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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:

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

Showing 1-25 of 49 citing articles:

Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2
T. Reid Alderson, Iva Pritišanac, Đesika Kolarić, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 44
Open Access | Times Cited: 117
ELM—the Eukaryotic Linear Motif resource—2024 update
Manjeet Kumar, Sushama Michael, Jesús Alvarado-Valverde, et al.
Nucleic Acids Research (2023) Vol. 52, Iss. D1, pp. D442-D455
Open Access | Times Cited: 51
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
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
Predictomes, a classifier-curated database of AlphaFold-modeled protein-protein interactions
E. Schmid, Johannes C. Walter
Molecular Cell (2025)
Open Access | Times Cited: 2
AlphaFold-Multimer accurately captures interactions and dynamics of intrinsically disordered protein regions
Alireza Omidi, Mirko Möller, Nawar Malhis, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 44
Closed Access | Times Cited: 13
The Physics-AI Dialogue in Drug Design
Pablo Andrés Vargas-Rosales, Amedeo Caflisch
RSC Medicinal Chemistry (2025)
Open Access | Times Cited: 1
Structural model of a bacterial focal adhesion complex
Christian Cambillau, Tâm Mignot
Communications Biology (2025) Vol. 8, Iss. 1
Open 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
PPI3D: a web server for searching, analyzing and modeling protein–protein, protein–peptide and protein–nucleic acid interactions
Justas Dapkūnas, Albertas Timinskas, Kliment Olechnovič, et al.
Nucleic Acids Research (2024) Vol. 52, Iss. W1, pp. W264-W271
Open Access | Times Cited: 5
Structures prediction and replica exchange molecular dynamics simulations of α-synuclein: A case study for intrinsically disordered proteins
Orkid Coskuner‐Weber
International Journal of Biological Macromolecules (2024) Vol. 276, pp. 133813-133813
Closed Access | Times Cited: 4
NHSL3 controls single and collective cell migration through two distinct mechanisms
Nikita M. Novikov, Jinmei Gao, Artem I. Fokin, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Selecting genes for analysis using historically contingent progress: from RNA changes to protein–protein interactions
Farhaan Lalit, Antony M Jose
Nucleic Acids Research (2025) Vol. 53, Iss. 1
Open Access
RNA3DClust: segmentation of RNA three-dimensional structures using a clustering-based approach
Quynh‐Thu Le, Éric Angel, Fariza Tahi, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access
High-throughput discovery of inhibitory protein fragments with AlphaFold
Andrew Savinov, Sebastian Swanson, Amy E. Keating, et al.
Proceedings of the National Academy of Sciences (2025) Vol. 122, Iss. 6
Open Access
A Deep Learning Method for Predicting Interactions for Intrinsically Disordered Regions of Proteins
Kartik Majila, Varun Ullanat, Shruthi Viswanath
(2025)
Closed Access
Rēs ipSAE loquunt: What′s wrong with AlphaFold′s ipTM score and how to fix it
Roland L. Dunbrack
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access
Machine learning methods to study sequence–ensemble–function relationships in disordered proteins
Sören von Bülow, Giulio Tesei, Kresten Lindorff‐Larsen
Current Opinion in Structural Biology (2025) Vol. 92, pp. 103028-103028
Open Access
Assessing scoring metrics for AlphaFold2 and AlphaFold3 protein complex predictions
Luca R. Genz, Sanjana Nair, Maya Topf
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access
Successful prediction of LC8 binding to intrinsically disordered proteins sheds light on AlphaFold’s black box
Douglas R. Walker, Gretchen Fujimura, Juan M. Vanegas, et al.
Frontiers in Molecular Biosciences (2025) Vol. 12
Open Access
Structural biology of single-stranded, positive-sense RNA viruses in the age of accurate atomic-scale predictions of protein structures
Stéphane Bressanelli, Sonia Fieulaine, Thibault Tubiana
Virology (2025) Vol. 608, pp. 110546-110546
Closed Access
Deep learning in GPCR drug discovery: benchmarking the path to accurate peptide binding
Luuk Robin Hoegen Dijkhof, Teemu Rönkkö, Hans C von Vegesack, et al.
Briefings in Bioinformatics (2025) Vol. 26, Iss. 2
Open Access
In silico prediction method for plant Nucleotide‐binding leucine‐rich repeat‐ and pathogen effector interactions
Alicia Fick, Jacobus Lukas Marthinus Fick, Velushka Swart, et al.
The Plant Journal (2025) Vol. 122, Iss. 2
Open Access
Deep-learning-based prediction framework for protein-peptide interactions with structure generation pipeline
Jingxuan Ge, Dejun Jiang, Huiyong Sun, et al.
Cell Reports Physical Science (2024) Vol. 5, Iss. 6, pp. 101980-101980
Open Access | Times Cited: 3
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