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:

Stability Oracle: a structure-based graph-transformer framework for identifying stabilizing mutations
Daniel J. Diaz, Chengyue Gong, Jeffrey Ouyang-Zhang, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 18

Showing 18 citing articles:

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

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

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

Transfer learning to leverage larger datasets for improved prediction of protein stability changes
Henry Dieckhaus, Michael Brocidiacono, Nicholas Z. Randolph, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 13

Empirical validation of ProteinMPNN’s efficiency in enhancing protein fitness
Tianshu Wang, Xiaocheng Jin, Xiaoli Lu, et al.
Frontiers in Genetics (2024) Vol. 14
Open Access | Times Cited: 2

The Nobel Prize in Chemistry: past, present, and future of AI in biology
Luciano A. Abriata
Communications Biology (2024) Vol. 7, Iss. 1
Open Access | Times Cited: 2

A general temperature-guided language model to design proteins of enhanced stability and activity
Fan Jiang, Mingchen Li, Jiajun Dong, et al.
Science Advances (2024) Vol. 10, Iss. 48
Closed Access | Times Cited: 2

Two sequence- and two structure-based ML models have learned different aspects of protein biochemistry
Anastasiya V. Kulikova, Daniel J. Diaz, Tianlong Chen, et al.
Scientific Reports (2023) Vol. 13, Iss. 1
Open Access | Times Cited: 6

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

A systematic evaluation of the language-of-viral-escape model using multiple machine learning frameworks
Brent Allman, Luiz Angêlo Vieira, Daniel J. Diaz, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1

Zero-shot transfer of protein sequence likelihood models to thermostability prediction
Shawn Reeves, Subha Kalyaanamoorthy
Nature Machine Intelligence (2024) Vol. 6, Iss. 9, pp. 1063-1076
Closed Access | Times Cited: 1

Distilling structural representations into protein sequence models
Jeffrey Ouyang-Zhang, Chengyue Gong, Yue Zhao, et al.
(2024)
Open Access | Times Cited: 1

Two sequence- and two structure-based ML models have learned different aspects of protein biochemistry
Anastasiya V. Kulikova, Daniel J. Diaz, Tianlong Chen, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 3

Exploring evolution to enhance mutational stability prediction
Pauline Hermans, Matsvei Tsishyn, Martin Schwersensky, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

HERMES: Holographic Equivariant neuRal network model for Mutational Effect and Stability prediction
Gian Marco Visani, Michael Neal Pun, William Galvin, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

Protein stability models fail to capture epistatic interactions of double point mutations
Henry Dieckhaus, Brian Kuhlman
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

Advances in Zero‐Shot Prediction‐Guided Enzyme Engineering Using Machine Learning
Chang Liu, Junxian Wu, Yongbo Chen, et al.
ChemCatChem (2024)
Closed Access

Exploring evolution to uncover insights into protein mutational stability
Pauline Hermans, Matsvei Tsishyn, Martin Schwersensky, et al.
Molecular Biology and Evolution (2024) Vol. 42, Iss. 1
Open Access

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