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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:

Spike Glycoprotein and Host Cell Determinants of SARS-CoV-2 Entry and Cytopathic Effects
Hanh T. Nguyen, Shijian Zhang, Qian Wang, et al.
Journal of Virology (2020) Vol. 95, Iss. 5
Open Access | Times Cited: 97

Showing 1-25 of 97 citing articles:

Immunogenicity of Ad26.COV2.S vaccine against SARS-CoV-2 variants in humans
Galit Alter, Jingyou Yu, Jinyan Liu, et al.
Nature (2021) Vol. 596, Iss. 7871, pp. 268-272
Open Access | Times Cited: 321
SARS-CoV-2 one year on: evidence for ongoing viral adaptation
Thomas P. Peacock, Rebekah Penrice-Randal, Julian A. Hiscox, et al.
Journal of General Virology (2021) Vol. 102, Iss. 4
Open Access | Times Cited: 168
The Mechanism and Consequences of SARS-CoV-2 Spike-Mediated Fusion and Syncytia Formation
Maaran Michael Rajah, Annie Bernier, Julian Buchrieser, et al.
Journal of Molecular Biology (2021) Vol. 434, Iss. 6, pp. 167280-167280
Open Access | Times Cited: 159
Structural basis and mode of action for two broadly neutralizing antibodies against SARS-CoV-2 emerging variants of concern
Wenwei Li, Yaozong Chen, Jérémie Prévost, et al.
Cell Reports (2021) Vol. 38, Iss. 2, pp. 110210-110210
Open Access | Times Cited: 128
ADAM10 and ADAM17 promote SARS‐CoV‐2 cell entry and spike protein‐mediated lung cell fusion
Georg Jocher, Vincent Grass, Sarah K. Tschirner, et al.
EMBO Reports (2022) Vol. 23, Iss. 6
Open Access | Times Cited: 103
S-acylation controls SARS-CoV-2 membrane lipid organization and enhances infectivity
Francisco S. Mesquita, Laurence Abrami, Oksana A. Sergeeva, et al.
Developmental Cell (2021) Vol. 56, Iss. 20, pp. 2790-2807.e8
Open Access | Times Cited: 104
SARS-CoV-2 and SARS-CoV Spike-Mediated Cell-Cell Fusion Differ in Their Requirements for Receptor Expression and Proteolytic Activation
Bojan F. Hörnich, Anna K. Großkopf, Sarah Schlagowski, et al.
Journal of Virology (2021) Vol. 95, Iss. 9
Open Access | Times Cited: 101
Functional importance of the D614G mutation in the SARS-CoV-2 spike protein
Cody B. Jackson, Lizhou Zhang, Michael Farzan, et al.
Biochemical and Biophysical Research Communications (2020) Vol. 538, pp. 108-115
Open Access | Times Cited: 100
Emergence and spread of a SARS-CoV-2 lineage A variant (A.23.1) with altered spike protein in Uganda
Daniel Lule Bugembe, My V. T. Phan, Isaac Ssewanyana, et al.
Nature Microbiology (2021) Vol. 6, Iss. 8, pp. 1094-1101
Open Access | Times Cited: 97
Evaluation of Cell-Based and Surrogate SARS-CoV-2 Neutralization Assays
Anton M. Sholukh, Andrew Fioré-Gartland, Emily S. Ford, et al.
Journal of Clinical Microbiology (2021) Vol. 59, Iss. 10
Open Access | Times Cited: 89
Palmitoylation of SARS-CoV-2 S protein is essential for viral infectivity
Zhuanchang Wu, Zhaoying Zhang, Xin Wang, et al.
Signal Transduction and Targeted Therapy (2021) Vol. 6, Iss. 1
Open Access | Times Cited: 69
An update review of emerging small-molecule therapeutic options for COVID-19
Dengke Tian, Yuzhi Liu, Chengyuan Liang, et al.
Biomedicine & Pharmacotherapy (2021) Vol. 137, pp. 111313-111313
