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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.

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Showing 14 citing articles:

Spatially Resolved Top-Down Proteomics of Tissue Sections Based on a Microfluidic Nanodroplet Sample Preparation Platform
Yen‐Chen Liao, James Fulcher, David J. Degnan, et al.
Molecular & Cellular Proteomics (2023) Vol. 22, Iss. 2, pp. 100491-100491
Open Access | Times Cited: 19
An optogenetic-phosphoproteomic study reveals dynamic Akt1 signaling profiles in endothelial cells
Wenping Zhou, Wenxue Li, Shisheng Wang, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 14
Data‐independent acquisition proteomics methods for analyzing post‐translational modifications
Yi Yang, Liang Qiao
PROTEOMICS (2022) Vol. 23, Iss. 7-8
Closed Access | Times Cited: 17
Turnover atlas of proteome and phosphoproteome across mouse tissues and brain regions
Wenxue Li, Abhijit Dasgupta, Ka Yang, et al.
Cell (2025)
Closed Access
Strategies for Acid and Amine Cross-linking and Labeling for Protein Structural Characterization Using Mass Spectrometry
Ashlyn N. Dollar, Ian Webb
Analytical Chemistry (2025)
Closed Access
Protein sequencing with single amino acid resolution discerns peptides that discriminate tropomyosin proteoforms
Natchanon Sittipongpittaya, Kenneth A. Skinner, Erin D. Jeffery, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 3
Localization and Quantification of Post-Translational Modifications of Proteins Using Electron Activated Dissociation Fragmentation on a Fast-Acquisition Time-of-Flight Mass Spectrometer
Joanna Bons, Christie L. Hunter, Rita Chupalov, et al.
Journal of the American Society for Mass Spectrometry (2023) Vol. 34, Iss. 10, pp. 2199-2210
Open Access | Times Cited: 7
Toward a hypothesis‐free understanding of how phosphorylation dynamically impacts protein turnover
Wenxue Li, Barbora Šalovská, Eugenio F. Fornasiero, et al.
PROTEOMICS (2022) Vol. 23, Iss. 3-4
Open Access | Times Cited: 7
Post‐translational modification and phenotype
Barbora Šalovská, Yansheng Liu
PROTEOMICS (2023) Vol. 23, Iss. 3-4
Open Access | Times Cited: 4
An Extensive Atlas of Proteome and Phosphoproteome Turnover Across Mouse Tissues and Brain Regions
Wenxue Li, Abhijit Dasgupta, Ka Yang, et al.
(2024)
Open Access
Spatially resolved top-down proteomics of tissue sections based on a microfluidic nanodroplet sample preparation platform
Yen‐Chen Liao, James Fulcher, David J. Degnan, et al.
(2022)
Open Access | Times Cited: 1
Localization and Quantification of Post-Translational Modifications of Proteins Using Electron Activated Dissociation Fragmentation on a Fast-Acquisition Time-of-Flight Mass Spectrometer
Joanna Bons, Christie L. Hunter, Rita Chupalov, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
A basic phosphoproteomic-DIA workflow integrating precise quantification of phosphosites in systems biology
Yi Di, Wenxue Li, Barbora Šalovská, et al.
Biophysics Reports (2023) Vol. 9, Iss. 2, pp. 82-98
Open Access
Spatially resolved top-down proteomics of tissue sections based on a microfluidic nanodroplet sample preparation platform
Yen‐Chen Liao, James Fulcher, David J. Degnan, et al.
(2022)
Open Access
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