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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:

Novel Strategies to Address the Challenges in Top-Down Proteomics
Jake A. Melby, David S. Roberts, Eli J. Larson, et al.
Journal of the American Society for Mass Spectrometry (2021) Vol. 32, Iss. 6, pp. 1278-1294
Open Access | Times Cited: 148

Showing 1-25 of 148 citing articles:

Paleoproteomics
Christina Warinner, Kristine Korzow Richter, Matthew J. Collins
Chemical Reviews (2022) Vol. 122, Iss. 16, pp. 13401-13446
Open Access | Times Cited: 89
Recent advances in proteomics and metabolomics in plants
Shijuan Yan, Ruchika Bhawal, Zhibin Yin, et al.
Molecular Horticulture (2022) Vol. 2, Iss. 1
Open Access | Times Cited: 70
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
Top-down proteomics
David S. Roberts, Joseph A. Loo, Yury O. Tsybin, et al.
Nature Reviews Methods Primers (2024) Vol. 4, Iss. 1
Open Access | Times Cited: 20
Establishing a Top-Down Proteomics Platform on a Time-of-Flight Instrument with Electron-Activated Dissociation
Richard Searfoss, Emily Zahn, Zongtao Lin, et al.
Journal of Proteome Research (2025)
Closed Access | Times Cited: 2
Proteomes Are of Proteoforms: Embracing the Complexity
Katrina Carbonara, Martin Andonovski, Jens R. Coorssen
Proteomes (2021) Vol. 9, Iss. 3, pp. 38-38
Open Access | Times Cited: 78
Structural O-Glycoform Heterogeneity of the SARS-CoV-2 Spike Protein Receptor-Binding Domain Revealed by Top-Down Mass Spectrometry
David S. Roberts, Morgan Mann, Jake A. Melby, et al.
Journal of the American Chemical Society (2021) Vol. 143, Iss. 31, pp. 12014-12024
Open Access | Times Cited: 63
Reversed-Phase Liquid Chromatography of Peptides for Bottom-Up Proteomics: A Tutorial
Juraj Lenčo, Siddharth Jadeja, Denis K. Naplekov, et al.
Journal of Proteome Research (2022) Vol. 21, Iss. 12, pp. 2846-2892
Open Access | Times Cited: 41
Deciphering combinatorial post-translational modifications by top-down mass spectrometry
Jennifer S. Brodbelt
Current Opinion in Chemical Biology (2022) Vol. 70, pp. 102180-102180
Open Access | Times Cited: 40
Improved Identification of Proteoforms in Top-Down Proteomics Using FAIMS with Internal CV Stepping
Philipp T. Kaulich, Liam Cassidy, Konrad Winkels, et al.
Analytical Chemistry (2022) Vol. 94, Iss. 8, pp. 3600-3607
Closed Access | Times Cited: 39
High sensitivity top–down proteomics captures single muscle cell heterogeneity in large proteoforms
Jake A. Melby, Kyle A. Brown, Zachery R. Gregorich, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 19
Open Access | Times Cited: 37
A global view of the human post-translational modification landscape
Naoya Kitamura, James J. Galligan
Biochemical Journal (2023) Vol. 480, Iss. 16, pp. 1241-1265
Open Access | Times Cited: 35
Top-Down Proteomics and the Challenges of True Proteoform Characterization
Allen Po, Claire E. Eyers
Journal of Proteome Research (2023) Vol. 22, Iss. 12, pp. 3663-3675
Open Access | Times Cited: 34
Emergence of mass spectrometry detergents for membrane proteomics
Jan‐Simon Behnke, Leonhard H. Urner
Analytical and Bioanalytical Chemistry (2023) Vol. 415, Iss. 18, pp. 3897-3909
Open Access | Times Cited: 29
Native Top-Down Mass Spectrometry for Characterizing Sarcomeric Proteins Directly from Cardiac Tissue Lysate
Emily A. Chapman, Brad H. Li, Boris Krichel, et al.
Journal of the American Society for Mass Spectrometry (2024) Vol. 35, Iss. 4, pp. 738-745
Closed Access | Times Cited: 10
Unlocking the potential of microalgae as sustainable bioresources from up to downstream processing: A critical review
Priskila Adjani Diankristanti, Ngai Hei Ernest Ho, Jih-Heng Chen, et al.
Chemical Engineering Journal (2024) Vol. 488, pp. 151124-151124
Closed Access | Times Cited: 10
Integrating the milk microbiome signatures in mastitis: milk-omics and functional implications
Rine Christopher Reuben, Cármen Torres
World Journal of Microbiology and Biotechnology (2025) Vol. 41, Iss. 2
Open Access | Times Cited: 1
Characterizing Endogenous Protein Complexes with Biological Mass Spectrometry
Rivkah Rogawski, Michal Sharon
Chemical Reviews (2021) Vol. 122, Iss. 8, pp. 7386-7414
Open Access | Times Cited: 50
Advances in mass spectrometry‐based glycomics—An update covering the period 2017–2021
Kaitlyn Donohoo, Junyao Wang, Mona Goli, et al.
Electrophoresis (2021) Vol. 43, Iss. 1-2, pp. 119-142
Closed Access | Times Cited: 44
MASH Native: a unified solution for native top-down proteomics data processing
Eli J. Larson, Melissa R. Pergande, Michelle E. Moss, et al.
Bioinformatics (2023) Vol. 39, Iss. 6
Open Access | Times Cited: 21
Defining the Sarcomeric Proteoform Landscape in Ischemic Cardiomyopathy by Top-Down Proteomics
Emily A. Chapman, Timothy J. Aballo, Jake A. Melby, et al.
Journal of Proteome Research (2023) Vol. 22, Iss. 3, pp. 931-941
Closed Access | Times Cited: 20
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
Top-Down Proteomics Analysis of Picogram-Level Complex Samples Using Spray-Capillary-Based Capillary Electrophoresis–Mass Spectrometry
Zhitao Zhao, Yanting Guo, Trishika Chowdhury, et al.
Analytical Chemistry (2024) Vol. 96, Iss. 21, pp. 8763-8771
Closed Access | Times Cited: 6
Influence of different sample preparation approaches on proteoform identification by top-down proteomics
Philipp T. Kaulich, Kyowon Jeong, Oliver Kohlbacher, et al.
Nature Methods (2024)
Open Access | Times Cited: 6
Size-Based Proteome Fractionation through Polyacrylamide Gel Electrophoresis Combined with LC–FAIMS–MS for In-Depth Top-Down Proteomics
Ayako Takemori, Philipp T. Kaulich, Liam Cassidy, et al.
Analytical Chemistry (2022) Vol. 94, Iss. 37, pp. 12815-12821
Closed Access | Times Cited: 25
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