Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

Cryo-EM structures of SARS-CoV-2 Omicron BA.2 spike
Victoria Stalls, Jared Lindenberger, S. Gobeil, et al.
Cell Reports (2022) Vol. 39, Iss. 13, pp. 111009-111009
Open Access | Times Cited: 91

Showing 1-25 of 91 citing articles:

Virological characteristics of the SARS-CoV-2 XBB variant derived from recombination of two Omicron subvariants
Tomokazu Tamura, Jumpei Ito, Keiya Uriu, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 256
Imprinted antibody responses against SARS-CoV-2 Omicron sublineages
Young‐Jun Park, Dora Pinto, Alexandra C. Walls, et al.
Science (2022) Vol. 378, Iss. 6620, pp. 619-627
Open Access | Times Cited: 193
Deep mutational scans for ACE2 binding, RBD expression, and antibody escape in the SARS-CoV-2 Omicron BA.1 and BA.2 receptor-binding domains
Tyler N. Starr, Allison J. Greaney, Cameron Stewart, et al.
PLoS Pathogens (2022) Vol. 18, Iss. 11, pp. e1010951-e1010951
Open Access | Times Cited: 163
Virological characteristics of the SARS-CoV-2 Omicron BA.2.75 variant
Akatsuki Saito, Tomokazu Tamura, Jiří Zahradník, et al.
Cell Host & Microbe (2022) Vol. 30, Iss. 11, pp. 1540-1555.e15
Open Access | Times Cited: 148
SARS-CoV-2 Omicron BA.5: Evolving tropism and evasion of potent humoral responses and resistance to clinical immunotherapeutics relative to viral variants of concern
Anupriya Aggarwal, Anouschka Akerman, Vanessa Milogiannakis, et al.
EBioMedicine (2022) Vol. 84, pp. 104270-104270
Open Access | Times Cited: 138
Neutralization, effector function and immune imprinting of Omicron variants
Amin Addetia, Luca Piccoli, James Brett Case, et al.
Nature (2023) Vol. 621, Iss. 7979, pp. 592-601
Open Access | Times Cited: 112
Determinants of Spike infectivity, processing, and neutralization in SARS-CoV-2 Omicron subvariants BA.1 and BA.2
Chiara Pastorio, Fabian Zech, Sabrina Noettger, et al.
Cell Host & Microbe (2022) Vol. 30, Iss. 9, pp. 1255-1268.e5
Open Access | Times Cited: 74
Structural dynamics in the evolution of SARS-CoV-2 spike glycoprotein
Valeria Calvaresi, Antoni G. Wrobel, Joanna Toporowska, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 43
SARS-CoV-2 variants of concern: spike protein mutational analysis and epitope for broad neutralization
Dhiraj Mannar, James W. Saville, Zehua Sun, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 56
SARS-CoV-2 spike N-terminal domain modulates TMPRSS2-dependent viral entry and fusogenicity
Bo Meng, Rawlings Datir, Jinwook Choi, et al.
Cell Reports (2022) Vol. 40, Iss. 7, pp. 111220-111220
Open Access | Times Cited: 40
Therapeutic and vaccine-induced cross-reactive antibodies with effector function against emerging Omicron variants
Amin Addetia, Luca Piccoli, James Brett Case, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 30
Markov State Models and Perturbation-Based Approaches Reveal Distinct Dynamic Signatures and Hidden Allosteric Pockets in the Emerging SARS-Cov-2 Spike Omicron Variant Complexes with the Host Receptor: The Interplay of Dynamics and Convergent Evolution Modulates Allostery and Functional Mechanisms
Sian Xiao, Mohammed Alshahrani, Grace Gupta, et al.
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 16, pp. 5272-5296
Open Access | Times Cited: 28
Evolution of the SARS-CoV-2 Omicron spike
Ruth Parsons, Priyamvada Acharya
Cell Reports (2023) Vol. 42, Iss. 12, pp. 113444-113444
Open Access | Times Cited: 28
Balancing Functional Tradeoffs between Protein Stability and ACE2 Binding in the SARS-CoV-2 Omicron BA.2, BA.2.75 and XBB Lineages: Dynamics-Based Network Models Reveal Epistatic Effects Modulating Compensatory Dynamic and Energetic Changes
Gennady M. Verkhivker, Mohammed Alshahrani, Grace Gupta
Viruses (2023) Vol. 15, Iss. 5, pp. 1143-1143
Open Access | Times Cited: 22
Altered receptor binding, antibody evasion and retention of T cell recognition by the SARS-CoV-2 XBB.1.5 spike protein
Dhiraj Mannar, James W. Saville, Chad Poloni, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 8
Antibody escape and cryptic cross-domain stabilization in the SARS-CoV-2 Omicron spike protein
Kamyab Javanmardi, Thomas H. Segall-Shapiro, Chia‐Wei Chou, et al.
Cell Host & Microbe (2022) Vol. 30, Iss. 9, pp. 1242-1254.e6
Open Access | Times Cited: 35
Structural and functional characteristics of the SARS-CoV-2 Omicron subvariant BA.2 spike protein
Jun Zhang, Weichun Tang, Hailong Gao, et al.
Nature Structural & Molecular Biology (2023) Vol. 30, Iss. 7, pp. 980-990
Closed Access | Times Cited: 20
Mechanism and evolution of human ACE2 binding by SARS-CoV-2 spike
Antoni G. Wrobel
Current Opinion in Structural Biology (2023) Vol. 81, pp. 102619-102619
Open Access | Times Cited: 18
Broad receptor tropism and immunogenicity of a clade 3 sarbecovirus
Jimin Lee, Samantha K. Zepeda, Young‐Jun Park, et al.
Cell Host & Microbe (2023) Vol. 31, Iss. 12, pp. 1961-1973.e11
Open Access | Times Cited: 18
Molecular Characterization of AZD7442 (Tixagevimab-Cilgavimab) Neutralization of SARS-CoV-2 Omicron Subvariants
Tiffany Barnes, Tyler Brady, Nicolette Schuko, et al.
Microbiology Spectrum (2023) Vol. 11, Iss. 2
Open Access | Times Cited: 16
Structural analysis of receptor engagement and antigenic drift within the BA.2 spike protein
James W. Saville, Dhiraj Mannar, Xing Zhu, et al.
Cell Reports (2023) Vol. 42, Iss. 1, pp. 111964-111964
Open Access | Times Cited: 15
S Protein, ACE2 and Host Cell Proteases in SARS-CoV-2 Cell Entry and Infectivity; Is Soluble ACE2 a Two Blade Sword? A Narrative Review
Reza Nejat, Maziar Fayaz Torshizi, David J. Najafi
Vaccines (2023) Vol. 11, Iss. 2, pp. 204-204
Open Access | Times Cited: 15
Biophysical principles predict fitness of SARS-CoV-2 variants
D. I. C. Wang, Marian Huot, Vaibhav Mohanty, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 23
Open Access | Times Cited: 6
SARS-CoV-2 Omicron XBB lineage spike structures, conformations, antigenicity, and receptor recognition
Qianyi E. Zhang, Jared Lindenberger, Ruth Parsons, et al.
Molecular Cell (2024) Vol. 84, Iss. 14, pp. 2747-2764.e7
Open Access | Times Cited: 5
Structural basis for the evolution and antibody evasion of SARS-CoV-2 BA.2.86 and JN.1 subvariants
Haonan Yang, Huimin Guo, Aojie Wang, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 5
Page 1 - Next Page

Scroll to top