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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:

Codon Usage Influences the Local Rate of Translation Elongation to Regulate Co-translational Protein Folding
Chien‐Hung Yu, Yunkun Dang, Zhipeng Zhou, et al.
Molecular Cell (2015) Vol. 59, Iss. 5, pp. 744-754
Open Access | Times Cited: 550

Showing 1-25 of 550 citing articles:

mRNA vaccines — a new era in vaccinology
Norbert Pardi, Michael J. Hogan, Frederick Porter, et al.
Nature Reviews Drug Discovery (2018) Vol. 17, Iss. 4, pp. 261-279
Open Access | Times Cited: 3551
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
Codon usage is an important determinant of gene expression levels largely through its effects on transcription
Zhipeng Zhou, Yunkun Dang, Mian Zhou, et al.
Proceedings of the National Academy of Sciences (2016) Vol. 113, Iss. 41
Open Access | Times Cited: 408
Synonymous Codons Direct Cotranslational Folding toward Different Protein Conformations
Florian Buhr, Sujata Jha, Michael Thommen, et al.
Molecular Cell (2016) Vol. 61, Iss. 3, pp. 341-351
Open Access | Times Cited: 352
Ribosomal frameshifting and transcriptional slippage: From genetic steganography and cryptography to adventitious use
John F. Atkins, Gary Loughran, Pramod R. Bhatt, et al.
Nucleic Acids Research (2016), pp. gkw530-gkw530
Open Access | Times Cited: 328
The DEAD-Box Protein Dhh1p Couples mRNA Decay and Translation by Monitoring Codon Optimality
Aditya Radhakrishnan, Ying-Hsin Chen, Sophie Martin, et al.
Cell (2016) Vol. 167, Iss. 1, pp. 122-132.e9
Open Access | Times Cited: 296
Codon identity regulates mRNA stability and translation efficiency during the maternal‐to‐zygotic transition
Ariel Bazzini, Florencia Del Viso, Miguel A. Moreno-Mateos, et al.
The EMBO Journal (2016) Vol. 35, Iss. 19, pp. 2087-2103
Open Access | Times Cited: 289
Codon Usage and 3′ UTR Length Determine Maternal mRNA Stability in Zebrafish
Yuichiro Mishima, Yukihide Tomari
Molecular Cell (2016) Vol. 61, Iss. 6, pp. 874-885
Open Access | Times Cited: 278
Translation affects mRNA stability in a codon-dependent manner in human cells
Qiushuang Wu, Santiago Gerardo Medina, Gopal Kushawah, et al.
eLife (2019) Vol. 8
Open Access | Times Cited: 242
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
The dark matter of the cancer genome: aberrations in regulatory elements, untranslated regions, splice sites, non‐coding RNA and synonymous mutations
Sven Diederichs, Lorenz Bartsch, Julia C. Berkmann, et al.
EMBO Molecular Medicine (2016) Vol. 8, Iss. 5, pp. 442-457
Open Access | Times Cited: 234
Techniques for the analysis of protein-protein interactions in vivo
Shuping Xing, Niklas Wallmeroth, Kenneth Wayne Berendzen, et al.
PLANT PHYSIOLOGY (2016), pp. pp.00470.2016-pp.00470.2016
Open Access | Times Cited: 224
Roadblocks and resolutions in eukaryotic translation
Anthony P. Schuller, Rachel Green
Nature Reviews Molecular Cell Biology (2018) Vol. 19, Iss. 8, pp. 526-541
Open Access | Times Cited: 217
A User’s Guide to Cell-Free Protein Synthesis
Nicole E. Gregorio, Max Z. Levine, Javin P. Oza
Methods and Protocols (2019) Vol. 2, Iss. 1, pp. 24-24
Open Access | Times Cited: 215
N1-methyl-pseudouridine in mRNA enhances translation through eIF2α-dependent and independent mechanisms by increasing ribosome density
Yuri V. Svitkin, Yi Cheng, Tirtha Chakraborty, et al.
Nucleic Acids Research (2017) Vol. 45, Iss. 10, pp. 6023-6036
Open Access | Times Cited: 211
A Review of Resistance Mechanisms of Synthetic Insecticides and Botanicals, Phytochemicals, and Essential Oils as Alternative Larvicidal Agents Against Mosquitoes
Sengottayan Senthil‐Nathan
Frontiers in Physiology (2020) Vol. 10
Open Access | Times Cited: 194
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
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
The roles of RNA processing in translating genotype to phenotype
Kassie S. Manning, Thomas A. Cooper
Nature Reviews Molecular Cell Biology (2016) Vol. 18, Iss. 2, pp. 102-114
Open Access | Times Cited: 186
A pan-cancer analysis of synonymous mutations
Yogita Sharma, Milad Miladi, Sandeep Dukare, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 184
A code within the genetic code: codon usage regulates co-translational protein folding
Yi Liu
Cell Communication and Signaling (2020) Vol. 18, Iss. 1
Open Access | Times Cited: 182
Synonymous codon substitutions perturb cotranslational protein folding in vivo and impair cell fitness
Ian M. Walsh, Micayla A. Bowman, Iker F. Soto Santarriaga, et al.
Proceedings of the National Academy of Sciences (2020) Vol. 117, Iss. 7, pp. 3528-3534
Open Access | Times Cited: 181
Circadian Oscillators: Around the Transcription–Translation Feedback Loop and on to Output
Jennifer Hurley, Jennifer Loros, Jay Dunlap
Trends in Biochemical Sciences (2016) Vol. 41, Iss. 10, pp. 834-846
Open Access | Times Cited: 179
Queuosine‐modified tRNAs confer nutritional control of protein translation
Francesca Tuorto, Carine Legrand, Cansu Cirzi, et al.
The EMBO Journal (2018) Vol. 37, Iss. 18
Open Access | Times Cited: 172
Ageing exacerbates ribosome pausing to disrupt cotranslational proteostasis
Kevin C. Stein, Fabián Morales-Polanco, Joris CJ van der Lienden, et al.
Nature (2022) Vol. 601, Iss. 7894, pp. 637-642
Open Access | Times Cited: 150
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