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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:

Dynamic Asymmetry Exposes 2019-nCoV Prefusion Spike
Susmita Roy, Akhilesh Jaiswar, Raju Sarkar
The Journal of Physical Chemistry Letters (2020) Vol. 11, Iss. 17, pp. 7021-7027
Open Access | Times Cited: 47

Showing 1-25 of 47 citing articles:

The antigenic anatomy of SARS-CoV-2 receptor binding domain
Wanwisa Dejnirattisai, Daming Zhou, Helen M. Ginn, et al.
Cell (2021) Vol. 184, Iss. 8, pp. 2183-2200.e22
Open Access | Times Cited: 394
Neutralization of SARS-CoV-2 by Destruction of the Prefusion Spike
Jiandong Huo, Yuguang Zhao, Jingshan Ren, et al.
Cell Host & Microbe (2020) Vol. 28, Iss. 3, pp. 445-454.e6
Open Access | Times Cited: 367
An infectivity-enhancing site on the SARS-CoV-2 spike protein targeted by antibodies
Yafei Liu, Wai Tuck Soh, Jun-ichi Kishikawa, et al.
Cell (2021) Vol. 184, Iss. 13, pp. 3452-3466.e18
Open Access | Times Cited: 262
A multiscale model of virus pandemic: Heterogeneous interactive entities in a globally connected world
Nicola Bellomo, Richard J. Bingham, Mark A. J. Chaplain, et al.
Mathematical Models and Methods in Applied Sciences (2020) Vol. 30, Iss. 08, pp. 1591-1651
Open Access | Times Cited: 166
Distant residues modulate conformational opening in SARS-CoV-2 spike protein
Dhiman Ray, Ly Le, Ioan Andricioaei
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 43
Open Access | Times Cited: 86
Challenges and opportunities for antiviral monoclonal antibodies as COVID-19 therapy
Carlos Cruz‐Teran, Karthik Tiruthani, Morgan D. McSweeney, et al.
Advanced Drug Delivery Reviews (2020) Vol. 169, pp. 100-117
Open Access | Times Cited: 79
Characterization of Structural and Energetic Differences between Conformations of the SARS-CoV-2 Spike Protein
Rodrigo A. Moreira, Horacio V. Guzman, Subramanian Boopathi, et al.
Materials (2020) Vol. 13, Iss. 23, pp. 5362-5362
Open Access | Times Cited: 54
Sterically confined rearrangements of SARS-CoV-2 Spike protein control cell invasion
Esteban Dodero‐Rojas, José N. Onuchic, Paul C. Whitford
eLife (2021) Vol. 10
Open Access | Times Cited: 50
The SARS-CoV-2 spike protein is vulnerable to moderate electric fields
Claudia R. Arbeitman, Pablo A. Rojas, Pedro Ojeda-May, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 43
A VDAC1-mediated NEET protein chain transfers [2Fe-2S] clusters between the mitochondria and the cytosol and impacts mitochondrial dynamics
Ola Karmi, Henri‐Baptiste Marjault, Fang Bai, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 7
Open Access | Times Cited: 38
Membrane attachment and fusion of HIV-1, influenza A, and SARS-CoV-2: resolving the mechanisms with biophysical methods
Geetanjali Negi, Anurag Sharma, Manorama Dey, et al.
Biophysical Reviews (2022) Vol. 14, Iss. 5, pp. 1109-1140
Open Access | Times Cited: 29
Comparative molecular dynamics study of the receptor-binding domains in SARS-CoV-2 and SARS-CoV and the effects of mutations on the binding affinity
Shokouh Rezaei, Yahya Sefidbakht, Vuk Uskoković
Journal of Biomolecular Structure and Dynamics (2020) Vol. 40, Iss. 10, pp. 4662-4681
Open Access | Times Cited: 35
Shedding Light on the Inhibitory Mechanisms of SARS-CoV-1/CoV-2 Spike Proteins by ACE2-Designed Peptides
Frederico Campos Freitas, Paulo Henrique Borges Ferreira, Denize C. Favaro, et al.
