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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:

Phosphoproteomic Approach to Characterize Protein Mono- and Poly(ADP-ribosyl)ation Sites from Cells
Casey M. Daniels, Shao‐En Ong, Anthony K. L. Leung
Journal of Proteome Research (2014) Vol. 13, Iss. 8, pp. 3510-3522
Open Access | Times Cited: 113

Showing 51-75 of 113 citing articles:

The Nucleolus and PARP1 in Cancer Biology
Marina Engbrecht, Aswin Mangerich
Cancers (2020) Vol. 12, Iss. 7, pp. 1813-1813
Open Access | Times Cited: 48
Poly(ADP-Ribose) Polymerases in Host-Pathogen Interactions, Inflammation, and Immunity
Pamlea N. Brady, Anupam Goel, Margaret A. Johnson
Microbiology and Molecular Biology Reviews (2019) Vol. 83, Iss. 1
Open Access | Times Cited: 46
Unanchored tri‐NEDD8 inhibits PARP‐1 to protect from oxidative stress‐induced cell death
Matthew J. Keuss, Roland Hjerpe, Oliver Hsia, et al.
The EMBO Journal (2019) Vol. 38, Iss. 6
Open Access | Times Cited: 44
Noncanonical mono(ADP-ribosyl)ation of zinc finger SZF proteins counteracts ubiquitination for protein homeostasis in plant immunity
Liang Kong, Baomin Feng, Yan Yan, et al.
Molecular Cell (2021) Vol. 81, Iss. 22, pp. 4591-4604.e8
Open Access | Times Cited: 34
Proteomics approaches to identify mono‐(ADP‐ribosyl)ated and poly(ADP‐ribosyl)ated proteins
Christina A. Vivelo, Anthony K. L. Leung
PROTEOMICS (2014) Vol. 15, Iss. 2-3, pp. 203-217
Open Access | Times Cited: 51
Mass spectrometry for serine ADP-ribosylation? Think o-glycosylation!
Juán José Bonfiglio, Thomas Colby, Ivan Matić
Nucleic Acids Research (2017) Vol. 45, Iss. 11, pp. 6259-6264
Open Access | Times Cited: 47
Characterization of TCDD-inducible poly-ADP-ribose polymerase (TIPARP/ARTD14) catalytic activity
Alvin Gomez, Christian Bindesbøll, Somisetty V. Satheesh, et al.
Biochemical Journal (2018) Vol. 475, Iss. 23, pp. 3827-3846
Open Access | Times Cited: 46
Extracellular Poly(ADP-Ribose) Is a Pro-inflammatory Signal for Macrophages
Kristin A. Krukenberg, Sujeong Kim, Edwin S. Tan, et al.
Chemistry & Biology (2015) Vol. 22, Iss. 4, pp. 446-452
Open Access | Times Cited: 43
The nucleosomal surface is the main target of histone ADP-ribosylation in response to DNA damage
Kelly R. Karch, Marie-France Langelier, John M. Pascal, et al.
Molecular BioSystems (2017) Vol. 13, Iss. 12, pp. 2660-2671
Open Access | Times Cited: 40
dELTA-MS: A Mass Spectrometry-Based Proteomics Approach for Identifying ADP-Ribosylation Sites and Forms
Isabel Uribe, Emily Zahn, Richard Searfoss, et al.
Journal of Proteome Research (2025)
Closed Access
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
Chemical proteomics reveals ADP-ribosylation of small GTPases during oxidative stress
Nathan P. Westcott, Joseph Fernandez, Henrik Molina, et al.
Nature Chemical Biology (2017) Vol. 13, Iss. 3, pp. 302-308
Open Access | Times Cited: 37
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
A Clickable Aminooxy Probe for Monitoring Cellular ADP-Ribosylation
Rory K. Morgan, Michael S. Cohen
ACS Chemical Biology (2015) Vol. 10, Iss. 8, pp. 1778-1784
Open Access | Times Cited: 35
An Integrated Chemical Proteomics Approach for Quantitative Profiling of Intracellular ADP-Ribosylation
Karunakaran Kalesh, Saulius Lukauskas, Aaron J. Borg, et al.
Scientific Reports (2019) Vol. 9, Iss. 1
Open Access | Times Cited: 31
PARP Inhibitors in Biliary Tract Cancer: A New Kid on the Block?
Angela Dalia Ricci, Alessandro Rizzo, Chiara Bonucci, et al.
Medicines (2020) Vol. 7, Iss. 9, pp. 54-54
Open Access | Times Cited: 28
The Regulatory Role of NAD in Human and Animal Cells
Veronika Kulikova, Darina Gromyko, Andrey Nikiforov
Biochemistry (Moscow) (2018) Vol. 83, Iss. 7, pp. 800-812
Closed Access | Times Cited: 32
Poly(ADP-Ribose) polymerase 1 as a key regulator of DNA repair
С. Н. Ходырева, Olga I. Lavrik
Molecular Biology (2016) Vol. 50, Iss. 4, pp. 580-595
Closed Access | Times Cited: 30
Proteome-Wide Identification of In Vivo ADP-Ribose Acceptor Sites by Liquid Chromatography–Tandem Mass Spectrometry
Sara C. Buch-Larsen, Mario Leutert, Vera Bilan, et al.
Methods in molecular biology (2017), pp. 149-162
Closed Access | Times Cited: 30
A Study into the ADP-Ribosylome of IFN-γ-Stimulated THP-1 Human Macrophage-like Cells Identifies ARTD8/PARP14 and ARTD9/PARP9 ADP-Ribosylation
Hideyuki Higashi, Takashi Maejima, Lang Ho Lee, et al.
Journal of Proteome Research (2019) Vol. 18, Iss. 4, pp. 1607-1622
Open Access | Times Cited: 28
The Making and Breaking of Serine-ADP-Ribosylation in the DNA Damage Response
Kira Schützenhofer, J.G.M. Rack, Ivan Ahel
Frontiers in Cell and Developmental Biology (2021) Vol. 9
Open Access | Times Cited: 18
AHR toxicity and signaling: Role of TIPARP and ADP-ribosylation
Jason Matthews
Current Opinion in Toxicology (2017) Vol. 2, pp. 50-57
Closed Access | Times Cited: 23
Site-specific ADP-ribosylation of histone H2B in response to DNA double strand breaks
Alina Rakhimova, Seiji Ura, Duen-Wei Hsu, et al.
Scientific Reports (2017) Vol. 7, Iss. 1
Open Access | Times Cited: 22
ADPredict: ADP-ribosylation site prediction based on physicochemical and structural descriptors
Matteo Lo Monte, Candida Manelfi, Marica Gemei, et al.
Bioinformatics (2018) Vol. 34, Iss. 15, pp. 2566-2574
Open Access | Times Cited: 21
Temporal and Site-Specific ADP-Ribosylation Dynamics upon Different Genotoxic Stresses
Sara C. Buch-Larsen, Alexandra K.L.F.S. Rebak, Ivo A. Hendriks, et al.
Cells (2021) Vol. 10, Iss. 11, pp. 2927-2927
Open Access | Times Cited: 16

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