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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:

Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry
Mowei Zhou, Carter Lantz, Kyle A. Brown, et al.
Chemical Science (2020) Vol. 11, Iss. 48, pp. 12918-12936
Open Access | Times Cited: 121

Showing 1-25 of 121 citing articles:

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
Native Mass Spectrometry: Recent Progress and Remaining Challenges
Kelly R. Karch, Dalton T. Snyder, Sophie R. Harvey, et al.
Annual Review of Biophysics (2022) Vol. 51, Iss. 1, pp. 157-179
Closed Access | Times Cited: 100
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
PEPPI-MS: gel-based sample pre-fractionation for deep top-down and middle-down proteomics
Ayako Takemori, Philipp T. Kaulich, Andreas Tholey, et al.
Nature Protocols (2025)
Closed Access | Times Cited: 2
Top-down proteomics: challenges, innovations, and applications in basic and clinical research
Kyle A. Brown, Jake A. Melby, David S. Roberts, et al.
Expert Review of Proteomics (2020) Vol. 17, Iss. 10, pp. 719-733
Open Access | Times Cited: 120
Surface-induced Dissociation Mass Spectrometry as a Structural Biology Tool
Dalton T. Snyder, Sophie R. Harvey, Vicki H. Wysocki
Chemical Reviews (2021) Vol. 122, Iss. 8, pp. 7442-7487
Open Access | Times Cited: 65
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
Mass Spectrometry Methods for Measuring Protein Stability
Daniel D. Vallejo, Carolina Rojas Ramírez, Kristine F. Parson, et al.
Chemical Reviews (2022) Vol. 122, Iss. 8, pp. 7690-7719
Open Access | Times Cited: 57
Studying protein structure and function by native separation–mass spectrometry
Guusje van Schaick, Rob Haselberg, Govert W. Somsen, et al.
Nature Reviews Chemistry (2022) Vol. 6, Iss. 3, pp. 215-231
Open Access | Times Cited: 47
Frequency chasing of individual megadalton ions in an Orbitrap analyser improves precision of analysis in single-molecule mass spectrometry
Tobias P. Wörner, Konstantin Aizikov, Joost Snijder, et al.
Nature Chemistry (2022) Vol. 14, Iss. 5, pp. 515-522
Open Access | Times Cited: 46
Native top‐down mass spectrometry for higher‐order structural characterization of proteins and complexes
Ruijie Liu, Shujun Xia, Huilin Li
Mass Spectrometry Reviews (2022) Vol. 42, Iss. 5, pp. 1876-1926
Closed 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
On the Chemistry of Aqueous Ammonium Acetate Droplets during Native Electrospray Ionization Mass Spectrometry
Lars Konermann, Liu Ze-yuan, Yousef Haidar, et al.
Analytical Chemistry (2023) Vol. 95, Iss. 37, pp. 13957-13966
Closed Access | Times Cited: 23
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
Not All Arms of IgM Are Equal: Following Hinge-Directed Cleavage by Online Native SEC-Orbitrap-Based CDMS
Victor Yin, Evolène Deslignière, Nadia J. Mokiem, et al.
Journal of the American Society for Mass Spectrometry (2024) Vol. 35, Iss. 6, pp. 1320-1329
Open Access | Times Cited: 10
Top-down mass spectrometry of native proteoforms and their complexes: a community study
Tanja Habeck, Kyle A. Brown, Benjamin J. Des Soye, et al.
Nature Methods (2024)
Open Access | Times Cited: 9
Mass Spectrometry Analysis of Chemically and Collisionally Dissociated Molecular Glue- and PROTAC-Mediated Protein Complexes Informs on Disassembly Pathways
Edvaldo Vasconcelos Soares Maciel, Jonathan Eisert, J. Müller, et al.
Journal of the American Society for Mass Spectrometry (2025)
Closed Access | Times Cited: 1
Native top-down proteomics enables discovery in endocrine-resistant breast cancer
Fábio Pereira Gomes, Kenneth R. Durbin, Kevin L. Schauer, et al.
Nature Chemical Biology (2025)
Closed Access | Times Cited: 1
Approaches to Heterogeneity in Native Mass Spectrometry
Amber D. Rolland, James S. Prell
Chemical Reviews (2021) Vol. 122, Iss. 8, pp. 7909-7951
Open Access | Times Cited: 55
High-throughput screening of the ReFRAME, Pandemic Box, and COVID Box drug repurposing libraries against SARS-CoV-2 nsp15 endoribonuclease to identify small-molecule inhibitors of viral activity
Ryan Choi, Mowei Zhou, Roger Shek, et al.
PLoS ONE (2021) Vol. 16, Iss. 4, pp. e0250019-e0250019
Open Access | Times Cited: 42
Native Top-Down Mass Spectrometry with Collisionally Activated Dissociation Yields Higher-Order Structure Information for Protein Complexes
Carter Lantz, Benqian Wei, Boyu Zhao, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 48, pp. 21826-21830
Open Access | Times Cited: 30
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
Infrared Multiphoton Dissociation Enables Top‐Down Characterization of Membrane Protein Complexes and G Protein‐Coupled Receptors
Corinne A. Lutomski, Tarick J. El‐Baba, Joshua D. Hinkle, et al.
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 36
Open Access | Times Cited: 20
Probing membrane protein–lipid interactions
Mark T. Agasid, Carol V. Robinson
Current Opinion in Structural Biology (2021) Vol. 69, pp. 78-85
Open Access | Times Cited: 35
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