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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:

Unrestrained poly-ADP-ribosylation provides insights into chromatin regulation and human disease
Evgeniia Prokhorova, Thomas Agnew, Anne R. Wondisford, et al.
Molecular Cell (2021) Vol. 81, Iss. 12, pp. 2640-2655.e8
Open Access | Times Cited: 82

Showing 1-25 of 82 citing articles:

The expanding universe of PARP1-mediated molecular and therapeutic mechanisms
Dan Huang, W. Lee Kraus
Molecular Cell (2022) Vol. 82, Iss. 12, pp. 2315-2334
Open Access | Times Cited: 159
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
CRISPR screens reveal genetic determinants of PARP inhibitor sensitivity and resistance in prostate cancer
Takuya Tsujino, Tomoaki Takai, Kunihiko Hinohara, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 56
HPF1-dependent histone ADP-ribosylation triggers chromatin relaxation to promote the recruitment of repair factors at sites of DNA damage
Rebecca Smith, Siham Zentout, Magdalena B. Rother, et al.
Nature Structural & Molecular Biology (2023) Vol. 30, Iss. 5, pp. 678-691
Open Access | Times Cited: 45
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
DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on protein substrates
Kang Zhu, Marcin J. Suskiewicz, Andrea Hloušek-Kasun, et al.
Science Advances (2022) Vol. 8, Iss. 40
Open Access | Times Cited: 67
HPF1 dynamically controls the PARP1/2 balance between initiating and elongating ADP-ribose modifications
Marie-France Langelier, Ramya Billur, Aleksandr Sverzhinsky, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 56
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
Clinical PARP inhibitors allosterically induce PARP2 retention on DNA
Marie-France Langelier, Xiaohui Lin, Shan Zha, et al.
Science Advances (2023) Vol. 9, Iss. 12
Open Access | Times Cited: 32
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: 25
PARP1 roles in DNA repair and DNA replication: The basi(c)s of PARP inhibitor efficacy and resistance
Petar-Bogomil Kanev, Aleksandar Atemin, Stoyno Stoynov, et al.
Seminars in Oncology (2023) Vol. 51, Iss. 1-2, pp. 2-18
Open Access | Times Cited: 25
ADP-ribose contributions to genome stability and PARP enzyme trapping on sites of DNA damage; paradigm shifts for a coming-of-age modification
Élise Rouleau-Turcotte, John M. Pascal
Journal of Biological Chemistry (2023) Vol. 299, Iss. 12, pp. 105397-105397
Open Access | Times Cited: 25
Preserving ester-linked modifications reveals glutamate and aspartate mono-ADP-ribosylation by PARP1 and its reversal by PARG
Edoardo José Longarini, Ivan Matić
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 16
The logic of protein post‐translational modifications (PTMs): Chemistry, mechanisms and evolution of protein regulation through covalent attachments
Marcin J. Suskiewicz
BioEssays (2024) Vol. 46, Iss. 3
Open Access | Times Cited: 9
Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal
J.G.M. Rack, Qiang Liu, Valentina Zorzini, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 48
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
Tackling PARP inhibitor resistance
Kasper Fugger, Graeme Hewitt, Stephen C. West, et al.
Trends in cancer (2021) Vol. 7, Iss. 12, pp. 1102-1118
Closed Access | Times Cited: 43
Serine ADP-ribosylation in Drosophila provides insights into the evolution of reversible ADP-ribosylation signalling
Pietro Fontana, Sara C. Buch-Larsen, Osamu Suyari, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 19
A molecular toolbox for ADP-ribosyl binding proteins
Sven T. Sowa, Albert Galera‐Prat, Sarah Wazir, et al.
Cell Reports Methods (2021) Vol. 1, Iss. 8, pp. 100121-100121
Open Access | Times Cited: 33
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
Medicinal Chemistry Perspective on Targeting Mono-ADP-Ribosylating PARPs with Small Molecules
Maria Giulia Nizi, Mirko M. Maksimainen, L. Lehtiö, et al.
Journal of Medicinal Chemistry (2022) Vol. 65, Iss. 11, pp. 7532-7560
Open Access | Times Cited: 25
The potential of PARP inhibitors in targeted cancer therapy and immunotherapy
Jaromir Hunia, Karol Gawalski, Aleksandra Szredzka, et al.
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 23
[1,2,4]Triazolo[3,4-b]benzothiazole Scaffold as Versatile Nicotinamide Mimic Allowing Nanomolar Inhibition of Different PARP Enzymes
Sudarshan Murthy, Maria Giulia Nizi, Mirko M. Maksimainen, et al.
Journal of Medicinal Chemistry (2023) Vol. 66, Iss. 2, pp. 1301-1320
Open Access | Times Cited: 15
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
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