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:

Cocktail of REGN Antibodies Binds More Strongly to SARS-CoV-2 Than Its Components, but the Omicron Variant Reduces Its Neutralizing Ability
Hung Van Nguyen, Pham Dang Lan, Daniel A. Nissley, et al.
The Journal of Physical Chemistry B (2022) Vol. 126, Iss. 15, pp. 2812-2823
Open Access | Times Cited: 16

Showing 16 citing articles:

SARS-CoV-2 spike S2-specific neutralizing antibodies
Chia‐Jung Li, Shih‐Chung Chang
Emerging Microbes & Infections (2023) Vol. 12, Iss. 2
Open Access | Times Cited: 35

Molnupiravir maintains antiviral activity against SARS-CoV-2 variants and exhibits a high barrier to the development of resistance
Julie Strizki, John M. Gaspar, John A. Howe, et al.
Antimicrobial Agents and Chemotherapy (2023) Vol. 68, Iss. 1
Open Access | Times Cited: 17

Current Status and Perspectives of Therapeutic Antibodies Targeting the Spike Protein S2 Subunit against SARS-CoV-2
Yuichiro Yamamoto, Tetsuya Inoue
Biological and Pharmaceutical Bulletin (2024) Vol. 47, Iss. 5, pp. 917-923
Open Access | Times Cited: 5

Antibody drugs targeting SARS-CoV-2: Time for a rethink?
Likeng Liang, Bo Wang, Qing Zhang, et al.
Biomedicine & Pharmacotherapy (2024) Vol. 176, pp. 116900-116900
Open Access | Times Cited: 4

Deciphering the free energy landscapes of SARS-CoV-2 wild type and Omicron variant interacting with human ACE2
Pham Dang Lan, Daniel A. Nissley, Edward P. O’Brien, et al.
The Journal of Chemical Physics (2024) Vol. 160, Iss. 5
Closed Access | Times Cited: 3

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

Exploring the ability of the MD+FoldX method to predict SARS-CoV-2 antibody escape mutations using large-scale data
L. América, Jonathan E. Barnes, Jagdish Suresh Patel, et al.
Scientific Reports (2024) Vol. 14, Iss. 1
Open Access | Times Cited: 2

Protein aggregation rate depends on mechanical stability of fibrillar structure
Tran Thi Minh Thu, Mai Suan Li
The Journal of Chemical Physics (2022) Vol. 157, Iss. 5
Closed Access | Times Cited: 10

Neutralizing antibodies and their cocktails against SARS-CoV-2 Omicron and other circulating variants
Yang Yang, Lanying Du
Cellular and Molecular Immunology (2022) Vol. 19, Iss. 8, pp. 962-964
Open Access | Times Cited: 8

Novel Polymyxin-Inspired Peptidomimetics Targeting the SARS-CoV-2 Spike:hACE2 Interface
Kelly Bugatti, Andrea Sartori, Lucia Battistini, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 10, pp. 8765-8765
Open Access | Times Cited: 4

Structure adaptation in Omicron SARS-CoV-2/hACE2: Biophysical origins of evolutionary driving forces
Ya‐Wen Hsiao, David J. Bray, Tseden Taddese, et al.
Biophysical Journal (2023) Vol. 122, Iss. 20, pp. 4057-4067
Open Access | Times Cited: 4

Fast Prediction of Binding Affinities of SARS-CoV-2 Spike Protein and Its Mutants with Antibodies through Intermolecular Interaction Modeling-Based Machine Learning
Alexander H. Williams, Chang‐Guo Zhan
The Journal of Physical Chemistry B (2022) Vol. 126, Iss. 28, pp. 5194-5206
Closed Access | Times Cited: 7

Binding of SARS-CoV-2 Nonstructural Protein 1 to 40S Ribosome Inhibits mRNA Translation
Hung Van Nguyen, Hoang Linh Nguyen, Mai Suan Li
The Journal of Physical Chemistry B (2024)
Open Access

Structure adaptation in Omicron SARS-CoV-2/hACE2: Biophysical origins of evolutionary driving forces
Ya‐Wen Hsiao, Tseden Taddese, Guadalupe Jiménez-Serratos, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 1

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