Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

Rapid protein stability prediction using deep learning representations
Lasse M. Blaabjerg, Maher M. Kassem, Lydia L. Good, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 103

Showing 1-25 of 103 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: 84
Discovering functionally important sites in proteins
Matteo Cagiada, Sandro Bottaro, Søren Lindemose, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 49
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: 44
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: 25
A mutational atlas for Parkin proteostasis
Lene Clausen, Vasileios Voutsinos, Matteo Cagiada, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 20
Site-saturation mutagenesis of 500 human protein domains
Antoni Beltran, Xuege Jiang, Yue Shen, et al.
Nature (2025)
Open Access | Times Cited: 4
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: 2
RosettaDDGPrediction for high‐throughput mutational scans: From stability to binding
Valentina Sora, Adrian Otamendi Laspiur, Kristine Degn, et al.
Protein Science (2022) Vol. 32, Iss. 1
Open Access | Times Cited: 41
FireProt 2.0: web-based platform for the fully automated design of thermostable proteins
Miloš Musil, Andrej Jezik, Jana Horackova, et al.
Briefings in Bioinformatics (2023) Vol. 25, Iss. 1
Open Access | Times Cited: 36
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: 11
Prediction of pyrazinamide resistance in Mycobacterium tuberculosis using structure-based machine-learning approaches
Joshua Carter, Timothy M. Walker, Timothy M. Walker, et al.
JAC-Antimicrobial Resistance (2024) Vol. 6, Iss. 2
Open Access | Times Cited: 11
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: 11
Learning the shape of protein microenvironments with a holographic convolutional neural network
Michael N. Pun, A. Ivanov, Quinn Bellamy, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 6
Open Access | Times Cited: 10
Functionally Important Residues from Graph Analysis of Coevolved Dynamic couplings
Min Xu, Sarath Chandra Dantu, James A. Garnett, et al.
eLife (2025) Vol. 14
Open Access | Times Cited: 1
Prospective Evaluation of Structure-Based Simulations Reveal Their Ability to Predict the Impact of Kinase Mutations on Inhibitor Binding
Sukrit Singh, Vytautas Gapsys, Matteo Aldeghi, et al.
The Journal of Physical Chemistry B (2025)
Open Access | Times Cited: 1
Correspondence between functional scores from deep mutational scans and predicted effects on protein stability
Lukas Gerasimavicius, Benjamin Livesey, Joseph A. Marsh
Protein Science (2023) Vol. 32, Iss. 7
Open Access | Times Cited: 18
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
Deep mutational scanning reveals a correlation between degradation and toxicity of thousands of aspartoacylase variants
Martin Grønbæk-Thygesen, Vasileios Voutsinos, Kristoffer E. Johansson, et al.
Nature Communications (2024) Vol. 15, Iss. 1
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
Predicted mechanistic impacts of human protein missense variants
Jürgen Jänes, Marc Müller, Senthil Selvaraj, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 7
MutationExplorer: a webserver for mutation of proteins and 3D visualization of energetic impacts
Michelle Philipp, Christopher W. Moth, Nikola Ristic, et al.
Nucleic Acids Research (2024) Vol. 52, Iss. W1, pp. W132-W139
Open Access | Times Cited: 6
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: 15
Prediction of cancer driver genes and mutations: the potential of integrative computational frameworks
Mona Nourbakhsh, Kristine B. Degn, Astrid Saksager, et al.
Briefings in Bioinformatics (2023) Vol. 25, Iss. 2
Open Access | Times Cited: 13
ASM variants in the spotlight: A structure-based atlas for unraveling pathogenic mechanisms in lysosomal acid sphingomyelinase
Simone Scrima, Matteo Lambrughi, Matteo Tiberti, et al.
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (2024) Vol. 1870, Iss. 7, pp. 167260-167260
Open Access | Times Cited: 5
Page 1 - Next Page

Scroll to top