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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:

Transfer learning to leverage larger datasets for improved prediction of protein stability changes
Henry Dieckhaus, Michael Brocidiacono, Nicholas Z. Randolph, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 6
Open Access | Times Cited: 34

Showing 1-25 of 34 citing articles:

Machine learning for functional protein design
Pascal Notin, Nathan Rollins, Yarin Gal, et al.
Nature Biotechnology (2024) Vol. 42, Iss. 2, pp. 216-228
Closed Access | Times Cited: 66
De novo protein design—From new structures to programmable functions
Tanja Kortemme
Cell (2024) Vol. 187, Iss. 3, pp. 526-544
Open Access | Times Cited: 63
Structure-based self-supervised learning enables ultrafast protein stability prediction upon mutation
Jinyuan Sun, Tong Zhu, Yinglu Cui, et al.
The Innovation (2025) Vol. 6, Iss. 1, pp. 100750-100750
Open Access | Times Cited: 1
Site-saturation mutagenesis of 500 human protein domains
Antoni Beltran, Xuege Jiang, Yue Shen, et al.
Nature (2025)
Open Access | Times Cited: 1
Biophysics-based protein language models for protein engineering
Sam Gelman, Bryce Johnson, Chase R. Freschlin, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 9
Site saturation mutagenesis of 500 human protein domains reveals the contribution of protein destabilization to genetic disease
Antoni Beltran, Xuege Jiang, Yue Shen, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 8
Predicting absolute protein folding stability using generative models
Matteo Cagiada, Sergey Ovchinnikov, Kresten Lindorff‐Larsen
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 7
An end-to-end framework for the prediction of protein structure and fitness from single sequence
Yinghui Chen, Yunxin Xu, Ди Лю, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 6
When “loss-of-function” means proteostasis burden: Thinking again about coding DNA variants
Claire L. Shovlin, Micheala A. Aldred
The American Journal of Human Genetics (2025) Vol. 112, Iss. 1, pp. 3-10
Closed Access
Deep learning–based assessment of missense variants in theCOG4gene presented with bilateral congenital cataract
Binghe Xiao, Shaohua Zhang, Maierdanjiang Ainiwaer, et al.
BMJ Open Ophthalmology (2025) Vol. 10, Iss. 1, pp. e001906-e001906
Open Access
Protein Engineering for Industrial Biocatalysis: Principles, Approaches, and Lessons from Engineered PETases
Konstantinos Grigorakis, Christina Ferousi, Evangelos Topakas
Catalysts (2025) Vol. 15, Iss. 2, pp. 147-147
Open Access
Sepsis subphenotypes: bridging the gaps in sepsis treatment strategies
Xue Zhang, Wei Zhang, Huan Zhang, et al.
Frontiers in Immunology (2025) Vol. 16
Open Access
Assessing computational tools for predicting protein stability changes upon missense mutations using a new dataset
Feifan Zheng, Yang Liu, Yan Yang, et al.
Protein Science (2023) Vol. 33, Iss. 1
Closed Access | Times Cited: 10
Exploring the anticancer mechanism of cardiac glycosides using proteome integral solubility alteration approach
Wenjie Qin, Yinhua Deng, Huan Ren, et al.
Cancer Medicine (2024) Vol. 13, Iss. 18
Open Access | Times Cited: 2
Enhancing predictions of protein stability changes induced by single mutations using MSA-based Language Models
Francesca Cuturello, Marco Celoria, Alessio Ansuini, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Improved prediction of stabilizing mutations in proteins by incorporation of mutational effects on ligand binding
Srivarshini Ganesan, Nidhi Mittal, Akash Bhat, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Enhancing predictions of protein stability changes induced by single mutations using MSA-based Language Models
Francesca Cuturello, Marco Celoria, Alessio Ansuini, et al.
Bioinformatics (2024) Vol. 40, Iss. 7
Open Access | Times Cited: 1
Improved Prediction of Stabilizing Mutations in Proteins by Incorporation of Mutational Effects on Ligand Binding
Srivarshini Ganesan, Nidhi Mittal, Akash Bhat, et al.
Proteins Structure Function and Bioinformatics (2024) Vol. 93, Iss. 1, pp. 384-395
Open Access | Times Cited: 1
Phosphate-binding proteins and peptides: from molecular mechanisms to potential applications
Brooke K. Mayer, Justin M. Hutchison, Eric S. McLamore, et al.
Current Opinion in Biotechnology (2024) Vol. 90, pp. 103199-103199
Closed Access | Times Cited: 1
SSEmb: A joint embedding of protein sequence and structure enables robust variant effect predictions
Lasse M. Blaabjerg, Nicolas Jonsson, Wouter Boomsma, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Closed Access | Times Cited: 1
Towards anchoring evolutionary fitness for protein stability with virtual chemical environment recovery
Zhiwei Nie, Yiming Ma, Jie Chen, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Closed Access
Deep-Learning Structure Elucidation from Single-Mutant Deep Mutational Scanning
Zachary C. Drake, Elijah Day, Paul D. Toth, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Aligning protein generative models with experimental fitness via Direct Preference Optimization
Talal Widatalla, Rafael Rafailov, Brian Hie
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
ProBASS: a language model with sequence and structural features for predicting the effect of mutations on binding affinity
Sagara N.S. Gurusinghe, Yibing Wu, William F. DeGrado, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Mapping kinase domain resistance mechanisms for the MET receptor tyrosine kinase via deep mutational scanning
Gabriella O. Estevam, Edmond M. Linossi, J. N. K. Rao, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
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