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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:

Interpretation of medium resolution cryoEM maps of multi-protein complexes
Ana Casañal, Shabih Shakeel, Lori A. Passmore
Current Opinion in Structural Biology (2019) Vol. 58, pp. 166-174
Open Access | Times Cited: 20

Showing 20 citing articles:

Leveraging crosslinking mass spectrometry in structural and cell biology
Andrea Graziadei, Juri Rappsilber
Structure (2021) Vol. 30, Iss. 1, pp. 37-54
Open Access | Times Cited: 77
Mechanism of antibody-specific deglycosylation and immune evasion by Streptococcal IgG-specific endoglycosidases
Beatriz Trastoy, Jonathan J. Du, Javier O. Cifuente, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 15
Protein structure dynamics by crosslinking mass spectrometry
Zhuo A. Chen, Juri Rappsilber
Current Opinion in Structural Biology (2023) Vol. 80, pp. 102599-102599
Closed Access | Times Cited: 12
Advancing structure modeling from cryo-EM maps with deep learning
Shu Li, Genki Terashi, Zicong Zhang, et al.
Biochemical Society Transactions (2025) Vol. 53, Iss. 01
Closed Access
Tightening the Crosslinking Distance Restraints for Better Resolution of Protein Structure and Dynamics
Zhou Gong, Shang-Xiang Ye, Chun Tang
Structure (2020) Vol. 28, Iss. 10, pp. 1160-1167.e3
Open Access | Times Cited: 21
Cross-linking and mass spectrometry as a tool for studying the structural biology of ribonucleoproteins
Chris P. Sarnowski, Maria Bikaki, Alexander Leitner
Structure (2022) Vol. 30, Iss. 4, pp. 441-461
Open Access | Times Cited: 11
Refinement of AlphaFold2 models against experimental and hybrid cryo-EM density maps
Maytha Alshammari, Willy Wriggers, Jiangwen Sun, et al.
QRB Discovery (2022) Vol. 3
Open Access | Times Cited: 11
Yeast Inner-Subunit PA–NZ-1 Labeling Strategy for Accurate Subunit Identification in a Macromolecular Complex through Cryo-EM Analysis
Huping Wang, Wenyu Han, Junichi Takagi, et al.
Journal of Molecular Biology (2018) Vol. 430, Iss. 10, pp. 1417-1425
Closed Access | Times Cited: 17
Elucidation of structure–function relationships in Methanocaldococcus jannaschii RNase P, a multi-subunit catalytic ribonucleoprotein
Hong‐Duc Phan, Andrew Norris, Chen Du, et al.
Nucleic Acids Research (2022) Vol. 50, Iss. 14, pp. 8154-8167
Open Access | Times Cited: 8
Refinement of AlphaFold2 Models against Experimental Cryo-EM Density Maps at 4-6Å Resolution
Maytha Alshammari, Jing He, Willy Wriggers
2021 IEEE International Conference on Bioinformatics and Biomedicine (BIBM) (2022), pp. 3423-3430
Closed Access | Times Cited: 6
Structural Insights into the Interaction between Bacillus subtilis SepF Assembly and FtsZ by Solid-State NMR Spectroscopy
Chang Zhang, Wenjing Liu, Jing Deng, et al.
The Journal of Physical Chemistry B (2022) Vol. 126, Iss. 28, pp. 5219-5230
Closed Access | Times Cited: 5
Crosslinker Nanocarriers Delivery to Chloroplasts for In Vivo Mapping of Photosynthetic Membrane Protein Complexes in Living Chlamydomonas reinhardtii Cells
Xinwei Li, Yuwan Chen, Jing Jiang, et al.
Analytical Chemistry (2023) Vol. 95, Iss. 25, pp. 9555-9563
Closed Access | Times Cited: 1
Three-Dimensional Graph Matching to Identify Secondary Structure Correspondence of Medium-Resolution Cryo-EM Density Maps
Bahareh Behkamal, Mahmoud Naghibzadeh, Mohammad Reza Saberi, et al.
Biomolecules (2021) Vol. 11, Iss. 12, pp. 1773-1773
Open Access | Times Cited: 3
Towards Molecular Mechanism in Long Non-coding RNAs: Linking Structure and Function
Karissa Y. Sanbonmatsu
Advances in experimental medicine and biology (2022), pp. 23-32
Closed Access | Times Cited: 1
Recommendation: Refinement of AlphaFold2 Models against Experimental and Hybrid Cryo-EM Density Maps — R1/PR4
Maytha Alshammari, Willy Wriggers, Jiangwen Sun, et al.
(2022)
Open Access
Recommendation: Refinement of AlphaFold2 Models against Experimental and Hybrid Cryo-EM Density Maps — R2/PR5
Maytha Alshammari, Willy Wriggers, Jiangwen Sun, et al.
(2022)
Open Access
Recommendation: Refinement of AlphaFold2 Models against Experimental and Hybrid Cryo-EM Density Maps — R0/PR3
Maytha Alshammari, Willy Wriggers, Jiangwen Sun, et al.
(2022)
Open Access
Review: Refinement of AlphaFold2 Models against Experimental and Hybrid Cryo-EM Density Maps — R0/PR2
Maytha Alshammari, Willy Wriggers, Jiangwen Sun, et al.
(2022)
Open Access
Review: Refinement of AlphaFold2 Models against Experimental and Hybrid Cryo-EM Density Maps — R0/PR1
Maytha Alshammari, Willy Wriggers, Jiangwen Sun, et al.
(2022)
Open Access
Cryo-EM structure of human Nup155 reveals the biochemical basis for atrial fibrillation linked genetic mutation R391H
Sangeeta Niranjan, Jyotsana Singh, Radha Chauhan
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access
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