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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:

PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes
Rebecca Gupte, Ziying Liu, W. Lee Kraus
Genes & Development (2017) Vol. 31, Iss. 2, pp. 101-126
Open Access | Times Cited: 618

Showing 26-50 of 618 citing articles:

Skeletal Aging and Osteoporosis: Mechanisms and Therapeutics
Abhishek Chandra, Jyotika Rajawat
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 7, pp. 3553-3553
Open Access | Times Cited: 161
(ADP-ribosyl)hydrolases: structure, function, and biology
J.G.M. Rack, Luca Palazzo, Ivan Ahel
Genes & Development (2020) Vol. 34, Iss. 5-6, pp. 263-284
Open Access | Times Cited: 159
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
The 89-kDa PARP1 cleavage fragment serves as a cytoplasmic PAR carrier to induce AIF-mediated apoptosis
Masato Mashimo, Mayu Onishi, Arina Uno, et al.
Journal of Biological Chemistry (2020) Vol. 296, pp. 100046-100046
Open Access | Times Cited: 154
ALC1 links chromatin accessibility to PARP inhibitor response in homologous recombination-deficient cells
Priyanka Verma, Yeqiao Zhou, Zhendong Cao, et al.
Nature Cell Biology (2021) Vol. 23, Iss. 2, pp. 160-171
Open Access | Times Cited: 122
The role of PARP1 in neurodegenerative diseases and aging
Kanmin Mao, Guo Zhang
FEBS Journal (2021) Vol. 289, Iss. 8, pp. 2013-2024
Open Access | Times Cited: 114
How cancer cells make and respond to interferon-I
HyeonJoo Cheon, Yuxin Wang, Samantha M. Wightman, et al.
Trends in cancer (2022) Vol. 9, Iss. 1, pp. 83-92
Open Access | Times Cited: 96
An Epigenetic Role of Mitochondria in Cancer
Yue Liu, Chao Chen, Xinye Wang, et al.
Cells (2022) Vol. 11, Iss. 16, pp. 2518-2518
Open Access | Times Cited: 87
Protein post-translational modifications in the regulation of cancer hallmarks
Haiying Wang, Liqian Yang, Minghui Liu, et al.
Cancer Gene Therapy (2022) Vol. 30, Iss. 4, pp. 529-547
Closed Access | Times Cited: 79
Pan-cancer analysis of post-translational modifications reveals shared patterns of protein regulation
Yifat Geffen, Shankara Anand, Yo Akiyama, et al.
Cell (2023) Vol. 186, Iss. 18, pp. 3945-3967.e26
Open Access | Times Cited: 75
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
A New Phase of Networking: The Molecular Composition and Regulatory Dynamics of Mammalian Stress Granules
Seán Millar, Jie Huang, Karl J. Schreiber, et al.
Chemical Reviews (2023) Vol. 123, Iss. 14, pp. 9036-9064
Open Access | Times Cited: 62
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
Post-translational control of NLRP3 inflammasome signaling
Meghan E O'Keefe, George Dubyak, Derek W. Abbott
Journal of Biological Chemistry (2024) Vol. 300, Iss. 6, pp. 107386-107386
Open Access | Times Cited: 23
Oxidative stress and metabolism meet epigenetic modulation in physical exercise
José Luis García‐Gimenez, Irene Cánovas-Cervera, Federico V. Pallardó
Free Radical Biology and Medicine (2024) Vol. 213, pp. 123-137
Open Access | Times Cited: 17
Serine ADP-ribosylation reversal by the hydrolase ARH3
Pietro Fontana, Juán José Bonfiglio, Luca Palazzo, et al.
eLife (2017) Vol. 6
Open Access | Times Cited: 165
Reversible mono‐ADP‐ribosylation of DNA breaks
Deeksha Munnur, Ivan Ahel
FEBS Journal (2017) Vol. 284, Iss. 23, pp. 4002-4016
Open Access | Times Cited: 142
NAD+ consumption by PARP1 in response to DNA damage triggers metabolic shift critical for damaged cell survival
Michael M. Murata, Xiangduo Kong, Emmanuel Moncada, et al.
Molecular Biology of the Cell (2019) Vol. 30, Iss. 20, pp. 2584-2597
Open Access | Times Cited: 142
Genome integrity and disease prevention in the nervous system
Peter J. McKinnon
Genes & Development (2017) Vol. 31, Iss. 12, pp. 1180-1194
Open Access | Times Cited: 141
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
The Enigmatic Function of PARP1: From PARylation Activity to PAR Readers
Tatiana Kamaletdinova, Zahra Fanaei‐Kahrani, Zhao‐Qi Wang
Cells (2019) Vol. 8, Iss. 12, pp. 1625-1625
Open Access | Times Cited: 133
Poly(ADP-ribose): A Dynamic Trigger for Biomolecular Condensate Formation
Anthony K. L. Leung
Trends in Cell Biology (2020) Vol. 30, Iss. 5, pp. 370-383
Open Access | Times Cited: 130
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
Structural Insights Into TDP-43 and Effects of Post-translational Modifications
Liberty François‐Moutal, Samantha Perez‐Miller, David D. Scott, et al.
Frontiers in Molecular Neuroscience (2019) Vol. 12
Open Access | Times Cited: 121
Bridging of DNA breaks activates PARP2–HPF1 to modify chromatin
Silvija Bilokapić, Marcin J. Suskiewicz, Ivan Ahel, et al.
Nature (2020) Vol. 585, Iss. 7826, pp. 609-613
Open Access | Times Cited: 119

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