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:
Neutralizing antibody 5-7 defines a distinct site of vulnerability in SARS-CoV-2 spike N-terminal domain
Gabriele Cerutti, Yicheng Guo, Pengfei Wang, et al.
Cell Reports (2021) Vol. 37, Iss. 5, pp. 109928-109928
Open Access | Times Cited: 69
Gabriele Cerutti, Yicheng Guo, Pengfei Wang, et al.
Cell Reports (2021) Vol. 37, Iss. 5, pp. 109928-109928
Open Access | Times Cited: 69
Showing 1-25 of 69 citing articles:
Striking antibody evasion manifested by the Omicron variant of SARS-CoV-2
Lihong Liu, Sho Iketani, Yicheng Guo, et al.
Nature (2021) Vol. 602, Iss. 7898, pp. 676-681
Open Access | Times Cited: 1271
Lihong Liu, Sho Iketani, Yicheng Guo, et al.
Nature (2021) Vol. 602, Iss. 7898, pp. 676-681
Open Access | Times Cited: 1271
Antibody evasion by SARS-CoV-2 Omicron subvariants BA.2.12.1, BA.4 and BA.5
Qian Wang, Yicheng Guo, Sho Iketani, et al.
Nature (2022) Vol. 608, Iss. 7923, pp. 603-608
Open Access | Times Cited: 720
Qian Wang, Yicheng Guo, Sho Iketani, et al.
Nature (2022) Vol. 608, Iss. 7923, pp. 603-608
Open Access | Times Cited: 720
Broadly neutralizing antibodies to SARS-CoV-2 and other human coronaviruses
Yanjia Chen, Xiaoyu Zhao, Hao Zhou, et al.
Nature reviews. Immunology (2022) Vol. 23, Iss. 3, pp. 189-199
Open Access | Times Cited: 284
Yanjia Chen, Xiaoyu Zhao, Hao Zhou, et al.
Nature reviews. Immunology (2022) Vol. 23, Iss. 3, pp. 189-199
Open Access | Times Cited: 284
Antibody evasion of SARS-CoV-2 Omicron BA.1, BA.1.1, BA.2, and BA.3 sub-lineages
Jingwen Ai, Xun Wang, Xinyi He, et al.
Cell Host & Microbe (2022) Vol. 30, Iss. 8, pp. 1077-1083.e4
Open Access | Times Cited: 171
Jingwen Ai, Xun Wang, Xinyi He, et al.
Cell Host & Microbe (2022) Vol. 30, Iss. 8, pp. 1077-1083.e4
Open Access | Times Cited: 171
Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529
Tongqing Zhou, Lingshu Wang, John Misasi, et al.
Science (2022) Vol. 376, Iss. 6591
Open Access | Times Cited: 153
Tongqing Zhou, Lingshu Wang, John Misasi, et al.
Science (2022) Vol. 376, Iss. 6591
Open Access | Times Cited: 153
A pseudovirus system enables deep mutational scanning of the full SARS-CoV-2 spike
Bernadeta Dadonaite, Katharine H. D. Crawford, Caelan E. Radford, et al.
Cell (2023) Vol. 186, Iss. 6, pp. 1263-1278.e20
Open Access | Times Cited: 145
Bernadeta Dadonaite, Katharine H. D. Crawford, Caelan E. Radford, et al.
Cell (2023) Vol. 186, Iss. 6, pp. 1263-1278.e20
Open Access | Times Cited: 145
Analysis of memory B cells identifies conserved neutralizing epitopes on the N-terminal domain of variant SARS-Cov-2 spike proteins
Zijun Wang, Frauke Muecksch, Alice Cho, et al.
Immunity (2022) Vol. 55, Iss. 6, pp. 998-1012.e8
Open Access | Times Cited: 133
Zijun Wang, Frauke Muecksch, Alice Cho, et al.
Immunity (2022) Vol. 55, Iss. 6, pp. 998-1012.e8
Open Access | Times Cited: 133
Homologous or heterologous booster of inactivated vaccine reduces SARS-CoV-2 Omicron variant escape from neutralizing antibodies
Xun Wang, Xiaoyu Zhao, Jieyu Song, et al.
