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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:

Protein complexes in cells by AI‐assisted structural proteomics
Francis J. O’Reilly, Andrea Graziadei, Christian Forbrig, et al.
Molecular Systems Biology (2023) Vol. 19, Iss. 4
Open Access | Times Cited: 94

Showing 1-25 of 94 citing articles:

PAE viewer: a webserver for the interactive visualization of the predicted aligned error for multimer structure predictions and crosslinks
Christoph Elfmann, Jörg Stülke
Nucleic Acids Research (2023) Vol. 51, Iss. W1, pp. W404-W410
Open Access | Times Cited: 64
From interaction networks to interfaces, scanning intrinsically disordered regions using AlphaFold2
Hélène Bret, Jinmei Gao, Diego Javier Zea, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 49
Systematic discovery of protein interaction interfaces using AlphaFold and experimental validation
Chop Yan Lee, Dalmira Hubrich, Julia K. Varga, et al.
Molecular Systems Biology (2024)
Open Access | Times Cited: 31
Modelling protein complexes with crosslinking mass spectrometry and deep learning
Kolja Stahl, Robert Warneke, Lorenz Demann, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 25
Predictomes: A classifier-curated database of AlphaFold-modeled protein-protein interactions
E. Schmid, Johannes C. Walter
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 22
Easy and accurate protein structure prediction using ColabFold
Gyuri Kim, Sewon Lee, Eli Levy Karin, et al.
Nature Protocols (2024)
Closed Access | Times Cited: 18
Enhanced Protein-Protein Interaction Discovery via AlphaFold-Multimer
Ah‐Ram Kim, Yanhui Hu, Aram Comjean, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 16
Bacillus subtilis, a Swiss Army Knife in Science and Biotechnology
Jörg Stülke, Anika Grüppen, Marc Bramkamp, et al.
Journal of Bacteriology (2023) Vol. 205, Iss. 5
Open Access | Times Cited: 37
Cross-linking mass spectrometry for mapping protein complex topologies in situ
Kitaik Lee, Francis J. O’Reilly
Essays in Biochemistry (2023) Vol. 67, Iss. 2, pp. 215-228
Open Access | Times Cited: 29
New advances in cross-linking mass spectrometry toward structural systems biology
Clinton Yu, Lan Huang
Current Opinion in Chemical Biology (2023) Vol. 76, pp. 102357-102357
Open Access | Times Cited: 25
Does AlphaFold2 model proteins’ intracellular conformations? An experimental test using cross-linking mass spectrometry of endogenous ciliary proteins
Caitlyn L McCafferty, Erin L. Pennington, Ophelia Papoulas, et al.
Communications Biology (2023) Vol. 6, Iss. 1
Open Access | Times Cited: 24
Modeling Flexible Protein Structure With AlphaFold2 and Crosslinking Mass Spectrometry
Karen Manalastas-Cantos, Kish R. Adoni, Matthias Pfeifer, et al.
Molecular & Cellular Proteomics (2024) Vol. 23, Iss. 3, pp. 100724-100724
Open Access | Times Cited: 13
Deep learning for protein structure prediction and design—progress and applications
Jürgen Jänes, Pedro Beltrão
Molecular Systems Biology (2024) Vol. 20, Iss. 3, pp. 162-169
Open Access | Times Cited: 13
Overview of AlphaFold2 and breakthroughs in overcoming its limitations
Lei Wang, Zehua Wen, Shiwei Liu, et al.
Computers in Biology and Medicine (2024) Vol. 176, pp. 108620-108620
Closed Access | Times Cited: 13
Leveraging Artificial Intelligence to Expedite Antibody Design and Enhance Antibody–Antigen Interactions
Doo Nam Kim, Andrew McNaughton, Neeraj Kumar
Bioengineering (2024) Vol. 11, Iss. 2, pp. 185-185
Open Access | Times Cited: 10
AlphaFold two years on: Validation and impact
Oleg Kovalevskiy, Juan Mateos-García, Kathryn Tunyasuvunakool
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 34
Open Access | Times Cited: 10
AlphaFold2 Predicts Whether Proteins Interact Amidst Confounding Structural Compatibility
Juliette Martin
Journal of Chemical Information and Modeling (2024) Vol. 64, Iss. 5, pp. 1473-1480
Open Access | Times Cited: 8
ModelArchive: a deposition database for computational macromolecular structural models
Gerardo Tauriello, Andrew Waterhouse, Juergen Haas, et al.
Journal of Molecular Biology (2025), pp. 168996-168996
Closed Access | Times Cited: 1
Bias in, bias out – AlphaFold-Multimer and the structural complexity of protein interfaces
Joelle Strom, Katja Luck
Current Opinion in Structural Biology (2025) Vol. 91, pp. 103002-103002
Closed Access | Times Cited: 1
Understudied proteins and understudied functions in the model bacterium Bacillus subtilis—A major challenge in current research
Dennis Wicke, Janek Meißner, Robert Warneke, et al.
Molecular Microbiology (2023) Vol. 120, Iss. 1, pp. 8-19
Open Access | Times Cited: 21
Modelling protein complexes with crosslinking mass spectrometry and deep learning
Kolja Stahl, Lorenz Demann, Rica Bremenkamp, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 20
Bacillus sp. as a microbial cell factory: Advancements and future prospects
Jingyi Qian, Yuzhou Wang, Zijian Hu, et al.
Biotechnology Advances (2023) Vol. 69, pp. 108278-108278
Closed Access | Times Cited: 18
Chemical cross-linking and mass spectrometry enabled systems-level structural biology
Luke Botticelli, Anna Bakhtina, Nathan K. Kaiser, et al.
Current Opinion in Structural Biology (2024) Vol. 87, pp. 102872-102872
Closed Access | Times Cited: 6
A Perspective on the Prospective Use of AI in Protein Structure Prediction
Raphaëlle Versini, Sujith Sritharan, Burcu Aykaç Fas, et al.
Journal of Chemical Information and Modeling (2023) Vol. 64, Iss. 1, pp. 26-41
Open Access | Times Cited: 16
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