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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:

Better, Faster, Cheaper: Recent Advances in Cryo–Electron Microscopy
Eugene Y.D. Chua, Joshua H. Mendez, Micah Rapp, et al.
Annual Review of Biochemistry (2022) Vol. 91, Iss. 1, pp. 1-32
Open Access | Times Cited: 92

Showing 26-50 of 92 citing articles:

Utilizing Molecular Dynamics Simulations, Machine Learning, Cryo-EM, and NMR Spectroscopy to Predict and Validate Protein Dynamics
Ahrum Son, Woojin Kim, Jongham Park, et al.
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 17, pp. 9725-9725
Open Access | Times Cited: 3
Big data in contemporary electron microscopy: challenges and opportunities in data transfer, compute and management
David Poger, Lisa Yen, Filip Braet
Histochemistry and Cell Biology (2023) Vol. 160, Iss. 3, pp. 169-192
Open Access | Times Cited: 9
Structural basis of sRNA RsmZ regulation of Pseudomonas aeruginosa virulence
Xinyu Jia, Zhiling Pan, Yang Yuan, et al.
Cell Research (2023) Vol. 33, Iss. 4, pp. 328-330
Open Access | Times Cited: 8
An Efficient Method for Isolating and Purifying Nuclei from Mice Brain for Single-Molecule Imaging Using High-Speed Atomic Force Microscopy
Yujia Qiu, Elma Sakinatus Sajidah, Sota Kondo, et al.
Cells (2024) Vol. 13, Iss. 3, pp. 279-279
Open Access | Times Cited: 2
The advent of preventive high-resolution structural histopathology by artificial-intelligence-powered cryogenic electron tomography
Jesús G. Galaz-Montoya
(2024)
Open Access | Times Cited: 2
Learning to automate cryo-electron microscopy data collection with Ptolemy
Paul T. Kim, Alex J. Noble, Anchi Cheng, et al.
IUCrJ (2022) Vol. 10, Iss. 1, pp. 90-102
Open Access | Times Cited: 13
Enabling cryo‐EM density interpretation from yeast native cell extracts by proteomics data and AlphaFold structures
Christian Tüting, Lisa Schmidt, Ioannis Skalidis, et al.
PROTEOMICS (2023) Vol. 23, Iss. 17
Open Access | Times Cited: 7
Interaction of Vanadium Complexes with Proteins: Revisiting the Reported Structures in the Protein Data Bank (PDB) since 2015
Marino F. A. Santos, João Costa Pessoa
Molecules (2023) Vol. 28, Iss. 18, pp. 6538-6538
Open Access | Times Cited: 6
Structure and molecular mechanism of bacterial transcription activation
Dmytro Kompaniiets, Dong Wang, Yang Yang, et al.
Trends in Microbiology (2023) Vol. 32, Iss. 4, pp. 379-397
Closed Access | Times Cited: 6
Structural basis of mRNA maturation: Time to put it together
Matthias K. Vorländer, Belén Pacheco-Fiallos, Clemens Plaschka
Current Opinion in Structural Biology (2022) Vol. 75, pp. 102431-102431
Open Access | Times Cited: 11
Graph-theoretical prediction of biological modules in quaternary structures of large protein complexes
Florian J. Gisdon, Mariella Zunker, Jan Niclas Wolf, et al.
Bioinformatics (2024) Vol. 40, Iss. 3
Open Access | Times Cited: 1
Safari with an Electron Gun: Visualization of Protein and Membrane Interactions in Mitochondria in Natural Environment
Semen V. Nesterov, Konstantin S. Plokhikh, Yu. M. Chesnokov, et al.
Biochemistry (Moscow) (2024) Vol. 89, Iss. 2, pp. 257-268
Closed Access | Times Cited: 1
Cryo-EM Map Anisotropy Can Be Attenuated by Map Post-Processing and a New Method for Its Estimation
Rubén Sánchez-García, Guillaume Gaullier, José Manuel Cuadra Troncoso, et al.
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 7, pp. 3959-3959
Open Access | Times Cited: 1
Preparation of oxygen-sensitive proteins for high-resolution cryoEM structure determination using (an)aerobic blot-free vitrification
B. Cook, Sarah M. Narehood, Kelly L. McGuire, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Improved automated model building for cryo-EM maps using CryFold
Baoquan Su, Kun Huang, Zhong Peng, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
A Frame-by-Frame Glance at Membrane Fusion Mechanisms: From Viral Infections to Fertilization
Farshad C. Azimi, Trevor T. Dean, Karine Minari, et al.
Biomolecules (2023) Vol. 13, Iss. 7, pp. 1130-1130
Open Access | Times Cited: 4
Embracing Heterogeneity: Challenging the Paradigm of Replisomes as Deterministic Machines
Jacob S. Lewis, Antoine M. van Oijen, Lisanne M. Spenkelink
Chemical Reviews (2023) Vol. 123, Iss. 23, pp. 13419-13440
Open Access | Times Cited: 4
Screening of Buffers and Additives for Protein Stabilization by Thermal Shift Assay: A Practical Approach
Filipa S. S. Engrola, João Paquete-Ferreira, Teresa Santos‐Silva, et al.
Methods in molecular biology (2023), pp. 199-213
Closed Access | Times Cited: 2
Overcoming Resolution Attenuation During Tilted Cryo-EM Data Collection
Sriram Aiyer, Philip R. Baldwin, Shi Min Tan, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 2
Mass spectrometers as cryoEM grid preparation instruments
Michael S. Westphall, Kenneth W. Lee, Austin Z. Salome, et al.
Current Opinion in Structural Biology (2023) Vol. 83, pp. 102699-102699
Open Access | Times Cited: 2
Single-Particle Cryo-EM Data Collection with Stage Tilt using Leginon
Sriram Aiyer, Timothy S. Strutzenberg, M.E. Bowman, et al.
Journal of Visualized Experiments (2022), Iss. 185
Open Access | Times Cited: 4
Exploring advances in single particle CryoEM with apoferritin: From blobs to true atomic resolution
Gowtham ThambraRajan Premageetha, Kutti R. Vinothkumar, Sucharita Bose
The International Journal of Biochemistry & Cell Biology (2024) Vol. 169, pp. 106536-106536
Closed Access
Miffi: Improving the accuracy of CNN-based cryo-EM micrograph filtering with fine-tuning and Fourier space information
Xu Da, Nozomi Ando
Journal of Structural Biology (2024) Vol. 216, Iss. 2, pp. 108072-108072
Open Access
From solution to structure: empowering inclusive cryo-EM with a pre-characterization pipeline for biological samples
Christoph Mueller‐Dieckmann, Alessandro Grinzato, Grégory Effantin, et al.
Journal of Applied Crystallography (2024) Vol. 57, Iss. 2, pp. 602-605
Open Access
High-Resolution Cryo-Electron Microscopy Structure Determination of Haemophilus influenzae Tellurite-Resistance Protein A via 200 kV Transmission Electron Microscopy
Nhi L. Tran, Skerdi Senko, Kyle W. Lucier, et al.
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 8, pp. 4528-4528
Open Access

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