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:

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

Showing 1-25 of 181 citing articles:

The Unfolded Protein Response: Detecting and Responding to Fluctuations in the Protein-Folding Capacity of the Endoplasmic Reticulum
G Elif Karagöz, Diego Acosta‐Alvear, Peter Walter
Cold Spring Harbor Perspectives in Biology (2019) Vol. 11, Iss. 9, pp. a033886-a033886
Open Access | Times Cited: 266

Synonymous mutations in representative yeast genes are mostly strongly non-neutral
Xukang Shen, Siliang Song, Chuan Li, et al.
Nature (2022) Vol. 606, Iss. 7915, pp. 725-731
Open Access | Times Cited: 226

Reprogramming the genetic code
Daniel de la Torre, Jason W. Chin
Nature Reviews Genetics (2020) Vol. 22, Iss. 3, pp. 169-184
Closed Access | Times Cited: 221

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 but Not Silent: The Codon Usage Code for Gene Expression and Protein Folding
Yi Liu, Qian Yang, Fangzhou Zhao
Annual Review of Biochemistry (2021) Vol. 90, Iss. 1, pp. 375-401
Open Access | Times Cited: 134

Computational scoring and experimental evaluation of enzymes generated by neural networks
Sean R. Johnson, Xiaozhi Fu, Sandra Viknander, et al.
Nature Biotechnology (2024)
Open Access | Times Cited: 26

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

How synonymous mutations alter enzyme structure and function over long timescales
Yang Jiang, Syam Sundar Neti, Ian Sitarik, et al.
Nature Chemistry (2022) Vol. 15, Iss. 3, pp. 308-318
Open Access | Times Cited: 60

mRNA-Based Therapeutics in Cancer Treatment
Han Sun, Yu Zhang, Ge Wang, et al.
Pharmaceutics (2023) Vol. 15, Iss. 2, pp. 622-622
Open Access | Times Cited: 31

Computational Scoring and Experimental Evaluation of Enzymes Generated by Neural Networks
Sean R. Johnson, Xiaozhi Fu, Sandra Viknander, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 27

CodonTransformer: a multispecies codon optimizer using context-aware neural networks
Adibvafa Fallahpour, Vincent Gureghian, Guillaume J. Filion, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 1

Sequence analysis of SARS-CoV-2 genome reveals features important for vaccine design
Jacob Kames, David D. Holcomb, Ofer Kimchi, et al.
Scientific Reports (2020) Vol. 10, Iss. 1
Open Access | Times Cited: 66

How Does the Ribosome Fold the Proteome?
Anaïs M. E. Cassaignau, Lisa D. Cabrita, John Christodoulou
Annual Review of Biochemistry (2020) Vol. 89, Iss. 1, pp. 389-415
Open Access | Times Cited: 62

Mechanisms of Disulfide Bond Formation in Nascent Polypeptides Entering the Secretory Pathway
Philip J. Robinson, Neil J. Bulleid
Cells (2020) Vol. 9, Iss. 9, pp. 1994-1994
Open Access | Times Cited: 60

When and how do sex‐linked regions become sex chromosomes?
Deborah Charlesworth
Evolution (2021) Vol. 75, Iss. 3, pp. 569-581
Open Access | Times Cited: 47

Codon-specific Ramachandran plots show amino acid backbone conformation depends on identity of the translated codon
Aviv A. Rosenberg, Ailie Marx, Alex Bronstein
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 37

A switch from α‐helical to β‐strand conformation during co‐translational protein folding
Xabier Agirrezabala, Ekaterina Samatova, Meline Macher, et al.
The EMBO Journal (2022) Vol. 41, Iss. 4
Open Access | Times Cited: 32

The Effects of Codon Usage on Protein Structure and Folding
McKenze J. Moss, Laura M. Chamness, Patricia L. Clark
Annual Review of Biophysics (2023) Vol. 53, Iss. 1, pp. 87-108
Closed Access | Times Cited: 17

Synonymous codon substitutions modulate transcription and translation of a divergent upstream gene by modulating antisense RNA production
Anabel Rodríguez, Jacob D. Diehl, Gabriel Wright, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 36
Closed Access | Times Cited: 6

Folding of heterologous proteins in bacterial cell factories: Cellular mechanisms and engineering strategies
Yixin Rong, Sheila Ingemann Jensen, Kresten Lindorff‐Larsen, et al.
Biotechnology Advances (2022) Vol. 63, pp. 108079-108079
Closed Access | Times Cited: 23

Translation Rates and Protein Folding
Anton A. Komar, Ekaterina Samatova, Marina V. Rodnina
Journal of Molecular Biology (2023) Vol. 436, Iss. 14, pp. 168384-168384
Open Access | Times Cited: 16

Navigating the complexities of multi-domain protein folding
Nandakumar Rajasekaran, Christian Kaiser
Current Opinion in Structural Biology (2024) Vol. 86, pp. 102790-102790
Open Access | Times Cited: 5

Transcription, mRNA Export, and Immune Evasion Shape the Codon Usage of Viruses
Christine Mordstein, Laura Cano, Atahualpa Castillo-Morales, et al.
Genome Biology and Evolution (2021) Vol. 13, Iss. 9
Open Access | Times Cited: 32

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