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:

HPF1 and nucleosomes mediate a dramatic switch in activity of PARP1 from polymerase to hydrolase
Johannes Rudolph, Genevieve Roberts, Uma M. Muthurajan, et al.
eLife (2021) Vol. 10
Open Access | Times Cited: 60

Showing 1-25 of 60 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

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

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 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

Serine-linked PARP1 auto-modification controls PARP inhibitor response
Evgeniia Prokhorova, Florian Zobel, Rebecca Smith, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 77

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

PARP inhibitors trap PARP2 and alter the mode of recruitment of PARP2 at DNA damage sites
Xiaohui Lin, Wenxia Jiang, Johannes Rudolph, et al.
Nucleic Acids Research (2022) Vol. 50, Iss. 7, pp. 3958-3973
Open Access | Times Cited: 41

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

XRCC1 protects transcription from toxic PARP1 activity during DNA base excision repair
Marek Adamowicz, Richard Hailstone, Annie Albert Demin, et al.
Nature Cell Biology (2021) Vol. 23, Iss. 12, pp. 1287-1298
Open Access | Times Cited: 46

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

PARP1 condensates differentially partition DNA repair proteins and enhance DNA ligation
Christopher Chin Sang, Gaelen Moore, Maria Tereshchenko, et al.
EMBO Reports (2024)
Closed Access | Times Cited: 8

Structural dynamics of DNA strand break sensing by PARP-1 at a single-molecule level
Anna Sefer, Eleni Kallis, Tobias Eilert, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 27

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: 16

PARP enzyme de novo synthesis of protein-free poly(ADP-ribose)
Marie-France Langelier, Manija Mirhasan, Karine Gilbert, et al.
Molecular Cell (2024)
Closed Access | Times Cited: 5

Serine ADP-ribosylation marks nucleosomes for ALC1-dependent chromatin remodeling
Jugal Mohapatra, Kyuto Tashiro, Ryan Beckner, et al.
eLife (2021) Vol. 10
Open Access | Times Cited: 28

The Role of Poly(ADP-ribose) Polymerase 1 in Nuclear and Mitochondrial Base Excision Repair
Geoffrey K. Herrmann, Y. Whitney Yin
Biomolecules (2023) Vol. 13, Iss. 8, pp. 1195-1195
Open Access | Times Cited: 11

Asymmetric nucleosome PARylation at DNA breaks mediates directional nucleosome sliding by ALC1
Luka Bačić, Guillaume Gaullier, Jugal Mohapatra, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 4

Histone ADP-ribosylation promotes resistance to PARP inhibitors by facilitating PARP1 release from DNA lesions
Siham Zentout, Victor Imburchia, Catherine Chapuis, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 25
Closed Access | Times Cited: 4

Dispensability of HPF1 for cellular removal of DNA single-strand breaks
Kristyna Hrychova, Kamila Burdová, Zuzana Polackova, et al.
Nucleic Acids Research (2024) Vol. 52, Iss. 18, pp. 10986-10998
Open Access | Times Cited: 4

HPF1 Regulates Pol β Efficiency in Nucleosomes via the Modulation of Total Poly(ADP-Ribose) Synthesis
Mikhail M. Kutuzov, Dinara Sayfullina, E. A. Belousova, et al.
International Journal of Molecular Sciences (2025) Vol. 26, Iss. 5, pp. 1794-1794
Open 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

Dual function of HPF1 in the modulation of PARP1 and PARP2 activities
Tatyana A. Kurgina, Nina Moor, Mikhail M. Kutuzov, et al.
Communications Biology (2021) Vol. 4, Iss. 1
Open Access | Times Cited: 26

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