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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:

Optimal analytical strategies for sensitive and quantitative phosphoproteomics using TMT‐based multiplexing
Claire Koenig, Ana Martínez‐Val, Giulia Franciosa, et al.
PROTEOMICS (2022) Vol. 22, Iss. 19-20
Open Access | Times Cited: 20

Showing 20 citing articles:

Hybrid-DIA: intelligent data acquisition integrates targeted and discovery proteomics to analyze phospho-signaling in single spheroids
Ana Martínez‐Val, Kyle L. Fort, Claire Koenig, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 37
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
Recent advances in kinase signaling network profiling by mass spectrometry
Giulia Franciosa, Marie Locard‐Paulet, Lars Juhl Jensen, et al.
Current Opinion in Chemical Biology (2023) Vol. 73, pp. 102260-102260
Open Access | Times Cited: 19
Fully automated workflow for integrated sample digestion and Evotip loading enabling high-throughput clinical proteomics
Anders H. Kverneland, Florian Harking, Joel Mario Vej-Nielsen, et al.
Molecular & Cellular Proteomics (2024) Vol. 23, Iss. 7, pp. 100790-100790
Open Access | Times Cited: 7
Proteome-scale tissue mapping using mass spectrometry based on label-free and multiplexed workflows
Yumi Kwon, Jongmin Jacob Woo, Fengchao Yu, et al.
Molecular & Cellular Proteomics (2024) Vol. 23, Iss. 11, pp. 100841-100841
Open Access | Times Cited: 6
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
Protocol for high-throughput semi-automated label-free- or TMT-based phosphoproteome profiling
Claire Koenig, Ana Martínez‐Val, Previn Naicker, et al.
STAR Protocols (2023) Vol. 4, Iss. 3, pp. 102536-102536
Open Access | Times Cited: 14
Enamel proteins reveal biological sex and genetic variability within southern AfricanParanthropus
Palesa P. Madupe, Claire Koenig, Ioannis Patramanis, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 13
Recent progress in quantitative phosphoproteomics
Katharina Zittlau, Payal Nashier, Claudia Cavarischia-Rega, et al.
Expert Review of Proteomics (2023) Vol. 20, Iss. 12, pp. 469-482
Closed Access | Times Cited: 11
Quantitative proteomics and phosphoproteomics analysis of patient-derived ovarian cancer stem cells
Giulia Franciosa, Valentina Nieddu, Chiara Battistini, et al.
Molecular & Cellular Proteomics (2025), pp. 100965-100965
Open Access
Multiplexed phosphoproteomics of low cell numbers using SPARCE
Emily J. Gaizley, Xiuyuan Chen, Amandeep Bhamra, et al.
Communications Biology (2025) Vol. 8, Iss. 1
Open Access
Chemogenomic Screening in a Patient‐Derived 3D Fatty Liver Disease Model Reveals the CHRM1‐TRPM8 Axis as a Novel Module for Targeted Intervention
Sonia Youhanna, Aurino M. Kemas, Shane C. Wright, et al.
Advanced Science (2024)
Open Access | Times Cited: 2
O-linked glycosylations in human milk casein and major whey proteins during lactation
Martin Nørmark Thesbjerg, Katrine Overgaard Poulsen, Julie Astono, et al.
International Journal of Biological Macromolecules (2024) Vol. 267, pp. 131613-131613
Open Access | Times Cited: 1
Stable isotope labeling-based two-step derivatization strategy for analysis of Phosphopeptides
Lunfei Zou, Yao Wang, Xingdan Wang, et al.
Journal of Proteomics (2024) Vol. 297, pp. 105128-105128
Closed 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
Isobaric labeling: Expanding the breadth, accuracy, depth, and diversity of sample multiplexing
João A. Paulo
PROTEOMICS (2022) Vol. 22, Iss. 19-20
Open Access | Times Cited: 5
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
Quantitative Phosphoproteomic Profiling of Mouse Sperm Maturation in Epididymis Revealed Kinases Important for Sperm Motility
Xiangzheng Zhang, Haixia Tu, Xin Zhou, et al.
Molecular & Cellular Proteomics (2024) Vol. 23, Iss. 8, pp. 100810-100810
Open Access
Multiplexed phosphoproteomics of low cell numbers using SPARCE
Emily J. Gaizley, Xiuyuan Chen, Amandeep Bhamra, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Hybrid-DIA: Intelligent Data Acquisition for Simultaneous Targeted and Discovery Phosphoproteomics in Single Spheroids
Ana Martínez‐Val, Kyle L. Fort, Claire Koenig, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 2
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