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:

Characterizing and Minimizing Aggregation and Particle Formation of Three Recombinant Fusion-Protein Bulk Antigens for Use in a Candidate Trivalent Rotavirus Vaccine
Sanjeev Agarwal, Neha Sahni, John M. Hickey, et al.
Journal of Pharmaceutical Sciences (2019) Vol. 109, Iss. 1, pp. 394-406
Open Access | Times Cited: 15

Showing 15 citing articles:

Immunoinformatics-guided approach for designing a pan-proteome multi-epitope subunit vaccine against African swine fever virus
Alea Maurice Simbulan, Edward C. Banico, Ella Mae Joy S. Sira, et al.
Scientific Reports (2024) Vol. 14, Iss. 1
Open Access | Times Cited: 15

Thermostability of tetanus toxoid vaccine encapsulated in metal-organic frameworks
Rohan Murty, Krista S. Walton, Mark R. Prausnitz
Drug Delivery and Translational Research (2025)
Open Access

Effect of Aluminum Adjuvant and Preservatives on Structural Integrity and Physicochemical Stability Profiles of Three Recombinant Subunit Rotavirus Vaccine Antigens
Sanjeev Agarwal, John M. Hickey, David McAdams, et al.
Journal of Pharmaceutical Sciences (2019) Vol. 109, Iss. 1, pp. 476-487
Open Access | Times Cited: 34

Formulation and preclinical studies with a trivalent rotavirus P2-VP8 subunit vaccine
Kyle Lakatos, David McAdams, Jessica A. White, et al.
Human Vaccines & Immunotherapeutics (2020) Vol. 16, Iss. 8, pp. 1957-1968
Open Access | Times Cited: 29

Concordance of in vitro and in vivo measures of non-replicating rotavirus vaccine potency
David McAdams, Marcus Estrada, David A. Holland, et al.
Vaccine (2022) Vol. 40, Iss. 34, pp. 5069-5078
Open Access | Times Cited: 14

Recombinant Subunit Rotavirus Trivalent Vaccine Candidate: Physicochemical Comparisons and Stability Evaluations of Three Protein Antigens
Sanjeev Agarwal, John M. Hickey, Neha Sahni, et al.
Journal of Pharmaceutical Sciences (2019) Vol. 109, Iss. 1, pp. 380-393
Open Access | Times Cited: 18

Rapid Developability Assessments to Formulate Recombinant Protein Antigens as Stable, Low-Cost, Multi-Dose Vaccine Candidates: Case-Study With Non-Replicating Rotavirus (NRRV) Vaccine Antigens
Nishant Sawant, Kawaljit Kaur, David A. Holland, et al.
Journal of Pharmaceutical Sciences (2020) Vol. 110, Iss. 3, pp. 1042-1053
Open Access | Times Cited: 17

The immune-evasive proline-283 substitution in influenza nucleoprotein increases aggregation propensity without altering the native structure
Jimin Yoon, Yu Meng Zhang, Cheenou Her, et al.
Science Advances (2024) Vol. 10, Iss. 16
Open Access | Times Cited: 1

Mechanism of Thimerosal-Induced Structural Destabilization of a Recombinant Rotavirus P[4] Protein Antigen Formulated as a Multi-Dose Vaccine
Kawaljit Kaur, Jian Xiong, Nishant Sawant, et al.
Journal of Pharmaceutical Sciences (2020) Vol. 110, Iss. 3, pp. 1054-1066
Open Access | Times Cited: 10

Crystallization of a nonreplicating rotavirus vaccine candidate
Moo Sun Hong, Kawaljit Kaur, Nishant Sawant, et al.
Biotechnology and Bioengineering (2021) Vol. 118, Iss. 4, pp. 1750-1756
Open Access | Times Cited: 4

Prediction of frozen virus stability based on degradation mechanisms, real-time data and modeling
Ying Homan, Daniel I. S. Rosenbloom, Sally C. Y. Wong, et al.
Bioanalysis (2022) Vol. 14, Iss. 17, pp. 1177-1190
Closed Access | Times Cited: 3

The CombE-IDMS Assay as an Alternate Potency Method for Adjuvanted Quadrivalent Influenza Vaccines
Jiang Qian, Matthew P. Donohue, Thomas R. Bowen, et al.
Analytical Chemistry (2023) Vol. 95, Iss. 34, pp. 12842-12850
Closed Access | Times Cited: 1

The Immune-Evasive Proline 283 Substitution in Influenza Nucleoprotein Increases Aggregation Propensity Without Altering the Native Structure
Jimin Yoon, Yu Meng Zhang, Cheenou Her, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 1

Inside and outside of virus-like particles HBc and HBc/4M2e: A comprehensive study of the structure
Egorov Vv, А. В. Швецов, Evgeny Pichkur, et al.
Biophysical Chemistry (2022) Vol. 293, pp. 106943-106943
Open Access | Times Cited: 2

Formulation design considerations and good practice for live attenuated vaccine development
Lee Smith, Paul S. Nelson
Elsevier eBooks (2021), pp. 27-78
Closed Access

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