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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:

Specificity of reversible ADP-ribosylation and regulation of cellular processes
Kerryanne Crawford, Juán José Bonfiglio, Andreja Mikoč, et al.
Critical Reviews in Biochemistry and Molecular Biology (2017) Vol. 53, Iss. 1, pp. 64-82
Closed Access | Times Cited: 91

Showing 1-25 of 91 citing articles:

Structural insights into SARS-CoV-2 proteins
Rimanshee Arya, Shweta Kumari, Bharati Pandey, et al.
Journal of Molecular Biology (2020) Vol. 433, Iss. 2, pp. 166725-166725
Open Access | Times Cited: 317
Programmed necrotic cell death of macrophages: Focus on pyroptosis, necroptosis, and parthanatos
Nirmal Robinson, Raja Ganesan, Csaba Hegedűs, et al.
Redox Biology (2019) Vol. 26, pp. 101239-101239
Open Access | Times Cited: 300
Niacin in the Central Nervous System: An Update of Biological Aspects and Clinical Applications
Valeria Gasperi, Matteo Sibilano, Isabella Savini, et al.
International Journal of Molecular Sciences (2019) Vol. 20, Iss. 4, pp. 974-974
Open Access | Times Cited: 219
HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation
Marcin J. Suskiewicz, Florian Zobel, T.E.H. Ogden, et al.
Nature (2020) Vol. 579, Iss. 7800, pp. 598-602
Open Access | Times Cited: 217
Serine is the major residue for ADP-ribosylation upon DNA damage
Luca Palazzo, Orsolya Leidecker, Evgeniia Prokhorova, et al.
eLife (2018) Vol. 7
Open Access | Times Cited: 207
PARP family enzymes: regulation and catalysis of the poly(ADP-ribose) posttranslational modification
Marie-France Langelier, Travis Eisemann, Amanda A. Riccio, et al.
Current Opinion in Structural Biology (2018) Vol. 53, pp. 187-198
Open Access | Times Cited: 163
(ADP-ribosyl)hydrolases: structure, function, and biology
J.G.M. Rack, Luca Palazzo, Ivan Ahel
Genes & Development (2020) Vol. 34, Iss. 5-6, pp. 263-284
Open Access | Times Cited: 159
Inhibitors of PARP: Number crunching and structure gazing
Johannes Rudolph, Karen Jung, Karolin Luger
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 11
Open Access | Times Cited: 85
Transcription–replication conflicts underlie sensitivity to PARP inhibitors
Michalis Petropoulos, Angeliki Karamichali, Giacomo G. Rossetti, et al.
Nature (2024) Vol. 628, Iss. 8007, pp. 433-441
Open Access | Times Cited: 58
Reversible ADP-ribosylation of RNA
Deeksha Munnur, Edward Bartlett, Petra Mikolčević, et al.
Nucleic Acids Research (2019) Vol. 47, Iss. 11, pp. 5658-5669
Open Access | Times Cited: 134
Crystal structures of SARS-CoV-2 ADP-ribose phosphatase: from the apo form to ligand complexes
K. Michalska, Youngchang Kim, R. Jedrzejczak, et al.
IUCrJ (2020) Vol. 7, Iss. 5, pp. 814-824
Open Access | Times Cited: 123
ADP-ribosylation signalling and human disease
Luca Palazzo, Petra Mikolčević, Andreja Mikoč, et al.
Open Biology (2019) Vol. 9, Iss. 4
Open Access | Times Cited: 92
Interplay of Histone Marks with Serine ADP-Ribosylation
Edward Bartlett, Juán José Bonfiglio, Evgeniia Prokhorova, et al.
Cell Reports (2018) Vol. 24, Iss. 13, pp. 3488-3502.e5
Open Access | Times Cited: 91
Parthanatos and its associated components: Promising therapeutic targets for cancer
Yunxiang Zhou, Lihong Liu, Sifeng Tao, et al.
Pharmacological Research (2020) Vol. 163, pp. 105299-105299
Closed Access | Times Cited: 90
An HPF1/PARP1-Based Chemical Biology Strategy for Exploring ADP-Ribosylation
Juán José Bonfiglio, Orsolya Leidecker, Helen Dauben, et al.
Cell (2020) Vol. 183, Iss. 4, pp. 1086-1102.e23
Open Access | Times Cited: 90
Poly(ADP-ribose) polymerase enzymes and the maintenance of genome integrity
Travis Eisemann, John M. Pascal
Cellular and Molecular Life Sciences (2019) Vol. 77, Iss. 1, pp. 19-33
Open Access | Times Cited: 89
The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome
Ivo A. Hendriks, Sara C. Buch-Larsen, Evgeniia Prokhorova, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 81
ADP-ribosylation of DNA and RNA
Joséphine Groslambert, Evgeniia Prokhorova, Ivan Ahel
DNA repair (2021) Vol. 105, pp. 103144-103144
Open Access | Times Cited: 79
Viral macrodomains: a structural and evolutionary assessment of the pharmacological potential
J.G.M. Rack, Valentina Zorzini, Zihan Zhu, et al.
Open Biology (2020) Vol. 10, Iss. 11
Open Access | Times Cited: 77
ADP-ribosylation of RNA and DNA: fromin vitrocharacterization toin vivofunction
Lisa Weixler, Katja Schäringer, Jeffrey Momoh, et al.
Nucleic Acids Research (2021) Vol. 49, Iss. 7, pp. 3634-3650
Open Access | Times Cited: 68
HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones
Fa-Hui Sun, Peng Zhao, Nan Zhang, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 66
Parthanatos: Mechanisms, modulation, and therapeutic prospects in neurodegenerative disease and stroke
Yang Liu, Lauren Guttman, Valina L. Dawson, et al.
Biochemical Pharmacology (2024) Vol. 228, pp. 116174-116174
Closed Access | Times Cited: 12
Engineering Af1521 improves ADP-ribose binding and identification of ADP-ribosylated proteins
Kathrin Nowak, Florian Rosenthal, T. Karlberg, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 67
(ADP-ribosyl)hydrolases: Structural Basis for Differential Substrate Recognition and Inhibition
J.G.M. Rack, A. Ariza, Bryon Drown, et al.
Cell chemical biology (2018) Vol. 25, Iss. 12, pp. 1533-1546.e12
Open Access | Times Cited: 63
Progress and outlook in studying the substrate specificities of PARPs and related enzymes
Marcin J. Suskiewicz, Luca Palazzo, R. J. M. Hughes, et al.
FEBS Journal (2020) Vol. 288, Iss. 7, pp. 2131-2142
Open Access | Times Cited: 52
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