Open Access Helper

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:

Coronavirus entry: how we arrived at SARS-CoV-2
Gary R. Whittaker, Susan Daniel, Jean K. Millet
Current Opinion in Virology (2021) Vol. 47, pp. 113-120
Open Access | Times Cited: 65

Showing 1-25 of 65 citing articles:

Structures and functions of coronavirus replication–transcription complexes and their relevance for SARS-CoV-2 drug design
Brandon Malone, Nadya Urakova, Eric J. Snijder, et al.
Nature Reviews Molecular Cell Biology (2021) Vol. 23, Iss. 1, pp. 21-39
Open Access | Times Cited: 389
Functional evaluation of the P681H mutation on the proteolytic activation of the SARS-CoV-2 variant B.1.1.7 (Alpha) spike
Bailey Lubinski, Maureen Hoch Vieira Fernandes, Laura E. Frazier, et al.
iScience (2021) Vol. 25, Iss. 1, pp. 103589-103589
Open Access | Times Cited: 194
Cellular host factors for SARS-CoV-2 infection
Jim Baggen, Els Vanstreels, Sander Jansen, et al.
Nature Microbiology (2021) Vol. 6, Iss. 10, pp. 1219-1232
Open Access | Times Cited: 185
Waves and variants of SARS-CoV-2: understanding the causes and effect of the COVID-19 catastrophe
Vikram Thakur, Shivam Bhola, Pryanka Thakur, et al.
Infection (2021) Vol. 50, Iss. 2, pp. 309-325
Open Access | Times Cited: 169
SARS-CoV-2 spike and its adaptable furin cleavage site
Gary R. Whittaker
The Lancet Microbe (2021) Vol. 2, Iss. 10, pp. e488-e489
Open Access | Times Cited: 82
Functional evaluation of the P681H mutation on the proteolytic activation the SARS-CoV-2 variant B.1.1.7 (Alpha) spike
Bailey Lubinski, Maureen Hoch Vieira Fernandes, Laura E. Frazier, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 68
A systematic review of Vaccine Breakthrough Infections by SARS-CoV-2 Delta Variant
Mengxin Zhang, Ying Liang, Dongsheng Yu, et al.
International Journal of Biological Sciences (2022) Vol. 18, Iss. 2, pp. 889-900
Open Access | Times Cited: 61
The Emergence of the Spike Furin Cleavage Site in SARS-CoV-2
Yujia A. Chan, Shing H. Zhan
Molecular Biology and Evolution (2021) Vol. 39, Iss. 1
Open Access | Times Cited: 60
Drug Combinations as a First Line of Defense against Coronaviruses and Other Emerging Viruses
Judith M. White, Joshua T. Schiffer, Rachel Bender Ignacio, et al.
mBio (2021) Vol. 12, Iss. 6
Open Access | Times Cited: 58
Spike Protein Cleavage-Activation in the Context of the SARS-CoV-2 P681R Mutation: an Analysis from Its First Appearance in Lineage A.23.1 Identified in Uganda
Bailey Lubinski, Laura E. Frazier, My V. T. Phan, et al.
Microbiology Spectrum (2022) Vol. 10, Iss. 4
Open Access | Times Cited: 43
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: 41
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
Viral Membrane Fusion: A Dance Between Proteins and Lipids
Judith M. White, Amanda E. Ward, Laura Odongo, et al.
Annual Review of Virology (2023) Vol. 10, Iss. 1, pp. 139-161
Open Access | Times Cited: 37
A Comparison of Conserved Features in the Human Coronavirus Family Shows That Studies of Viruses Less Pathogenic than SARS-CoV-2, Such as HCoV-OC43, Are Good Model Systems for Elucidating Basic Mechanisms of Infection and Replication in Standard Laboratories
Audrey L. Heffner, Tracey A. Rouault
Viruses (2025) Vol. 17, Iss. 2, pp. 256-256
Open Access | Times Cited: 1
Spike protein cleavage-activation mediated by the SARS-CoV-2 P681R mutation: a case-study from its first appearance in variant of interest (VOI) A.23.1 identified in Uganda
Bailey Lubinski, Laura E. Frazier, My V. T. Phan, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 49
Binding of SARS-CoV-2 Fusion Peptide to Host Endosome and Plasma Membrane
Stefan L. Schaefer, Hendrik Jung, Gerhard Hummer
The Journal of Physical Chemistry B (2021) Vol. 125, Iss. 28, pp. 7732-7741
Open Access | Times Cited: 43
Precision nutrition to reset virus-induced human metabolic reprogramming and dysregulation (HMRD) in long-COVID
A. Satyanarayan Naidu, Chin‐Kun Wang, Pingfan Rao, et al.
npj Science of Food (2024) Vol. 8, Iss. 1
Open Access | Times Cited: 8
Inhibitors of L-Type Calcium Channels Show Therapeutic Potential for Treating SARS-CoV-2 Infections by Preventing Virus Entry and Spread
Marco R. Straus, Miya K. Bidon, Tiffany Tang, et al.
ACS Infectious Diseases (2021) Vol. 7, Iss. 10, pp. 2807-2815
Open Access | Times Cited: 40
Natural and Recombinant SARS-CoV-2 Isolates Rapidly Evolve In Vitro to Higher Infectivity through More Efficient Binding to Heparan Sulfate and Reduced S1/S2 Cleavage
Nikita Shiliaev, Tetyana Lukash, Oksana Palchevska, et al.
Journal of Virology (2021) Vol. 95, Iss. 21
Open Access | Times Cited: 38
Monoclonal antibody targeting the conserved region of the SARS-CoV-2 spike protein to overcome viral variants
Wan-Ling Wu, Chen-Yi Chiang, Szu-Chia Lai, et al.
JCI Insight (2022) Vol. 7, Iss. 8
Open Access | Times Cited: 28
Merging microfluidics with luminescence immunoassays for urgent point-of-care diagnostics of COVID-19
Huijuan Yuan, Peng Chen, Chao Wan, et al.
TrAC Trends in Analytical Chemistry (2022) Vol. 157, pp. 116814-116814
Open Access | Times Cited: 22
CAML Model for Computational Biology
Parimal Pal Chaudhuri, Adip Dutta, Somshubhro Pal Choudhury, et al.
(2025), pp. 131-300
Closed Access
A weak COPI binding motif in the cytoplasmic tail of SARS‐CoV‐2 spike glycoprotein is necessary for its cleavage, glycosylation, and localization
Benjamin C. Jennings, Stuart Kornfeld, Balraj Doray
FEBS Letters (2021) Vol. 595, Iss. 13, pp. 1758-1767
Open Access | Times Cited: 27
Proteases and variants: context matters for SARS-CoV-2 entry assays
Christian S. Stevens, Kasopefoluwa Y. Oguntuyo, Benhur Lee
Current Opinion in Virology (2021) Vol. 50, pp. 49-58
Open Access | Times Cited: 26
Genome-wide bioinformatics analysis of human protease capacity for proteolytic cleavage of the SARS-CoV-2 spike glycoprotein
Э. В. Матвеев, Gennady V. Ponomarev, Marat D. Kazanov
Microbiology Spectrum (2024) Vol. 12, Iss. 2
Open Access | Times Cited: 3
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