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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-throughput functional characterization of protein phosphorylation sites in yeast
Cristina Viéitez, Bede P. Busby, David Ochoa, et al.
Nature Biotechnology (2021) Vol. 40, Iss. 3, pp. 382-390
Open Access | Times Cited: 37

Showing 1-25 of 37 citing articles:

Insulin signalling and GLUT4 trafficking in insulin resistance
Julian van Gerwen, Amber S. Shun-Shion, Daniel J. Fazakerley
Biochemical Society Transactions (2023) Vol. 51, Iss. 3, pp. 1057-1069
Open Access | Times Cited: 54
PTMNavigator: interactive visualization of differentially regulated post-translational modifications in cellular signaling pathways
Julian Müller, Florian Bayer, Mathias Wilhelm, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 1
The evolution of post-translational modifications
David Bradley
Current Opinion in Genetics & Development (2022) Vol. 76, pp. 101956-101956
Closed Access | Times Cited: 37
The regulatory landscape of the yeast phosphoproteome
Mario Leutert, Anthony S. Barente, Noelle K. Fukuda, et al.
Nature Structural & Molecular Biology (2023) Vol. 30, Iss. 11, pp. 1761-1773
Open Access | Times Cited: 21
The impact of genomic variation on protein phosphorylation states and regulatory networks
Jan Großbach, Ludovic Gillet, Mathieu Clément‐Ziza, et al.
Molecular Systems Biology (2022) Vol. 18, Iss. 5
Open Access | Times Cited: 28
Ion mobility‐resolved phosphoproteomics with dia‐PASEF and short gradients
Denys Oliinyk, Florian Meier
PROTEOMICS (2022) Vol. 23, Iss. 7-8
Open Access | Times Cited: 27
µPhos: a scalable and sensitive platform for high-dimensional phosphoproteomics
Denys Oliinyk, Andreas Will, Felix R Schneidmadel, et al.
Molecular Systems Biology (2024) Vol. 20, Iss. 8, pp. 972-995
Open Access | Times Cited: 6
Stability-based approaches in chemoproteomics
Amy L. George, María Emilia Dueñas, José Luis Marín‐Rubio, et al.
Expert Reviews in Molecular Medicine (2024) Vol. 26
Open Access | Times Cited: 5
MMFuncPhos: A Multi‐Modal Learning Framework for Identifying Functional Phosphorylation Sites and Their Regulatory Types
Juan Xie, Ruihan Dong, Jintao Zhu, et al.
Advanced Science (2025)
Open Access
Uncovering protein glycosylation dynamics and heterogeneity using deep quantitative glycoprofiling (DQGlyco)
Clément M. Potel, Mira Lea Burtscher, Martín Garrido‐Rodríguez, et al.
Nature Structural & Molecular Biology (2025)
Open Access
Mass-spectrometry-based proteomics: from single cells to clinical applications
Tiannan Guo, Judith A. Steen, Matthias Mann
Nature (2025) Vol. 638, Iss. 8052, pp. 901-911
Closed Access
Non-enzymatic acetylation inhibits glycolytic enzymes in Escherichia coli
Evgeniya Schastnaya, Peter F. Doubleday, Luca Maurer, et al.
Cell Reports (2023) Vol. 42, Iss. 1, pp. 111950-111950
Open Access | Times Cited: 12
Mitochondrial dysfunction rapidly modulates the abundance and thermal stability of cellular proteins
Carina Groh, Per Haberkant, Frank Stein, et al.
Life Science Alliance (2023) Vol. 6, Iss. 6, pp. e202201805-e202201805
Open Access | Times Cited: 10
Cellular control of protein levels: A systems biology perspective
Victoria Munro, Van Kelly, Christoph B. Messner, et al.
PROTEOMICS (2023) Vol. 24, Iss. 12-13
Open Access | Times Cited: 10
More than two components: complexities in bacterial phosphosignaling
Andrew Frando, Christoph Grundner
mSystems (2024) Vol. 9, Iss. 5
Open Access | Times Cited: 3
Phosphoproteomics reveals rewiring of the insulin signaling network and multi-nodal defects in insulin resistance
Daniel J. Fazakerley, Julian van Gerwen, Kristen C. Cooke, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 15
Leveraging Protein Dynamics to Identify Functional Phosphorylation Sites using Deep Learning Models
Fei Zhu, Sijie Yang, Fanwang Meng, et al.
Journal of Chemical Information and Modeling (2022) Vol. 62, Iss. 14, pp. 3331-3345
Closed Access | Times Cited: 14
Obtaining Functional Proteomics Insights From Thermal Proteome Profiling Through Optimized Melt Shift Calculation and Statistical Analysis With InflectSSP
Neil A. McCracken, Hao Liu, Avery M. Runnebohm, et al.
Molecular & Cellular Proteomics (2023) Vol. 22, Iss. 9, pp. 100630-100630
Open Access | Times Cited: 6
Molecular profiling of sponge deflation reveals an ancient relaxant-inflammatory response
Fabian Ruperti, Isabelle Becher, Anniek Stokkermans, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 5
Posttranslational modifications in bacteria during phage infection
Hannelore Longin, Nand Broeckaert, Vera van Noort, et al.
Current Opinion in Microbiology (2024) Vol. 77, pp. 102425-102425
Open Access | Times Cited: 1
Functional profiling of serine, threonine and tyrosine sites
Yizhou Li, Tao Xu, Huazheng Ma, et al.
Nature Chemical Biology (2024)
Closed Access | Times Cited: 1
Ion mobility-resolved phosphoproteomics with dia-PASEF and short gradients
Denys Oliinyk, Florian Meier
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 8
µPhos: a scalable and sensitive platform for functional phosphoproteomics
Denys Oliinyk, Andreas Will, Felix R. Schneidmadel, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 4
Metabolomics and Microbial Metabolism: Toward a Systematic Understanding
Duncan Holbrook‐Smith, Julian Trouillon, Uwe Sauer
Annual Review of Biophysics (2023) Vol. 53, Iss. 1, pp. 41-64
Closed Access | Times Cited: 4
The regulatory landscape of the yeast phosphoproteome
Mario Leutert, Anthony S. Barente, Noelle K. Fukuda, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 7
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