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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:

A delicate balance between antibody evasion and ACE2 affinity for Omicron BA.2.75
Jiandong Huo, Aiste Dijokaite-Guraliuc, Chang Liu, et al.
Cell Reports (2022) Vol. 42, Iss. 1, pp. 111903-111903
Open Access | Times Cited: 56

Showing 1-25 of 56 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: 269
Convergent evolution of SARS-CoV-2 Omicron subvariants leading to the emergence of BQ.1.1 variant
Jumpei Ito, Rigel Suzuki, Keiya Uriu, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 122
SARS-CoV-2 BA.2.86 enters lung cells and evades neutralizing antibodies with high efficiency
Lu Zhang, Amy Kempf, Inga Nehlmeier, et al.
Cell (2024) Vol. 187, Iss. 3, pp. 596-608.e17
Closed Access | Times Cited: 79
Mutations in the SARS-CoV-2 spike receptor binding domain and their delicate balance between ACE2 affinity and antibody evasion
Song Xue, Yuru Han, Fan Wu, et al.
Protein & Cell (2024) Vol. 15, Iss. 6, pp. 403-418
Open Access | Times Cited: 25
Omicron Spike confers enhanced infectivity and interferon resistance to SARS-CoV-2 in human nasal tissue
Guoli Shi, Tiansheng Li, Kin Kui Lai, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 19
A structure-function analysis shows SARS-CoV-2 BA.2.86 balances antibody escape and ACE2 affinity
Chang Liu, Daming Zhou, Aiste Dijokaite-Guraliuc, et al.
Cell Reports Medicine (2024) Vol. 5, Iss. 5, pp. 101553-101553
Open Access | Times Cited: 19
Rapid escape of new SARS-CoV-2 Omicron variants from BA.2-directed antibody responses
Aiste Dijokaite-Guraliuc, Raksha Das, Daming Zhou, et al.
Cell Reports (2023) Vol. 42, Iss. 4, pp. 112271-112271
Open Access | Times Cited: 39
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: 31
Reversal of the unique Q493R mutation increases the affinity of Omicron S1-RBD for ACE2
Angelin M. Philip, Wesam S. Ahmed, Kabir H. Biswas
Computational and Structural Biotechnology Journal (2023) Vol. 21, pp. 1966-1977
Open Access | Times Cited: 28
Antigenic evolution of SARS coronavirus 2
Anna Z. Mykytyn, Ron A. M. Fouchier, Bart L. Haagmans
Current Opinion in Virology (2023) Vol. 62, pp. 101349-101349
Open Access | Times Cited: 26
The SARS-CoV-2 neutralizing antibody response to SD1 and its evasion by BA.2.86
Daming Zhou, Piyada Supasa, Chang Liu, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 16
SARS-CoV-2 Omicron Subvariants Do Not Differ Much in Binding Affinity to Human ACE2: A Molecular Dynamics Study
Hoang Linh Nguyen, Thai Quoc Nguyen, Mai Suan Li
The Journal of Physical Chemistry B (2024) Vol. 128, Iss. 14, pp. 3340-3349
Open Access | Times Cited: 11
Reverse mutational scanning of SARS-CoV-2 spike BA.2.86 identifies epitopes contributing to immune escape from polyclonal sera
Najat Bdeir, Tatjana Lüddecke, Henrike Maaß, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 1
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
Prevalence of symptoms, comorbidities, and reinfections in individuals infected with Wild-Type SARS-CoV-2, Delta, or Omicron variants: a comparative study in western Mexico
Marcela Peña‐Rodríguez, Jorge Hernández‐Bello, Natali Vega‐Magaña, et al.
Frontiers in Public Health (2023) Vol. 11
Open Access | Times Cited: 19
Ensemble-Based Mutational Profiling and Network Analysis of the SARS-CoV-2 Spike Omicron XBB Lineages for Interactions with the ACE2 Receptor and Antibodies: Cooperation of Binding Hotspots in Mediating Epistatic Couplings Underlies Binding Mechanism and Immune Escape
Nishank Raisinghani, Mohammed Alshahrani, Grace Gupta, et al.
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 8, pp. 4281-4281
Open Access | Times Cited: 8
Predicting Functional Conformational Ensembles and Binding Mechanisms of Convergent Evolution for SARS-CoV-2 Spike Omicron Variants Using AlphaFold2 Sequence Scanning Adaptations and Molecular Dynamics Simulations
Nishank Raisinghani, Mohammed Alshahrani, Grace Gupta, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 7
Probing conformational landscapes of binding and allostery in the SARS-CoV-2 omicron variant complexes using microsecond atomistic simulations and perturbation-based profiling approaches: hidden role of omicron mutations as modulators of allosteric signaling and epistatic relationships
Gennady M. Verkhivker, Mohammed Alshahrani, Grace Gupta, et al.
Physical Chemistry Chemical Physics (2023) Vol. 25, Iss. 32, pp. 21245-21266
Open Access | Times Cited: 13
Spike Protein Mutation-Induced Changes in the Kinetic and Thermodynamic Behavior of Its Receptor Binding Domains Explain Their Higher Propensity to Attain Open States in SARS-CoV-2 Variants of Concern
Jasdeep Singh, Shubham Vashishtha, Bishwajit Kundu
ACS Central Science (2023) Vol. 9, Iss. 10, pp. 1894-1904
Open Access | Times Cited: 13
Reverse mutational scanning of spike BA.2.86 identifies the epitopes contributing to immune escape from polyclonal sera
Najat Bdeir, Tatjana Lüddecke, Henrike Maaß, et al.
medRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 5
Overcoming antibody-resistant SARS-CoV-2 variants with bispecific antibodies constructed using non-neutralizing antibodies
Tetsuya Inoue, Yuichiro Yamamoto, Kaoru Sato, et al.
iScience (2024) Vol. 27, Iss. 4, pp. 109363-109363
Open Access | Times Cited: 5
Exploring Conformational Landscapes and Binding Mechanisms of Convergent Evolution for the SARS-CoV-2 Spike Omicron Variant Complexes with the ACE2 Receptor Using AlphaFold2-Based Structural Ensembles and Molecular Dynamics Simulations
Nishank Raisinghani, Mohammed Alshahrani, Grace Gupta, et al.
Physical Chemistry Chemical Physics (2024) Vol. 26, Iss. 25, pp. 17720-17744
Closed Access | Times Cited: 5
Molecular and structural insights into SARS-CoV-2 evolution: from BA.2 to XBB subvariants
Hisano Yajima, Tomo Nomai, Kaho Okumura, et al.
mBio (2024) Vol. 15, Iss. 10
Open Access | Times Cited: 5
Additional mutations based on Omicron BA.2.75 mediate its further evasion from broadly neutralizing antibodies
Huimin Guo, Jie Jiang, Senlin Shen, et al.
iScience (2023) Vol. 26, Iss. 4, pp. 106283-106283
Open Access | Times Cited: 12
AlphaFold2-Enabled Atomistic Modeling of Structure, Conformational Ensembles, and Binding Energetics of the SARS-CoV-2 Omicron BA.2.86 Spike Protein with ACE2 Host Receptor and Antibodies: Compensatory Functional Effects of Binding Hotspots in Modulating Mechanisms of Receptor Binding and Immune Escape
Nishank Raisinghani, Mohammed Alshahrani, Grace Gupta, et al.
Journal of Chemical Information and Modeling (2024) Vol. 64, Iss. 5, pp. 1657-1681
Closed Access | Times Cited: 4
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