Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

ADP-ribose and analogues bound to the deMARylating macrodomain from the bat coronavirus HKU4
Robert G. Hammond, Norbert Schormann, Robert Lyle McPherson, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 2
Open Access | Times Cited: 11

Showing 11 citing articles:

The mechanisms of catalysis and ligand binding for the SARS-CoV-2 NSP3 macrodomain from neutron and x-ray diffraction at room temperature
G.J. Correy, Daniel W. Kneller, G.N. Phillips, et al.
Science Advances (2022) Vol. 8, Iss. 21
Open Access | Times Cited: 37
Mutation of a highly conserved isoleucine residue in loop 2 of several š›½-coronavirus macrodomains indicates that enhanced ADP-ribose binding is detrimental to infection
Catherine M. Kerr, Jessica J. Pfannenstiel, Yousef M. Alhammad, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 6
Derivatives of MOPS: promising scaffolds for SARS coronaviruses Macro domainā€targeted inhibition
Oney Ortega Granda, Karine Alvarez, Benjamin Morin, et al.
FEBS Journal (2025)
Open Access
Reversible modification of mitochondrial ADP/ATP translocases by paired Legionella effector proteins
Tomoko Kubori, Junyup Lee, Hyunmin Kim, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 23
Open Access | Times Cited: 17
Mutation of a highly conserved isoleucine residue in loop 2 of several Ī²-coronavirus macrodomains indicates that enhanced ADP-ribose binding is detrimental for replication
Catherine M. Kerr, Jessica J. Pfannenstiel, Yousef M. Alhammad, et al.
Journal of Virology (2024) Vol. 98, Iss. 11
Closed Access | Times Cited: 3
Structure Prediction and Analysis of Hepatitis E Virus Non-Structural Proteins from the Replication and Transcription Machinery by AlphaFold2
Adeline Goulet, Christian Cambillau, Alain Roussel, et al.
Viruses (2022) Vol. 14, Iss. 7, pp. 1537-1537
Open Access | Times Cited: 16
Metabolic Activation of PARP as a SARS-CoV-2 Therapeutic Targetā€”Is It a Bait for the Virus or the Best Deal We Could Ever Make with the Virus? Is AMBICA the Potential Cure?
Prasanth Puthanveetil
Biomolecules (2023) Vol. 13, Iss. 2, pp. 374-374
Open Access | Times Cited: 2
Insights into mechanisms of ubiquitin ADP-ribosylation reversal
Zhengrui Zhang, Chittaranjan Das
Biochemical Society Transactions (2024)
Closed Access
Designing a Light-Induced Glycosylation Reaction for Poststage Synthesis of ADP-2ā€³-Deoxyribosyl Derivatives
Jiaojiao Shen, Gongming Zhu, Yanbo You, et al.
Organic Letters (2023) Vol. 25, Iss. 21, pp. 3961-3966
Closed Access | Times Cited: 1
Identification of a series of pyrrolo-pyrimidine based SARS-CoV-2 Mac1 inhibitors that repress coronavirus replication
Jessica J. Pfannenstiel, Men Thi Hoai Duong, Daniel Cluff, et al.
(2024)
Open Access
The mechanisms of catalysis and ligand binding for the SARS-CoV-2 NSP3 macrodomain from neutron and X-ray diffraction at room temperature
G.J. Correy, Daniel W. Kneller, G.N. Phillips, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 2
Page 1

Scroll to top