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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:

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: 35

Showing 1-25 of 35 citing articles:

NanoNet: Rapid and accurate end-to-end nanobody modeling by deep learning
Tomer Cohen, Matan Halfon, Dina Schneidman‐Duhovny
Frontiers in Immunology (2022) Vol. 13
Open Access | Times Cited: 66
Cryo-EM structure determination of small proteins by nanobody-binding scaffolds (Legobodies)
Xudong Wu, Tom A. Rapoport
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 41
Open Access | Times Cited: 75
A structural view of the SARS-CoV-2 virus and its assembly
Nathan J. Hardenbrook, Peijun Zhang
Current Opinion in Virology (2021) Vol. 52, pp. 123-134
Open Access | Times Cited: 65
NeutrobodyPlex—monitoring SARS‐CoV‐2 neutralizing immune responses using nanobodies
Teresa R. Wagner, E. Ostertag, Philipp D. Kaiser, et al.
EMBO Reports (2021) Vol. 22, Iss. 5
Open Access | Times Cited: 58
Research Progress and Applications of Multivalent, Multispecific and Modified Nanobodies for Disease Treatment
Jiewen Wang, Guangbo Kang, Haibin Yuan, et al.
Frontiers in Immunology (2022) Vol. 12
Open Access | Times Cited: 55
Biparatopic sybodies neutralize SARS‐CoV‐2 variants of concern and mitigate drug resistance
Justin D. Walter, Melanie Scherer, Cedric A. J. Hutter, et al.
EMBO Reports (2022) Vol. 23, Iss. 4
Open Access | Times Cited: 39
Shark nanobodies with potent SARS-CoV-2 neutralizing activity and broad sarbecovirus reactivity
Wei‐Hung Chen, Agnes Hajduczki, Elizabeth J. Martinez, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 25
Passive Immunotherapy Against SARS-CoV-2: From Plasma-Based Therapy to Single Potent Antibodies in the Race to Stay Ahead of the Variants
William R. Strohl, Zhiqiang Ku, Zhiqiang An, et al.
BioDrugs (2022) Vol. 36, Iss. 3, pp. 231-323
Open Access | Times Cited: 32
Structure and Mutations of SARS-CoV-2 Spike Protein: A Focused Overview
Rukmankesh Mehra, Kasper P. Kepp
ACS Infectious Diseases (2021) Vol. 8, Iss. 1, pp. 29-58
Open Access | Times Cited: 39
Outlook of therapeutic and diagnostic competency of nanobodies against SARS-CoV-2: A systematic review
Hamid Aria, Fatemeh Mahmoodi, Hooria Seyedhosseini Ghaheh, et al.
Analytical Biochemistry (2022) Vol. 640, pp. 114546-114546
Open Access | Times Cited: 25
Hetero-bivalent nanobodies provide broad-spectrum protection against SARS-CoV-2 variants of concern including Omicron
Huan Ma, Xinghai Zhang, Peiyi Zheng, et al.
Cell Research (2022) Vol. 32, Iss. 9, pp. 831-842
Open Access | Times Cited: 24
A universal reagent for detection of emerging diseases using bioengineered multifunctional yeast nanofragments
Junrong Li, Christopher B. Howard, Shuvashis Dey, et al.
Nature Nanotechnology (2023) Vol. 18, Iss. 10, pp. 1222-1229
Open Access | Times Cited: 13
Nanobodies to multiple spike variants and inhalation of nanobody-containing aerosols neutralize SARS-CoV-2 in cell culture and hamsters
Metin Aksu, Priya Kumar, Thomas Güttler, et al.
Antiviral Research (2023) Vol. 221, pp. 105778-105778
Open Access | Times Cited: 11
Structural Biology of Nanobodies against the Spike Protein of SARS-CoV-2
Qilong Tang, Raymond J. Owens, James H. Naismith
Viruses (2021) Vol. 13, Iss. 11, pp. 2214-2214
Open Access | Times Cited: 24
Structural and Computational Studies of the SARS-CoV-2 Spike Protein Binding Mechanisms with Nanobodies: From Structure and Dynamics to Avidity-Driven Nanobody Engineering
Gennady M. Verkhivker
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 6, pp. 2928-2928
Open Access | Times Cited: 16
Interaction of SARS-CoV-2 with host cells and antibodies: experiment and simulation
Hung Van Nguyen, Hoang Linh Nguyen, Pham Dang Lan, et al.
Chemical Society Reviews (2023) Vol. 52, Iss. 18, pp. 6497-6553
Closed Access | Times Cited: 9
SARS-CoV-2 antibodies recognize 23 distinct epitopic sites on the receptor binding domain
Jiansheng Jiang, Christopher T. Boughter, Javeed Ahmad, et al.
Communications Biology (2023) Vol. 6, Iss. 1
Open Access | Times Cited: 9
Potent neutralizing nanobodies resist convergent circulating variants of SARS-CoV-2 by targeting novel and conserved epitopes
Dapeng Sun, Zhe Sang, Yong Joon Kim, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 18
Analysis of the molecular mechanism of SARS-CoV-2 antibodies
Dongfu Jin, Jing Wei, Jian Sun
Biochemical and Biophysical Research Communications (2021) Vol. 566, pp. 45-52
Open Access | Times Cited: 18
Nanobodies: COVID-19 and Future Perspectives
G Valenzuela, Zaray Miranda-Chacón, Constanza Salinas-Rebolledo, et al.
Frontiers in Drug Discovery (2022) Vol. 2
Open Access | Times Cited: 13
A nanobody recognizes a unique conserved epitope and potently neutralizes SARS-CoV-2 omicron variants
Naphak Modhiran, Simon Lauer, Alberto A. Amarilla, et al.
iScience (2023) Vol. 26, Iss. 7, pp. 107085-107085
Open Access | Times Cited: 7
Structural Characterization of a Neutralizing Nanobody With Broad Activity Against SARS-CoV-2 Variants
Tingting Li, Bingjie Zhou, Zhipu Luo, et al.
Frontiers in Microbiology (2022) Vol. 13
Open Access | Times Cited: 10
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
A single-domain antibody library based on a stability-engineered human VH3 scaffold
Nam‐Ju Lee, Mooyoung Jung, Hye Young Yang, et al.
Scientific Reports (2024) Vol. 14, Iss. 1
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
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