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:

AlphaFold predictions of fold-switched conformations are driven by structure memorization
Devlina Chakravarty, Joseph W. Schafer, Ethan A. Chen, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 25

Showing 25 citing articles:

Proteins with alternative folds reveal blind spots in AlphaFold-based protein structure prediction
Devlina Chakravarty, Myeongsang Lee, Lauren L. Porter
Current Opinion in Structural Biology (2025) Vol. 90, pp. 102973-102973
Open Access | Times Cited: 7

Sequence clustering confounds AlphaFold2
Joseph W. Schafer, Myeongsang Lee, Devlina Chakravarty, et al.
Nature (2025) Vol. 638, Iss. 8051, pp. E8-E12
Open Access | Times Cited: 1

AFsample2 predicts multiple conformations and ensembles with AlphaFold2
Yogesh Kalakoti, Björn Wallner
Communications Biology (2025) Vol. 8, Iss. 1
Open Access | Times Cited: 1

AlphaFold3 versus experimental structures: assessment of the accuracy in ligand-bound G protein-coupled receptors
Xinheng He, Jia Li, Shi-yi Shen, et al.
Acta Pharmacologica Sinica (2024)
Closed Access | Times Cited: 6

Leveraging AI to Explore Structural Contexts of Post-Translational Modifications in Drug Binding
Kirill E. Medvedev, R. Dustin Schaeffer, Nick V. Grishin
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access

Structure and self-association of Arrestin-1
David Salom, Krzysztof Palczewski
Journal of Structural Biology (2025), pp. 108173-108173
Closed Access

Has AlphaFold 3 Solved the Protein Folding Problem for D-Peptides?
Henry R. Childs, Pei Zhou, Bruce R. Donald
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Closed Access

Artificial intelligence goes from predicting structure to predicting stability
Gary J. Pielak, Conggang Li, Maili Liu
Magnetic Resonance Letters (2025), pp. 200176-200176
Open Access

The Physics-AI Dialogue in Drug Design
Pablo Andrés Vargas-Rosales, Amedeo Caflisch
RSC Medicinal Chemistry (2025)
Open Access

AFflecto: A web server to generate conformational ensembles of flexible proteins from AlphaFold models
Mátyás Pajkos, Ilinka Clerc, Christophe Zanon, et al.
Journal of Molecular Biology (2025), pp. 169003-169003
Open Access

Advancements in protein structure prediction: A comparative overview of AlphaFold and its derivatives
Yuktika Malhotra, Jerry R. John, Deepika Yadav, et al.
Computers in Biology and Medicine (2025) Vol. 188, pp. 109842-109842
Closed Access

Prediction of structural variation
Yogesh Kalakoti, Airy Sanjeev, Björn Wallner
Current Opinion in Structural Biology (2025) Vol. 91, pp. 103003-103003
Open Access

AlphaFold2's training set powers its predictions of some fold‐switched conformations
Joseph W. Schafer, Lauren L. Porter
Protein Science (2025) Vol. 34, Iss. 4
Open Access

The mechanics of protein sweet spots
Qian-Yuan Tang
Nature Physics (2025)
Closed Access

Protein structure prediction via deep learning: an in-depth review
Yajie Meng, Zhuang Zhang, Chang Zhou, et al.
Frontiers in Pharmacology (2025) Vol. 16
Open Access

AlphaFold3: An Overview of Applications and Performance Insights
Marios G. Krokidis, Dimitrios E. Koumadorakis, Konstantinos Lazaros, et al.
International Journal of Molecular Sciences (2025) Vol. 26, Iss. 8, pp. 3671-3671
Open Access

Emerging frontiers in protein structure prediction following the AlphaFold revolution
Martin L. Rennie, Michael R. Oliver
Journal of The Royal Society Interface (2025) Vol. 22, Iss. 225
Open Access

Probing Functional Allosteric States and Conformational Ensembles of the Allosteric Protein Kinase States and Mutants: Atomistic Modeling and Comparative Analysis of AlphaFold2, OmegaFold, and AlphaFlow Approaches and Adaptations
Nishank Raisinghani, Mohammed Merae Alshahrani, Grace Gupta, et al.
The Journal of Physical Chemistry B (2024) Vol. 128, Iss. 45, pp. 11088-11107
Closed Access | Times Cited: 3

Non-standard proteins in the lenses of AlphaFold3 - case study of amyloids
Alicja W. Wojciechowska, Jakub W. Wojciechowski, Małgorzata Kotulska
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 2

AlphaFold2's training set powers its predictions of fold-switched conformations
Joseph W. Schafer, Lauren L. Porter
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1

Revealing missing protein-ligand interactions using AlphaFold predictions
Nahuel Escobedo, Tadeo E. Saldaño, Juan Mac Donagh, et al.
Journal of Molecular Biology (2024) Vol. 436, Iss. 23, pp. 168852-168852
Closed Access | Times Cited: 1

ProCyon: A multimodal foundation model for protein phenotypes
Owen Queen, Yepeng Huang, Robert Calef, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1

Insights into the Activation and Self-Association of Arrestin-1
David Salom, Philip D. Kiser, Krzysztof Palczewski
Biochemistry (2024)
Closed Access | Times Cited: 1

Page 1

Scroll to top