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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:

Computational Enzyme Stabilization Can Affect Folding Energy Landscapes and Lead to Catalytically Enhanced Domain-Swapped Dimers
Klára Marková, Antonín Kunka, Klaudia Chmelova, et al.
ACS Catalysis (2021) Vol. 11, Iss. 21, pp. 12864-12885
Closed Access | Times Cited: 11

Showing 11 citing articles:

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: 27
Regulating the Orientation of Homobivalent Small Binders Through 3d Domain-Swapping Design
Shota Shiga, Hideki Watanabe, Koki Makabe, et al.
(2025)
Closed Access
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
In-depth analysis of biocatalysts by microfluidics: An emerging source of data for machine learning
Michal Vasina, David Kovář, Jir̆ı́ Damborský, et al.
Biotechnology Advances (2023) Vol. 66, pp. 108171-108171
Closed Access | Times Cited: 12
Computer-Aided Tunnel Engineering: A Promising Strategy for Improving Lipase Applications in Esterification Reactions
Wenya Chong, Qi Yuan, Liran Ji, et al.
ACS Catalysis (2023) Vol. 14, Iss. 1, pp. 67-83
Closed Access | Times Cited: 11
Integrating dynamics into enzyme engineering
Claudèle Lemay-St-Denis, Nicolas Doucet, Joelle N. Pelletier
Protein Engineering Design and Selection (2022) Vol. 35
Closed Access | Times Cited: 8
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
CalFitter 2.0: Leveraging the power of singular value decomposition to analyse protein thermostability
Antonín Kunka, David Lacko, Jan Štourač, et al.
Nucleic Acids Research (2022) Vol. 50, Iss. W1, pp. W145-W151
Open Access | Times Cited: 4
Site‐specific crosslinking and assembly of tetrameric β‐glucuronidase improve glycyrrhizin hydrolysis
Qibin Wang, Yingying Wang, Xing Jian, et al.
Biotechnology and Bioengineering (2023) Vol. 120, Iss. 12, pp. 3570-3584
Closed Access | Times Cited: 1
Improving the thermal stability and branching efficiency of Pyrococcus horikoshii OT3 glycogen branching enzyme
Jing Zhu, Jie Long, Xingfei Li, et al.
International Journal of Biological Macromolecules (2023) Vol. 255, pp. 128010-128010
Closed Access | Times Cited: 1
State-of-the-art experimental and computational approaches to investigate structure, substrate recognition, and catalytic mechanism of enzymes
C.R. Santos, Clelton A. Santos, Evandro Ares de Araújo, et al.
Elsevier eBooks (2023), pp. 75-107
Closed Access
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