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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:

Structural Biology outside the box — inside the cell
Jürgen M. Plitzko, Benjamin Schuler, Philipp Selenko
Current Opinion in Structural Biology (2017) Vol. 46, pp. 110-121
Open Access | Times Cited: 91

Showing 1-25 of 91 citing articles:

Critical assessment of protein intrinsic disorder prediction
Marco Necci, Damiano Piovesan, Md Tamjidul Hoque, et al.
Nature Methods (2021) Vol. 18, Iss. 5, pp. 472-481
Open Access | Times Cited: 282
The molecular basis for cellular function of intrinsically disordered protein regions
Alex S. Holehouse, Birthe B. Kragelund
Nature Reviews Molecular Cell Biology (2023) Vol. 25, Iss. 3, pp. 187-211
Open Access | Times Cited: 235
MobiDB 3.0: more annotations for intrinsic disorder, conformational diversity and interactions in proteins
Damiano Piovesan, Francesco Tabaro, Lisanna Paladin, et al.
Nucleic Acids Research (2017) Vol. 46, Iss. D1, pp. D471-D476
Open Access | Times Cited: 212
Single-molecule FRET imaging of GPCR dimers in living cells
Wesley B. Asher, Peter Geggier, Michael D. Holsey, et al.
Nature Methods (2021) Vol. 18, Iss. 4, pp. 397-405
Open Access | Times Cited: 162
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
Serial Lift-Out: sampling the molecular anatomy of whole organisms
Oda Helene Schiøtz, Christoph J. O. Kaiser, Sven Klumpe, et al.
Nature Methods (2023) Vol. 21, Iss. 9, pp. 1684-1692
Open Access | Times Cited: 56
Molecular Crowding: The History and Development of a Scientific Paradigm
Caterina Alfano, Yann Fichou, Klaus Huber, et al.
Chemical Reviews (2024) Vol. 124, Iss. 6, pp. 3186-3219
Open Access | Times Cited: 37
Multiscale methods in drug design bridge chemical and biological complexity in the search for cures
Rommie E. Amaro, Adrian J. Mulholland
Nature Reviews Chemistry (2018) Vol. 2, Iss. 4
Open Access | Times Cited: 153
Depletion interactions modulate the binding between disordered proteins in crowded environments
Franziska Zosel, Andrea Soranno, Karin Buholzer, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 24, pp. 13480-13489
Open Access | Times Cited: 123
Fully automated, sequential focused ion beam milling for cryo-electron tomography
Tobias Zachs, Andreas Schertel, João M. Medeiros, et al.
eLife (2020) Vol. 9
Open Access | Times Cited: 115
Intrinsically disordered proteins in crowded milieu: when chaos prevails within the cellular gumbo
Alexander V. Fonin, April L. Darling, Irina М. Kuznetsova, et al.
Cellular and Molecular Life Sciences (2018) Vol. 75, Iss. 21, pp. 3907-3929
Open Access | Times Cited: 93
The functional importance of structure in unstructured protein regions
Norman E. Davey
Current Opinion in Structural Biology (2019) Vol. 56, pp. 155-163
Open Access | Times Cited: 89
Nitroxide spin labels and EPR spectroscopy: A powerful association for protein dynamics studies
Francesco Torricella, Annalisa Pierro, Elisabetta Mileo, et al.
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (2021) Vol. 1869, Iss. 7, pp. 140653-140653
Open Access | Times Cited: 82
Mode of action of teixobactins in cellular membranes
Rhythm Shukla, João Medeiros‐Silva, Anish Parmar, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 76
Biomolecular and Biological Applications of Solid-State NMR with Dynamic Nuclear Polarization Enhancement
Wing Ying Chow, Gaël De Paëpe, Sabine Hediger
Chemical Reviews (2022) Vol. 122, Iss. 10, pp. 9795-9847
Open Access | Times Cited: 65
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
Interaction Dynamics of Intrinsically Disordered Proteins from Single-Molecule Spectroscopy
Aritra Chowdhury, Daniel Nettels, Benjamin Schuler
Annual Review of Biophysics (2023) Vol. 52, Iss. 1, pp. 433-462
Open Access | Times Cited: 33
Advanced Techniques for Detecting Protein Misfolding and Aggregation in Cellular Environments
Yulong Bai, Shengnan Zhang, Hui Dong, et al.
Chemical Reviews (2023) Vol. 123, Iss. 21, pp. 12254-12311
Closed Access | Times Cited: 27
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
Protein structure and interactions elucidated with in-cell NMR for different cell cycle phases and in 3D human tissue models
Jan Ryneš, Eva Ištvánková, Michaela Krafčíková, et al.
Communications Biology (2025) Vol. 8, Iss. 1
Open Access | Times Cited: 1
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
Unravelling molecular complexity in structural cell biology
Stefan Pfeffer, Julia Mahamid
Current Opinion in Structural Biology (2018) Vol. 52, pp. 111-118
Closed Access | Times Cited: 62
Cellular and Structural Studies of Eukaryotic Cells by Cryo-Electron Tomography
Miriam S. Weber, Matthias Wojtynek, Ohad Medalia
Cells (2019) Vol. 8, Iss. 1, pp. 57-57
Open Access | Times Cited: 56
Characterizing proteins in a native bacterial environment using solid-state NMR spectroscopy
Siddarth Narasimhan, Cecilia de Agrela Pinto, Alessandra Lucini Paioni, et al.
Nature Protocols (2021) Vol. 16, Iss. 2, pp. 893-918
Closed Access | Times Cited: 46
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
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