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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
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 103

Showing 1-25 of 103 citing articles:

Atomic structures of respiratory complex III2, complex IV, and supercomplex III2-IV from vascular plants
María Maldonado, Fei Guo, James A. Letts
eLife (2021) Vol. 10
Open Access | Times Cited: 678
CryoDRGN: reconstruction of heterogeneous cryo-EM structures using neural networks
Ellen D. Zhong, Tristan Bepler, Bonnie Berger, et al.
Nature Methods (2021) Vol. 18, Iss. 2, pp. 176-185
Open Access | Times Cited: 496
Structure of the bacterial ribosome at 2 Å resolution
Zoe L. Watson, Fred R. Ward, Raphaël Méheust, et al.
eLife (2020) Vol. 9
Open Access | Times Cited: 212
Cryo-EM structures of the SARS-CoV-2 endoribonuclease Nsp15 reveal insight into nuclease specificity and dynamics
Monica C. Pillon, Meredith N. Frazier, Lucas Dillard, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 118
SARS-CoV-2 RBD in vitro evolution follows contagious mutation spread, yet generates an able infection inhibitor
Jiří Zahradník, Shir Marciano, Maya Shemesh, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 116
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
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
Structural Basis of Drug Recognition by the Multidrug Transporter ABCG2
Julia Kowal, Dongchun Ni, Scott M. Jackson, et al.
Journal of Molecular Biology (2021) Vol. 433, Iss. 13, pp. 166980-166980
Open Access | Times Cited: 69
Conformational heterogeneity and probability distributions from single-particle cryo-electron microscopy
Wai Shing Tang, Ellen D. Zhong, Sonya M. Hanson, et al.
Current Opinion in Structural Biology (2023) Vol. 81, pp. 102626-102626
Closed Access | Times Cited: 33
Methods for Cryo-EM Single Particle Reconstruction of Macromolecules Having Continuous Heterogeneity
Bogdan Toader, Fred J. Sigworth, Roy R. Lederman
Journal of Molecular Biology (2023) Vol. 435, Iss. 9, pp. 168020-168020
Open Access | Times Cited: 32
Present and Emerging Methodologies in Cryo-EM Single-Particle Analysis
Mengyu Wu, Gabriel C. Lander
Biophysical Journal (2020) Vol. 119, Iss. 7, pp. 1281-1289
Open Access | Times Cited: 59
Cryo-EM structure of the lysosomal chloride-proton exchanger CLC-7 in complex with OSTM1
Marina Schrecker, Julia Korobenko, Richard K. Hite
eLife (2020) Vol. 9
Open Access | Times Cited: 58
Cryo-EM structure and kinetics reveal electron transfer by 2D diffusion of cytochrome c in the yeast III-IV respiratory supercomplex
Agnes Moe, Justin M. Di Trani, John L. Rubinstein, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 11
Open Access | Times Cited: 49
An atomic model for the human septin hexamer by cryo-EM
Deborah C. Mendonça, Samuel Leite Guimarães, H.M. Pereira, et al.
Journal of Molecular Biology (2021) Vol. 433, Iss. 15, pp. 167096-167096
Closed Access | Times Cited: 44
A Bayesian approach to extracting free-energy profiles from cryo-electron microscopy experiments
Julian Giraldo-Barreto, Sebastian Ortiz, Erik H. Thiede, et al.
Scientific Reports (2021) Vol. 11, Iss. 1
Open Access | Times Cited: 42
Structure and lipid dynamics in the maintenance of lipid asymmetry inner membrane complex of A. baumannii
Daniel Mann, Junping Fan, Kamolrat Somboon, et al.
Communications Biology (2021) Vol. 4, Iss. 1
Open Access | Times Cited: 39
CryoDRGN2: Ab initio neural reconstruction of 3D protein structures from real cryo-EM images
Ellen D. Zhong, Adam Lerer, Joseph H. Davis, et al.
2021 IEEE/CVF International Conference on Computer Vision (ICCV) (2021), pp. 4046-4055
Closed Access | Times Cited: 39
Structures of β1-adrenergic receptor in complex with Gs and ligands of different efficacies
Minfei Su, Navid Paknejad, Lan Zhu, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 24
Resting mitochondrial complex I from Drosophila melanogaster adopts a helix-locked state
Abhilash Padavannil, Anjaneyulu Murari, Shauna-Kay Rhooms, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 14
Advances in integrative structural biology: Towards understanding protein complexes in their cellular context
Samantha J. Ziegler, S.J.B. Mallinson, Peter C. St. John, et al.
Computational and Structural Biotechnology Journal (2020) Vol. 19, pp. 214-225
Open Access | Times Cited: 39
The cryo-EM structure of the human uromodulin filament core reveals a unique assembly mechanism
Jessica J. Stanisich, Dawid Zyla, Pavel Afanasyev, et al.
eLife (2020) Vol. 9
Open Access | Times Cited: 37
Molecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD
Timothy P. Newing, Aaron J. Oakley, Michael Miller, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 34
A molecular mechanism for the generation of ligand-dependent differential outputs by the epidermal growth factor receptor
Yongjian Huang, Jana Ognjenović, Deepti Karandur, et al.
eLife (2021) Vol. 10
Open Access | Times Cited: 29
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