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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:

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

Showing 1-25 of 212 citing articles:

Computed structures of core eukaryotic protein complexes
Ian R. Humphreys, Jimin Pei, Minkyung Baek, et al.
Science (2021) Vol. 374, Iss. 6573
Open Access | Times Cited: 456
A comprehensive review of m6A/m6Am RNA methyltransferase structures
Stephanie Oerum, Vincent Meynier, Marjorie Catala, et al.
Nucleic Acids Research (2021) Vol. 49, Iss. 13, pp. 7239-7255
Open Access | Times Cited: 352
Origin and Evolution of the Ribosome
George E. Fox
Cold Spring Harbor Perspectives in Biology (2010) Vol. 2, Iss. 9, pp. a003483-a003483
Open Access | Times Cited: 258
Nucleic acid nanoassembly-enhanced RNA therapeutics and diagnosis
Mengnan Zhao, Rujing Wang, Kunmeng Yang, et al.
Acta Pharmaceutica Sinica B (2022) Vol. 13, Iss. 3, pp. 916-941
Open Access | Times Cited: 84
ArtiaX: An electron tomography toolbox for the interactive handling of sub‐tomograms in UCSF ChimeraX
Utz H. Ermel, Serena M. Arghittu, Achilleas S. Frangakis
Protein Science (2022) Vol. 31, Iss. 12
Open Access | Times Cited: 78
Structural conservation of antibiotic interaction with ribosomes
Helge Paternoga, Caillan Crowe‐McAuliffe, Lars V. Bock, et al.
Nature Structural & Molecular Biology (2023) Vol. 30, Iss. 9, pp. 1380-1392
Open Access | Times Cited: 48
The translating bacterial ribosome at 1.55 Å resolution generated by cryo-EM imaging services
Simon A. Fromm, Kate M. O’Connor, Michael D. Purdy, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 44
The structure of the human 80S ribosome at 1.9 Å resolution reveals the molecular role of chemical modifications and ions in RNA
Samuel Holvec, Charles Barchet, Antony Lechner, et al.
Nature Structural & Molecular Biology (2024) Vol. 31, Iss. 8, pp. 1251-1264
Closed Access | Times Cited: 18
Metals in Motion: Understanding Labile Metal Pools in Bacteria
John D. Helmann
Biochemistry (2025)
Closed Access | Times Cited: 3
Ligand-binding pockets in RNA, and where to find them
Seth D. Veenbaas, Jordan T. Koehn, Patrick S. Irving, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access | Times Cited: 2
Translational Control by Ribosome Pausing in Bacteria: How a Non-uniform Pace of Translation Affects Protein Production and Folding
Ekaterina Samatova, Jan Daberger, Marija Liutkute, et al.
Frontiers in Microbiology (2021) Vol. 11
Open Access | Times Cited: 79
Structural basis of ABCF-mediated resistance to pleuromutilin, lincosamide, and streptogramin A antibiotics in Gram-positive pathogens
Caillan Crowe‐McAuliffe, Victoriia Murina, Kathryn Jane Turnbull, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 62
Structural basis for PoxtA-mediated resistance to phenicol and oxazolidinone antibiotics
Caillan Crowe‐McAuliffe, Victoriia Murina, Kathryn Jane Turnbull, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 43
How does RNA fold dynamically?
David Z. Bushhouse, Edric K. Choi, Laura Hertz, et al.
Journal of Molecular Biology (2022) Vol. 434, Iss. 18, pp. 167665-167665
Open Access | Times Cited: 42
Frozen in time: analyzing molecular dynamics with time-resolved cryo-EM
Sascha Josef Amann, Demian Keihsler, Tatyana Bodrug, et al.
Structure (2022) Vol. 31, Iss. 1, pp. 4-19
Open Access | Times Cited: 40
Glycosylated queuosines in tRNAs optimize translational rate and post-embryonic growth
Xuewei Zhao, Ding Ma, Kensuke Ishiguro, et al.
Cell (2023) Vol. 186, Iss. 25, pp. 5517-5535.e24
Open Access | Times Cited: 35
A viral ADP-ribosyltransferase attaches RNA chains to host proteins
Maik Wolfram-Schauerte, Nadiia Pozhydaieva, Julia Grawenhoff, et al.
Nature (2023) Vol. 620, Iss. 7976, pp. 1054-1062
Open Access | Times Cited: 29
Cryo-EM captures early ribosome assembly in action
Bo Qin, Simon Lauer, Annika Balke, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 28
Rock, scissors, paper: How RNA structure informs function
Sarah M. Assmann, Hong‐Li Chou, Philip C. Bevilacqua
The Plant Cell (2023) Vol. 35, Iss. 6, pp. 1671-1707
Open Access | Times Cited: 27
Mutation signature filtering enables high-fidelity RNA structure probing at all four nucleobases with DMS
David Mitchell, Jennifer A. Cotter, Irfana Saleem, et al.
Nucleic Acids Research (2023) Vol. 51, Iss. 16, pp. 8744-8757
Open Access | Times Cited: 24
Direct Nanopore Sequencing for the 17 RNA Modification Types in 36 Locations in the E. coli Ribosome Enables Monitoring of Stress-Dependent Changes
Aaron M. Fleming, Praneeth Bommisetti, Songjun Xiao, et al.
ACS Chemical Biology (2023) Vol. 18, Iss. 10, pp. 2211-2223
Open Access | Times Cited: 24
Atomistic simulations of the Escherichia coli ribosome provide selection criteria for translationally active substrates
Zoe L. Watson, Isaac J. Knudson, Fred R. Ward, et al.
Nature Chemistry (2023) Vol. 15, Iss. 7, pp. 913-921
Open Access | Times Cited: 23
The SecM arrest peptide traps a pre-peptide bond formation state of the ribosome
Felix Gersteuer, Martino Morici, Sara Gabrielli, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 15
Mitoribosome structure with cofactors and modifications reveals mechanism of ligand binding and interactions with L1 stalk
Vivek Singh, Yuzuru Itoh, Samuel Del’Olio, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 15
Scientific Rationale and Clinical Basis for Clindamycin Use in the Treatment of Dermatologic Disease
Maria K. Armillei, Ivan B. Lomakin, J.Q. Del Rosso, et al.
Antibiotics (2024) Vol. 13, Iss. 3, pp. 270-270
Open Access | Times Cited: 12
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