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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 Perspective on the Structural and Functional Constraints for Immune Evasion: Insights from Influenza Virus
Nicholas C. Wu, Ian A. Wilson
Journal of Molecular Biology (2017) Vol. 429, Iss. 17, pp. 2694-2709
Open Access | Times Cited: 154

Showing 1-25 of 154 citing articles:

Exploitation of glycosylation in enveloped virus pathobiology
Yasunori Watanabe, Thomas A. Bowden, Ian A. Wilson, et al.
Biochimica et Biophysica Acta (BBA) - General Subjects (2019) Vol. 1863, Iss. 10, pp. 1480-1497
Open Access | Times Cited: 473
A Universal Influenza Vaccine: The Strategic Plan for the National Institute of Allergy and Infectious Diseases
Emily J. Erbelding, Diane J. Post, Erik J. Stemmy, et al.
The Journal of Infectious Diseases (2018) Vol. 218, Iss. 3, pp. 347-354
Open Access | Times Cited: 406
Vulnerabilities in coronavirus glycan shields despite extensive glycosylation
Yasunori Watanabe, Zachary T. Berndsen, Jayna Raghwani, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 364
Next-generation influenza vaccines: opportunities and challenges
Chih‐Jen Wei, Michelle C. Crank, John W. Shiver, et al.
Nature Reviews Drug Discovery (2020) Vol. 19, Iss. 4, pp. 239-252
Open Access | Times Cited: 266
Passive immunotherapy of viral infections: 'super-antibodies' enter the fray
Laura M. Walker, Dennis R. Burton
Nature reviews. Immunology (2018) Vol. 18, Iss. 5, pp. 297-308
Open Access | Times Cited: 258
A Site of Vulnerability on the Influenza Virus Hemagglutinin Head Domain Trimer Interface
Sandhya Bangaru, Shanshan Lang, Michael Schotsaert, et al.
Cell (2019) Vol. 177, Iss. 5, pp. 1136-1152.e18
Open Access | Times Cited: 219
Universal protection against influenza infection by a multidomain antibody to influenza hemagglutinin
Nick S. Laursen, Robert H. Friesen, Xueyong Zhu, et al.
Science (2018) Vol. 362, Iss. 6414, pp. 598-602
Open Access | Times Cited: 197
Antibody responses to viral infections: a structural perspective across three different enveloped viruses
Charles D. Murin, Ian A. Wilson, Andrew B. Ward
Nature Microbiology (2019) Vol. 4, Iss. 5, pp. 734-747
Open Access | Times Cited: 193
Influenza Hemagglutinin Structures and Antibody Recognition
Nicholas C. Wu, Ian A. Wilson
Cold Spring Harbor Perspectives in Medicine (2019) Vol. 10, Iss. 8, pp. a038778-a038778
Open Access | Times Cited: 149
Medicinal Plants and Isolated Molecules Demonstrating Immunomodulation Activity as Potential Alternative Therapies for Viral Diseases Including COVID-19
Hassan A. Alhazmi, Asim Najmi, Sadique A. Javed, et al.
Frontiers in Immunology (2021) Vol. 12
Open Access | Times Cited: 105
Impact of antigenic evolution and original antigenic sin on SARS-CoV-2 immunity
Muriel Aguilar-Bretones, Ron A. M. Fouchier, Marion Koopmans, et al.
Journal of Clinical Investigation (2023) Vol. 133, Iss. 1
Open Access | Times Cited: 81
Co-evolution of immunity and seasonal influenza viruses
Alvin X. Han, Simon P. J. de Jong, Colin A. Russell
Nature Reviews Microbiology (2023) Vol. 21, Iss. 12, pp. 805-817
Closed Access | Times Cited: 42
Activation Dynamics and Immunoglobulin Evolution of Pre-existing and Newly Generated Human Memory B cell Responses to Influenza Hemagglutinin
Sarah F. Andrews, Michael Chambers, Chaim A. Schramm, et al.
Immunity (2019) Vol. 51, Iss. 2, pp. 398-410.e5
Open Access | Times Cited: 123
Mapping person-to-person variation in viral mutations that escape polyclonal serum targeting influenza hemagglutinin
Juhye Lee, Rachel Eguia, Seth J. Zost, et al.
eLife (2019) Vol. 8
Open Access | Times Cited: 119
Persistent Antibody Clonotypes Dominate the Serum Response to Influenza over Multiple Years and Repeated Vaccinations
Jiwon Lee, Philipp Paparoditis, Andrew P. Horton, et al.
Cell Host & Microbe (2019) Vol. 25, Iss. 3, pp. 367-376.e5
Open Access | Times Cited: 111
VH1-69 antiviral broadly neutralizing antibodies: genetics, structures, and relevance to rational vaccine design
Fang Chen, N. Tzarum, Ian A. Wilson, et al.
Current Opinion in Virology (2019) Vol. 34, pp. 149-159
Open Access | Times Cited: 108
Structural insights into the design of novel anti-influenza therapies
Nicholas C. Wu, Ian A. Wilson
Nature Structural & Molecular Biology (2018) Vol. 25, Iss. 2, pp. 115-121
Open Access | Times Cited: 91
Germline-Encoded Affinity for Cognate Antigen Enables Vaccine Amplification of a Human Broadly Neutralizing Response against Influenza Virus
Maya Sangesland, Larance Ronsard, Samuel W. Kazer, et al.
Immunity (2019) Vol. 51, Iss. 4, pp. 735-749.e8
Open Access | Times Cited: 82
Glycosylation is a key in SARS-CoV-2 infection
Celso A. Reis, R Tauber, Véronique Blanchard
Journal of Molecular Medicine (2021) Vol. 99, Iss. 8, pp. 1023-1031
Open Access | Times Cited: 66
C1q enables influenza hemagglutinin stem binding antibodies to block viral attachment and broadens the antibody escape repertoire
Ivan Košík, Jefferson Santos, Mathew Angel, et al.
Science Immunology (2024) Vol. 9, Iss. 93
Closed Access | Times Cited: 8
Age-dependent heterogeneity in the antigenic effects of mutations to influenza hemagglutinin
Frances C. Welsh, Rachel Eguia, Juhye Lee, et al.
Cell Host & Microbe (2024) Vol. 32, Iss. 8, pp. 1397-1411.e11
Open Access | Times Cited: 8
An explainable language model for antibody specificity prediction using curated influenza hemagglutinin antibodies
Yiquan Wang, Huibin Lv, Qi Wen Teo, et al.
Immunity (2024) Vol. 57, Iss. 10, pp. 2453-2465.e7
Open Access | Times Cited: 7
Immunodominance and Antigenic Variation of Influenza Virus Hemagglutinin: Implications for Design of Universal Vaccine Immunogens
Seth J. Zost, Nicholas C. Wu, Scott E. Hensley, et al.
The Journal of Infectious Diseases (2018) Vol. 219, Iss. Supplement_1, pp. S38-S45
Open Access | Times Cited: 80
A complex epistatic network limits the mutational reversibility in the influenza hemagglutinin receptor-binding site
Nicholas C. Wu, Andrew J. Thompson, Jia Xie, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 72
Why Glycosylation Matters in Building a Better Flu Vaccine
Deborah Chang, Joseph Zaia
Molecular & Cellular Proteomics (2019) Vol. 18, Iss. 12, pp. 2348-2358
Open Access | Times Cited: 72
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