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:

Fundamentals of HDX-MS
Vanesa Vinciauskaite, Glenn R. Masson
Essays in Biochemistry (2022) Vol. 67, Iss. 2, pp. 301-314
Open Access | Times Cited: 33

Showing 1-25 of 33 citing articles:

Ion Mobility Mass Spectrometry (IM-MS) for Structural Biology: Insights Gained by Measuring Mass, Charge, and Collision Cross Section
Emilia Christofi, Perdita E. Barran
Chemical Reviews (2023) Vol. 123, Iss. 6, pp. 2902-2949
Open Access | Times Cited: 99

Spartin-mediated lipid transfer facilitates lipid droplet turnover
Neng Wan, Zhouping Hong, Matthew AH Parson, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 3
Open Access | Times Cited: 6

Hydrogen/Deuterium Exchange Mass Spectrometry: Fundamentals, Limitations, and Opportunities
Lars Konermann, Pablo M. Scrosati
Molecular & Cellular Proteomics (2024) Vol. 23, Iss. 11, pp. 100853-100853
Open Access | Times Cited: 6

Hydrogen–Deuterium Exchange Mass Spectrometry Identifies Local and Long-Distance Interactions within the Multicomponent Radical SAM Enzyme, PqqE
Wen Zhu, Anthony T. Iavarone, Judith P. Klinman
ACS Central Science (2024) Vol. 10, Iss. 2, pp. 251-263
Open Access | Times Cited: 4

Higher-Order Structure of Adeno-Associated Virus Serotype 8 by Hydrogen/Deuterium Exchange Mass Spectrometry
Tomohiko Ikeda, Yuki Yamaguchi, Hiroaki Oyama, et al.
Viruses (2024) Vol. 16, Iss. 4, pp. 585-585
Open Access | Times Cited: 4

Neurofilament Light Chain under the Lens of Structural Mass Spectrometry
Salomé Coppens, Dea Gogishvili, Valentina Faustinelli, et al.
ACS Chemical Neuroscience (2025) Vol. 16, Iss. 2, pp. 141-151
Open Access

TRAMP assembly alters the conformation and RNA binding of Mtr4 and Trf4-Air2
Joshua Denson, Naifu Zhang, Darby Ball, et al.
Proceedings of the National Academy of Sciences (2025) Vol. 122, Iss. 1
Open Access

Structural insights into the interplay between microtubule polymerases, γ-tubulin complexes and their receptors
Anjun Zheng, Bram J. A. Vermeulen, Martin Würtz, et al.
Nature Communications (2025) Vol. 16, 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

Two-Component System Sensor Kinase Inhibitors Target the ATP-Lid of PmrB to Disrupt Colistin Resistance in Acinetobacter baumannii
Alexander D. Hondros, Milah M. Young, Felicia E. Jaimes, et al.
Biochemistry (2025)
Closed Access

Kingfisher: An open‐sourced web‐based platform for the analysis of hydrogen exchange mass spectrometry data
Nathan McLaughlin, Juan P. Rincon Pabon, Samantha Gies, et al.
Protein Science (2025) Vol. 34, Iss. 4
Closed Access

HRaDeX: R Package and Web Server for Computing High-Resolution Deuterium Uptake Rates for HDX–MS Data
Weronika Puchała, Michał Kistowski, Liliya Zhukova, et al.
Journal of Proteome Research (2025)
Open Access

Mapping the structural heterogeneity of Pup ligase PafA using H/D exchange mass spectrometry
Alicia Plourde, Jacquelyn C. Ogata-Bean, Siavash Vahidi
Journal of Biological Chemistry (2025), pp. 108437-108437
Open Access

The molecular properties of the bHLH TCF4 protein as an intrinsically disordered hub transcription factor
Nikola Sozańska, Barbara P. Klepka, Anna Niedźwiecka, et al.
Cell Communication and Signaling (2025) Vol. 23, Iss. 1
Open Access

Mechanism of allosteric activation in human mitochondrial ClpP protease
Monica M. Goncalves, Adwaith B. Uday, Taylor J. B. Forrester, et al.
Proceedings of the National Academy of Sciences (2025) Vol. 122, Iss. 16
Open Access

The metabolic sensor AMPK: Twelve enzymes in one
William J. Smiles, Ashley J. Ovens, Jonathan S. Oakhill, et al.
Molecular Metabolism (2024) Vol. 90, pp. 102042-102042
Open Access | Times Cited: 3

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

Exploring snake venoms beyond the primary sequence: From proteoforms to protein-protein interactions
C. Ruth Wang, Lewis O. McFarlane, Tara L. Pukala
Toxicon (2024) Vol. 247, pp. 107841-107841
Open Access | Times Cited: 2

Cyclic Ion Mobility for Hydrogen/Deuterium Exchange-Mass Spectrometry Applications
Damon Griffiths, Malcolm Anderson, Keith Richardson, et al.
Analytical Chemistry (2024) Vol. 96, Iss. 15, pp. 5869-5877
Open Access | Times Cited: 1

Inclusion of deuterated glycopeptides provides increased sequence coverage in hydrogen/deuterium exchange mass spectrometry analysis of SARS‐CoV‐2 spike glycoprotein
Christopher A. Haynes, Theodore R. Keppel, Betlehem Mekonnen, et al.
Rapid Communications in Mass Spectrometry (2024) Vol. 38, Iss. 5
Open Access

Elucidation of the Reversible Self-Association Interface of a Diabody–Interleukin Fusion Protein Using Hydrogen-Exchange Mass Spectrometry and In Silico Modeling
Martin Eisinger, Harri Rahn, Yong Chen, et al.
Molecular Pharmaceutics (2024) Vol. 21, Iss. 9, pp. 4285-4296
Closed Access

Phosphorylation-induced flexibility of proto-oncogenic Bcl3 regulates transcriptional activation by NF-κB p52 homodimer
Wenfei Pan, Tapan Biswas, Shandy Shahabi, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Closed Access

TRAMP assembly alters the conformation and RNA binding of Mtr4 and Trf4-Air2
Joshua Denson, Naifu Zhang, Darby Ball, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

HDX-MS Analysis of Catalytic Activation of IKK2 in the IκB Kinase Complex
William Suryajaya, Tapan Biswas, Shandy Shahabi, et al.
Biochemistry (2024) Vol. 63, Iss. 18, pp. 2323-2334
Closed Access

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