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:

The characterization of protein interactions – what, how and how much?
Louise J. Walport, Jason K. K. Low, Jacqueline M. Matthews, et al.
Chemical Society Reviews (2021) Vol. 50, Iss. 22, pp. 12292-12307
Closed Access | Times Cited: 41

Showing 1-25 of 41 citing articles:

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: 23

Protein codes promote selective subcellular compartmentalization
Henry R. Kilgore, Itamar Chinn, Peter G. Mikhael, et al.
Science (2025)
Closed Access | Times Cited: 5

Machine learning solutions for predicting protein–protein interactions
Rita Casadio, Pier Luigi Martelli, Castrense Savojardo
Wiley Interdisciplinary Reviews Computational Molecular Science (2022) Vol. 12, Iss. 6
Open Access | Times Cited: 52

Target Discovery Driven by Chemical Biology and Computational Biology
B J Lyu, Wenfeng Gou, Feifei Xu, et al.
The Chemical Record (2025)
Closed Access | Times Cited: 1

Covalent hits and where to find them
Simon C. C. Lucas, J. Henry Blackwell, Sarah H. Hewitt, et al.
SLAS DISCOVERY (2024) Vol. 29, Iss. 3, pp. 100142-100142
Open Access | Times Cited: 7

ReLo is a simple and rapid colocalization assay to identify and characterize direct protein–protein interactions
Harpreet Kaur Salgania, J. Metz, Mandy Jeske
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 7

Illuminating the dark protein-protein interactome
Mehdi Sharifi Tabar, Chirag Parsania, Hong Chen, et al.
Cell Reports Methods (2022) Vol. 2, Iss. 8, pp. 100275-100275
Open Access | Times Cited: 28

Microscale Thermophoresis as a Tool to Study Protein Interactions and Their Implication in Human Diseases
Romain Magnez, Christian Bailly, Xavier Thuru
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 14, pp. 7672-7672
Open Access | Times Cited: 25

Targeting the ATG5-ATG16L1 Protein–Protein Interaction with a Hydrocarbon-Stapled Peptide Derived from ATG16L1 for Autophagy Inhibition
Jin Cui, Yuta Ogasawara, Ikuko Kurata, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 38, pp. 17671-17679
Closed Access | Times Cited: 23

Near Infrared Light‐Triggered Photocatalytic Decaging for Remote‐Controlled Spatiotemporal Activation in Living Mice**
Xuan Liang, Shan Qian, Zhizheng Lou, et al.
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 48
Closed Access | Times Cited: 14

ACE2 Receptor‐Targeted Inhaled Nanoemulsions Inhibit SARS‐CoV‐2 and Attenuate Inflammatory Responses
H Wang, Shuang Luo, Mingxin Xie, et al.
Advanced Materials (2024) Vol. 36, Iss. 14
Closed Access | Times Cited: 6

Emerging affinity methods for protein-drug interaction analysis
Xinxin Zheng, Huiting Zhu, Xue Zhao, et al.
Journal of Pharmaceutical and Biomedical Analysis (2024) Vol. 249, pp. 116371-116371
Closed Access | Times Cited: 6

Protein Function Analysis through Machine Learning
Chris Avery, John A. Patterson, Tyler Grear, et al.
Biomolecules (2022) Vol. 12, Iss. 9, pp. 1246-1246
Open Access | Times Cited: 21

Protein codes promote selective subcellular compartmentalization
Henry R. Kilgore, Itamar Chinn, Peter G. Mikhael, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 4

A comprehensive review of recombinant technology in the food industry: Exploring expression systems, application, and future challenges
Ming Liu, Ran Xiao, Xiaolin Li, et al.
Comprehensive Reviews in Food Science and Food Safety (2025) Vol. 24, Iss. 2
Closed Access

Rapid Profiling of the Glycosylation Effects on the Binding of SARS-CoV-2 Spike Protein to Angiotensin-Converting Enzyme 2 Using MALDI-MS with High Mass Detection
Yuye Zhou, Congrui Tan, Renato Zenobi
Analytical Chemistry (2024) Vol. 96, Iss. 5, pp. 1898-1905
Closed Access | Times Cited: 3

Discovery and Structure-Based Design of Macrocyclic Peptides Targeting STUB1
Simon Ng, Alexander C. Brueckner, Soheila Bahmanjah, et al.
Journal of Medicinal Chemistry (2022) Vol. 65, Iss. 14, pp. 9789-9801
Closed Access | Times Cited: 14

Methods for the Discovery and Identification of Small Molecules Targeting Oxidative Stress-Related Protein–Protein Interactions: An Update
Xuexuan Wu, Qiuyue Zhang, Yuqi Guo, et al.
Antioxidants (2022) Vol. 11, Iss. 4, pp. 619-619
Open Access | Times Cited: 12

Multivalent binding kinetics resolved by fluorescence proximity sensing
Clemens Schulte, Alice Soldà, Sebastian Spänig, et al.
Communications Biology (2022) Vol. 5, Iss. 1
Open Access | Times Cited: 12

Exploring Protein S-Palmitoylation: Mechanisms, Detection, and Strategies for Inhibitor Discovery
Shaojun Pei, Hai‐long Piao
ACS Chemical Biology (2024) Vol. 19, Iss. 9, pp. 1868-1882
Closed Access | Times Cited: 2

Single-molecule digital sizing of proteins in solution
Georg Krainer, Raphaël P. B. Jacquat, Matthias M. Schneider, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 2

Study of FOXO1-interacting proteins using TurboID-based proximity labeling technology
Yanting Su, Yuanyuan Guo, Jieyu Guo, et al.
BMC Genomics (2023) Vol. 24, Iss. 1
Open Access | Times Cited: 5

Determination of dissociation constants via quantitative mass spectrometry
Jonathan Schulte, Jan‐Niklas Tants, Julian von Ehr, et al.
Frontiers in Analytical Science (2023) Vol. 3
Open Access | Times Cited: 5

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