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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 Poly(ADP-ribose)-Binding Proteins with Photoaffinity-Based Proteomics
Morgan Dasovich, Morgan Q. Beckett, Scott Bailey, et al.
Journal of the American Chemical Society (2021) Vol. 143, Iss. 8, pp. 3037-3042
Open Access | Times Cited: 63

Showing 1-25 of 63 citing articles:

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
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: 75
Poly(ADP-ribosyl)ation enhances nucleosome dynamics and organizes DNA damage repair components within biomolecular condensates
Michael L. Nosella, Tae Hun Kim, Shuya Kate Huang, et al.
Molecular Cell (2024) Vol. 84, Iss. 3, pp. 429-446.e17
Closed Access | Times Cited: 21
The BRCT domain of PARP1 binds intact DNA and mediates intrastrand transfer
Johannes Rudolph, Uma M. Muthurajan, Megan Palacio, et al.
Molecular Cell (2021) Vol. 81, Iss. 24, pp. 4994-5006.e5
Open Access | Times Cited: 73
Poly(ADP-ribose) drives condensation of FUS via a transient interaction
Kevin Rhine, Morgan Dasovich, Joseph Yoniles, et al.
Molecular Cell (2022) Vol. 82, Iss. 5, pp. 969-985.e11
Open Access | Times Cited: 61
Photoaffinity labelling strategies for mapping the small molecule–protein interactome
Nikolas R. Burton, Philip Kim, Keriann M. Backus
Organic & Biomolecular Chemistry (2021) Vol. 19, Iss. 36, pp. 7792-7809
Open Access | Times Cited: 59
DDX18 prevents R-loop-induced DNA damage and genome instability via PARP-1
Wen-Ling Lin, Jung-Kuei Chen, Xuemei Wen, et al.
Cell Reports (2022) Vol. 40, Iss. 3, pp. 111089-111089
Open Access | Times Cited: 42
Modular antibodies reveal DNA damage-induced mono-ADP-ribosylation as a second wave of PARP1 signaling
Edoardo José Longarini, Helen Dauben, Carolina Locatelli, et al.
Molecular Cell (2023) Vol. 83, Iss. 10, pp. 1743-1760.e11
Open Access | Times Cited: 38
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
PARPs and ADP-ribosylation-mediated biomolecular condensates: determinants, dynamics, and disease implications
Hongrui Liu, Meenakshi Pillai, Anthony K. L. Leung
Trends in Biochemical Sciences (2025)
Closed Access | Times Cited: 1
SERBP1 interacts with PARP1 and is present in PARylation-dependent protein complexes regulating splicing, cell division, and ribosome biogenesis
Kira Breunig, X. Lei, Mauro Montalbano, et al.
eLife (2025) Vol. 13
Open Access | Times Cited: 1
Why structure and chain length matter: on the biological significance underlying the structural heterogeneity of poly(ADP-ribose)
Julia M. Reber, Aswin Mangerich
Nucleic Acids Research (2021) Vol. 49, Iss. 15, pp. 8432-8448
Open Access | Times Cited: 45
Mono-ADP-ribosylation by PARP10 and PARP14 in genome stability
Ashna Dhoonmoon, Claudia M. Nicolae
NAR Cancer (2023) Vol. 5, Iss. 1
Open Access | Times Cited: 18
PAR recognition by PARP1 regulates DNA‐dependent activities and independently stimulates catalytic activity of PARP1
Waghela Deeksha, Suman Abhishek, Eerappa Rajakumara
FEBS Journal (2023) Vol. 290, Iss. 21, pp. 5098-5113
Open Access | Times Cited: 18
Molecular Targeted Therapies in Metastatic Prostate Cancer: Recent Advances and Future Challenges
Carlo Sorrentino, Emma Di Carlo
Cancers (2023) Vol. 15, Iss. 11, pp. 2885-2885
Open Access | Times Cited: 17
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: 40
Regulation of Biomolecular Condensates by Poly(ADP-ribose)
Kevin Rhine, Hana M. Odeh, James Shorter, et al.
Chemical Reviews (2023) Vol. 123, Iss. 14, pp. 9065-9093
Closed Access | Times Cited: 15
DNA repair and anti-cancer mechanisms in the longest-living mammal: the bowhead whale
Denis Firsanov, Max Zacher, Xiao Tian, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 15
Pyruvate Kinase M (PKM) binds ribosomes in a poly-ADP ribosylation dependent manner to induce translational stalling
Nevraj S. Kejiou, Lena Ilan, Stefan Aigner, et al.
Nucleic Acids Research (2023) Vol. 51, Iss. 12, pp. 6461-6478
Open Access | Times Cited: 14
Switch-like compaction of poly(ADP-ribose) upon cation binding
Mohsen Badiee, Adam Kenet, Laura R. Ganser, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 19
Open Access | Times Cited: 13
Cation-induced intramolecular coil-to-globule transition in poly(ADP-ribose)
Tong Wang, Kush Coshic, Mohsen Badiee, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 4
Regulation of stress granule maturation and dynamics by poly(ADP-ribose) interaction with PARP13
Shang-Jung Cheng, Temitope Gafaar, Jijin R. A. Kuttiyatveetil, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Poly-(ADP-ribose) serves as a scaffold for the methyltransferase METTL3/14 complex in the DNA damage response
Claudia Gonzalez-Leal, Jin Cai, Bram A F J de Groot, et al.
Nucleic Acids Research (2025) Vol. 53, Iss. 7
Open Access
Recent advances in the synthesis of poly (ADP-ribose)
Yidan Wu, Tang Li, Qiang Liu
Bioorganic & Medicinal Chemistry (2025) Vol. 125, pp. 118202-118202
Closed Access
Serine ADP-ribosylation in DNA-damage response regulation
Luca Palazzo, Marcin J. Suskiewicz, Ivan Ahel
Current Opinion in Genetics & Development (2021) Vol. 71, pp. 106-113
Open Access | Times Cited: 27
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