Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

The role of poly ADP-ribosylation in the first wave of DNA damage response
Chao Liu, Aditi Vyas, Muzaffer Ahmad Kassab, et al.
Nucleic Acids Research (2017) Vol. 45, Iss. 14, pp. 8129-8141
Open Access | Times Cited: 198

Showing 26-50 of 198 citing articles:

Immediate-Early, Early, and Late Responses to DNA Double Stranded Breaks
Shaylee R. Kieffer, Noel F. Lowndes
Frontiers in Genetics (2022) Vol. 13
Open Access | Times Cited: 49
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
Emerging role of RNA acetylation modification ac4C in diseases: Current advances and future challenges
Jie Luo, Jingsong Cao, Cong Chen, et al.
Biochemical Pharmacology (2023) Vol. 213, pp. 115628-115628
Closed Access | Times Cited: 34
An inventory of crosstalk between ubiquitination and other post-translational modifications in orchestrating cellular processes
Haithem Barbour, Nadine Sen Nkwe, Benjamin Estavoyer, et al.
iScience (2023) Vol. 26, Iss. 5, pp. 106276-106276
Open Access | Times Cited: 26
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
A methylation-phosphorylation switch determines Plk1 kinase activity and function in DNA damage repair
Weizhe Li, Hongyan Wang, Xiaolu Zhao, et al.
Science Advances (2019) Vol. 5, Iss. 3
Open Access | Times Cited: 64
Poly(ADP-ribose)-dependent chromatin unfolding facilitates the association of DNA-binding proteins with DNA at sites of damage
Rebecca Smith, Théo Lebeaupin, Szilvia Juhász, et al.
Nucleic Acids Research (2019) Vol. 47, Iss. 21, pp. 11250-11267
Open Access | Times Cited: 63
The taming of PARP1 and its impact on NAD+ metabolism
Sarah Hurtado-Bagès, G. Knobloch, Andreas G. Ladurner, et al.
Molecular Metabolism (2020) Vol. 38, pp. 100950-100950
Open Access | Times Cited: 62
DELTEX2 C-terminal domain recognizes and recruits ADP-ribosylated proteins for ubiquitination
Syed Feroj Ahmed, Lori Buetow, Mads Gabrielsen, et al.
Science Advances (2020) Vol. 6, Iss. 34
Open Access | Times Cited: 60
Imaging the response to DNA damage in heterochromatin domains reveals core principles of heterochromatin maintenance
Anna Fortuny, Audrey Chansard, Pierre Caron, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 53
Progress and outlook in studying the substrate specificities of PARPs and related enzymes
Marcin J. Suskiewicz, Luca Palazzo, R. J. M. Hughes, et al.
FEBS Journal (2020) Vol. 288, Iss. 7, pp. 2131-2142
Open Access | Times Cited: 52
PARP1 and CHK1 coordinate PLK1 enzymatic activity during the DNA damage response to promote homologous recombination-mediated repair
Bin Peng, R. Shi, Jing Bian, et al.
Nucleic Acids Research (2021) Vol. 49, Iss. 13, pp. 7554-7570
Open Access | Times Cited: 47
Proteins from the DNA Damage Response: Regulation, Dysfunction, and Anticancer Strategies
Caroline Molinaro, Alain Martoriati, Katia Cailliau
Cancers (2021) Vol. 13, Iss. 15, pp. 3819-3819
Open Access | Times Cited: 42
Truncated PARP1 mediates ADP-ribosylation of RNA polymerase III for apoptosis
Qian Chen, Kai Ma, Xiuhua Liu, et al.
Cell Discovery (2022) Vol. 8, Iss. 1
Open Access | Times Cited: 31
Nimbolide targets RNF114 to induce the trapping of PARP1 and synthetic lethality in BRCA -mutated cancer
Peng Li, Yuanli Zhen, Chiho Kim, et al.
Science Advances (2023) Vol. 9, Iss. 43
Open Access | Times Cited: 20
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
The RNA m5C modification in R-loops as an off switch of Alt-NHEJ
Haibo Yang, Emily M. Lachtara, Xiaojuan Ran, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 19
TKT-PARP1 axis induces radioresistance by promoting DNA double-strand break repair in hepatocellular carcinoma
Longpo Geng, Mingming Zhu, Dongjun Luo, et al.
Oncogene (2024) Vol. 43, Iss. 9, pp. 682-692
Open Access | Times Cited: 8
CHK1 inhibitor induced PARylation by targeting PARG causes excessive replication and metabolic stress and overcomes chemoresistance in ovarian cancer
Ganesh Acharya, Chinnadurai Mani, Naresh Sah, et al.
Cell Death Discovery (2024) Vol. 10, Iss. 1
Open Access | Times Cited: 8
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
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
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
NADP+ is an endogenous PARP inhibitor in DNA damage response and tumor suppression
Chunjing Bian, Chao Zhang, Tao Luo, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 53
Cellular Compartmentation and the Redox/Nonredox Functions of NAD+
Chaitanya A. Kulkarni, Paul S. Brookes
Antioxidants and Redox Signaling (2019) Vol. 31, Iss. 9, pp. 623-642
Open Access | Times Cited: 52
ADP‐ribosylation of histone variant H2AX promotes base excision repair
Qian Chen, Chunjing Bian, Xin Wang, et al.
The EMBO Journal (2020) Vol. 40, Iss. 2
Open Access | Times Cited: 44

Scroll to top