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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:

Identifying Family-Member-Specific Targets of Mono-ARTDs by Using a Chemical Genetics Approach
Ian Carter-O’Connell, Haihong Jin, Rory K. Morgan, et al.
Cell Reports (2016) Vol. 14, Iss. 3, pp. 621-631
Open Access | Times Cited: 79

Showing 1-25 of 79 citing articles:

PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes
Rebecca Gupte, Ziying Liu, W. Lee Kraus
Genes & Development (2017) Vol. 31, Iss. 2, pp. 101-126
Open Access | Times Cited: 618
Chemical genetic discovery of PARP targets reveals a role for PARP-1 in transcription elongation
Bryan A. Gibson, Yajie Zhang, Hong Jiang, et al.
Science (2016) Vol. 353, Iss. 6294, pp. 45-50
Open Access | Times Cited: 341
Insights into the biogenesis, function, and regulation of ADP-ribosylation
Michael S. Cohen, Paul Chang
Nature Chemical Biology (2018) Vol. 14, Iss. 3, pp. 236-243
Open Access | Times Cited: 272
ADP-Ribosylation, a Multifaceted Posttranslational Modification Involved in the Control of Cell Physiology in Health and Disease
Bernhard Lüscher, Mareike Bütepage, Laura Eckei, et al.
Chemical Reviews (2017) Vol. 118, Iss. 3, pp. 1092-1136
Closed Access | Times Cited: 224
(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
Parps in immune response: Potential targets for cancer immunotherapy
S Wang, Jingling Huang, T. X. Zeng, et al.
Biochemical Pharmacology (2025) Vol. 234, pp. 116803-116803
Closed Access | Times Cited: 2
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
ADP‐ribosylation: new facets of an ancient modification
Luca Palazzo, Andreja Mikoč, Ivan Ahel
FEBS Journal (2017) Vol. 284, Iss. 18, pp. 2932-2946
Open Access | Times Cited: 129
Body Temperature Measurements for Metabolic Phenotyping in Mice
Carola W. Meyer, Youichirou Ootsuka, Andrej A. Romanovsky
Frontiers in Physiology (2017) Vol. 8
Open Access | Times Cited: 109
PARPs in lipid metabolism and related diseases
Magdolna Szántó, Rebecca Gupte, W. Lee Kraus, et al.
Progress in Lipid Research (2021) Vol. 84, pp. 101117-101117
Open Access | Times Cited: 102
PARP1-produced poly-ADP-ribose causes the PARP12 translocation to stress granules and impairment of Golgi complex functions
Giuliana Catara, Giovanna Grimaldi, Laura Schembri, et al.
Scientific Reports (2017) Vol. 7, Iss. 1
Open Access | Times Cited: 93
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
Interplay between compartmentalized NAD+ synthesis and consumption: a focus on the PARP family
Michael S. Cohen
Genes & Development (2020) Vol. 34, Iss. 5-6, pp. 254-262
Open Access | Times Cited: 77
Chemical genetics and proteome-wide site mapping reveal cysteine MARylation by PARP-7 on immune-relevant protein targets
Kelsie M. Rodriguez, Sara C. Buch-Larsen, Ilsa T. Kirby, et al.
eLife (2021) Vol. 10
Open Access | Times Cited: 63
System-wide identification and prioritization of enzyme substrates by thermal analysis
Amir Ata Saei, Christian M. Beusch, Pierre Sabatier, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 63
PARPs and ADP-ribosylation: Deciphering the complexity with molecular tools
Morgan Dasovich, Anthony K. L. Leung
Molecular Cell (2023) Vol. 83, Iss. 10, pp. 1552-1572
Open Access | Times Cited: 34
A Poly-ADP-Ribose Trigger Releases the Auto-Inhibition of a Chromatin Remodeling Oncogene
Hari Singh, Aurelio Pio Nardozza, Ingvar R. Möller, et al.
Molecular Cell (2017) Vol. 68, Iss. 5, pp. 860-871.e7
Open Access | Times Cited: 82
New directions in poly(ADP‐ribose) polymerase biology
Florian J. Bock, Paul Chang
FEBS Journal (2016) Vol. 283, Iss. 22, pp. 4017-4031
Open Access | Times Cited: 77
The Bump-and-Hole Tactic: Expanding the Scope of Chemical Genetics
Kabirul Islam
Cell chemical biology (2018) Vol. 25, Iss. 10, pp. 1171-1184
Open Access | Times Cited: 76
The PARP Enzyme Family and the Hallmarks of Cancer Part 1. Cell Intrinsic Hallmarks
Máté Á. Demény, László Virág
Cancers (2021) Vol. 13, Iss. 9, pp. 2042-2042
Open Access | Times Cited: 53
ADPriboDB: The database of ADP-ribosylated proteins
Christina A. Vivelo, Ricky Wat, Charul Agrawal, et al.
Nucleic Acids Research (2016) Vol. 45, Iss. D1, pp. D204-D209
Open Access | Times Cited: 60
PARPs in genome stability and signal transduction: implications for cancer therapy
Luca Palazzo, Ivan Ahel
Biochemical Society Transactions (2018) Vol. 46, Iss. 6, pp. 1681-1695
Open Access | Times Cited: 59
A Potent and Selective PARP11 Inhibitor Suggests Coupling between Cellular Localization and Catalytic Activity
Ilsa T. Kirby, Ana Kojic, Moriah R. Arnold, et al.
Cell chemical biology (2018) Vol. 25, Iss. 12, pp. 1547-1553.e12
Open Access | Times Cited: 57
In vivo vizualisation of mono-ADP-ribosylation by dPARP16 upon amino-acid starvation
Angelica Aguilera-Gomez, Marinke M. van Oorschot, Tineke Veenendaal, et al.
eLife (2016) Vol. 5
Open Access | Times Cited: 56
Combining Chemical Genetics with Proximity-Dependent Labeling Reveals Cellular Targets of Poly(ADP-ribose) Polymerase 14 (PARP14)
Ian Carter-O’Connell, Anke Vermehren‐Schmaedick, Haihong Jin, et al.
ACS Chemical Biology (2018) Vol. 13, Iss. 10, pp. 2841-2848
Closed Access | Times Cited: 56
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