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:
Molecular insight into the specific interactions of the SARS‐Coronavirus ‐2 nucleocapsid with RNA and host protein
Eunjeong Lee, Jasmina S. Redzic, Anthony J. Saviola, et al.
Protein Science (2023) Vol. 32, Iss. 4
Open Access | Times Cited: 8
Eunjeong Lee, Jasmina S. Redzic, Anthony J. Saviola, et al.
Protein Science (2023) Vol. 32, Iss. 4
Open Access | Times Cited: 8
Showing 8 citing articles:
A specific phosphorylation-dependent conformational switch of SARS-CoV-2 nucleoprotein inhibits RNA binding
Maiia Botova, Aldo R. Camacho‐Zarco, Jacqueline Tognetti, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 6
Maiia Botova, Aldo R. Camacho‐Zarco, Jacqueline Tognetti, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 6
RNA structure and multiple weak interactions balance the interplay between RNA binding and phase separation of SARS-CoV-2 nucleocapsid
Aidan Estelle, Heather M. Forsythe, Zhentao Yu, et al.
PNAS Nexus (2023) Vol. 2, Iss. 10
Open Access | Times Cited: 13
Aidan Estelle, Heather M. Forsythe, Zhentao Yu, et al.
PNAS Nexus (2023) Vol. 2, Iss. 10
Open Access | Times Cited: 13
A specific phosphorylation-dependent conformational switch in SARS-CoV-2 nucleocapsid protein inhibits RNA binding
Maiia Botova, Aldo R. Camacho‐Zarco, Jacqueline Tognetti, et al.
Science Advances (2024) Vol. 10, Iss. 31
Open Access | Times Cited: 4
Maiia Botova, Aldo R. Camacho‐Zarco, Jacqueline Tognetti, et al.
Science Advances (2024) Vol. 10, Iss. 31
Open Access | Times Cited: 4
The immune-evasive proline-283 substitution in influenza nucleoprotein increases aggregation propensity without altering the native structure
Jimin Yoon, Yu Meng Zhang, Cheenou Her, et al.
Science Advances (2024) Vol. 10, Iss. 16
Open Access | Times Cited: 1
Jimin Yoon, Yu Meng Zhang, Cheenou Her, et al.
Science Advances (2024) Vol. 10, Iss. 16
Open Access | Times Cited: 1
Evolutionary Adaptations in Biliverdin Reductase B: Insights into Coenzyme Dynamics and Catalytic Efficiency
Eunjeong Lee, Jasmina S. Redzic, Elan Eisenmesser
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 24, pp. 13233-13233
Open Access
Eunjeong Lee, Jasmina S. Redzic, Elan Eisenmesser
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 24, pp. 13233-13233
Open Access
The Immune-Evasive Proline 283 Substitution in Influenza Nucleoprotein Increases Aggregation Propensity Without Altering the Native Structure
Jimin Yoon, Yu Meng Zhang, Cheenou Her, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 1
Jimin Yoon, Yu Meng Zhang, Cheenou Her, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 1
RNA structure and multiple weak interactions balance the interplay between RNA binding and phase separation of SARS-CoV-2 nucleocapsid
Aidan Estelle, Heather M. Forsythe, Zhen Yu, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
Aidan Estelle, Heather M. Forsythe, Zhen Yu, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