Journal of Chemical Information and Modeling (2021) Vol. 61, Iss. 3, pp. 1226-1243
Open Access | Times Cited: 29
All-Atom Simulations of Human ACE2-Spike Protein RBD Complexes for SARS-CoV-2 and Some of its Variants: Nature of Interactions and Free Energy Diagrams for Dissociation of the Protein Complexes
Saheb Dutta, Bhavana Panthi, Amalendu Chandra
The Journal of Physical Chemistry B (2022) Vol. 126, Iss. 29, pp. 5375-5389
Closed Access | Times Cited: 20
Omicron mutations increase interdomain interactions and reduce epitope exposure in the SARS-CoV-2 spike
Miłosz Wieczór, Phu K. Tang, Modesto Orozco, et al.
iScience (2023) Vol. 26, Iss. 2, pp. 105981-105981
Open Access | Times Cited: 12
Ultra-large-scale ab initio quantum chemical computation of bio-molecular systems: The case of spike protein of SARS-CoV-2 virus
W. Y. Ching, Puja Adhikari, Bahaa Jawad, et al.
Computational and Structural Biotechnology Journal (2021) Vol. 19, pp. 1288-1301
Open Access | Times Cited: 26
Characterization of structural and energetic differences between conformations of the SARS-CoV-2 spike protein
Rodrigo A. Moreira, Horacio V. Guzman, Subramanian Boopathi, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 25
Evolution of Sequence and Structure of SARS-CoV-2 Spike Protein: A Dynamic Perspective
Anushree Sinha, Satyam Sangeet, Susmita Roy
ACS Omega (2023) Vol. 8, Iss. 26, pp. 23283-23304
Open Access | Times Cited: 9
Physicochemical effects of emerging exchanges on the spike protein's RBM of the SARS-CoV-2 Omicron subvariants BA.1-BA.5 and its influence on the biological properties and attributes developed by these subvariants
Robério Amorim de Almeida Pondé
Virology (2023) Vol. 587, pp. 109850-109850
Closed Access | Times Cited: 9
Distant Residues Modulate Conformational Opening in SARS-CoV-2 Spike Protein
Dhiman Ray, Ly Le, Ioan Andricioaei
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 18
Frustration-driven allosteric regulation and signal transmission in the SARS-CoV-2 spike omicron trimer structures: a crosstalk of the omicron mutation sites allosterically regulates tradeoffs of protein stability and conformational adaptability
Gennady M. Verkhivker, Steve Agajanian, Ryan Kassab, et al.
Physical Chemistry Chemical Physics (2022) Vol. 24, Iss. 29, pp. 17723-17743
Closed Access | Times Cited: 11
An infectivity-enhancing site on the SARS-CoV-2 spike protein is targeted by COVID-19 patient antibodies
Yafei Liu, Wai Tuck Soh, Asa Tada, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Closed Access | Times Cited: 16
Nano-size dependence in the adsorption by the SARS-CoV-2 spike protein over gold colloid
Kazushige Yokoyama, Akane Ichiki
Colloids and Surfaces A Physicochemical and Engineering Aspects (2021) Vol. 615, pp. 126275-126275
Open Access | Times Cited: 14
Different Binding Modes of SARS-CoV-1 and SARS-CoV-2 Fusion Peptides to Cell Membranes: The Influence of Peptide Helix Length
Hujun Shen, Zhenhua Wu, Ling Chen
The Journal of Physical Chemistry B (2022) Vol. 126, Iss. 23, pp. 4261-4271
Closed Access | Times Cited: 9
How Antibodies Recognize Pathogenic Viruses: Structural Correlates of Antibody Neutralization of HIV-1, SARS-CoV-2, and Zika
Morgan E. Abernathy, Kim-Marie A. Dam, Shannon R. Esswein, et al.
Viruses (2021) Vol. 13, Iss. 10, pp. 2106-2106
Open Access | Times Cited: 11
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