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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:

Non-equilibrium coupling of protein structure and function to translation–elongation kinetics
Ajeet K. Sharma, Edward P. O’Brien
Current Opinion in Structural Biology (2018) Vol. 49, pp. 94-103
Open Access | Times Cited: 60

Showing 1-25 of 60 citing articles:

Mechanisms of Cotranslational Maturation of Newly Synthesized Proteins
Günter Krämer, Ayala Shiber, Bernd Bukau
Annual Review of Biochemistry (2018) Vol. 88, Iss. 1, pp. 337-364
Open Access | Times Cited: 175
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
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
Chloroplast translational regulation uncovers nonessential photosynthesis genes as key players in plant cold acclimation
Yang Gao, Wolfram Thiele, Omar Saleh, et al.
The Plant Cell (2022) Vol. 34, Iss. 5, pp. 2056-2079
Open Access | Times Cited: 44
Successes and challenges in simulating the folding of large proteins
Anne Gershenson, Shachi Gosavi, Pietro Faccioli, et al.
Journal of Biological Chemistry (2019) Vol. 295, Iss. 1, pp. 15-33
Open Access | Times Cited: 70
A chemical kinetic basis for measuring translation initiation and elongation rates from ribosome profiling data
Ajeet K. Sharma, Pietro Sormanni, Nabeel Ahmed, et al.
PLoS Computational Biology (2019) Vol. 15, Iss. 5, pp. e1007070-e1007070
Open Access | Times Cited: 68
Universal protein misfolding intermediates can bypass the proteostasis network and remain soluble and less functional
Daniel A. Nissley, Yang Jiang, Fabio Trovato, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 37
Is Protein Folding a Thermodynamically Unfavorable, Active, Energy-Dependent Process?
Irina Sorokina, Arcady Mushegian, Eugene V. Koonin
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 1, pp. 521-521
Open Access | Times Cited: 36
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: 57
A ribosome-associated chaperone enables substrate triage in a cotranslational protein targeting complex
Hao-Hsuan Hsieh, Jae Ho Lee, Sowmya Chandrasekar, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 48
Effect of mRNA/tRNA mutations on translation speed: Implications for human diseases
Marcos Davyt, Nikhil Bharti, Zoya Ignatova
Journal of Biological Chemistry (2023) Vol. 299, Iss. 9, pp. 105089-105089
Open Access | Times Cited: 15
Energetic dependencies dictate folding mechanism in a complex protein
Kaixian Liu, Xiuqi Chen, Christian Kaiser
Proceedings of the National Academy of Sciences (2019) Vol. 116, Iss. 51, pp. 25641-25648
Open Access | Times Cited: 41
Negative reciprocity, not ordered assembly, underlies the interaction of Sox2 and Oct4 on DNA
John Biddle, Maximilian Nguyen, Jeremy Gunawardena
eLife (2019) Vol. 8
Open Access | Times Cited: 35
A Code Within a Code: How Codons Fine-Tune Protein Folding in the Cell
Anton A. Komar
Biochemistry (Moscow) (2021) Vol. 86, Iss. 8, pp. 976-991
Open Access | Times Cited: 21
The Molecular Biodiversity of Protein Targeting and Protein Transport Related to the Endoplasmic Reticulum
Andrea Tirincsi, Mark Sicking, Drazena Hadzibeganovic, et al.
International Journal of Molecular Sciences (2021) Vol. 23, Iss. 1, pp. 143-143
Open Access | Times Cited: 20
Experimental demonstration and pan-structurome prediction of climate-associated riboSNitches in Arabidopsis
Ángel Ferrero‐Serrano, Megan M. Sylvia, Peter C. Forstmeier, et al.
Genome biology (2022) Vol. 23, Iss. 1
Open Access | Times Cited: 14
How soluble misfolded proteins bypass chaperones at the molecular level
Ritaban Halder, Daniel A. Nissley, Ian Sitarik, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 7
Identifying A- and P-site locations on ribosome-protected mRNA fragments using Integer Programming
Nabeel Ahmed, Pietro Sormanni, Prajwal Ciryam, et al.
Scientific Reports (2019) Vol. 9, Iss. 1
Open Access | Times Cited: 22
Aminoglycoside drugs induce efficient read-through ofCDKL5nonsense mutations, slightly restoring its kinase activity
Maria Fazzari, Angelisa Frasca, Francesco Bifari, et al.
RNA Biology (2019) Vol. 16, Iss. 10, pp. 1414-1423
Open Access | Times Cited: 20
Effect of Protein Structure on Evolution of Cotranslational Folding
Victor Y. Zhao, William M. Jacobs, Eugene I. Shakhnovich
Biophysical Journal (2020) Vol. 119, Iss. 6, pp. 1123-1134
Open Access | Times Cited: 20
Validation of DBFOLD: An efficient algorithm for computing folding pathways of complex proteins
Amir Bitran, William M. Jacobs, Eugene I. Shakhnovich
PLoS Computational Biology (2020) Vol. 16, Iss. 11, pp. e1008323-e1008323
Open Access | Times Cited: 17
Pairs of amino acids at the P- and A-sites of the ribosome predictably and causally modulate translation-elongation rates
Nabeel Ahmed, Ulrike Friedrich, Pietro Sormanni, et al.
Journal of Molecular Biology (2020) Vol. 432, Iss. 24, pp. 166696-166696
Open Access | Times Cited: 12
Quantitative Modeling of Protein Synthesis Using Ribosome Profiling Data
Vandana Yadav, Inayat Ullah Irshad, Hemant Kumar, et al.
Frontiers in Molecular Biosciences (2021) Vol. 8
Open Access | Times Cited: 11
Programmed Trade-offs in Protein Folding Networks
Sebastian Pechmann
Structure (2020) Vol. 28, Iss. 12, pp. 1361-1375.e4
Open Access | Times Cited: 11
tRNA modifications tune decoding of codon pairs to prevent cellular quality control responses
Jie Wu, Cristián Eggers, Olga Sin, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
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