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:

Predicting protein stability changes upon mutation using a simple orientational potential
Iván Martín Hernández, Yves Dehouck, Ugo Bastolla, et al.
Bioinformatics (2023) Vol. 39, Iss. 1
Open Access | Times Cited: 16

Showing 16 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
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
Improving the prediction of protein stability changes upon mutations by geometric learning and a pre-training strategy
Yunxin Xu, Ди Лю, Haipeng Gong
Nature Computational Science (2024) Vol. 4, Iss. 11, pp. 840-850
Closed Access | Times Cited: 4
SPIRED-Fitness: an end-to-end framework for the prediction of protein structure and fitness from single sequence
Yinghui Chen, Yunxin Xu, Ди Лю, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 3
Unbiased curriculum learning enhanced global-local graph neural network for protein thermodynamic stability prediction
Haifan Gong, Yumeng Zhang, Chenhe Dong, et al.
Bioinformatics (2023) Vol. 39, Iss. 10
Open Access | Times Cited: 5
Prediction of mutation-induced protein stability changes based on the geometric representations learned by a self-supervised method
Shanshan Li, Zhao Ming Liu, Jian Li, et al.
BMC Bioinformatics (2024) Vol. 25, Iss. 1
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
Machine learning meets enzyme engineering: examples in the design of polyethylene terephthalate hydrolases
Rohan Ali, Yifei Zhang
Frontiers of Chemical Science and Engineering (2024) Vol. 18, Iss. 12
Closed Access | Times Cited: 1
Zero-Shot Transfer of Protein Sequence Likelihood Models to Thermostability Prediction
Shawn Reeves, Subha Kalyaanamoorthy
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 4
Improving the prediction of protein stability changes upon mutations by geometric learning and a pre-training strategy
Yunxin Xu, Ди Лю, Haipeng Gong
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 2
SPIRED-Fitness: an end-to-end framework for the prediction of protein structure and fitness from single sequence
Haipeng Gong, Yinghui Chen, Yunxin Xu, et al.
Research Square (Research Square) (2024)
Open Access
Exploring evolution to enhance mutational stability prediction
Pauline Hermans, Matsvei Tsishyn, Martin Schwersensky, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
AI Prediction of Structural Stability of Nanoproteins Based on Structures and Residue Properties by Mean Pooled Dual Graph Convolutional Network
Daixi Li, Yuqi Zhu, Wujie Zhang, et al.
Interdisciplinary Sciences Computational Life Sciences (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
Influence of Model Structures on Predictors of Protein Stability Changes from Single-Point Mutations
Cesare Rollo, Corrado Pancotti, Giovanni Birolo, et al.
Genes (2023) Vol. 14, Iss. 12, pp. 2228-2228
Open Access | Times Cited: 1
Intra-FCY1: a novel system to identify mutations that cause protein misfolding
Ning Quan, Yukinori Eguchi, Kerry Geiler‐Samerotte
Frontiers in Genetics (2023) Vol. 14
Open Access
Page 1

Scroll to top