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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.

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Showing 23 citing articles:

Advances in SARS-CoV-2 receptor-binding domain-based COVID-19 vaccines
Xiao‐Qing Guan, Yang Yang, Lanying Du
Expert Review of Vaccines (2023) Vol. 22, Iss. 1, pp. 422-439
Open Access | Times Cited: 16
A Live-Cell Imaging-Based Fluorescent SARS-CoV-2 Neutralization Assay by Antibody-Mediated Blockage of Receptor Binding Domain-ACE2 Interaction
Jorge L. Arias-Arias, Laura Monturiol‐Gross, Eugenia Corrales‐Aguilar
BioTech (2025) Vol. 14, Iss. 1, pp. 10-10
Open Access
SARS‐CoV‐2 spike trimer vaccine expressed in Nicotiana benthamiana adjuvanted with Alum elicits protective immune responses in mice
Shi‐Jian Song, Heeyeon Kim, Eun Young Jang, et al.
Plant Biotechnology Journal (2022) Vol. 20, Iss. 12, pp. 2298-2312
Open Access | Times Cited: 14
Biophysical studies of amorphous protein aggregation and in vivo immunogenicity
Yutaka Kuroda
Biophysical Reviews (2022) Vol. 14, Iss. 6, pp. 1495-1501
Open Access | Times Cited: 12
Stable production of recombinant SARS-CoV-2 receptor-binding domain in mammalian cells with co-expression of a fluorescent reporter and its validation as antigenic target for COVID-19 serology testing
Jorge L. Arias-Arias, Silvia Molina‐Castro, Laura Monturiol‐Gross, et al.
Biotechnology Reports (2022) Vol. 37, pp. e00780-e00780
Open Access | Times Cited: 9
Protein Expression Platforms and the Challenges of Viral Antigen Production
Jamie Sookhoo, Zachary Schiffman, Aruna Ambagala, et al.
Vaccines (2024) Vol. 12, Iss. 12, pp. 1344-1344
Open Access | Times Cited: 1
Utilization of Receptor-Binding Domain of SARS-CoV-2 Spike Protein Expressed in Escherichia coli for the Development of Neutralizing Antibody Assay
Termsak Tantiwiwat, Apisitt Thaiprayoon, Ake-kavitch Siriatcharanon, et al.
Molecular Biotechnology (2022)
Open Access | Times Cited: 8
Recombinant expression of SARS-CoV-2 receptor binding domain (RBD) in Escherichia coli and its immunogenicity in mice.
Zahra Rahbar, Shahram Nazarian, Ruhollah Dorostkar, et al.
DOAJ (DOAJ: Directory of Open Access Journals) (2022) Vol. 25, Iss. 9, pp. 1110-1116
Closed Access | Times Cited: 8
Production and Purification of LTB-RBD: A Potential Antigen for Mucosal Vaccine Development against SARS-CoV-2
Karla Ivón Solís-Andrade, Omar González‐Ortega, Dania O. Govea‐Alonso, et al.
Vaccines (2022) Vol. 10, Iss. 10, pp. 1759-1759
Open Access | Times Cited: 8
Unglycosylated Soluble SARS-CoV-2 Receptor Binding Domain (RBD) Produced in E. coli Combined with the Army Liposomal Formulation Containing QS21 (ALFQ) Elicits Neutralizing Antibodies against Mismatched Variants
Arasu Balasubramaniyam, Emma Ryan, Dallas R. Brown, et al.
Vaccines (2022) Vol. 11, Iss. 1, pp. 42-42
Open Access | Times Cited: 8
<i>E. coli</i> production of a multi-disulfide bonded SARS-CoV-2 Omicron BA.5 RBD exhibiting native-like biochemical and biophysical properties
Rawiwan Wongnak, Subbaian Brindha, Takahiro Yoshizue, et al.
Biophysics and Physicobiology (2023) Vol. 20, Iss. 4, pp. n/a-n/a
Open Access | Times Cited: 4
An Escherichia coli Expressed Multi-Disulfide Bonded SARS-CoV-2 RBD Shows Native-like Biophysical Properties and Elicits Neutralizing Antisera in a Mouse Model
Subbaian Brindha, Takahiro Yoshizue, Rawiwan Wongnak, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 24, pp. 15744-15744
Open Access | Times Cited: 6
Antisera Produced Using an E. coli-Expressed SARS-CoV-2 RBD and Complemented with a Minimal Dose of Mammalian-Cell-Expressed S1 Subunit of the Spike Protein Exhibits Improved Neutralization
Takahiro Yoshizue, Subbaian Brindha, Rawiwan Wongnak, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 13, pp. 10583-10583
Open Access | Times Cited: 3
The Immunogenicity of DENV1–4 ED3s Strongly Differ despite Their Almost Identical Three-Dimensional Structures and High Sequence Similarities
Md. Din Islam, Tahmina Sharmin, Imrul Hasan Tipo, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 3, pp. 2393-2393
Open Access | Times Cited: 2
Oral administration of a recombinant modified RBD antigen of SARS-CoV-2 as a possible immunostimulant for the care of COVID-19
Norma A. Valdez‐Cruz, Diego Rosiles-Becerril, Constanza Estefanía Martínez-Olivares, et al.
Microbial Cell Factories (2024) Vol. 23, Iss. 1
Open Access
Amyloidogenesis of SARS-CoV-2 Delta Plus and Omicron Variants Receptor-Binding Domain (RBD): Impact of SUMO Fusion Tag
Sadegh Zargan, Hasan Jalili, Bahareh Dabirmanesh, et al.
Research Square (Research Square) (2024)
Open Access
Aspergillus oryzae as a host for SARS-CoV-2 RBD and NTD expression
Elif Karaman, Serdar Uysal
Biotech Studies (2024) Vol. 33, Iss. 2, pp. 9-20
Closed Access
Diverse Approaches to Express Recombinant Spike Protein: A Comprehensive Review
Jk Nithya Shree, T Premika, S Sharlin, et al.
Protein Expression and Purification (2024) Vol. 223, pp. 106556-106556
Closed Access
Amyloidogenesis of SARS-CoV-2 delta plus and omicron variants receptor-binding domain (RBD): impact of SUMO fusion tag
Sadegh Zargan, Hasan Jalili, Bahareh Dabirmanesh, et al.
Biotechnology Letters (2024) Vol. 46, Iss. 6, pp. 1037-1048
Open Access
Co-translational formation of disulfides guides folding of the SARS-CoV-2 receptor binding domain
Amir Bitran, Kibum Park, Eugene Serebryany, et al.
Biophysical Journal (2023) Vol. 122, Iss. 16, pp. 3238-3253
Open Access | Times Cited: 1
Produksi Antibodi Poliklonal Menggunakan Protein Rekombinan RBD-spike Untuk Deteksi SARS-CoV-2
Iryani Endah Febrianti, Yayuk Fatmawati, Intan Ria Neliana, et al.
AL-Kauniyah Jurnal Biologi (2023) Vol. 16, Iss. 2, pp. 336-346
Open Access
The biophysical nature and not only the size of protein aggregates determines the strength of the immune response against dengue ED3
Md Golam Kibria, Yukari Shiwaku, Subbaian Brindha, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access
Cotranslational formation of disulfides guides folding of the SARS COV-2 receptor binding domain
Amir Bitran, Kibum Park, Eugene Serebryany, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access
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