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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 51-75 of 618 citing articles:

Generation and Characterization of Recombinant Antibody-like ADP-Ribose Binding Proteins
Bryan A. Gibson, Lesley B. Conrad, Dan Huang, et al.
Biochemistry (2017) Vol. 56, Iss. 48, pp. 6305-6316
Open Access | Times Cited: 113
Analysis of PARP inhibitor toxicity by multidimensional fluorescence microscopy reveals mechanisms of sensitivity and resistance
Jone Michelena, Aleksandra Lezaja, Federico Teloni, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 109
Characterization of DNA ADP-ribosyltransferase activities of PARP2 and PARP3: new insights into DNA ADP-ribosylation
Gabriella Zarkovic, E. A. Belousova, Ibtissam Talhaoui, et al.
Nucleic Acids Research (2017) Vol. 46, Iss. 5, pp. 2417-2431
Open Access | Times Cited: 105
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
Selective small molecule PARG inhibitor causes replication fork stalling and cancer cell death
Jerry H. Houl, Zu Ye, Chris A. Brosey, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 102
PARPs in lipid metabolism and related diseases
Magdolna Szántó, Rebecca Gupte, W. Lee Kraus, et al.
Progress in Lipid Research (2021) Vol. 84, pp. 101117-101117
Open Access | Times Cited: 102
The Role of PARPs in Inflammation—And Metabolic—Related Diseases: Molecular Mechanisms and Beyond
Yueshuang Ke, Chenxin Wang, Jiaqi Zhang, et al.
Cells (2019) Vol. 8, Iss. 9, pp. 1047-1047
Open Access | Times Cited: 100
Location, Location, Location: Compartmentalization of NAD+ Synthesis and Functions in Mammalian Cells
Xiaolu A. Cambronne, W. Lee Kraus
Trends in Biochemical Sciences (2020) Vol. 45, Iss. 10, pp. 858-873
Open Access | Times Cited: 100
Nuclear poly(ADP-ribose) activity is a therapeutic target in amyotrophic lateral sclerosis
Leeanne McGurk, Jelena Mojsilovic‐Petrovic, Vivianna M. Van Deerlin, et al.
Acta Neuropathologica Communications (2018) Vol. 6, Iss. 1
Open Access | Times Cited: 99
The Viral Macrodomain Counters Host Antiviral ADP-Ribosylation
Yousef M. Alhammad, Anthony R. Fehr
Viruses (2020) Vol. 12, Iss. 4, pp. 384-384
Open Access | Times Cited: 99
Nuclear PARPs and genome integrity
Kameron Azarm, Susan Smith
Genes & Development (2020) Vol. 34, Iss. 5-6, pp. 285-301
Open Access | Times Cited: 98
The Ubiquitin Ligase TRIP12 Limits PARP1 Trapping and Constrains PARP Inhibitor Efficiency
Marco Gatti, Ralph Imhof, Qingyao Huang, et al.
Cell Reports (2020) Vol. 32, Iss. 5, pp. 107985-107985
Open Access | Times Cited: 95
Niacin
James B. Kirkland, Mirella L. Meyer‐Ficca
Advances in food and nutrition research (2018), pp. 83-149
Closed Access | Times Cited: 95
PARP1-produced poly-ADP-ribose causes the PARP12 translocation to stress granules and impairment of Golgi complex functions
Giuliana Catara, Giovanna Grimaldi, Laura Schembri, et al.
Scientific Reports (2017) Vol. 7, Iss. 1
Open Access | Times Cited: 93
ATRX/EZH2 complex epigenetically regulates FADD/PARP1 axis, contributing to TMZ resistance in glioma
Bo Han, Xiangqi Meng, Pengfei Wu, et al.
Theranostics (2020) Vol. 10, Iss. 7, pp. 3351-3365
Open Access | Times Cited: 93
ADP-ribosylation signalling and human disease
Luca Palazzo, Petra Mikolčević, Andreja Mikoč, et al.
Open Biology (2019) Vol. 9, Iss. 4
Open Access | Times Cited: 92
Specificity of reversible ADP-ribosylation and regulation of cellular processes
Kerryanne Crawford, Juán José Bonfiglio, Andreja Mikoč, et al.
Critical Reviews in Biochemistry and Molecular Biology (2017) Vol. 53, Iss. 1, pp. 64-82
Closed Access | Times Cited: 91
Interplay of Histone Marks with Serine ADP-Ribosylation
Edward Bartlett, Juán José Bonfiglio, Evgeniia Prokhorova, et al.
Cell Reports (2018) Vol. 24, Iss. 13, pp. 3488-3502.e5
Open Access | Times Cited: 91
Regulation of Glucose Metabolism by NAD+ and ADP-Ribosylation
Ann-Katrin Hopp, Patrick Grüter, Michael O. Hottiger
Cells (2019) Vol. 8, Iss. 8, pp. 890-890
Open Access | Times Cited: 90
An HPF1/PARP1-Based Chemical Biology Strategy for Exploring ADP-Ribosylation
Juán José Bonfiglio, Orsolya Leidecker, Helen Dauben, et al.
Cell (2020) Vol. 183, Iss. 4, pp. 1086-1102.e23
Open Access | Times Cited: 90
Whole proteome analysis of human tankyrase knockout cells reveals targets of tankyrase-mediated degradation
Amit Bhardwaj, Yan‐Ling Yang, Beatrix Ueberheide, et al.
Nature Communications (2017) Vol. 8, Iss. 1
Open Access | Times Cited: 89
PARP-1 protects against colorectal tumor induction, but promotes inflammation-driven colorectal tumor progression
Bastian Dörsam, Nina Seiwert, Sebastian Foersch, et al.
Proceedings of the National Academy of Sciences (2018) Vol. 115, Iss. 17
Open Access | Times Cited: 85
MORC2 regulates DNA damage response through a PARP1-dependent pathway
Lin Zhang, Da‐Qiang Li
Nucleic Acids Research (2019) Vol. 47, Iss. 16, pp. 8502-8520
Open Access | Times Cited: 84
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
Unrestrained poly-ADP-ribosylation provides insights into chromatin regulation and human disease
Evgeniia Prokhorova, Thomas Agnew, Anne R. Wondisford, et al.
Molecular Cell (2021) Vol. 81, Iss. 12, pp. 2640-2655.e8
Open Access | Times Cited: 82

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