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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:

High-resolutionde novostructure prediction from primary sequence
Ruidong Wu, Fan Ding, Rui Wang, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 258

Showing 1-25 of 258 citing articles:

Accurate structure prediction of biomolecular interactions with AlphaFold 3
Josh Abramson, Jonas Adler, Jack Dunger, et al.
Nature (2024) Vol. 630, Iss. 8016, pp. 493-500
Open Access | Times Cited: 1915
Evolutionary-scale prediction of atomic-level protein structure with a language model
Zeming Lin, Halil Akin, Roshan Rao, et al.
Science (2023) Vol. 379, Iss. 6637, pp. 1123-1130
Open Access | Times Cited: 1818
De novo design of protein structure and function with RFdiffusion
Joseph L. Watson, David Juergens, Nathaniel R. Bennett, et al.
Nature (2023) Vol. 620, Iss. 7976, pp. 1089-1100
Open Access | Times Cited: 593
Generalized biomolecular modeling and design with RoseTTAFold All-Atom
Rohith Krishna, Jue Wang, Woody Ahern, et al.
Science (2024) Vol. 384, Iss. 6693
Open Access | Times Cited: 235
AlphaFold2 and its applications in the fields of biology and medicine
Zhenyu Yang, Xiaoxi Zeng, Yi Zhao, et al.
Signal Transduction and Targeted Therapy (2023) Vol. 8, Iss. 1
Open Access | Times Cited: 206
Illuminating protein space with a programmable generative model
John Ingraham, Max Baranov, Zak Costello, et al.
Nature (2023) Vol. 623, Iss. 7989, pp. 1070-1078
Open Access | Times Cited: 160
OpenFold: Retraining AlphaFold2 yields new insights into its learning mechanisms and capacity for generalization
Gustaf Ahdritz, Nazim Bouatta, Christina Floristean, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Closed Access | Times Cited: 122
Broadly applicable and accurate protein design by integrating structure prediction networks and diffusion generative models
Joseph L. Watson, David Juergens, Nathaniel R. Bennett, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 118
Prediction of effector protein structures from fungal phytopathogens enables evolutionary analyses
Kyungyong Seong, Ksenia V. Krasileva
Nature Microbiology (2023) Vol. 8, Iss. 1, pp. 174-187
Open Access | Times Cited: 112
OpenFold: retraining AlphaFold2 yields new insights into its learning mechanisms and capacity for generalization
Gustaf Ahdritz, Nazim Bouatta, Christina Floristean, et al.
Nature Methods (2024) Vol. 21, Iss. 8, pp. 1514-1524
Open Access | Times Cited: 95
Efficient and accurate prediction of protein structure using RoseTTAFold2
Minkyung Baek, Ivan Anishchenko, Ian R. Humphreys, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 85
Protein structure prediction with in-cell photo-crosslinking mass spectrometry and deep learning
Kolja Stahl, Andrea Graziadei, Therese Dau, et al.
Nature Biotechnology (2023) Vol. 41, Iss. 12, pp. 1810-1819
Open Access | Times Cited: 78
Contrastive learning in protein language space predicts interactions between drugs and protein targets
Rohit Singh, Samuel Sledzieski, Bryan D. Bryson, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 24
Open Access | Times Cited: 71
Computer-Aided Drug Design and Drug Discovery: A Prospective Analysis
Sarfaraz K. Niazi, Zamara Mariam
Pharmaceuticals (2023) Vol. 17, Iss. 1, pp. 22-22
Open Access | Times Cited: 67
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
Generalized Biomolecular Modeling and Design with RoseTTAFold All-Atom
Rohith Krishna, Jue Wang, Woody Ahern, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 62
xTrimoPGLM: Unified 100B-Scale Pre-trained Transformer for Deciphering the Language of Protein
Bo Chen, Xingyi Cheng, Li Pan, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 52
Opportunities and Challenges for Machine Learning-Assisted Enzyme Engineering
Jason Yang, Francesca-Zhoufan Li, Frances H. Arnold
ACS Central Science (2024) Vol. 10, Iss. 2, pp. 226-241
Open Access | Times Cited: 51
Protein remote homology detection and structural alignment using deep learning
Tymor Hamamsy, James T. Morton, Robert Blackwell, et al.
Nature Biotechnology (2023) Vol. 42, Iss. 6, pp. 975-985
Open Access | Times Cited: 50
Protein generation with evolutionary diffusion: sequence is all you need
Sarah Alamdari, Nitya Thakkar, Rianne van den Berg, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 47
Protein structure generation via folding diffusion
Kevin Wu, Kevin Yang, Rianne van den Berg, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 45
Score-based generative modeling for de novo protein design
Jin Seop Lee, Ji‐Sun Kim, Philip M. Kim
Nature Computational Science (2023) Vol. 3, Iss. 5, pp. 382-392
Open Access | Times Cited: 43
Improving deep learning protein monomer and complex structure prediction using DeepMSA2 with huge metagenomics data
Wei Zheng, Qiqige Wuyun, Yang Li, et al.
Nature Methods (2024) Vol. 21, Iss. 2, pp. 279-289
Open Access | Times Cited: 38
State-specific protein–ligand complex structure prediction with a multiscale deep generative model
Zhuoran Qiao, Weili Nie, Arash Vahdat, et al.
Nature Machine Intelligence (2024) Vol. 6, Iss. 2, pp. 195-208
Closed Access | Times Cited: 37
Critical Assessment of Methods for Predicting the 3D Structure of Proteins and Protein Complexes
Shoshana J. Wodak, Sándor Vajda, Marc F. Lensink, et al.
Annual Review of Biophysics (2023) Vol. 52, Iss. 1, pp. 183-206
Open Access | Times Cited: 36
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