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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:

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

Showing 1-25 of 92 citing articles:

Click Chemistry in Proteomic Investigations
Christopher G. Parker, Matthew R. Pratt
Cell (2020) Vol. 180, Iss. 4, pp. 605-632
Open Access | Times Cited: 294
Multifaceted Role of PARP-1 in DNA Repair and Inflammation: Pathological and Therapeutic Implications in Cancer and Non-Cancer Diseases
Simonetta Pazzaglia, Claudio Pioli
Cells (2019) Vol. 9, Iss. 1, pp. 41-41
Open Access | Times Cited: 170
Fragment binding to the Nsp3 macrodomain of SARS-CoV-2 identified through crystallographic screening and computational docking
M. Schuller, G.J. Correy, Stefan Gahbauer, et al.
Science Advances (2021) Vol. 7, Iss. 16
Open Access | Times Cited: 161
Mechanistic Basis and Clinical Evidence for the Applications of Nicotinamide (Niacinamide) to Control Skin Aging and Pigmentation
Yong Chool Boo
Antioxidants (2021) Vol. 10, Iss. 8, pp. 1315-1315
Open Access | Times Cited: 116
Targeting protein modifications in metabolic diseases: molecular mechanisms and targeted therapies
Xiumei Wu, Mengyun Xu, M. Geng, et al.
Signal Transduction and Targeted Therapy (2023) Vol. 8, Iss. 1
Open Access | Times Cited: 96
Recombinant protein expression: Challenges in production and folding related matters
Azadeh Beygmoradi, Ahmad Homaei, Roohullah Hemmati, et al.
International Journal of Biological Macromolecules (2023) Vol. 233, pp. 123407-123407
Closed Access | Times Cited: 48
Molecular basis for the reversible ADP-ribosylation of guanosine bases
M. Schuller, Roberto Raggiaschi, Petra Mikolčević, et al.
Molecular Cell (2023) Vol. 83, Iss. 13, pp. 2303-2315.e6
Open Access | Times Cited: 28
Chemoenzymatic and Synthetic Approaches To Investigate Aspartate- and Glutamate-ADP-Ribosylation
Kyuto Tashiro, Sven Wijngaarden, Jugal Mohapatra, et al.
Journal of the American Chemical Society (2023) Vol. 145, Iss. 25, pp. 14000-14009
Open Access | Times Cited: 24
Biallelic Mutations in ADPRHL2, Encoding ADP-Ribosylhydrolase 3, Lead to a Degenerative Pediatric Stress-Induced Epileptic Ataxia Syndrome
Shereen G. Ghosh, Kerstin Becker, He Huang, et al.
The American Journal of Human Genetics (2018) Vol. 103, Iss. 3, pp. 431-439
Open Access | Times Cited: 77
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
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
The Conserved Macrodomain Is a Potential Therapeutic Target for Coronaviruses and Alphaviruses
Anthony K. L. Leung, Diane E. Griffin, Jürgen Bosch, et al.
Pathogens (2022) Vol. 11, Iss. 1, pp. 94-94
Open Access | Times Cited: 32
The KU-PARP14 axis differentially regulates DNA resection at stalled replication forks by MRE11 and EXO1
Ashna Dhoonmoon, Claudia M. Nicolae, George‐Lucian Moldovan
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 30
Synthesis of ADP-Ribosylated Histones Reveals Site-Specific Impacts on Chromatin Structure and Function
Nir Hananya, Sara K. Daley, John D. Bagert, et al.
Journal of the American Chemical Society (2021) Vol. 143, Iss. 29, pp. 10847-10852
Closed Access | Times Cited: 39
Reading ADP-ribosylation signaling using chemical biology and interaction proteomics
Katarzyna W. Kliza, Qiang Liu, Laura W.M. Roosenboom, et al.
Molecular Cell (2021) Vol. 81, Iss. 21, pp. 4552-4567.e8
Open Access | Times Cited: 38
Beyond protein modification: the rise of non-canonical ADP-ribosylation
M. Schuller, Ivan Ahel
Biochemical Journal (2022) Vol. 479, Iss. 4, pp. 463-477
Open Access | Times Cited: 27
Structural basis of tankyrase activation by polymerization
Nisha Pillay, Laura Mariotti, Mariola Zaleska, et al.
Nature (2022) Vol. 612, Iss. 7938, pp. 162-169
Open Access | Times Cited: 23
Discovery and Development Strategies for SARS-CoV-2 NSP3 Macrodomain Inhibitors
M. Schuller, Tryfon Zarganes‐Tzitzikas, James M. Bennett, et al.
Pathogens (2023) Vol. 12, Iss. 2, pp. 324-324
Open Access | Times Cited: 14
1H, 13C and 15N chemical shift assignments of Rubella virus macro domain in the free and in the ADPr bound state
Danai Moschidi, Nikolaos K. Fourkiotis, Christos Sideras-Bisdekis, et al.
Biomolecular NMR Assignments (2025)
Open Access
Epigenetic deregulation in cancer: Enzyme players and non-coding RNAs
Ammad Ahmad Farooqı, Sundas Fayyaz, Palmiro Poltronieri, et al.
Seminars in Cancer Biology (2020) Vol. 83, pp. 197-207
Open Access | Times Cited: 38
On the Need to Tell Apart Fraternal Twins eEF1A1 and eEF1A2, and Their Respective Outfits
Alberto Mills, Federico Gago
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 13, pp. 6973-6973
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
Design, synthesis and evaluation of inhibitors of the SARS-CoV-2 nsp3 macrodomain
Lavinia M. Sherrill, Elva E. Joya, AnnMarie Walker, et al.
Bioorganic & Medicinal Chemistry (2022) Vol. 67, pp. 116788-116788
Open Access | Times Cited: 20
dELTA-MS: A Mass Spectrometry-Based Proteomics Approach for Identifying ADP-Ribosylation Sites and Forms
Isabel Uribe, Emily Zahn, Richard Searfoss, et al.
Journal of Proteome Research (2025)
Closed Access
Posttranslational Modification in Bone Homeostasis and Osteoporosis
Yuzhe Lin, Shide Jiang, Yuming Yao, et al.
MedComm (2025) Vol. 6, Iss. 4
Open Access
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