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:

Fusion Peptide of SARS-CoV-2 Spike Rearranges into a Wedge Inserted in Bilayered Micelles
Rama K. Koppisetti, Yan G. Fulcher, Steven R. Van Doren
Journal of the American Chemical Society (2021) Vol. 143, Iss. 33, pp. 13205-13211
Open Access | Times Cited: 69

Showing 1-25 of 69 citing articles:

Mutations and Evolution of the SARS-CoV-2 Spike Protein
Nicholas Magazine, Tianyi Zhang, Yingying Wu, et al.
Viruses (2022) Vol. 14, Iss. 3, pp. 640-640
Open Access | Times Cited: 191

SARS-CoV-2 evolved variants optimize binding to cellular glycocalyx
Sang Hoon Kim, Fiona L. Kearns, Mia A. Rosenfeld, et al.
Cell Reports Physical Science (2023) Vol. 4, Iss. 4, pp. 101346-101346
Open Access | Times Cited: 43

An overview on nanoparticle-based strategies to fight viral infections with a focus on COVID-19
Saman Yasamineh, Hesam Ghafouri Kalajahi, Pooneh Yasamineh, et al.
Journal of Nanobiotechnology (2022) Vol. 20, Iss. 1
Open Access | Times Cited: 62

High-throughput identification of prefusion-stabilizing mutations in SARS-CoV-2 spike
Timothy J.C. Tan, Zongjun Mou, Ruipeng Lei, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 24

Lassa virus glycoprotein complex review: insights into its unique fusion machinery
Hallie N. Pennington, Jinwoo Lee
Bioscience Reports (2022) Vol. 42, Iss. 2
Open Access | Times Cited: 29

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: 16

Mutation N856K in spike reduces fusogenicity and infectivity of Omicron BA.1
Chunyun Sun, Huiyu Wang, Ji Yang, et al.
Signal Transduction and Targeted Therapy (2023) Vol. 8, Iss. 1
Open Access | Times Cited: 15

Inhibition of Cell Motility by Cell-Penetrating Dynamic Covalent Cascade Exchangers: Integrins Participate in Thiol-Mediated Uptake
Filipe Coelho, Saidbakhrom Saidjalolov, Dimitri Moreau, et al.
JACS Au (2023) Vol. 3, Iss. 4, pp. 1010-1016
Open Access | Times Cited: 15

Functional and antigenic characterization of SARS-CoV-2 spike fusion peptide by deep mutational scanning
Ruipeng Lei, Enya Qing, Abby Odle, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 6

Intrinsically Disordered Proteins: Perspective on COVID-19 Infection and Drug Discovery
Rumiana Tenchov, Qiongqiong Angela Zhou
ACS Infectious Diseases (2022) Vol. 8, Iss. 3, pp. 422-432
Open Access | Times Cited: 22

Antibody-mediated immunity to SARS-CoV-2 spike
John M. Errico, Lucas J. Adams, Daved H. Fremont
Advances in immunology (2022), pp. 1-69
Open Access | Times Cited: 21

Membrane cholesterol regulates the oligomerization and fusogenicity of SARS-CoV fusion peptide: implications in viral entry
Geetanjali Meher, Surajit Bhattacharjya, Hirak Chakraborty
Physical Chemistry Chemical Physics (2023) Vol. 25, Iss. 11, pp. 7815-7824
Open Access | Times Cited: 11

Cyclic Thiosulfonates for Thiol-Mediated Uptake: Cascade Exchangers, Transporters, Inhibitors
Takehiro Kato, Bumhee Lim, Yangyang Cheng, et al.
JACS Au (2022) Vol. 2, Iss. 4, pp. 839-852
Open Access | Times Cited: 19

Exploring the pH dependence of the SARS‐CoV‐2 complete fusion domain and the role of its unique structural features
Daniel Birtles, Anna E. Oh, Jinwoo Lee
Protein Science (2022) Vol. 31, Iss. 9
Open Access | Times Cited: 19

Structural understanding of SARS-CoV-2 virus entry to host cells
Kim Le, Shrute Kannappan, Truc Kim, et al.
Frontiers in Molecular Biosciences (2023) Vol. 10
Open Access | Times Cited: 10

Probing SARS-CoV-2 membrane binding peptide via single-molecule AFM-based force spectroscopy
Qingrong Zhang, Ricardo de Souza Rosa, Ankita Ray, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access

SARS-CoV-2 FP1 Destabilizes Lipid Membranes and Facilitates Pore Formation
Maria Sumarokova, Rais Pavlov, Tatiana Lavushchenko, et al.
International Journal of Molecular Sciences (2025) Vol. 26, Iss. 2, pp. 686-686
Open Access

Targeting the early life stages of SARS-CoV-2 using a multi-peptide conjugate vaccine
Lauren Myburgh, Haiko Karsjens, Athanasios Blanas, et al.
Vaccine (2025) Vol. 54, pp. 126989-126989
Open Access

Cholesterol and Ceramide Facilitate Membrane Fusion Mediated by the Fusion Peptide of the SARS-CoV-2 Spike Protein
Kristina Niort, Julia Dancourt, Erwan Boedec, et al.
ACS Omega (2023) Vol. 8, Iss. 36, pp. 32729-32739
Open Access | Times Cited: 9

Interaction of SARS-CoV-2 with host cells and antibodies: experiment and simulation
Hung Van Nguyen, Hoang Linh Nguyen, Pham Dang Lan, et al.
Chemical Society Reviews (2023) Vol. 52, Iss. 18, pp. 6497-6553
Closed Access | Times Cited: 9

A novel bispecific antibody dual-targeting approach for enhanced neutralization against fast-evolving SARS-CoV-2 variants
Ji Woong Kim, Hyun Jung Kim, Kyun Heo, et al.
Frontiers in Immunology (2023) Vol. 14
Open Access | Times Cited: 9

Circularized fluorescent nanodiscs for probing protein–lipid interactions
Qian Ren, Shanwen Zhang, Huan Bao
Communications Biology (2022) Vol. 5, Iss. 1
Open Access | Times Cited: 14

Progressive membrane-binding mechanism of SARS-CoV-2 variant spike proteins
Michael Overduin, Troy A. Kervin, Anh Tran
iScience (2022) Vol. 25, Iss. 8, pp. 104722-104722
Open Access | Times Cited: 13

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