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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:

The genetic architecture of protein stability
André J. Faure, Aina Martí-Aranda, Cristina Hidalgo-Carcedo, et al.
Nature (2024)
Open Access | Times Cited: 14

Showing 14 citing articles:

Opportunities and Challenges for Machine Learning-Assisted Enzyme Engineering
Jason Yang, Francesca-Zhoufan Li, Frances H. Arnold
ACS Central Science (2024) Vol. 10, Iss. 2, pp. 226-241
Open Access | Times Cited: 70
Site-saturation mutagenesis of 500 human protein domains
Antoni Beltran, Xuege Jiang, Yue Shen, et al.
Nature (2025)
Open Access | Times Cited: 5
Protein codes promote selective subcellular compartmentalization
Henry R. Kilgore, Itamar Chinn, Peter G. Mikhael, et al.
Science (2025)
Closed Access | Times Cited: 5
High Throughput Mutational Scanning of a Protein via Alchemistry on a High‐Performance Computing Resource
Tandac F. Guclu, Busra Tayhan, Ebru Çetin, et al.
Concurrency and Computation Practice and Experience (2025) Vol. 37, Iss. 3
Open Access | Times Cited: 2
MoCHI: neural networks to fit interpretable models and quantify energies, energetic couplings, epistasis, and allostery from deep mutational scanning data
André J. Faure, Ben Lehner
Genome biology (2024) Vol. 25, Iss. 1
Open Access | Times Cited: 6
Epistasis facilitates functional evolution in an ancient transcription factor
Brian P. H. Metzger, Yeonwoo Park, Tyler N. Starr, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 11
Protein stability is determined by single-site bias rather than pairwise covariance
Matt Sternke, Katherine W. Tripp, Doug Barrick
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access
Mass testing of mutant enzymes involved in photosynthesis

Nature (2025)
Closed Access
Machine learning in molecular biophysics: Protein allostery, multi-level free energy simulations, and lipid phase transitions
Qiang Cui
Biophysics Reviews (2025) Vol. 6, Iss. 1
Closed Access
Identification and Understanding of Allostery Hotspots in Proteins: Integration of Deep Mutational Scanning and Multi-faceted Computational Analyses
Qiang Cui
Journal of Molecular Biology (2025), pp. 168998-168998
Closed Access
Computational and Experimental Exploration of Protein Fitness Landscapes: Navigating Smooth and Rugged Terrains
Mahakaran Sandhu, John Z. Chen, Dana S. Matthews, et al.
Biochemistry (2025)
Open Access
Small Molecular Fluorescent Probes Featuring Protein-Assisted Functional Amplification for Improved Biosensing and Cancer Therapeutics
Ye Chen, Hong‐Wen Liu, Dailiang Zhang
Chemical Communications (2025)
Closed Access
Energetic portrait of the amyloid beta nucleation transition state
Anna Arutyunyan, Mireia Seuma, André J. Faure, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
A pharmacological chaperone stabilizer rescues the expression of the vast majority of pathogenic variants in a G protein-coupled receptor
Taylor L. Mighell, Ben Lehner
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Protein stability models fail to capture epistatic interactions of double point mutations
Henry Dieckhaus, Brian Kuhlman
Protein Science (2024) Vol. 34, Iss. 1
Open Access
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