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:

Structural Investigation of Therapeutic Antibodies Using Hydroxyl Radical Protein Footprinting Methods
Corie Y. Ralston, Joshua S. Sharp
Antibodies (2022) Vol. 11, Iss. 4, pp. 71-71
Open Access | Times Cited: 11

Showing 11 citing articles:

Hydrogen/Deuterium Exchange and Protein Oxidative Footprinting with Mass Spectrometry Collectively Discriminate the Binding of Small-Molecule Therapeutics to Bcl-2
Yan Sun, Damian J. Houde, Roxana E. Iacob, et al.
Analytical Chemistry (2025) Vol. 97, Iss. 8, pp. 4329-4340
Closed Access | Times Cited: 1

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: 18

Extracting Residue Solvent Exposure from Covalent Labeling Data with Machine Learning: A Hybrid Approach for Protein Structure Prediction
Elijah H. Day, Steffen Lindert
Journal of the American Society for Mass Spectrometry (2025)
Closed Access

Recent advances in structural mass spectrometry methods in the context of biosimilarity assessment: from sequence heterogeneities to higher order structures
J.-G. Castel, S. Delaux, Oscar Hernandez‐Alba, et al.
Journal of Pharmaceutical and Biomedical Analysis (2023) Vol. 236, pp. 115696-115696
Open Access | Times Cited: 8

Evaluating Mass Spectrometry-Based Hydroxyl Radical Protein Footprinting of a Benchtop Flash Oxidation System against a Synchrotron X-ray Beamline
Rohit Jain, Nanak S. Dhillon, Vijaya Lakshmi Kanchustambham, et al.
Journal of the American Society for Mass Spectrometry (2024) Vol. 35, Iss. 3, pp. 476-486
Closed Access | Times Cited: 2

Characterization of Higher Order Structural Changes of a Thermally Stressed Monoclonal Antibody via Mass Spectrometry Footprinting and Other Biophysical Approaches
Yanchun Lin, Austin B. Moyle, V. Beaumont, et al.
Analytical Chemistry (2023) Vol. 95, Iss. 46, pp. 16840-16849
Closed Access | Times Cited: 6

Biophysical and Integrative Characterization of Protein Intrinsic Disorder as a Prime Target for Drug Discovery
Shuqi Luo, Samuel Wohl, Wenwei Zheng, et al.
Biomolecules (2023) Vol. 13, Iss. 3, pp. 530-530
Open Access | Times Cited: 4

Systematic Fe(II)-EDTA Method of Dose-Dependent Hydroxyl Radical Generation for Protein Oxidative Footprinting
Jessica R. Chapman, Max Paukner, Micheal Leser, et al.
Analytical Chemistry (2023) Vol. 95, Iss. 50, pp. 18316-18325
Open Access | Times Cited: 4

Epitope mapping of SARS-CoV-2 RBDs by hydroxyl radical protein footprinting reveals the importance of including negative antibody controls
Daniel Nyberg Larsen, Jakub Zbigniew Kaczmarek, Yaseelan Palarasah, et al.
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (2024) Vol. 1872, Iss. 4, pp. 141011-141011
Open Access

Residue-Specific Epitope Mapping of the PD-1/Nivolumab Interaction Using X-ray Footprinting Mass Spectrometry
Line G. Kristensen, Sayan Gupta, Yan Chen, et al.
Antibodies (2024) Vol. 13, Iss. 3, pp. 77-77
Open Access

Epitope mapping of SARS-CoV-2 RBDs by hydroxyl radical protein footprinting reveals the importance of including negative antibody controls
Daniel Nyberg Larsen, Jakub Zbigniew Kaczmarek, Yaseelan Palarasah, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access

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