaobao Cao, Tomáš Buryška, Tianjin Yang, et al.
Lab on a Chip (2023) Vol. 23, Iss. 8, pp. 2029-2038
Open Access | Times Cited: 7
Engineering Dehalogenase Enzymes using Variational Autoencoder-Generated Latent Spaces and Microfluidics
Pavel Kohout, Michal Vasina, Marika Majerova, et al.
(2024)
Open Access | Times Cited: 1
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: 1
Functional characterization of luciferase in a brittle star indicates parallel evolution influenced by genomic availability of haloalkane dehalogenase
Emily S. Lau, Marika Majerova, Nicholai M. Hensley, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Expanding the β‐Lactamase Family in the Human Microbiome
Baolei Jia, Ju Hye Baek, Jae Kyeong Lee, et al.
Advanced Science (2024)
Open Access | Times Cited: 1
Design of Enzymes for Biocatalysis, Bioremediation, and Biosensing using Variational Autoencoder-Generated Latent Spaces
Pavel Kohout, Michal Vasina, Marika Majerova, et al.
(2023)
Open Access | Times Cited: 3
Multimeric structure of a subfamily III haloalkane dehalogenase‐like enzyme solved by combination of cryo‐EM and x‐ray crystallography
Klaudia Chmelova, Tadeja Gao, Martin Polák, et al.
Protein Science (2023) Vol. 32, Iss. 10
Open Access | Times Cited: 2
Efficient synthesis of 7-oxo-lithocholic acid using a newly identified 7α-hydroxysteroid dehydrogenase
Jiang-Tao Xue, Zhi‐Neng You, Bing-Yi Yang, et al.
Molecular Catalysis (2023) Vol. 553, pp. 113739-113739
Closed Access | Times Cited: 2
Evaluating advancements and opportunities in electro-assisted biodehalogenation of emerging halogenated contaminants
Zimeng Zhang, Zhiling Li, Jun Nan, et al.
Bioresource Technology (2024), pp. 132011-132011
Closed Access
Tapping into abiological reaction chemistries in biocatalysis
Niels A. W. de Kok, Sandy Schmidt
Chem Catalysis (2023) Vol. 3, Iss. 3, pp. 100493-100493
Open Access | Times Cited: 1
Atypical homodimerization revealed by the structure of the (S)-enantioselective haloalkane dehalogenase DmmarA from Mycobacterium marinum
Karolina Snajdarova, Sérgio M. Marques, Jiřı́ Damborský, et al.
Acta Crystallographica Section D Structural Biology (2023) Vol. 79, Iss. 11, pp. 956-970
Open Access
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