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:

Structural diversity of the SARS-CoV-2 Omicron spike
S. Gobeil, Rory Henderson, Victoria Stalls, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 35

Showing 1-25 of 35 citing articles:

Structural and functional impact by SARS-CoV-2 Omicron spike mutations
Jun Zhang, Yongfei Cai, Christy L. Lavine, et al.
Cell Reports (2022) Vol. 39, Iss. 4, pp. 110729-110729
Open Access | Times Cited: 143

PDBx/mmCIF Ecosystem: Foundational Semantic Tools for Structural Biology
John D. Westbrook, Jasmine Young, Chenghua Shao, et al.
Journal of Molecular Biology (2022) Vol. 434, Iss. 11, pp. 167599-167599
Open Access | Times Cited: 69

SARS-CoV-2 Omicron spike H655Y mutation is responsible for enhancement of the endosomal entry pathway and reduction of cell surface entry pathways
Mizuki Yamamoto, Keiko Tomita, Youko Hirayama, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 38

The Spike Protein of SARS-CoV-2 Is Adapting Because of Selective Pressures
Georgina I. López-Cortés, Miryam Palacios-Pérez, Hannya F. Veledíaz, et al.
Vaccines (2022) Vol. 10, Iss. 6, pp. 864-864
Open Access | Times Cited: 24

Could a Lower Toll-like Receptor (TLR) and NF-κB Activation Due to a Changed Charge Distribution in the Spike Protein Be the Reason for the Lower Pathogenicity of Omicron?
Ralf Kircheis, Oliver Planz
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 11, pp. 5966-5966
Open Access | Times Cited: 20

Role of N343 glycosylation on the SARS-CoV-2 S RBD structure and co-receptor binding across variants of concern
Callum M. Ives, Linh Nguyen, Carl A. Fogarty, et al.
eLife (2024) Vol. 13
Open Access | Times Cited: 4

Computer Simulations and Network-Based Profiling of Binding and Allosteric Interactions of SARS-CoV-2 Spike Variant Complexes and the Host Receptor: Dissecting the Mechanistic Effects of the Delta and Omicron Mutations
Gennady M. Verkhivker, Steve Agajanian, Ryan Kassab, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 8, pp. 4376-4376
Open Access | Times Cited: 18

Omicron’s molecular structure could help explain its global takeover
Diana Kwon
Nature (2022) Vol. 602, Iss. 7897, pp. 373-374
Closed Access | Times Cited: 16

A structural dynamic explanation for observed escape of SARS-CoV-2 BA.2 variant mutation S371L/F
Nathaniel L. Miller, Thomas A. Clark, Rahul Raman, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 11

Novel chimeric proteins mimicking SARS-CoV-2 spike epitopes with broad inhibitory activity
Mario Cano‐Muñoz, Daniel Polo-Megías, A. Cámara-Artigas, et al.
International Journal of Biological Macromolecules (2022) Vol. 222, pp. 2467-2478
Open Access | Times Cited: 10

Analyzing the immunogenicity of bivalent booster vaccinations in healthcare workers: The SWITCH ON trial protocol
Ngoc H. Tan, Roos S. G. Sablerolles, Wim J. R. Rietdijk, et al.
Frontiers in Immunology (2022) Vol. 13
Open Access | Times Cited: 9

Preserved recognition of Omicron spike following COVID-19 messenger RNA vaccination in pregnancy
Yannic C. Bartsch, Caroline Atyeo, Jaewon Kang, et al.
American Journal of Obstetrics and Gynecology (2022) Vol. 227, Iss. 3, pp. 493.e1-493.e7
Open Access | Times Cited: 7

Role of N343 glycosylation on the SARS-CoV-2 S RBD structure and co-receptor binding across variants of concern
Callum M. Ives, Linh Nguyen, Carl A. Fogarty, et al.
eLife (2024) Vol. 13
Open Access | Times Cited: 1

Efficient Neutralization of SARS-CoV-2 Omicron and Other VOCs by a Broad Spectrum Antibody 8G3
Hang Ma, Chien‐Te K. Tseng, Huifang Zong, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 6

A broadly neutralising monoclonal antibody overcomes the mutational landscape of emerging SARS-CoV2 variant of concerns
Rajesh Kumar, Hilal Parray, Naveen Narayan, et al.
Research Square (Research Square) (2022)
Open Access | Times Cited: 3

Temporary COVID-19 Specialized Hospital: Management Strategies for Public Health Emergencies
Bei Tian, Zhongping Ning, Ping-An Tu
Journal of Multidisciplinary Healthcare (2023) Vol. Volume 16, pp. 1699-1704
Open Access | Times Cited: 1

Clinical Characteristics of COVID-19 Reinfection: A Retrospective Study in China
Chaochao Qiu, Xiaoqing Lin, Qiang Zhang, et al.
Research Square (Research Square) (2024)
Open Access

Assessing pH-dependent Conformational Changes in the Fusion Peptide Proximal Region of the SARS-CoV-2 spike glycoprotein
Darya Stepanenko, Yuzhang Wang, Carlos Simmerling
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

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