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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:

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

Showing 1-25 of 27 citing articles:

Acquisition and Analysis of DIA-Based Proteomic Data: A Comprehensive Survey in 2023
Ronghui Lou, Wenqing Shui
Molecular & Cellular Proteomics (2024) Vol. 23, Iss. 2, pp. 100712-100712
Open Access | Times Cited: 39
Instrumentation at the Leading Edge of Proteomics
Trenton M. Peters-Clarke, Joshua J. Coon, Nicholas M. Riley
Analytical Chemistry (2024) Vol. 96, Iss. 20, pp. 7976-8010
Closed Access | Times Cited: 24
diaTracer enables spectrum-centric analysis of diaPASEF proteomics data
Kai Li, Guo Ci Teo, Kevin Yang, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 3
Fast and deep phosphoproteome analysis with the Orbitrap Astral mass spectrometer
Noah M. Lancaster, Pavel Sinitcyn, Patrick Forny, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 14
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: 9
An accessible workflow for high-sensitivity proteomics using parallel accumulation–serial fragmentation (PASEF)
Patricia Skowronek, Georg Wallmann, Maria Wahle, et al.
Nature Protocols (2025)
Closed Access | Times Cited: 1
High-Throughput Proteomics and Phosphoproteomics of Rat Tissues Using Microflow Zeno SWATH
Erin M. Humphries, Dylan Xavier, Keith Ashman, et al.
Journal of Proteome Research (2024) Vol. 23, Iss. 7, pp. 2355-2366
Closed Access | Times Cited: 7
Recent advances of data‐independent acquisition mass spectrometry‐based proteomics
Tiannan Guo, Ruedi Aebersold
PROTEOMICS (2023) Vol. 23, Iss. 7-8
Open Access | Times Cited: 15
Considerations for defining +80 Da mass shifts in mass spectrometry-based proteomics: phosphorylation and beyond
Leonard A. Daly, C Clarke, Allen Po, et al.
Chemical Communications (2023) Vol. 59, Iss. 77, pp. 11484-11499
Open Access | Times Cited: 8
diaTracer enables spectrum-centric analysis of diaPASEF proteomics data
Kai Li, Guo Ci Teo, Kevin Yang, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 3
Evaluation of DDA Library-Free Strategies for Phosphoproteomics and Ubiquitinomics Data-Independent Acquisition Data
Chengwen Wen, Xiurong Wu, Guanzhong Lin, et al.
Journal of Proteome Research (2023) Vol. 22, Iss. 7, pp. 2232-2245
Closed Access | Times Cited: 8
Peptide collision cross sections of 22 post-translational modifications
Andreas Will, Denys Oliinyk, Christian Bleiholder, et al.
Analytical and Bioanalytical Chemistry (2023) Vol. 415, Iss. 27, pp. 6633-6645
Open Access | Times Cited: 7
Spike-in enhanced phosphoproteomics uncovers synergistic signaling responses to MEK inhibition in colon cancer cells
Mirjam van Bentum, Bertram Klinger, Anja Sieber, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 2
Mass spectrometry-based phosphoproteomics in clinical applications
Xiaofeng Wu, Yi‐Kai Liu, Anton Iliuk, et al.
TrAC Trends in Analytical Chemistry (2023) Vol. 163, pp. 117066-117066
Open Access | Times Cited: 6
Optimum collision energies for proteomics: The impact of ion mobility separation
Kinga Nagy, Gabriella Gellén, Dávid Papp, et al.
Journal of Mass Spectrometry (2023) Vol. 58, Iss. 9
Open Access | Times Cited: 6
Fast and Deep Phosphoproteome Analysis with the Orbitrap Astral Mass Spectrometer
Noah M. Lancaster, Pavel Sinitcyn, Patrick Forny, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 6
Phosphorylation Sites of the Gastric Inhibitory Polypeptide Receptor (GIPR) Revealed by Trapped-Ion-Mobility Spectrometry Coupled to Time-of-Flight Mass Spectrometry (TIMS-TOF MS)
Kyle A. Brown, Rylie K. Morris, S. Eckhardt, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 51, pp. 28030-28037
Closed Access | Times Cited: 5
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
Analyzing Posttranslational Modifications in Single Cells
Benjamin C. Orsburn
Methods in molecular biology (2024), pp. 145-156
Closed Access | Times Cited: 1
Mass Spectrometry-Based Multi-omics Analysis Reveals Distinct Molecular Features in Early and Advanced Stages of Hepatocellular Carcinoma
Mingzhu Fan, Jin Hu, Xiaoyan Xu, et al.
Heliyon (2024) Vol. 10, Iss. 19, pp. e38182-e38182
Open Access | Times Cited: 1
Advancements in Global Phosphoproteomics Profiling: Overcoming Challenges in Sensitivity and Quantification
Gul Muneer, Ciao‐Syuan Chen, Yu‐Ju Chen
PROTEOMICS (2024)
Open Access | Times Cited: 1
Simulation of mass spectrometry-based proteomics data with Synthedia
Michael G. Leeming, Ching‐Seng Ang, Shuai Nie, et al.
Bioinformatics Advances (2022) Vol. 3, Iss. 1
Open Access | Times Cited: 6
Proteome-scale tissue mapping using mass spectrometry based on label-free and multiplexed workflows
Yumi Kwon, Jongmin Jacob Woo, Fengchao Yu, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Exploiting ion‐mobility mass spectrometry for unraveling proteome complexity
Stan Perchepied, Zhuoheng Zhou, Goran Mitulović, et al.
Journal of Separation Science (2023) Vol. 46, Iss. 18
Open Access | Times Cited: 1
Identifying post-translational modifications with single cell proteomics
Benjamin C. Orsburn
(2023)
Open Access
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