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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:

The ribosome in action: Tuning of translational efficiency and protein folding
Marina V. Rodnina
Protein Science (2016) Vol. 25, Iss. 8, pp. 1390-1406
Open Access | Times Cited: 189

Showing 1-25 of 189 citing articles:

Codon optimality, bias and usage in translation and mRNA decay
Gavin Hanson, Jeff Coller
Nature Reviews Molecular Cell Biology (2017) Vol. 19, Iss. 1, pp. 20-30
Open Access | Times Cited: 695
Translation in Prokaryotes
Marina V. Rodnina
Cold Spring Harbor Perspectives in Biology (2018) Vol. 10, Iss. 9, pp. a032664-a032664
Open Access | Times Cited: 241
Mitochondrial Protein Synthesis Adapts to Influx of Nuclear-Encoded Protein
Ricarda Richter‐Dennerlein, Silke Oeljeklaus, Isotta Lorenzi, et al.
Cell (2016) Vol. 167, Iss. 2, pp. 471-483.e10
Open Access | Times Cited: 199
Synonymous Codons: Choose Wisely for Expression
Christina E. Brule, Elizabeth J. Grayhack
Trends in Genetics (2017) Vol. 33, Iss. 4, pp. 283-297
Open Access | Times Cited: 192
A short translational ramp determines the efficiency of protein synthesis
Manasvi Verma, Junhong Choi, Kyle A. Cottrell, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 149
Ribosome collisions trigger cis-acting feedback inhibition of translation initiation
Szymon Juszkiewicz, Greg Slodkowicz, Zhewang Lin, et al.
eLife (2020) Vol. 9
Open Access | Times Cited: 145
Ribosome states signal RNA quality control
Karole N. D’Orazio, Rachel Green
Molecular Cell (2021) Vol. 81, Iss. 7, pp. 1372-1383
Open Access | Times Cited: 120
Causes, functions, and therapeutic possibilities of RNA secondary structure ensembles and alternative states
Ritwika Bose, Irfana Saleem, Anthony M. Mustoe
Cell chemical biology (2024) Vol. 31, Iss. 1, pp. 17-35
Open Access | Times Cited: 16
The stop-and-go traffic regulating protein biogenesis: How translation kinetics controls proteostasis
Kevin C. Stein, Judith Frydman
Journal of Biological Chemistry (2018) Vol. 294, Iss. 6, pp. 2076-2084
Open Access | Times Cited: 154
Ribosome pausing, a dangerous necessity for co-translational events
Martine A. Collart, Benjamin Weiss
Nucleic Acids Research (2019) Vol. 48, Iss. 3, pp. 1043-1055
Open Access | Times Cited: 132
Nature and Regulation of Protein Folding on the Ribosome
Christopher A. Waudby, Christopher M. Dobson, John Christodoulou
Trends in Biochemical Sciences (2019) Vol. 44, Iss. 11, pp. 914-926
Open Access | Times Cited: 126
Co-translational protein folding: progress and methods
Michael Thommen, Wolf Holtkamp, Marina V. Rodnina
Current Opinion in Structural Biology (2016) Vol. 42, pp. 83-89
Closed Access | Times Cited: 113
Autism-Misregulated eIF4G Microexons Control Synaptic Translation and Higher Order Cognitive Functions
Thomas Gonatopoulos-Pournatzis, Rieko Niibori, Eric W. Salter, et al.
Molecular Cell (2020) Vol. 77, Iss. 6, pp. 1176-1192.e16
Open Access | Times Cited: 94
Disome-seq reveals widespread ribosome collisions that promote cotranslational protein folding
Taolan Zhao, Yanming Chen, Yu Li, et al.
Genome biology (2021) Vol. 22, Iss. 1
Open Access | Times Cited: 88
Alzheimer’s disease beyond amyloid: Can the repetitive failures of amyloid-targeted therapeutics inform future approaches to dementia drug discovery?
Kevin Mullane, Michael Williams
Biochemical Pharmacology (2020) Vol. 177, pp. 113945-113945
Closed Access | Times Cited: 85
High-throughput method characterizes hundreds of previously unknown antibiotic resistance mutations
Matthew J. Jago, Jake K. Soley, Stepan Denisov, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 1
Quality over quantity: optimizing co-translational protein folding with non-‘optimal’ synonymous codons
Giselle N Jacobson, Patricia L. Clark
Current Opinion in Structural Biology (2016) Vol. 38, pp. 102-110
Open Access | Times Cited: 71
Targeting the Human 80S Ribosome in Cancer: From Structure to Function and Drug Design for Innovative Adjuvant Therapeutic Strategies
Arnaud Gilles, Léo Fréchin, Kundhavai Natchiar, et al.
Cells (2020) Vol. 9, Iss. 3, pp. 629-629
Open Access | Times Cited: 59
Direct measurements of mRNA translation kinetics in living cells
Mikhail Metelev, Erik Lundin, Ivan L. Volkov, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 29
Transcriptional and post-transcriptional controls for tuning gene expression in plants
Vivian Zhong, Bella N. Archibald, Jennifer A. N. Brophy
Current Opinion in Plant Biology (2022) Vol. 71, pp. 102315-102315
Open Access | Times Cited: 29
A small single-domain protein folds through the same pathway on and off the ribosome
Emily J. Guinn, Pengfei Tian, Mia Shin, et al.
Proceedings of the National Academy of Sciences (2018) Vol. 115, Iss. 48, pp. 12206-12211
Open Access | Times Cited: 56
Toward a Kinetic Understanding of Eukaryotic Translation
Masaaki Sokabe, Christopher S. Fraser
Cold Spring Harbor Perspectives in Biology (2018) Vol. 11, Iss. 2, pp. a032706-a032706
Open Access | Times Cited: 52
tRNA tracking for direct measurements of protein synthesis kinetics in live cells
Ivan L. Volkov, Martin Lindén, Javier Aguirre Rivera, et al.
Nature Chemical Biology (2018) Vol. 14, Iss. 6, pp. 618-626
Open Access | Times Cited: 49
Functionality of membrane proteins overexpressed and purified from E. coli is highly dependent upon the strain
Khadija Mathieu, Waqas Javed, Sylvain D. Vallet, et al.
Scientific Reports (2019) Vol. 9, Iss. 1
Open Access | Times Cited: 43
Gradual compaction of the nascent peptide during cotranslational folding on the ribosome
Marija Liutkute, Manisankar Maiti, Ekaterina Samatova, et al.
eLife (2020) Vol. 9
Open Access | Times Cited: 43
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