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.

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Showing 17 citing articles:

The preference signature of the SARS-CoV-2 Nucleocapsid NTD for its 5’-genomic RNA elements
Sophie Marianne Korn, Karthikeyan Dhamotharan, Cy M. Jeffries, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 28

Phosphorylation in the Ser/Arg-rich region of the nucleocapsid of SARS-CoV-2 regulates phase separation by inhibiting self-association of a distant helix
Hannah Stuwe, Patrick N. Reardon, Zhen Yu, et al.
Journal of Biological Chemistry (2024) Vol. 300, Iss. 6, pp. 107354-107354
Open Access | Times Cited: 10

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

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

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: 5

Characterization of the binding features between SARS-CoV-2 5’-proximal transcripts of genomic RNA and nucleocapsid proteins
Shih-Cheng Chen, Cui-Ting Xu, Chuan-Fu Chang, et al.
RNA Biology (2025) Vol. 22, Iss. 1, pp. 1-16
Open Access

SARS-CoV-2 variant-specific differences in inhibiting the effects of the PKR-activated integrated stress response
Wanda Christ, Jonas Klingström, Janne Tynell
Virus Research (2023) Vol. 339, pp. 199271-199271
Open Access | Times Cited: 4

Condensates of SARS-CoV-2 Nucleoprotein on Viral RNA and Their Small Molecule Modulators (A Review)
Yu. I. Svetlova, Iuliia Pavlova, Andrey V. Aralov, et al.
Russian Journal of Bioorganic Chemistry (2023) Vol. 49, Iss. 5, pp. 917-929
Closed Access | Times Cited: 3

NMR of proteins and nucleic acids
Roger Atkinson
Royal Society of Chemistry eBooks (2023), pp. 200-221
Closed Access | Times Cited: 3

Raman Fingerprints of SARS-CoV-2 Omicron Subvariants: Molecular Roots of Virological Characteristics and Evolutionary Directions
Giuseppe Pezzotti, Eriko Ohgitani, Yuki Fujita, et al.
ACS Infectious Diseases (2023) Vol. 9, Iss. 11, pp. 2226-2251
Open Access | Times Cited: 2

Nuclear Magnetic Resonance Spectroscopy to Study Virus Structure
José L. Neira
Sub-cellular biochemistry/Subcellular biochemistry (2024), pp. 171-206
Closed Access

Involvement of 5' and 3' UTRs on SARS-CoV-2 Genome Packaging
Zhang Zhang, Kun Yang, Fangze Shao, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

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

Condensates of SARS-CoV-2 Nucleoprotein on Viral RNA and Their Small Molecule Modulators
Julia Svetlova, Iu. I. Pavlova, Andrey V. Aralov, et al.
Биоорганическая химия (2023) Vol. 49, Iss. 5, pp. 443-454
Closed Access

SARS-CoV-2 Variant-Specific Differences in Inhibiting the Effects of the PKR-Activated Integrated Stress Response
Wanda Christ, Jonas Klingström, Janne Tynell
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access

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