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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:

Engineering the protein dynamics of an ancestral luciferase
Andrea Schenkmayerová, Gaspar Pinto, Martin Toul, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 80

Showing 1-25 of 80 citing articles:

Loop dynamics and the evolution of enzyme activity
Marina Corbella, Gaspar Pinto, Shina Caroline Lynn Kamerlin
Nature Reviews Chemistry (2023) Vol. 7, Iss. 8, pp. 536-547
Closed Access | Times Cited: 65
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
Big data mining, rational modification, and ancestral sequence reconstruction inferred multiple xylose isomerases for biorefinery
Sitong Chen, Zhaoxian Xu, Boning Ding, et al.
Science Advances (2023) Vol. 9, Iss. 5
Open Access | Times Cited: 44
Catalytic mechanism for Renilla-type luciferases
Andrea Schenkmayerová, Martin Toul, Daniel Pluskal, et al.
Nature Catalysis (2023) Vol. 6, Iss. 1, pp. 23-38
Open Access | Times Cited: 36
Hot spots-making directed evolution easier
Haoran Yu, Shuang Ma, Yiwen Li, et al.
Biotechnology Advances (2022) Vol. 56, pp. 107926-107926
Open Access | Times Cited: 56
Insertions and deletions in protein evolution and engineering
Simone Savino, Tom Desmet, Jorick Franceus
Biotechnology Advances (2022) Vol. 60, pp. 108010-108010
Open Access | Times Cited: 51
Making Enzymes Suitable for Organic Chemistry by Rational Protein Design
Manfred T. Reetz
ChemBioChem (2022) Vol. 23, Iss. 14
Open Access | Times Cited: 50
Computational enzyme redesign: large jumps in function
Yinglu Cui, Jinyuan Sun, Bian Wu
Trends in Chemistry (2022) Vol. 4, Iss. 5, pp. 409-419
Closed Access | Times Cited: 36
Engineering Substrate Promiscuity of Nucleoside Phosphorylase Via an Insertions–Deletions Strategy
Gaofei Liu, Jialing Wang, Jianlin Chu, et al.
JACS Au (2024) Vol. 4, Iss. 2, pp. 454-464
Open Access | Times Cited: 10
Sequence – dynamics – function relationships in protein tyrosine phosphatases
Rory Crean, Marina Corbella, Ana Rita Calixto, et al.
QRB Discovery (2024) Vol. 5
Open Access | Times Cited: 7
Quantitative Measurement of Molecular Permeability to a Synthetic Bacterial Microcompartment Shell System
Eric J. Young, Henning Kirst, Matthew E. Dwyer, et al.
ACS Synthetic Biology (2025)
Open 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
Insertions and Deletions (Indels): A Missing Piece of the Protein Engineering Jigsaw
C.M. Miton, Nobuhiko Tokuriki
Biochemistry (2022) Vol. 62, Iss. 2, pp. 148-157
Closed Access | Times Cited: 29
Insights into the importance of WPD-loop sequence for activity and structure in protein tyrosine phosphatases
Ruidan Shen, Rory Crean, Keith J. Olsen, et al.
Chemical Science (2022) Vol. 13, Iss. 45, pp. 13524-13540
Open Access | Times Cited: 26
Illuminating the mechanism and allosteric behavior of NanoLuc luciferase
Michal Nemergut, Daniel Pluskal, Jana Horackova, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 15
Creatinase: Using Increased Entropy to Improve the Activity and Thermostability
Fan Jiang, Jiahao Bian, Hao Liu, et al.
The Journal of Physical Chemistry B (2023) Vol. 127, Iss. 12, pp. 2671-2682
Closed Access | Times Cited: 14
Remote loop evolution reveals a complex biological function for chitinase enzymes beyond the active site
Dan Kozome, Adnan Sljoka, Paola Laurino
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 4
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: 37
LoopGrafter: a web tool for transplanting dynamical loops for protein engineering
Joan Planas-Iglesias, Filip Opálený, Pavol Ulbrich, et al.
Nucleic Acids Research (2022) Vol. 50, Iss. W1, pp. W465-W473
Open Access | Times Cited: 22
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
Deep indel mutagenesis reveals the impact of amino acid insertions and deletions on protein stability and function
Magdalena Topolska, Toni Beltran, Ben Lehner
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open 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
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
Multidisciplinary approaches for enzyme biocatalysis in pharmaceuticals: protein engineering, computational biology, and nanoarchitectonics
Suhyeon Kim, Seongmin Ga, Hayeon Bae, et al.
EES Catalysis (2023) Vol. 2, Iss. 1, pp. 14-48
Open Access | Times Cited: 10
Correlated Motions in Structural Biology
Xu Da, Steve P. Meisburger, Nozomi Ando
Biochemistry (2021) Vol. 60, Iss. 30, pp. 2331-2340
Open Access | Times Cited: 25
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