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:

How SARS-CoV-2 and Other Viruses Build an Invasion Route to Hijack the Host Nucleocytoplasmic Trafficking System
Elma Sakinatus Sajidah, Keesiang Lim, Richard W. Wong
Cells (2021) Vol. 10, Iss. 6, pp. 1424-1424
Open Access | Times Cited: 26

Showing 1-25 of 26 citing articles:

Impact of SARS-CoV-2 ORF6 and its variant polymorphisms on host responses and viral pathogenesis
Thomas Kehrer, Anastasija Čupić, Chengjin Ye, et al.
Cell Host & Microbe (2023) Vol. 31, Iss. 10, pp. 1668-1684.e12
Open Access | Times Cited: 56

Millisecond dynamic of SARS‐CoV‐2 spike and its interaction with ACE2 receptor and small extracellular vesicles
Keesiang Lim, Goro Nishide, Takeshi Yoshida, et al.
Journal of Extracellular Vesicles (2021) Vol. 10, Iss. 14
Open Access | Times Cited: 46

An Efficient Method for Isolating and Purifying Nuclei from Mice Brain for Single-Molecule Imaging Using High-Speed Atomic Force Microscopy
Yujia Qiu, Elma Sakinatus Sajidah, Sota Kondo, et al.
Cells (2024) Vol. 13, Iss. 3, pp. 279-279
Open Access | Times Cited: 5

NSP9 of SARS-CoV-2 attenuates nuclear transport by hampering nucleoporin 62 dynamics and functions in host cells
Kei Makiyama, Masaharu Hazawa, Akiko Kobayashi, et al.
Biochemical and Biophysical Research Communications (2021) Vol. 586, pp. 137-142
Open Access | Times Cited: 29

SARS-CoV-2 and the Nucleus
Mengqi Chen, Yue Ma, Wakam Chang
International Journal of Biological Sciences (2022) Vol. 18, Iss. 12, pp. 4731-4743
Open Access | Times Cited: 21

Spatiotemporal tracking of small extracellular vesicle nanotopology in response to physicochemical stresses revealed by HS‐AFM
Elma Sakinatus Sajidah, Keesiang Lim, Tomoyoshi Yamano, et al.
Journal of Extracellular Vesicles (2022) Vol. 11, Iss. 11
Open Access | Times Cited: 20

Nanoscopic Assessment of Anti-SARS-CoV-2 Spike Neutralizing Antibody Using High-Speed AFM
Keesiang Lim, Goro Nishide, Elma Sakinatus Sajidah, et al.
Nano Letters (2023) Vol. 23, Iss. 2, pp. 619-628
Open Access | Times Cited: 11

Quantitative comparison of nuclear transport inhibition by SARS coronavirus ORF6 reveals the importance of oligomerization
Tae Yeon Yoo, Timothy J. Mitchison
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 4
Open Access | Times Cited: 4

Impact of SARS-CoV-2 ORF6 and its variant polymorphisms on host responses and viral pathogenesis
Thomas Kehrer, Anastasija Čupić, Chengjin Ye, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 18

Characterization of host substrates of SARS-CoV-2 main protease
Ivonne Melano, Yan-Chung Lo, Wen‐Chi Su
Frontiers in Microbiology (2023) Vol. 14
Open Access | Times Cited: 10

Strategies for the Viral Exploitation of Nuclear Pore Transport Pathways
Xin Zhang, Keesiang Lim, Yujia Qiu, et al.
Viruses (2025) Vol. 17, Iss. 2, pp. 151-151
Open Access

Nanoscopic Elucidation of Spontaneous Self-Assembly of Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) Open Reading Frame 6 (ORF6) Protein
Goro Nishide, Keesiang Lim, M. Tamura, et al.
The Journal of Physical Chemistry Letters (2023) Vol. 14, Iss. 38, pp. 8385-8396
Open Access | Times Cited: 7

Nanoimaging of SARS-CoV-2 viral invasion toward the nucleus and genome
Elma Sakinatus Sajidah, Keesiang Lim, Masaharu Hazawa, et al.
Cell Reports Physical Science (2024) Vol. 5, Iss. 9, pp. 102111-102111
Open Access | Times Cited: 2

New Activities of the Nuclear Pore Complexes
Richard W. Wong
Cells (2021) Vol. 10, Iss. 8, pp. 2123-2123
Open Access | Times Cited: 14

Potential therapeutic landscape of COVID-19: molecular targets, repurposed drugs, and nano- and cell-based intervention
Sarika Tomar, Priyanka Surya, R. Pandey, et al.
Elsevier eBooks (2024), pp. 139-157
Closed Access | Times Cited: 1

Splicing factor SF3B3, a NS5-binding protein, restricts ZIKV infection by targeting GCH1
Tanxiu Chen, Yang Hao, Penghui Liu, et al.
Virologica Sinica (2022) Vol. 38, Iss. 2, pp. 222-232
Open Access | Times Cited: 6

Physical model of the nuclear membrane permeability mechanism
L. A. Minasbekyan, Hamlet Badalyan
Biophysical Reviews (2023) Vol. 15, Iss. 5, pp. 1195-1207
Closed Access | Times Cited: 3

Nuclear export inhibitor Selinexor targeting XPO1 enhances coronavirus replication
Masmudur M. Rahman, Bereket Estifanos, Honor L. Glenn, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 2

Quantification of nuclear transport inhibition by SARS-CoV-2 ORF6 using a broadly applicable live-cell dose-response pipeline
Tae Yeon Yoo, Timothy J. Mitchison
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 4

Unravelling the interaction between Influenza virus and the nuclear pore complex: insights into viral replication and host immune response
Madhu Khanna, Kajal Sharma, Shailendra K. Saxena, et al.
VirusDisease (2024) Vol. 35, Iss. 2, pp. 231-242
Closed Access

Ibetazol, a novel inhibitor of importin β1-mediated nuclear import
Thomas Vercruysse, Els Vanstreels, Maarten Jacquemyn, et al.
Communications Biology (2024) Vol. 7, Iss. 1
Closed Access

Structure–function mapping and mechanistic insights on the SARS CoV2 Nsp1
Bruno A. Salgueiro, Margarida Saramago, Mark D. Tully, et al.
Protein Science (2024) Vol. 33, Iss. 12
Closed Access

Understanding COVID-19 Pathogenesis: A Drug-Repurposing Effort to Disrupt Nsp-1 Binding to Export Machinery Receptor Complex
Sona Vasudevan, James N. Baraniuk
Pathogens (2021) Vol. 10, Iss. 12, pp. 1634-1634
Open Access | Times Cited: 3

Effects of Glutamine Starvation on SHVV Replication by Quantitative Proteomics Analysis
Junlin Liu, Yulei Zhang, Xiaoyan Liu, et al.
Fishes (2022) Vol. 7, Iss. 6, pp. 315-315
Open Access | Times Cited: 1

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