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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:

Improving Spectral Validation Rates in Hydrogen–Deuterium Exchange Data Analysis
Shaunak Raval, Vladimir Sarpe, Morgan Hepburn, et al.
Analytical Chemistry (2021) Vol. 93, Iss. 9, pp. 4246-4254
Closed Access | Times Cited: 21

Showing 21 citing articles:

Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems
Ellie I. James, Taylor A. Murphree, Clint Vorauer, et al.
Chemical Reviews (2021) Vol. 122, Iss. 8, pp. 7562-7623
Open Access | Times Cited: 217
Novobiocin blocks nucleic acid binding to Polθ and inhibits stimulation of its ATPase activity
Aleem Syed, František Filandr, Jeffrey Patterson-Fortin, et al.
Nucleic Acids Research (2023) Vol. 51, Iss. 18, pp. 9920-9937
Open Access | Times Cited: 18
Hydrogen deuterium exchange and other mass spectrometry- based approaches for epitope mapping
Prashant N. Jethva, Michael L. Gross
Frontiers in Analytical Science (2023) Vol. 3
Open Access | Times Cited: 17
Automating data analysis for hydrogen/deuterium exchange mass spectrometry using data-independent acquisition methodology
František Filandr, Vladimir Sarpe, Shaunak Raval, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 8
The HisRS-like domain of GCN2 is a pseudoenzyme that can bind uncharged tRNA
Jay Z. Yin, Alexander F. A. Keszei, Scott Houliston, et al.
Structure (2024) Vol. 32, Iss. 6, pp. 795-811.e6
Closed Access | Times Cited: 7
Arsenal of nanobodies shows broad-spectrum neutralization against SARS-CoV-2 variants of concern in vitro and in vivo in hamster models
Martín A. Rossotti, Henk van Faassen, Anh Tran, et al.
Communications Biology (2022) Vol. 5, Iss. 1
Open Access | Times Cited: 26
Single-molecule analysis reveals that IPMK enhances the DNA-binding activity of the transcription factor SRF
Hyoungjoon Ahn, Jeongmin Yu, Kwangmin Ryu, et al.
Nucleic Acids Research (2025) Vol. 53, Iss. 1
Open Access
Recalibrating Protection Factors Using Millisecond Hydrogen/Deuterium Exchange Mass Spectrometry
Michele Stofella, Neeleema Seetaloo, Alexander N. St John, et al.
Analytical Chemistry (2025)
Open Access
Examining Instrumental Factors Influencing the Performance of Data-Independent Acquisition Methods in Hydrogen/Deuterium Exchange Mass Spectrometry
František Filandr, Morgan Hepburn, Vladimir Sarpe, et al.
Analytical Chemistry (2025)
Closed Access
Advancing Structural Biology and Protein-Ligand Interactions through Hydrogen/Deuterium Exchange Mass Spectrometry (HDX-MS)
Kanika Arora, Konrad Celejewski, Dominic Narang
Methods in molecular biology (2025), pp. 181-192
Closed Access
Broadly neutralizing aptamers to SARS-CoV-2: A diverse panel of modified DNA antiviral agents
Amy D. Gelinas, Tiong Kit Tan, Sai Liu, et al.
Molecular Therapy — Nucleic Acids (2023) Vol. 31, pp. 370-382
Open Access | Times Cited: 10
Elucidating Protein–Ligand Interactions in Cell Lysates Using High-Throughput Hydrogen–Deuterium Exchange Mass Spectrometry with Integrated Protein Thermal Depletion
Mulin Fang, Oliver Wu, Kellye A. Cupp‐Sutton, et al.
Analytical Chemistry (2023) Vol. 95, Iss. 3, pp. 1805-1810
Closed Access | Times Cited: 7
Computational Tools for Hydrogen–Deuterium Exchange Mass Spectrometry Data Analysis
Michele Stofella, Anna Grimaldi, Jochem H. Smit, et al.
Chemical Reviews (2024) Vol. 124, Iss. 21, pp. 12242-12263
Open Access | Times Cited: 2
Apparatus for Automated Continuous Hydrogen Deuterium Exchange Mass Spectrometry Measurements from Milliseconds to Hours
Joseph F. Anacleto, Cristina Lento, Vladimir Sarpe, et al.
Analytical Chemistry (2023) Vol. 95, Iss. 9, pp. 4421-4428
Open Access | Times Cited: 6
The Deuterium Calculator: An Open-Source Tool for Hydrogen–Deuterium Exchange Mass Spectrometry Analysis
Kellye A. Cupp‐Sutton, Thomas Welborn, Mulin Fang, et al.
Journal of Proteome Research (2023) Vol. 22, Iss. 2, pp. 532-538
Closed Access | Times Cited: 5
Probing Antibody Structures by Hydrogen/Deuterium Exchange Mass Spectrometry
Z. Kalaninová, Lukáš Fojtík, Josef Chmelı́k, et al.
Methods in molecular biology (2023), pp. 303-334
Closed Access | Times Cited: 2
Influence of variant-specific mutations, temperature and pH on conformations of a large set of SARS-CoV-2 spike trimer vaccine antigen candidates
Matthew Stuible, Joseph D. Schrag, Joey G. Sheff, et al.
Scientific Reports (2023) Vol. 13, Iss. 1
Open Access | Times Cited: 2
Chaperone requirements for de novo folding of Saccharomyces cerevisiae septins
Daniel Hassell, Ashley S. Denney, Emily Singer, et al.
Molecular Biology of the Cell (2022) Vol. 33, Iss. 12
Open Access | Times Cited: 3
Automating data analysis for hydrogen/deuterium exchange mass spectrometry using data-independent acquisition methodology
František Filandr, Vladimir Sarpe, Shaunak Raval, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 1
Arsenal of Nanobodies for Broad-Spectrum Countermeasures against Current and Future SARS-CoV-2 Variants of Concerns
Martín A. Rossotti, Henk van Faassen, Anh Tran, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 2
Chaperone Requirements for De Novo Folding of Saccharomyces cerevisiae Septins
Daniel Hassell, Ashley S. Denney, Emily Singer, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access
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