Emerging Microbes & Infections (2022) Vol. 11, Iss. 1, pp. 477-481
Open Access | Times Cited: 129
Xun Wang, Xiaoyu Zhao, Jieyu Song, et al.
Emerging Microbes & Infections (2022) Vol. 11, Iss. 1, pp. 477-481
Open Access | Times Cited: 129
Antibody-mediated neutralization of SARS-CoV-2
Henning Gruell, Kanika Vanshylla, Timm Weber, et al.
Immunity (2022) Vol. 55, Iss. 6, pp. 925-944
Open Access | Times Cited: 121
Henning Gruell, Kanika Vanshylla, Timm Weber, et al.
Immunity (2022) Vol. 55, Iss. 6, pp. 925-944
Open Access | Times Cited: 121
Cryo-EM structure of the SARS-CoV-2 Omicron spike
Gabriele Cerutti, Yicheng Guo, Lihong Liu, et al.
Cell Reports (2022) Vol. 38, Iss. 9, pp. 110428-110428
Open Access | Times Cited: 95
Gabriele Cerutti, Yicheng Guo, Lihong Liu, et al.
Cell Reports (2022) Vol. 38, Iss. 9, pp. 110428-110428
Open Access | Times Cited: 95
A structural view of the SARS-CoV-2 virus and its assembly
Nathan Hardenbrook, Peijun Zhang
Current Opinion in Virology (2021) Vol. 52, pp. 123-134
Open Access | Times Cited: 65
Nathan Hardenbrook, Peijun Zhang
Current Opinion in Virology (2021) Vol. 52, pp. 123-134
Open Access | Times Cited: 65
SARS-CoV-2’s Variants of Concern: A Brief Characterization
Aline Miranda Scovino, Elizabeth Chen Dahab, Gustavo Fioravanti Vieira, et al.
Frontiers in Immunology (2022) Vol. 13
Open Access | Times Cited: 55
Aline Miranda Scovino, Elizabeth Chen Dahab, Gustavo Fioravanti Vieira, et al.
Frontiers in Immunology (2022) Vol. 13
Open Access | Times Cited: 55
Diverse array of neutralizing antibodies elicited upon Spike Ferritin Nanoparticle vaccination in rhesus macaques
Rajeshwer S. Sankhala, Kerri G. Lal, Jaime L. Jensen, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 10
Rajeshwer S. Sankhala, Kerri G. Lal, Jaime L. Jensen, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 10
Striking Antibody Evasion Manifested by the Omicron Variant of SARS-CoV-2
Lihong Liu, Sho Iketani, Yicheng Guo, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 54
Lihong Liu, Sho Iketani, Yicheng Guo, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 54
Antibody escape and cryptic cross-domain stabilization in the SARS-CoV-2 Omicron spike protein
Kamyab Javanmardi, Thomas H. Segall-Shapiro, Chia‐Wei Chou, et al.
Cell Host & Microbe (2022) Vol. 30, Iss. 9, pp. 1242-1254.e6
Open Access | Times Cited: 36
Kamyab Javanmardi, Thomas H. Segall-Shapiro, Chia‐Wei Chou, et al.
Cell Host & Microbe (2022) Vol. 30, Iss. 9, pp. 1242-1254.e6
Open Access | Times Cited: 36
Modular Label-Free Electrochemical Biosensor Loading Nature-Inspired Peptide toward the Widespread Use of COVID-19 Antibody Tests
Ana Cristina Honorato de Castro, Ítalo R. S. Bezerra, Aline M. Pascon, et al.
ACS Nano (2022) Vol. 16, Iss. 9, pp. 14239-14253
Closed Access | Times Cited: 34
Ana Cristina Honorato de Castro, Ítalo R. S. Bezerra, Aline M. Pascon, et al.
ACS Nano (2022) Vol. 16, Iss. 9, pp. 14239-14253
Closed Access | Times Cited: 34
Passive Immunotherapy Against SARS-CoV-2: From Plasma-Based Therapy to Single Potent Antibodies in the Race to Stay Ahead of the Variants
William R. Strohl, Zhiqiang Ku, Zhiqiang An, et al.
