
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 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
Benjamin C. Jennings, Stuart Kornfeld, Balraj Doray
FEBS Letters (2021) Vol. 595, Iss. 13, pp. 1758-1767
Open Access | Times Cited: 27
Showing 1-25 of 27 citing articles:
The glycosylation in SARS-CoV-2 and its receptor ACE2
Yanqiu Gong, Suideng Qin, Lunzhi Dai, et al.
Signal Transduction and Targeted Therapy (2021) Vol. 6, Iss. 1
Open Access | Times Cited: 172
Yanqiu Gong, Suideng Qin, Lunzhi Dai, et al.
Signal Transduction and Targeted Therapy (2021) Vol. 6, Iss. 1
Open Access | Times Cited: 172
COVID-19 Biogenesis and Intracellular Transport
Alexander A. Mirоnоv, M.A. Savin, Galina V. Beznoussenko
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 5, pp. 4523-4523
Open Access | Times Cited: 12
Alexander A. Mirоnоv, M.A. Savin, Galina V. Beznoussenko
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 5, pp. 4523-4523
Open Access | Times Cited: 12
Combinatorial Approach with Mass Spectrometry and Lectin Microarray Dissected Site-Specific Glycostem and Glycoleaf Features of the Virion-Derived Spike Protein of Ancestral and γ Variant SARS-CoV-2 Strains
Takahiro Hiono, Hiroaki Sakaue, Azusa Tomioka, et al.
Journal of Proteome Research (2024) Vol. 23, Iss. 4, pp. 1408-1419
Closed Access | Times Cited: 4
Takahiro Hiono, Hiroaki Sakaue, Azusa Tomioka, et al.
Journal of Proteome Research (2024) Vol. 23, Iss. 4, pp. 1408-1419
Closed Access | Times Cited: 4
Production and cryo-electron microscopy structure of an internally tagged SARS-CoV-2 spike ecto-domain construct
Suruchi Singh, Yi Liu, Meghan C. Burke, et al.
Journal of Structural Biology X (2025) Vol. 11, pp. 100123-100123
Open Access
Suruchi Singh, Yi Liu, Meghan C. Burke, et al.
Journal of Structural Biology X (2025) Vol. 11, pp. 100123-100123
Open Access
Sequences in the Cytoplasmic Tail Contribute to the Intracellular Trafficking and the Cell Surface Localization of SARS-CoV-2 Spike Protein
Evgeniya E. Burkova, Irina A. Bakhno
Biomolecules (2025) Vol. 15, Iss. 2, pp. 280-280
Open Access
Evgeniya E. Burkova, Irina A. Bakhno
Biomolecules (2025) Vol. 15, Iss. 2, pp. 280-280
Open Access
An extended motif in the SARS-CoV-2 spike modulates binding and release of host coatomer in retrograde trafficking
Debajit Dey, Suruchi Singh, S. Khan, et al.
Communications Biology (2022) Vol. 5, Iss. 1
Open Access | Times Cited: 18
Debajit Dey, Suruchi Singh, S. Khan, et al.
Communications Biology (2022) Vol. 5, Iss. 1
Open Access | Times Cited: 18
A single C-terminal residue controls SARS-CoV-2 spike trafficking and incorporation into VLPs
Debajit Dey, Enya Qing, Yanan He, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 9
Debajit Dey, Enya Qing, Yanan He, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 9
Cytoplasmic tail determines the membrane trafficking and localization of SARS-CoV-2 spike protein
Qinlin Li, Yihan Liu, Leiliang Zhang
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 12
Qinlin Li, Yihan Liu, Leiliang Zhang
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 12
Global organelle profiling reveals subcellular localization and remodeling at proteome scale
Marco Y. Hein, Duo Peng, Verina Todorova, et al.
Cell (2024)
Open Access | Times Cited: 2
Marco Y. Hein, Duo Peng, Verina Todorova, et al.
Cell (2024)
Open Access | Times Cited: 2
SARS-CoV-2 Spike Protein Mutation at Cysteine-488 Impairs Its Golgi Localization and Intracellular S1/S2 Processing
Yuichiro Yamamoto, Tetsuya Inoue, Miyu Inoue, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 24, pp. 15834-15834
Open Access | Times Cited: 9
Yuichiro Yamamoto, Tetsuya Inoue, Miyu Inoue, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 24, pp. 15834-15834
Open Access | Times Cited: 9
Gag Virus-like Particles Functionalized with SARS-CoV-2 Variants: Generation, Characterization and Recognition by COVID-19 Convalescent Patients’ Sera
Arnau Boix‐Besora, Francesc Gòdia, Laura Cervera
Vaccines (2023) Vol. 11, Iss. 11, pp. 1641-1641
Open Access | Times Cited: 5
Arnau Boix‐Besora, Francesc Gòdia, Laura Cervera
Vaccines (2023) Vol. 11, Iss. 11, pp. 1641-1641
Open Access | Times Cited: 5
Antigen-display exosomes provide adjuvant-free protection against SARS-CoV-2 disease at nanogram levels of spike protein
Chenxu Guo, Jaiprasath Sachithanandham, William Zhong, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Chenxu Guo, Jaiprasath Sachithanandham, William Zhong, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
COVID-19 pandemic: A multidisciplinary perspective on the pathogenesis of a novel coronavirus from infection, immunity and pathological responses
Jia Yi, Jiameng Miao, Qingwei Zuo, et al.
