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:

A CHO stable pool production platform for rapid clinical development of trimeric SARS‐CoV‐2 spike subunit vaccine antigens
Simon Joubert, Matthew Stuible, Simon Lord‐Dufour, et al.
Biotechnology and Bioengineering (2023) Vol. 120, Iss. 7, pp. 1746-1761
Open Access | Times Cited: 23

Showing 23 citing articles:

Scalable bioprocess for high-yield production of SARS-CoV-2 trimeric spike protein-based immunogen (IMT-CVAX) using suspension CHO cells
Sneha Singh, B. Vikram Kumar, Jitender, et al.
Process Biochemistry (2024) Vol. 147, pp. 332-346
Closed Access | Times Cited: 2

An unconventional strategy for purifying recombinant SARS-CoV-2 spike protein
Mrunal Ingawale, Mohammad Riaz, Yves Durocher, et al.
Journal of Chromatography B (2024) Vol. 1247, pp. 124328-124328
Open Access | Times Cited: 2

Preclinical evaluation of manufacturable SARS-CoV-2 spike virus-like particles produced in Chinese Hamster Ovary cells
Sergio P. Alpuche-Lazcano, Matthew Stuible, Bassel Akache, et al.
Communications Medicine (2023) Vol. 3, Iss. 1
Open Access | Times Cited: 6

Production, purification and immunogenicity of Gag virus-like particles carrying SARS-CoV-2 components
Anahita Bakhshizadeh Gashti, Gerard Agbayani, Sabahudin Hrapovic, et al.
Vaccine (2023) Vol. 42, Iss. 1, pp. 40-52
Open Access | Times Cited: 5

Rapid and Scalable Production of Functional SARS-CoV-2 Virus-like Particles (VLPs) by a Stable HEK293 Cell Pool
Sitthiphol Puarattana-aroonkorn, Kannan Tharakaraman, Disapan Suriyawipada, et al.
Vaccines (2024) Vol. 12, Iss. 6, pp. 561-561
Open Access | Times Cited: 1

Characterization of biotinylated human ACE2 and SARS-CoV-2 Omicron BA.4/5 spike protein reference materials
Bradley B. Stocks, Marie-Pier Thibeault, Denis L’Abbé, et al.
Analytical and Bioanalytical Chemistry (2024) Vol. 416, Iss. 22, pp. 4861-4872
Open Access | Times Cited: 1

SiMPl‐GS: Advancing Cell Line Development via Synthetic Selection Marker for Next‐Generation Biopharmaceutical Production
Chansik Yoon, Eun‐ji Lee, Dong‐Il Kim, et al.
Advanced Science (2024) Vol. 11, Iss. 38
Open Access | Times Cited: 1

CHO stable pool fed‐batch process development of SARSCoV‐2 spike protein production: Impact of aeration conditions and feeding strategies
Sebastian‐Juan Reyes, Phuong Lan Pham, Yves Durocher, et al.
Biotechnology Progress (2024)
Open Access | Times Cited: 1

Repressing expression of difficult‐to‐express recombinant proteins during the selection process increases productivity of CHO stable pools
Jean‐Sébastien Maltais, Simon Lord‐Dufour, Audrey Morasse, et al.
Biotechnology and Bioengineering (2023) Vol. 120, Iss. 10, pp. 2840-2852
Open Access | Times Cited: 4

Development of a novel tyrosine-based selection system for generation of recombinant Chinese hamster ovary cells
Jun Cheng, Yanmin Zhang, Yuan Tian, et al.
Journal of Bioscience and Bioengineering (2024) Vol. 137, Iss. 3, pp. 221-229
Closed Access

Fast and robust recombinant protein production utilizing episomal stable pools in WAVE bioreactors
Melanie Dannemeyer, Anna Berling, Sara Kanje, et al.
Protein Expression and Purification (2024) Vol. 221, pp. 106505-106505
Open Access

Recombinant Protein Production from Stable CHO Cell Pools
Laurence Delafosse, Simon Lord‐Dufour, Alex Pelletier, et al.
Methods in molecular biology (2024), pp. 99-121
Closed Access

Synthetic G-quadruplex components for predictable, precise two-level control of mammalian recombinant protein expression
Melinda Pohle, Edward Curry, Suzanne J. Gibson, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Closed Access

SARS-CoV-2 spike-based virus-like particles incorporate influenza H1/N1 antigens and induce dual immunity in mice
Zalma V. Sanchez-Martinez, Sergio P. Alpuche-Lazcano, Matthew Stuible, et al.
Vaccine (2024) Vol. 42, Iss. 26, pp. 126463-126463
Open Access

Discovery of broad-spectrum high-affinity peptide ligands of spike protein for the vaccine purification of SARS-CoV-2 and Omicron variants
Jing Ma, Yongdong Huang, Guodong Jia, et al.
International Journal of Biological Macromolecules (2024) Vol. 283, pp. 137059-137059
Closed Access

An alternating flow-direction method for increasing productivity in the purification of large biotherapeutic modalities using size exclusion chromatography
Mrunal Ingawale, Taylan Dalkan, Yves Durocher, et al.
Journal of Chromatography A (2024) Vol. 1740, pp. 465592-465592
Open Access

Simplifying glycan monitoring of complex antigens such as the SARS-CoV-2 spike to accelerate vaccine development
Janelle Sauvageau, Izel Koyuturk, Frank St. Michael, et al.
Communications Chemistry (2023) Vol. 6, Iss. 1
Open Access | Times Cited: 1

Influence of variant-specific mutations, temperature and pH on conformations of a large set of SARS-CoV-2 spike trimer vaccine antigen candidates
Matthew Stuible, Joseph D. Schrag, Joey Sheff, et al.
Scientific Reports (2023) Vol. 13, Iss. 1
Open Access | Times Cited: 1

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