BioDrugs (2022) Vol. 36, Iss. 3, pp. 231-323
Open Access | Times Cited: 32
William R. Strohl, Zhiqiang Ku, Zhiqiang An, et al.
BioDrugs (2022) Vol. 36, Iss. 3, pp. 231-323
Open Access | Times Cited: 32
Antibody evasion by SARS-CoV-2 Omicron subvariants BA.2.12.1, BA.4, and BA.5
Qian Wang, Yicheng Guo, Sho Iketani, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 32
Qian Wang, Yicheng Guo, Sho Iketani, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 32
An antibody targeting the N-terminal domain of SARS-CoV-2 disrupts the spike trimer
Naveenchandra Suryadevara, Andrea R. Shiakolas, Laura A. VanBlargan, et al.
Journal of Clinical Investigation (2022) Vol. 132, Iss. 11
Open Access | Times Cited: 29
Naveenchandra Suryadevara, Andrea R. Shiakolas, Laura A. VanBlargan, et al.
Journal of Clinical Investigation (2022) Vol. 132, Iss. 11
Open Access | Times Cited: 29
Heme binding to the SARS-CoV-2 spike glycoprotein
Samuel L. Freeman, A. Sofia F. Oliveira, Andrea E. Gallio, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 8, pp. 105014-105014
Open Access | Times Cited: 20
Samuel L. Freeman, A. Sofia F. Oliveira, Andrea E. Gallio, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 8, pp. 105014-105014
Open Access | Times Cited: 20
Antibodies targeting a quaternary site on SARS-CoV-2 spike glycoprotein prevent viral receptor engagement by conformational locking
Lihong Liu, Ryan G. Casner, Yicheng Guo, et al.
Immunity (2023) Vol. 56, Iss. 10, pp. 2442-2455.e8
Open Access | Times Cited: 20
Lihong Liu, Ryan G. Casner, Yicheng Guo, et al.
Immunity (2023) Vol. 56, Iss. 10, pp. 2442-2455.e8
Open Access | Times Cited: 20
Antibody Responses to BNT162b2 Vaccination in Japan: Monitoring Vaccine Efficacy by Measuring IgG Antibodies against the Receptor-Binding Domain of SARS-CoV-2
Hidetsugu Fujigaki, Yasuko Yamamoto, Takenao Koseki, et al.
Microbiology Spectrum (2022) Vol. 10, Iss. 1
Open Access | Times Cited: 28
Hidetsugu Fujigaki, Yasuko Yamamoto, Takenao Koseki, et al.
Microbiology Spectrum (2022) Vol. 10, Iss. 1
Open Access | Times Cited: 28
Arsenal of nanobodies shows broad-spectrum neutralization against SARS-CoV-2 variants of concern in vitro and in vivo in hamster models
Martín A. Rossotti, Henk van Faassen, Anh Tran, et al.
Communications Biology (2022) Vol. 5, Iss. 1
Open Access | Times Cited: 27
Martín A. Rossotti, Henk van Faassen, Anh Tran, et al.
Communications Biology (2022) Vol. 5, Iss. 1
Open Access | Times Cited: 27
Combating the SARS-CoV-2 Omicron (BA.1) and BA.2 with potent bispecific antibodies engineered from non-Omicron neutralizing antibodies
Ying-Dan Wang, Xiang Zhang, Yunping Ma, et al.
Cell Discovery (2022) Vol. 8, Iss. 1
Open Access | Times Cited: 25
Ying-Dan Wang, Xiang Zhang, Yunping Ma, et al.
Cell Discovery (2022) Vol. 8, Iss. 1
Open Access | Times Cited: 25
Molecular probes of spike ectodomain and its subdomains for SARS-CoV-2 variants, Alpha through Omicron
I‐Ting Teng, Alexandra F. Nazzari, Misook Choe, et al.
PLoS ONE (2022) Vol. 17, Iss. 5, pp. e0268767-e0268767
Open Access | Times Cited: 24
I‐Ting Teng, Alexandra F. Nazzari, Misook Choe, et al.
PLoS ONE (2022) Vol. 17, Iss. 5, pp. e0268767-e0268767
Open Access | Times Cited: 24