Frontiers in Immunology (2022) Vol. 13
Open Access | Times Cited: 7
Jia Yi, Jiameng Miao, Qingwei Zuo, et al.
Frontiers in Immunology (2022) Vol. 13
Open Access | Times Cited: 7
Delta-1 variant of SARS-COV-2 acquires spike V1264L and drives the pandemic in Indonesia, Singapore and Malaysia
Xiang‐Jiao Yang
Research Square (Research Square) (2021)
Closed Access | Times Cited: 9
Xiang‐Jiao Yang
Research Square (Research Square) (2021)
Closed Access | Times Cited: 9
A new intracellular targeting motif in the cytoplasmic tail of the spike protein may act as a target to inhibit SARS-CoV-2 assembly
Longbo Hu, Yongjie Tang, Lingling Mei, et al.
Antiviral Research (2022) Vol. 209, pp. 105509-105509
Open Access | Times Cited: 6
Longbo Hu, Yongjie Tang, Lingling Mei, et al.
Antiviral Research (2022) Vol. 209, pp. 105509-105509
Open Access | Times Cited: 6
A single C-terminal residue controls SARS-CoV-2 spike trafficking and virion assembly
Debajit Dey, Enya Qing, Yanan He, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 3
Debajit Dey, Enya Qing, Yanan He, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 3
Strategies for rapid production of crystallization quality coatomer WD40 domains
Debajit Dey, S. Saif Hasan
Protein Expression and Purification (2023) Vol. 212, pp. 106358-106358
Open Access | Times Cited: 3
Debajit Dey, S. Saif Hasan
Protein Expression and Purification (2023) Vol. 212, pp. 106358-106358
Open Access | Times Cited: 3
SARS-Cov-2 Spike Protein Mutation at Cysteine-488 Impairs Its Golgi Localization And Intracellular S1/S2 Processing
Yuichiro Yamamoto, Tetsuya Inoue, Mana Murae, et al.
(2022)
Open Access | Times Cited: 5
Yuichiro Yamamoto, Tetsuya Inoue, Mana Murae, et al.
(2022)
Open Access | Times Cited: 5
Two years into COVID‐19 – Lessons in SARS‐CoV‐2 and a perspective from papers in FEBS Letters
Urs F. Greber
FEBS Letters (2021) Vol. 595, Iss. 23, pp. 2847-2853
Open Access | Times Cited: 5
Urs F. Greber
FEBS Letters (2021) Vol. 595, Iss. 23, pp. 2847-2853
Open Access | Times Cited: 5
δ subvariants of SARS-COV-2 in Israel, Qatar and Bahrain: Optimal vaccination as an effective strategy to block viral evolution and control the pandemic
Xiang‐Jiao Yang
medRxiv (Cold Spring Harbor Laboratory) (2021)
Closed Access | Times Cited: 4
Xiang‐Jiao Yang
medRxiv (Cold Spring Harbor Laboratory) (2021)
Closed Access | Times Cited: 4
Evidence that the SARS-CoV-2 S protein undergoes a conformational change at the Golgi Complex that leads to the formation of virus neutralising antibody binding epitopes in the S1 protein subunit.
Richard J. Sugrue, Boon Huan Tan, Soak Kuan Lai, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Richard J. Sugrue, Boon Huan Tan, Soak Kuan Lai, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Evidence that the SARS-CoV-2 S protein undergoes a conformational change at the Golgi complex that leads to the formation of virus neutralising antibody binding epitopes in the S1 protein subunit
Yanjun Wu, Soak Kuan Lai, Conrad En-Zuo Chan, et al.
Virology (2024) Vol. 598, pp. 110187-110187
Open Access
Yanjun Wu, Soak Kuan Lai, Conrad En-Zuo Chan, et al.
Virology (2024) Vol. 598, pp. 110187-110187
Open Access
SARS-CoV-2 Assembly: Gaining Infectivity and Beyond
Harshita Katiyar, Ariana Arduini, Yi‐Chen Li, et al.
Viruses (2024) Vol. 16, Iss. 11, pp. 1648-1648
Open Access
Harshita Katiyar, Ariana Arduini, Yi‐Chen Li, et al.
Viruses (2024) Vol. 16, Iss. 11, pp. 1648-1648
Open Access
Retro-2 alters Golgi structure
Xihua Yue, Bopil Gim, Lianhui Zhu, et al.
Scientific Reports (2022) Vol. 12, Iss. 1
Open Access | Times Cited: 1
Xihua Yue, Bopil Gim, Lianhui Zhu, et al.
Scientific Reports (2022) Vol. 12, Iss. 1
Open Access | Times Cited: 1
An Extended Motif in the SARS-CoV-2 Spike Modulates Binding and Release of Host Coatomer in Retrograde Trafficking
Debajit Dey, Suruchi Singh, S. Khan, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 1
Debajit Dey, Suruchi Singh, S. Khan, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 1