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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:

Highly accurate protein structure prediction with AlphaFold
John Jumper, Richard Evans, Alexander Pritzel, et al.
Nature (2021) Vol. 596, Iss. 7873, pp. 583-589
Open Access | Times Cited: 28635

Showing 1-25 of 28635 citing articles:

ColabFold: making protein folding accessible to all
Milot Mirdita, Konstantin Schütze, Yoshitaka Moriwaki, et al.
Nature Methods (2022) Vol. 19, Iss. 6, pp. 679-682
Open Access | Times Cited: 6147
AlphaFold Protein Structure Database: massively expanding the structural coverage of protein-sequence space with high-accuracy models
Mihály Váradi, Stephen Anyango, Mandar Deshpande, et al.
Nucleic Acids Research (2021) Vol. 50, Iss. D1, pp. D439-D444
Open Access | Times Cited: 5805
Protein complex prediction with AlphaFold-Multimer
Richard Evans, M. E. O’Neill, Alexander Pritzel, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 2744
Highly accurate protein structure prediction for the human proteome
Kathryn Tunyasuvunakool, Jonas Adler, Zachary Wu, et al.
Nature (2021) Vol. 596, Iss. 7873, pp. 590-596
Open Access | Times Cited: 2421
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: 1977
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: 1867
InterPro in 2022
Typhaine Paysan-Lafosse, Matthias Blum, Sara Chuguransky, et al.
Nucleic Acids Research (2022) Vol. 51, Iss. D1, pp. D418-D427
Open Access | Times Cited: 1548
Large language models in medicine
Arun James Thirunavukarasu, Darren Shu Jeng Ting, Kabilan Elangovan, et al.
Nature Medicine (2023) Vol. 29, Iss. 8, pp. 1930-1940
Closed Access | Times Cited: 1195
A guide to machine learning for biologists
Joe G. Greener, Shaun M. Kandathil, Lewis Moffat, et al.
Nature Reviews Molecular Cell Biology (2021) Vol. 23, Iss. 1, pp. 40-55
Open Access | Times Cited: 1156
UCSF ChimeraX: Tools for structure building and analysis
Elaine C. Meng, Thomas D. Goddard, Eric F. Pettersen, et al.
Protein Science (2023) Vol. 32, Iss. 11
Open Access | Times Cited: 1015
Altered TMPRSS2 usage by SARS-CoV-2 Omicron impacts infectivity and fusogenicity
Bo Meng, Adam Abdullahi, Isabella A. T. M. Ferreira, et al.
Nature (2022) Vol. 603, Iss. 7902, pp. 706-714
Open Access | Times Cited: 948
SARS-CoV-2 Omicron-B.1.1.529 leads to widespread escape from neutralizing antibody responses
Wanwisa Dejnirattisai, Jiandong Huo, Daming Zhou, et al.
Cell (2022) Vol. 185, Iss. 3, pp. 467-484.e15
Open Access | Times Cited: 919
Fast and accurate protein structure search with Foldseek
Michel van Kempen, Stephanie S. Kim, Charlotte Tumescheit, et al.
Nature Biotechnology (2023) Vol. 42, Iss. 2, pp. 243-246
Open Access | Times Cited: 881
Harnessing protein folding neural networks for peptide–protein docking
Tomer Tsaban, Julia K. Varga, Orly Avraham, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 869
Why 90% of clinical drug development fails and how to improve it?
Duxin Sun, Wei Gao, Hongxiang Hu, et al.
Acta Pharmaceutica Sinica B (2022) Vol. 12, Iss. 7, pp. 3049-3062
Open Access | Times Cited: 764
Robust deep learning–based protein sequence design using ProteinMPNN
Justas Dauparas, Ivan Anishchenko, Nathaniel R. Bennett, et al.
Science (2022) Vol. 378, Iss. 6615, pp. 49-56
Open Access | Times Cited: 711
Accurate proteome-wide missense variant effect prediction with AlphaMissense
Jun Cheng, Guido Novati, Joshua Pan, et al.
Science (2023) Vol. 381, Iss. 6664
Open Access | Times Cited: 685
Improved prediction of protein-protein interactions using AlphaFold2
Patrick Bryant, Gabriele Pozzati, Arne Elofsson
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 650
Foundation models for generalist medical artificial intelligence
Michael Moor, Oishi Banerjee, Zahra Shakeri Hossein Abad, et al.
Nature (2023) Vol. 616, Iss. 7956, pp. 259-265
Open Access | Times Cited: 641
Ensembl 2023
Fergal J. Martin, M Ridwan Amode, Alisha Aneja, et al.
Nucleic Acids Research (2022) Vol. 51, Iss. D1, pp. D933-D941
Open Access | Times Cited: 637
Dali server: structural unification of protein families
Liisa Holm
Nucleic Acids Research (2022) Vol. 50, Iss. W1, pp. W210-W215
Open Access | Times Cited: 630
Database Resources of the National Genomics Data Center, China National Center for Bioinformation in 2022
Yongbiao Xue, Yīmíng Bào, Zhang Zhang, et al.
Nucleic Acids Research (2021) Vol. 50, Iss. D1, pp. D27-D38
Open Access | Times Cited: 629
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: 614
Scientific discovery in the age of artificial intelligence
Hanchen Wang, Tianfan Fu, Yuanqi Du, et al.
Nature (2023) Vol. 620, Iss. 7972, pp. 47-60
Closed Access | Times Cited: 588
ColabFold - Making protein folding accessible to all
Milot Mirdita, Konstantin Schütze, Yoshitaka Moriwaki, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 554
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