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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:

HPF1 remodels the active site of PARP1 to enable the serine ADP-ribosylation of histones
Fa-Hui Sun, Peng Zhao, Nan Zhang, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 66

Showing 1-25 of 66 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
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
PARP1: Structural insights and pharmacological targets for inhibition
Jacob O. Spiegel, Bennett Van Houten, Jacob D. Durrant
DNA repair (2021) Vol. 103, pp. 103125-103125
Open Access | Times Cited: 63
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
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
PARP1: Liaison of Chromatin Remodeling and Transcription
Wen Zong, Yamin Gong, Wenli Sun, et al.
Cancers (2022) Vol. 14, Iss. 17, pp. 4162-4162
Open Access | Times Cited: 48
Captured snapshots of PARP1 in the active state reveal the mechanics of PARP1 allostery
Élise Rouleau-Turcotte, Dragomir B. Krastev, Stephen J. Pettitt, et al.
Molecular Cell (2022) Vol. 82, Iss. 16, pp. 2939-2951.e5
Open Access | Times Cited: 43
Updated protein domain annotation of the PARP protein family sheds new light on biological function
Marcin J. Suskiewicz, Deeksha Munnur, Øyvind Strømland, et al.
Nucleic Acids Research (2023) Vol. 51, Iss. 15, pp. 8217-8236
Open Access | Times Cited: 36
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
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
Enhancer–promoter specificity in gene transcription: molecular mechanisms and disease associations
Meyer J. Friedman, Tobias Wagner, Haram Lee, et al.
Experimental & Molecular Medicine (2024) Vol. 56, Iss. 4, pp. 772-787
Open Access | Times Cited: 13
Chemical proteomics approaches for protein post-translational modification studies
Nan Zhang, Jinghua Wu, Qingfei Zheng
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (2024) Vol. 1872, Iss. 4, pp. 141017-141017
Open Access | Times Cited: 10
A unified mechanism for PARP inhibitor-induced PARP1 chromatin retention at DNA damage sites in living cells
Petar-Bogomil Kanev, Sylvia Varhoshkova, Irina Georgieva, et al.
Cell Reports (2024) Vol. 43, Iss. 5, pp. 114234-114234
Open Access | Times Cited: 10
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
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
A two-step mechanism governing PARP1-DNA retention by PARP inhibitors
Huijun Xue, Amit Bhardwaj, Yandong Yin, et al.
Science Advances (2022) Vol. 8, Iss. 36
Open Access | Times Cited: 38
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
Linking DNA repair and cell cycle progression through serine ADP-ribosylation of histones
Julien Brustel, Tetsuya Muramoto, Kazuki Fumimoto, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 24
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
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
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
A PARP2 active site helix melts to permit DNA damage-induced enzymatic activation
Emily S Smith-Pillet, Ramya Billur, Marie-France Langelier, et al.
Molecular Cell (2025)
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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