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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:

A Cell-Line-Specific Atlas of PARP-Mediated Protein Asp/Glu-ADP-Ribosylation in Breast Cancer
Yuanli Zhen, Yajie Zhang, Yonghao Yu
Cell Reports (2017) Vol. 21, Iss. 8, pp. 2326-2337
Open Access | Times Cited: 58

Showing 1-25 of 58 citing articles:

Activation of PARP-1 by snoRNAs Controls Ribosome Biogenesis and Cell Growth via the RNA Helicase DDX21
Dae-Seok Kim, Cristel V. Camacho, Anusha Nagari, et al.
Molecular Cell (2019) Vol. 75, Iss. 6, pp. 1270-1285.e14
Open Access | Times Cited: 214
Serine is the major residue for ADP-ribosylation upon DNA damage
Luca Palazzo, Orsolya Leidecker, Evgeniia Prokhorova, et al.
eLife (2018) Vol. 7
Open Access | Times Cited: 207
PARP-1 Activation Directs FUS to DNA Damage Sites to Form PARG-Reversible Compartments Enriched in Damaged DNA
Anastasia S. Singatulina, Loïc Hamon, Maria V. Sukhanova, et al.
Cell Reports (2019) Vol. 27, Iss. 6, pp. 1809-1821.e5
Open Access | Times Cited: 191
Systems-wide Analysis of Serine ADP-Ribosylation Reveals Widespread Occurrence and Site-Specific Overlap with Phosphorylation
Sara C. Buch-Larsen, Ivo A. Hendriks, David Lyon, et al.
Cell Reports (2018) Vol. 24, Iss. 9, pp. 2493-2505.e4
Open Access | Times Cited: 163
Emerging roles of eraser enzymes in the dynamic control of protein ADP-ribosylation
Julia O’Sullivan, Maria Tedim Ferreira, Jean‐Philippe Gagné, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 141
PARPs and ADP-ribosylation in RNA biology: from RNA expression and processing to protein translation and proteostasis
Dae-Seok Kim, Sridevi Challa, Aarin Jones, et al.
Genes & Development (2020) Vol. 34, Iss. 5-6, pp. 302-320
Open Access | Times Cited: 122
PARP1 Suppresses the Transcription of PD-L1 by Poly(ADP-Ribosyl)ating STAT3
Ling Ding, Xi Chen, Xiaqing Xu, et al.
Cancer Immunology Research (2018) Vol. 7, Iss. 1, pp. 136-149
Open Access | Times Cited: 103
Uncoupling of PARP1 trapping and inhibition using selective PARP1 degradation
Shuai Wang, Lei Han, Jungsoo Han, et al.
Nature Chemical Biology (2019) Vol. 15, Iss. 12, pp. 1223-1231
Open Access | Times Cited: 84
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
A PARP1 PROTAC as a novel strategy against PARP inhibitor resistance via promotion of ferroptosis in p53-positive breast cancer
Ge Li, Shanshan Lin, Zelei Yu, et al.
Biochemical Pharmacology (2022) Vol. 206, pp. 115329-115329
Closed Access | Times Cited: 40
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
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
ELTA: Enzymatic Labeling of Terminal ADP-Ribose
Yoshinari Ando, Elad Elkayam, Robert Lyle McPherson, et al.
Molecular Cell (2019) Vol. 73, Iss. 4, pp. 845-856.e5
Open Access | Times Cited: 65
Unconventional protein post-translational modifications: the helmsmen in breast cancer
Jiena Liu, Qin Wang, Yujuan Kang, et al.
Cell & Bioscience (2022) Vol. 12, Iss. 1
Open Access | Times Cited: 34
PARP1 at the crossroad of cellular senescence and nucleolar processes
Kinga Kołacz, Agnieszka Robaszkiewicz
Ageing Research Reviews (2024) Vol. 94, pp. 102206-102206
Closed Access | Times Cited: 8
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
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
Pre-ribosomal RNA reorganizes DNA damage repair factors in nucleus during meiotic prophase and DNA damage response
Xiaochen Gai, Di Xin, Duo Wu, et al.
Cell Research (2022) Vol. 32, Iss. 3, pp. 254-268
Open Access | Times Cited: 28
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
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
Nucleolar-nucleoplasmic shuttling of TARG1 and its control by DNA damage-induced poly-ADP-ribosylation and by nucleolar transcription
Mareike Bütepage, Christian Preisinger, Alex von Kriegsheim, et al.
Scientific Reports (2018) Vol. 8, Iss. 1
Open Access | Times Cited: 38
Proteomic Analysis of the Downstream Signaling Network of PARP1
Yuanli Zhen, Yonghao Yu
Biochemistry (2018) Vol. 57, Iss. 4, pp. 429-440
Open Access | Times Cited: 36
RACK1 MARylation regulates translation and stress granules in ovarian cancer cells
Sridevi Challa, Tulip Nandu, Hyung Bum Kim, et al.
The Journal of Cell Biology (2025) Vol. 224, Iss. 2
Open Access
Targeting dePARylation in cancer therapy
Peng Li, Duo Wu, Xiaochun Yu
DNA repair (2025) Vol. 148, pp. 103824-103824
Closed Access
A large-scale method to measure the absolute stoichiometries of protein Poly-ADP-Ribosylation
Peng Li, Yajie Zhang, Yonghao Yu
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access
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