Open Access Helper

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:

Structures of synthetic nanobody–SARS-CoV-2 receptor-binding domain complexes reveal distinct sites of interaction
Javeed Ahmad, Jiansheng Jiang, Lisa F. Boyd, et al.
Journal of Biological Chemistry (2021) Vol. 297, Iss. 4, pp. 101202-101202
Open Access | Times Cited: 36

Showing 26-50 of 36 citing articles:

Structure-Guided Development of Bivalent Aptamers Blocking SARS-CoV-2 Infection
Md Shafiqur Rahman, Min Jung Han, Sang Won Kim, et al.
Molecules (2023) Vol. 28, Iss. 12, pp. 4645-4645
Open Access | Times Cited: 5
In Silico Optimization of SARS-CoV-2 Spike Specific Nanobodies
Xiaohong Zhu, Ke An, Junfang Yan, et al.
Frontiers in Bioscience-Landmark (2023) Vol. 28, Iss. 4
Open Access | Times Cited: 4
Broad Epitope Coverage of Therapeutic Multi-Antibody Combinations Targeting SARS-CoV-2 Boosts In Vivo Protection and Neutralization Potency to Corner an Immune-Evading Virus
Ilse Roodink, Maartje van Erp, Andra Li, et al.
Biomedicines (2024) Vol. 12, Iss. 3, pp. 642-642
Open Access | Times Cited: 1
Facilitating and restraining virus infection using cell-attachable soluble viral receptors
Heng Zhang, Zhengli Wang, Huong T. T. Nguyen, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 45
Open Access | Times Cited: 1
Cryo-EM technique and its application: Structure of steroid hormone receptors
Raj Kumar
Vitamins and hormones (2023), pp. 385-397
Closed Access | Times Cited: 2
SARS-CoV-2 antibodies recognize 23 distinct epitopic sites on the receptor binding domain
Jiansheng Jiang, Christopher T. Boughter, Javeed Ahmad, et al.
Research Square (Research Square) (2023)
Open Access | Times Cited: 2
Design and Immunogenicity of SARS-CoV-2 DNA Vaccine Encoding RBD-PVXCP Fusion Protein
Dmitri Dormeshkin, Mikalai Katsin, Maria Stegantseva, et al.
Vaccines (2023) Vol. 11, Iss. 6, pp. 1014-1014
Open Access | Times Cited: 2
Determining the International Spread of B.1.1.523 SARS-CoV-2 Lineage with a Set of Mutations Highly Associated with Reduced Immune Neutralization
Lukas Žemaitis, Gediminas Alzbutas, Dovydas Gečys, et al.
Microorganisms (2022) Vol. 10, Iss. 7, pp. 1356-1356
Open Access | Times Cited: 3
Binding of synthetic nanobodies to the SARS-CoV-2 receptor-binding domain: the importance of salt bridges
Hujun Shen, Hengxiu Yang
Physical Chemistry Chemical Physics (2023) Vol. 25, Iss. 35, pp. 24129-24142
Closed Access | Times Cited: 1
Hetero-bivalent Nanobodies Provide Broad-spectrum Protection against SARS-CoV-2 Variants of Concern including Omicron
Huan Ma, Xinghai Zhang, Peiyi Zheng, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 1
An alpaca-derived nanobody recognizes a unique conserved epitope and retains potent activity against the SARS-CoV-2 omicron variant
Naphak Modhiran, Simon Lauer, Alberto A. Amarilla, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access
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