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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:

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

Showing 16 citing articles:

PARP1 proximity proteomics reveals interaction partners at stressed replication forks
Thorsten Mosler, H. Irem Baymaz, Justus F. Gräf, et al.
Nucleic Acids Research (2022) Vol. 50, Iss. 20, pp. 11600-11618
Open Access | Times Cited: 41
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
Mimetics of ADP-Ribosylated Histidine through Copper(I)-Catalyzed Click Chemistry
Hugo Minnee, J.G.M. Rack, Gijsbert A. van der Marel, et al.
Organic Letters (2022) Vol. 24, Iss. 21, pp. 3776-3780
Open Access | Times Cited: 14
The interplay of TARG1 and PARG protects against genomic instability
Joséphine Groslambert, Evgeniia Prokhorova, Anne R. Wondisford, et al.
Cell Reports (2023) Vol. 42, Iss. 9, pp. 113113-113113
Open Access | Times Cited: 8
Solid‐Phase Synthesis and Biological Evaluation of Peptides ADP‐Ribosylated at Histidine
Hugo Minnee, J.G.M. Rack, Gijsbert A. van der Marel, et al.
Angewandte Chemie International Edition (2023) Vol. 63, Iss. 4
Open Access | Times Cited: 7
Synthetic Dual Cysteine-ADP Ribosylated Peptides from the Androgen Receptor are Recognized by the DTX3L/PARP9 Complex
Sven Wijngaarden, Chunsong Yang, Carlos Vela‐Rodríguez, et al.
ACS Chemical Biology (2023) Vol. 18, Iss. 11, pp. 2377-2384
Open Access | Times Cited: 7
Dispensability of HPF1 for cellular removal of DNA single-strand breaks
Kristyna Hrychova, Kamila Burdová, Zuzana Polackova, et al.
Nucleic Acids Research (2024) Vol. 52, Iss. 18, pp. 10986-10998
Open Access | Times Cited: 2
The fast-growing business of Serine ADP-ribosylation
Edoardo José Longarini, Ivan Matić
DNA repair (2022) Vol. 118, pp. 103382-103382
Closed Access | Times Cited: 10
Uncommon posttranslational modifications in proteomics: ADP‐ribosylation, tyrosine nitration, and tyrosine sulfation
Aarti Bashyal, Jennifer S. Brodbelt
Mass Spectrometry Reviews (2022) Vol. 43, Iss. 2, pp. 289-326
Closed Access | Times Cited: 10
The dynamic process of covalent and non-covalent PARylation in the maintenance of genome integrity: a focus on PARP inhibitors
Adèle Beneyton, Louis Nonfoux, Jean‐Philippe Gagné, et al.
NAR Cancer (2023) Vol. 5, Iss. 3
Open Access | Times Cited: 6
NBS1 dePARylation by NUDT16 is critical for DNA double-strand break repair
Zhen Zhang, William E. Samsa, Zihua Gong
Molecular and Cellular Biochemistry (2024)
Closed Access | Times Cited: 1
Characterizing ADP-Ribosylation Sites Using Af1521 Enrichment Coupled to ETD-Based Mass Spectrometry
Holda A. Anagho, Jonas D. Elsborg, Ivo A. Hendriks, et al.
Methods in molecular biology (2022), pp. 251-270
Closed Access | Times Cited: 6
Poly(ADP-Ribose) Polymerases 1 and 2: Classical Functions and Interaction with New Histone Poly(ADP-Ribosyl)ation Factor HPF1
Tatyana A. Kurgina, Olga I. Lavrik
Molecular Biology (2023) Vol. 57, Iss. 2, pp. 245-257
Closed Access | Times Cited: 2
Mono‐ADP‐ribosylation of peptides: an overview of synthetic and chemoenzymatic methodologies
Hugo Minnee, Jeroen D. C. Codée, Dmitri V. Filippov
ChemBioChem (2024)
Open Access
Poly(ADP-ribose)polymerases 1 and 2: Classical Functions and Interaction with HPF1 ‒ New Histone Poly(ADP-ribosyl)ation Factor
Tatyana A. Kurgina, Olga I. Lavrik
Молекулярная биология (2023) Vol. 57, Iss. 2, pp. 254-268
Closed Access | Times Cited: 1
Solid‐Phase Synthesis and Biological Evaluation of Peptides ADP‐Ribosylated at Histidine
Hugo Minnee, J.G.M. Rack, Gijsbert A. van der Marel, et al.
Angewandte Chemie (2023) Vol. 136, Iss. 4
Open Access
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