Open Access | Times Cited: 63
Impact of temperature on the affinity of SARS-CoV-2 Spike glycoprotein for host ACE2
Jérémie Prévost, Jonathan Richard, Romain Gasser, et al.
Journal of Biological Chemistry (2021) Vol. 297, Iss. 4, pp. 101151-101151
Open Access | Times Cited: 58
SARS-CoV-2 Spike Furin Cleavage Site and S2′ Basic Residues Modulate the Entry Process in a Host Cell-Dependent Manner
Muriel Lavie, Jean Dubuisson, Sandrine Belouzard
Journal of Virology (2022) Vol. 96, Iss. 13
Open Access | Times Cited: 39
Diagnostics and analysis of SARS-CoV-2: current status, recent advances, challenges and perspectives
Tao Dong, Mingyang Wang, Junchong Liu, et al.
Chemical Science (2023) Vol. 14, Iss. 23, pp. 6149-6206
Open Access | Times Cited: 38
Palmitoylation at a conserved cysteine residue facilitates gasdermin D-mediated pyroptosis and cytokine release
Zhonghua Liu, S. Li, Chuanping Wang, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 29
Open Access | Times Cited: 16
An Engineered SARS-CoV-2 S1 Glycoprotein Produced in Pichia pastoris as a Candidate Vaccine Antigen
Sanaz Majidi, Khosrow Aghaiypour Kolyani, Meisam Akrami, et al.
Molecular Biotechnology (2025)
Closed Access | Times Cited: 1
A SARS-CoV-2 lineage A variant (A.23.1) with altered spike has emerged and is dominating the current Uganda epidemic
Daniel Lule Bugembe, My V. T. Phan, Isaac Ssewanyana, et al.
medRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 49
Palmitoylation of SARS‐CoV‐2 S protein is critical for S‐mediated syncytia formation and virus entry
Daoqun Li, Yihan Liu, Yue Lu, et al.
Journal of Medical Virology (2021) Vol. 94, Iss. 1, pp. 342-348
Open Access | Times Cited: 46
Identification of SARS-CoV-2 Spike Palmitoylation Inhibitors That Results in Release of Attenuated Virus with Reduced Infectivity
Ahmed Ramadan, Karthick Mayilsamy, Andrew R. McGill, et al.
Viruses (2022) Vol. 14, Iss. 3, pp. 531-531
Open Access | Times Cited: 38
Functional properties of the spike glycoprotein of the emerging SARS-CoV-2 variant B.1.1.529
Qian Wang, Saumya Anang, Sho Iketani, et al.
Cell Reports (2022) Vol. 39, Iss. 11, pp. 110924-110924
Open Access | Times Cited: 31
Temperature-dependent Spike-ACE2 interaction of Omicron subvariants is associated with viral transmission
Mehdi Benlarbi, Shilei Ding, Étienne Bélanger, et al.
mBio (2024) Vol. 15, Iss. 8
Open Access | Times Cited: 7
Analysis of Glycosylation and Disulfide Bonding of Wild-Type SARS-CoV-2 Spike Glycoprotein
Shijian Zhang, Eden P. Go, Haitao Ding, et al.
Journal of Virology (2021) Vol. 96, Iss. 3
Open Access | Times Cited: 34
Identification and differential usage of a host metalloproteinase entry pathway by SARS-CoV-2 Delta and Omicron
Mehdi Benlarbi, Geneviève Laroche, Corby Fink, et al.
iScience (2022) Vol. 25, Iss. 11, pp. 105316-105316
Open Access | Times Cited: 27
Sertraline Is an Effective SARS-CoV-2 Entry Inhibitor Targeting the Spike Protein
Yuliu Chen, Yan Wu, Shaoying Chen, et al.
Journal of Virology (2022) Vol. 96, Iss. 24
Open Access | Times Cited: 24
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