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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:

In-cell destabilization of a homodimeric protein complex detected by DEER spectroscopy
Yin Yang, Shen-Na Chen, Feng Yang, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 34, pp. 20566-20575
Open Access | Times Cited: 68

Showing 1-25 of 68 citing articles:

Macromolecular Crowding Is More than Hard-Core Repulsions
Shannon L. Speer, Claire J. Stewart, Liel Sapir, et al.
Annual Review of Biophysics (2022) Vol. 51, Iss. 1, pp. 267-300
Open Access | Times Cited: 96
In-Cell Structural Biology by NMR: The Benefits of the Atomic Scale
François‐Xavier Theillet
Chemical Reviews (2022) Vol. 122, Iss. 10, pp. 9497-9570
Open Access | Times Cited: 81
The intracellular environment affects protein–protein interactions
Shannon L. Speer, Wenwen Zheng, Xin Jiang, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 11
Open Access | Times Cited: 78
Exploring protein conformations in vitro and in cell with EPR distance measurements
Daniella Goldfarb
Current Opinion in Structural Biology (2022) Vol. 75, pp. 102398-102398
Open Access | Times Cited: 61
The ABC transporter MsbA adopts the wide inward-open conformation in E. coli cells
Laura Galazzo, Gianmarco Meier, Dovile Januliene, et al.
Science Advances (2022) Vol. 8, Iss. 41
Open Access | Times Cited: 59
Ultrafast Bioorthogonal Spin-Labeling and Distance Measurements in Mammalian Cells Using Small, Genetically Encoded Tetrazine Amino Acids
Subhashis Jana, Eric G.B. Evans, Hyo Sang Jang, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 27, pp. 14608-14620
Open Access | Times Cited: 42
Exploring the dynamics and structure of PpiB in living Escherichia coli cells using electron paramagnetic resonance spectroscopy
Yasmin Ben‐Ishay, Yoav Barak, Akiva Feintuch, et al.
Protein Science (2024) Vol. 33, Iss. 3
Open Access | Times Cited: 12
In-Cell Double Electron–Electron Resonance at Nanomolar Protein Concentrations
Svetlana Kucher, Christina Elsner, Mariya Safonova, et al.
The Journal of Physical Chemistry Letters (2021) Vol. 12, Iss. 14, pp. 3679-3684
Closed Access | Times Cited: 46
Visualizing Proteins in Mammalian Cells by 19F NMR Spectroscopy
Wenkai Zhu, Alex J. Guseman, Fatema Bhinderwala, et al.
Angewandte Chemie International Edition (2022) Vol. 61, Iss. 23
Open Access | Times Cited: 38
In-cell NMR: Why and how?
François‐Xavier Theillet, Enrico Luchinat
Progress in Nuclear Magnetic Resonance Spectroscopy (2022) Vol. 132-133, pp. 1-112
Open Access | Times Cited: 38
Electron paramagnetic resonance spectroscopy in structural-dynamic studies of large protein complexes
Laura Galazzo, Enrica Bordignon
Progress in Nuclear Magnetic Resonance Spectroscopy (2022) Vol. 134-135, pp. 1-19
Open Access | Times Cited: 36
Peptide-RNA Coacervates as a Cradle for the Evolution of Folded Domains
Manas Seal, Orit Weil‐Ktorza, Dragana Despotović, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 31, pp. 14150-14160
Open Access | Times Cited: 33
GdIII‐19F Distance Measurements for Proteins in Cells by Electron‐Nuclear Double Resonance
Manas Seal, Wenkai Zhu, Arina Dalaloyan, et al.
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 20
Open Access | Times Cited: 22
Dance with spins: site-directed spin labeling coupled to electron paramagnetic resonance spectroscopy directly inside cells
Annalisa Pierro, Malte Drescher
Chemical Communications (2023) Vol. 59, Iss. 10, pp. 1274-1284
Open Access | Times Cited: 17
Intracellular environment can change protein conformational dynamics in cells through weak interactions
Mengting Wang, Xiangfei Song, Jingfei Chen, et al.
Science Advances (2023) Vol. 9, Iss. 29
Open Access | Times Cited: 17
Protein-complex stability in cells and in vitro under crowded conditions
Samantha S. Stadmiller, Gary J. Pielak
Current Opinion in Structural Biology (2020) Vol. 66, pp. 183-192
Open Access | Times Cited: 45
Characteristics of Gd(III) spin labels for the study of protein conformations
Angeliki Giannoulis, Yasmin Ben‐Ishay, Daniella Goldfarb
Methods in enzymology on CD-ROM/Methods in enzymology (2021), pp. 235-290
Closed Access | Times Cited: 34
Nanomolar Pulse Dipolar EPR Spectroscopy in Proteins: CuII–CuII and Nitroxide–Nitroxide Cases
Katrin Ackermann, Joshua L. Wort, Bela E. Bode
The Journal of Physical Chemistry B (2021) Vol. 125, Iss. 20, pp. 5358-5364
Open Access | Times Cited: 33
Cleavage-Resistant Protein Labeling With Hydrophilic Trityl Enables Distance Measurements In-Cell
Zikri Hasanbasri, Kevin Singewald, Teresa D. Gluth, et al.
The Journal of Physical Chemistry B (2021) Vol. 125, Iss. 20, pp. 5265-5274
Open Access | Times Cited: 28
Robustness and Sensitivity of Gd(III)–Gd(III) Double Electron–Electron Resonance (DEER) Measurements: Comparative Study of High-Frequency EPR Spectrometer Designs and Spin Label Variants
Elena M. Mocanu, Yasmin Ben‐Ishay, Lydia Topping, et al.
Applied Magnetic Resonance (2025) Vol. 56, Iss. 5, pp. 591-611
Open Access
Rigid and stable nitroxide spin label for high-resolution distance measurements on proteins by DEER experiments
Yating Chen, Xing Zhang, Jia‐Liang Chen, et al.
Magnetic Resonance Letters (2025), pp. 200194-200194
Open Access
Quantifying protein-drug lifetimes in human cells by 19F NMR spectroscopy
Wenkai Zhu, Fatema Bhinderwala, Sarah Rambo, et al.
Journal of Biomolecular NMR (2025)
Closed Access
Crowding‐induced stabilization and destabilization in a single protein
Jordyn M. Markle, Tarynn D. Neal, Hania S. Kantzer, et al.
Protein Science (2025) Vol. 34, Iss. 5
Closed Access
Conformational Flexibility of the Protein Insertase BamA in the Native Asymmetric Bilayer Elucidated by ESR Spectroscopy
Aathira Gopinath, Benesh Joseph
Angewandte Chemie International Edition (2021) Vol. 61, Iss. 2
Open Access | Times Cited: 23
Light-induced pulsed dipolar EPR spectroscopy for distance and orientation analysis
Arnau Bertran, Antonio Barbon, Alice M. Bowen, et al.
Methods in enzymology on CD-ROM/Methods in enzymology (2022), pp. 171-231
Closed Access | Times Cited: 16
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