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:

Speeding up enzyme discovery and engineering with ultrahigh-throughput methods
H. Adrian Bunzel, Xavier Garrabou, Moritz Pott, et al.
Current Opinion in Structural Biology (2018) Vol. 48, pp. 149-156
Open Access | Times Cited: 122

Showing 26-50 of 122 citing articles:

Focused rational iterative site-specific mutagenesis (FRISM)
Danyang Li, Qi Wu, Manfred T. Reetz
Methods in enzymology on CD-ROM/Methods in enzymology (2020), pp. 225-242
Closed Access | Times Cited: 57

Recent advances in artificial enzyme cascades for the production of value-added chemicals
Zilong Wang, Balaji Sundara Sekar, Zhi Li
Bioresource Technology (2020) Vol. 323, pp. 124551-124551
Closed Access | Times Cited: 52

Machine-Learning-Guided Library Design Cycle for Directed Evolution of Enzymes: The Effects of Training Data Composition on Sequence Space Exploration
Yutaka Saitô, Misaki Oikawa, Takumi Sato, et al.
ACS Catalysis (2021) Vol. 11, Iss. 23, pp. 14615-14624
Open Access | Times Cited: 46

Tools for computational design and high-throughput screening of therapeutic enzymes
Michal Vasina, Jan Velecký, Joan Planas-Iglesias, et al.
Advanced Drug Delivery Reviews (2022) Vol. 183, pp. 114143-114143
Closed Access | Times Cited: 33

EnzyHTP: A High-Throughput Computational Platform for Enzyme Modeling
Qianzhen Shao, Yaoyukun Jiang, Zhongyue Yang
Journal of Chemical Information and Modeling (2022) Vol. 62, Iss. 3, pp. 647-655
Closed Access | Times Cited: 31

Substantial Improvement of an Epimerase for the Synthesis of D‐Allulose by Biosensor‐Based High‐Throughput Microdroplet Screening
Chao Li, Xin Gao, Hongbin Qi, et al.
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 10
Closed Access | Times Cited: 17

Expanding biological applications using cell-free metabolic engineering: An overview
James R. Swartz
Metabolic Engineering (2018) Vol. 50, pp. 156-172
Closed Access | Times Cited: 57

Peptide Assembly Directed and Quantified Using Megadalton DNA Nanostructures
Juan Jin, Emily G. Baker, Christopher W. Wood, et al.
ACS Nano (2019) Vol. 13, Iss. 9, pp. 9927-9935
Open Access | Times Cited: 52

Die zentrale Rolle der Methodenentwicklung in der gerichteten Evolution selektiver Enzyme
Ge Qu, Aitao Li, Carlos G. Acevedo‐Rocha, et al.
Angewandte Chemie (2019) Vol. 132, Iss. 32, pp. 13304-13333
Closed Access | Times Cited: 42

Fruity, sticky, stinky, spicy, bitter, addictive, and deadly: evolutionary signatures of metabolic complexity in the Solanaceae
Paul D. Fiesel, Hannah M. Parks, Robert L. Last, et al.
Natural Product Reports (2022) Vol. 39, Iss. 7, pp. 1438-1464
Open Access | Times Cited: 24

Model predictive control and moving horizon estimation for adaptive optimal bolus feeding in high-throughput cultivation of E. coli
Jong Woo Kim, Niels Krausch, Judit Aizpuru, et al.
Computers & Chemical Engineering (2023) Vol. 172, pp. 108158-108158
Closed Access | Times Cited: 13

Fluorescence coupling strategies in fluorescence-activated droplet sorting (FADS) for ultrahigh-throughput screening of enzymes, metabolites, and antibodies
Jingjie Jiang, Guangyu Yang, Fuqiang Ma
Biotechnology Advances (2023) Vol. 66, pp. 108173-108173
Closed Access | Times Cited: 13

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

Molecular docking and metagenomics assisted mitigation of microplastic pollution
Dinesh Parida, Konica Katare, Atmaadeep Ganguly, et al.
Chemosphere (2024) Vol. 351, pp. 141271-141271
Closed Access | Times Cited: 3

Functional Enhancement of Flavin-Containing Monooxygenase through Machine Learning Methodology
Takuma Matsushita, Shinji Kishimoto, Kodai Hara, et al.
ACS Catalysis (2024) Vol. 14, Iss. 9, pp. 6945-6951
Closed Access | Times Cited: 3

Directed evolution methods for overcoming trade‐offs between protein activity and stability
Samuel D. Stimple, Matthew D. Smith, Peter M. Tessier
AIChE Journal (2019) Vol. 66, Iss. 3
Open Access | Times Cited: 41

Winning the numbers game in enzyme evolution – fast screening methods for improved biotechnology proteins
Y. V. Sheludko, Wolf‐Dieter Fessner
Current Opinion in Structural Biology (2020) Vol. 63, pp. 123-133
Closed Access | Times Cited: 32

Predicting protein stability and solubility changes upon mutations: data perspective
Stanislav Mazurenko
ChemCatChem (2020) Vol. 12, Iss. 22, pp. 5590-5598
Open Access | Times Cited: 31

Recent advances in droplet microfluidics for enzyme and cell factory engineering
Jianhua Yang, Ran Tu, Huiling Yuan, et al.
Critical Reviews in Biotechnology (2021) Vol. 41, Iss. 7, pp. 1023-1045
Closed Access | Times Cited: 27

Mutexa: A Computational Ecosystem for Intelligent Protein Engineering
Zhongyue Yang, Qianzhen Shao, Yaoyukun Jiang, et al.
Journal of Chemical Theory and Computation (2023) Vol. 19, Iss. 21, pp. 7459-7477
Open Access | Times Cited: 9

Stereodivergent Evolution of Artificial Enzymes for the Michael Reaction
Xavier Garrabou, Duncan Stuart Macdonald, Basile I. M. Wicky, et al.
Angewandte Chemie International Edition (2018) Vol. 57, Iss. 19, pp. 5288-5291
Closed Access | Times Cited: 35

The Impact of Recent Developments in Technologies which Enable the Increased Use of Biocatalysts
Aoife Foley, Anita R. Maguire
European Journal of Organic Chemistry (2019) Vol. 2019, Iss. 23, pp. 3713-3734
Open Access | Times Cited: 29

Artificial enzymes bringing together computational design and directed evolution
Beatriz de Pina Mariz, Sara Carvalho, Íris L. Batalha, et al.
Organic & Biomolecular Chemistry (2021) Vol. 19, Iss. 9, pp. 1915-1925
Closed Access | Times Cited: 25

Methods for enzyme library creation: Which one will you choose?
Lorea Alejaldre, Joelle N. Pelletier, Daniela Quaglia
BioEssays (2021) Vol. 43, Iss. 8
Open Access | Times Cited: 25

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