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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:

A novel predicted ADP-ribosyltransferase-like family conserved in eukaryotic evolution
Zbigniew Wyżewski, Marcin Gradowski, Marianna Krysińska, et al.
PeerJ (2021) Vol. 9, pp. e11051-e11051
Open Access | Times Cited: 13

Showing 13 citing articles:

ADP‐ribosyltransferases, an update on function and nomenclature
Bernhard Lüscher, Ivan Ahel, Matthias Altmeyer, et al.
FEBS Journal (2021) Vol. 289, Iss. 23, pp. 7399-7410
Open Access | Times Cited: 238
ADP-ribosylation from molecular mechanisms to therapeutic implications
Marcin J. Suskiewicz, Evgeniia Prokhorova, J.G.M. Rack, et al.
Cell (2023) Vol. 186, Iss. 21, pp. 4475-4495
Open Access | Times Cited: 72
Updated protein domain annotation of the PARP protein family sheds new light on biological function
Marcin J. Suskiewicz, Deeksha Munnur, Øyvind Strømland, et al.
Nucleic Acids Research (2023) Vol. 51, Iss. 15, pp. 8217-8236
Open Access | Times Cited: 35
Uncovering the Invisible: Mono-ADP-ribosylation Moved into the Spotlight
Ann-Katrin Hopp, Michael O. Hottiger
Cells (2021) Vol. 10, Iss. 3, pp. 680-680
Open Access | Times Cited: 28
ADP-Ribosylation Post-Translational Modification: An Overview with a Focus on RNA Biology and New Pharmacological Perspectives
Giuseppe Manco, Giuseppina Lacerra, Elena Porzio, et al.
Biomolecules (2022) Vol. 12, Iss. 3, pp. 443-443
Open Access | Times Cited: 21
Docking and Dynamics Studies: Identifying the Binding Ability of Quercetin Analogs to the ADP-Ribose Phosphatase of SARS CoV-2
Arfan Arfan
Jurnal Kartika Kimia (2023) Vol. 5, Iss. 2
Open Access | Times Cited: 10
Conserved islands of divergence associated with adaptive variation in sockeye salmon are maintained by multiple mechanisms
Peter T. Euclide, Wesley A. Larson, Yue Shi, et al.
Molecular Ecology (2023) Vol. 33, Iss. 24
Open Access | Times Cited: 10
Bid Protein: A Participant in the Apoptotic Network with Roles in Viral Infections
Zbigniew Wyżewski, Karolina P. Gregorczyk-Zboroch, Matylda Barbara Mielcarska, et al.
International Journal of Molecular Sciences (2025) Vol. 26, Iss. 6, pp. 2385-2385
Open Access
Emerging functions of pseudoenzymes
Timea Goldberg, Anju Sreelatha
Biochemical Journal (2023) Vol. 480, Iss. 10, pp. 715-728
Open Access | Times Cited: 9
Functional roles of ADP-ribosylation writers, readers and erasers
Ping Li, Yushuang Lei, Qi Jia, et al.
Frontiers in Cell and Developmental Biology (2022) Vol. 10
Open Access | Times Cited: 12
LRRC46 Accumulates at the Midpiece of Sperm Flagella and Is Essential for Spermiogenesis and Male Fertility in Mouse
Yingying Yin, Wenyu Mu, Xiaochen Yu, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 15, pp. 8525-8525
Open Access | Times Cited: 11
ADP-Ribosylation as Post-Translational Modification of Proteins: Use of Inhibitors in Cancer Control
Palmiro Poltronieri, Masanao Miwa, Mitsuko Masutani
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 19, pp. 10829-10829
Open Access | Times Cited: 11
A survey of ADP-ribosyltransferase families in the pathogenicLegionella
Marianna Krysińska, Marcin Gradowski, Bartosz Baranowski, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
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