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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:

3D variability analysis: Resolving continuous flexibility and discrete heterogeneity from single particle cryo-EM
Ali Punjani, David J. Fleet
Journal of Structural Biology (2021) Vol. 213, Iss. 2, pp. 107702-107702
Open Access | Times Cited: 817

Showing 26-50 of 817 citing articles:

Structural basis for clearing of ribosome collisions by the RQT complex
Katharina Best, Ken Ikeuchi, Lukas Kater, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 44
How Pol α-primase is targeted to replisomes to prime eukaryotic DNA replication
Morgan Jones, Valentina Aria, Yasemin Baris, et al.
Molecular Cell (2023) Vol. 83, Iss. 16, pp. 2911-2924.e16
Open Access | Times Cited: 43
Time-resolved cryo-EM of G-protein activation by a GPCR
Makaía M. Papasergi-Scott, Guillermo Pérez‐Hernández, Hossein Batebi, et al.
Nature (2024) Vol. 629, Iss. 8014, pp. 1182-1191
Open Access | Times Cited: 43
Menin “reads” H3K79me2 mark in a nucleosomal context
Jianwei Lin, Yiping Wu, Gaofei Tian, et al.
Science (2023) Vol. 379, Iss. 6633, pp. 717-723
Closed Access | Times Cited: 42
Targeting cancer with small-molecule pan-KRAS degraders
Johannes Popow, William Farnaby, Andreas Gollner, et al.
Science (2024) Vol. 385, Iss. 6715, pp. 1338-1347
Open Access | Times Cited: 35
Co-opting the E3 ligase KLHDC2 for targeted protein degradation by small molecules
Christopher M. Hickey, Katherine M. Digianantonio, Kurt Zimmermann, et al.
Nature Structural & Molecular Biology (2024) Vol. 31, Iss. 2, pp. 311-322
Closed Access | Times Cited: 25
Transition of human γ-tubulin ring complex into a closed conformation during microtubule nucleation
Cláudia Brito, Marina Serna, Pablo Guerra, et al.
Science (2024) Vol. 383, Iss. 6685, pp. 870-876
Closed Access | Times Cited: 25
Learning structural heterogeneity from cryo-electron sub-tomograms with tomoDRGN
Barrett M. Powell, Joseph H. Davis
Nature Methods (2024) Vol. 21, Iss. 8, pp. 1525-1536
Closed Access | Times Cited: 24
Structure and interactions of the endogenous human Commander complex
Saara Laulumaa, Esa‐Pekka Kumpula, Juha T. Huiskonen, et al.
Nature Structural & Molecular Biology (2024) Vol. 31, Iss. 6, pp. 925-938
Open Access | Times Cited: 22
Structure of human phagocyte NADPH oxidase in the activated state
Xiaoyu Liu, Yiting Shi, Rui Liu, et al.
Nature (2024) Vol. 627, Iss. 8002, pp. 189-195
Closed Access | Times Cited: 21
Mechanism of single-stranded DNA annealing by RAD52–RPA complex
Chih-Chao Liang, Luke A. Greenhough, Laura Masino, et al.
Nature (2024) Vol. 629, Iss. 8012, pp. 697-703
Open Access | Times Cited: 21
Stepwise activation of a metabotropic glutamate receptor
Kaavya Krishna Kumar, Haoqing Wang, Chris Habrian, et al.
Nature (2024) Vol. 629, Iss. 8013, pp. 951-956
Closed Access | Times Cited: 17
Structural mechanisms of α7 nicotinic receptor allosteric modulation and activation
Sean M. Burke, Mariia Avstrikova, Colleen Noviello, et al.
Cell (2024) Vol. 187, Iss. 5, pp. 1160-1176.e21
Open Access | Times Cited: 16
Structural and functional analysis of the Nipah virus polymerase complex
Side Hu, Heesu Kim, Pan Yang, et al.
Cell (2025)
Open Access | Times Cited: 2
AI-based methods for biomolecular structure modeling for Cryo-EM
Farhanaz Farheen, Genki Terashi, Han Zhu, et al.
Current Opinion in Structural Biology (2025) Vol. 90, pp. 102989-102989
Closed Access | Times Cited: 2
Asymmetric activation of the calcium-sensing receptor homodimer
Yang Gao, Michael J. Robertson, Sabrina N. Rahman, et al.
Nature (2021) Vol. 595, Iss. 7867, pp. 455-459
Open Access | Times Cited: 101
Deep learning-based mixed-dimensional Gaussian mixture model for characterizing variability in cryo-EM
Muyuan Chen, Steven J. Ludtke
Nature Methods (2021) Vol. 18, Iss. 8, pp. 930-936
Open Access | Times Cited: 93
Structure determination of GPCRs: cryo-EM compared with X-ray crystallography
Javier García‐Nafría, Christopher G. Tate
Biochemical Society Transactions (2021) Vol. 49, Iss. 5, pp. 2345-2355
Open Access | Times Cited: 85
Cryo-EM structures of human RNA polymerase III in its unbound and transcribing states
Mathias Girbig, Agata D. Misiaszek, Matthias K. Vorländer, et al.
Nature Structural & Molecular Biology (2021) Vol. 28, Iss. 2, pp. 210-219
Open Access | Times Cited: 83
Structure of human GABAB receptor in an inactive state
Jinseo Park, Ziao Fu, Aurel Frangaj, et al.
Nature (2020) Vol. 584, Iss. 7820, pp. 304-309
Open Access | Times Cited: 81
Structural and mechanistic basis of the EMC-dependent biogenesis of distinct transmembrane clients
Lakshmi E. Miller-Vedam, Bastian Bräuning, Katerina D. Popova, et al.
eLife (2020) Vol. 9
Open Access | Times Cited: 80
The role of structural dynamics in GPCR‐mediated signaling
Daniel Hilger
FEBS Journal (2021) Vol. 288, Iss. 8, pp. 2461-2489
Open Access | Times Cited: 80
Cryo-EM of NHEJ supercomplexes provides insights into DNA repair
Amanda K. Chaplin, Steven W. Hardwick, Antonia Kefala Stavridi, et al.
Molecular Cell (2021) Vol. 81, Iss. 16, pp. 3400-3409.e3
Open Access | Times Cited: 80
Type VII secretion systems: structure, functions and transport models
Ángel Rivera-Calzada, N. Famelis, Óscar Llorca, et al.
Nature Reviews Microbiology (2021) Vol. 19, Iss. 9, pp. 567-584
Closed Access | Times Cited: 78
Structures of ABCG2 under turnover conditions reveal a key step in the drug transport mechanism
Qin Yu, Dongchun Ni, Julia Kowal, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 74

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