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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:

Systems-wide Analysis of Serine ADP-Ribosylation Reveals Widespread Occurrence and Site-Specific Overlap with Phosphorylation
Sara C. Buch-Larsen, Ivo A. Hendriks, David Lyon, et al.
Cell Reports (2018) Vol. 24, Iss. 9, pp. 2493-2505.e4
Open Access | Times Cited: 163

Showing 26-50 of 163 citing articles:

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
Preserving ester-linked modifications reveals glutamate and aspartate mono-ADP-ribosylation by PARP1 and its reversal by PARG
Edoardo José Longarini, Ivan Matić
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 16
Poly(ADP-ribosyl)ation of TIMELESS limits DNA replication stress and promotes stalled fork protection
Julie Rageul, Natalie Lo, Amy L Phi, et al.
Cell Reports (2024) Vol. 43, Iss. 3, pp. 113845-113845
Open Access | Times Cited: 10
SERBP1 interacts with PARP1 and is present in PARylation-dependent protein complexes regulating splicing, cell division, and ribosome biogenesis
Kira Breunig, X. Lei, Mauro Montalbano, et al.
eLife (2025) Vol. 13
Open Access | Times Cited: 1
ELTA: Enzymatic Labeling of Terminal ADP-Ribose
Yoshinari Ando, Elad Elkayam, Robert Lyle McPherson, et al.
Molecular Cell (2019) Vol. 73, Iss. 4, pp. 845-856.e5
Open Access | Times Cited: 65
Perspectives on PARPs in S Phase
Hana Hanzlíková, Keith W. Caldecott
Trends in Genetics (2019) Vol. 35, Iss. 6, pp. 412-422
Closed Access | Times Cited: 61
Functional Interplay between Histone H2B ADP-Ribosylation and Phosphorylation Controls Adipogenesis
Dan Huang, Cristel V. Camacho, Rohit Setlem, et al.
Molecular Cell (2020) Vol. 79, Iss. 6, pp. 934-949.e14
Open Access | Times Cited: 58
The PARP Enzyme Family and the Hallmarks of Cancer Part 1. Cell Intrinsic Hallmarks
Máté Á. Demény, László Virág
Cancers (2021) Vol. 13, Iss. 9, pp. 2042-2042
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
Mitochondrial NAD+ Controls Nuclear ARTD1-Induced ADP-Ribosylation
Ann-Katrin Hopp, Federico Teloni, Lavinia Bisceglie, et al.
Molecular Cell (2021) Vol. 81, Iss. 2, pp. 340-354.e5
Open Access | Times Cited: 49
Multifaceted Role of PARP1 in Maintaining Genome Stability Through Its Binding to Alternative DNA Structures
Natalie Laspata, Daniela Muoio, Elise Fouquerel
Journal of Molecular Biology (2023) Vol. 436, Iss. 1, pp. 168207-168207
Open Access | Times Cited: 22
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
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
PARP trapping is governed by the PARP inhibitor dissociation rate constant
Angelica A. Gopal, Bianca Fernandez, Justin Delano, et al.
Cell chemical biology (2024) Vol. 31, Iss. 7, pp. 1373-1382.e10
Closed Access | Times Cited: 7
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
ADPriboDB 2.0: an updated database of ADP-ribosylated proteins
Vinay Ayyappan, Ricky Wat, Calvin Barber, et al.
Nucleic Acids Research (2020) Vol. 49, Iss. D1, pp. D261-D265
Open Access | Times Cited: 42
Reading ADP-ribosylation signaling using chemical biology and interaction proteomics
Katarzyna W. Kliza, Qiang Liu, Laura W.M. Roosenboom, et al.
Molecular Cell (2021) Vol. 81, Iss. 21, pp. 4552-4567.e8
Open Access | Times Cited: 40
PARP7 and Mono-ADP-Ribosylation Negatively Regulate Estrogen Receptor α Signaling in Human Breast Cancer Cells
Marit Rasmussen, Susanna Tan, Venkata S. Somisetty, et al.
Cells (2021) Vol. 10, Iss. 3, pp. 623-623
Open Access | Times Cited: 34
Deficiency of PARP-1 and PARP-2 in the mouse uterus results in decidualization failure and pregnancy loss
Andrew M. Kelleher, Rohit Setlem, Françoise Dantzer, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 40
Open Access | Times Cited: 34
Beyond protein modification: the rise of non-canonical ADP-ribosylation
M. Schuller, Ivan Ahel
Biochemical Journal (2022) Vol. 479, Iss. 4, pp. 463-477
Open Access | Times Cited: 27
Linking DNA repair and cell cycle progression through serine ADP-ribosylation of histones
Julien Brustel, Tetsuya Muramoto, Kazuki Fumimoto, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 24
The potential of PARP inhibitors in targeted cancer therapy and immunotherapy
Jaromir Hunia, Karol Gawalski, Aleksandra Szredzka, et al.
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 23
Nicotinamide N-Methyltransferase (NNMT): A New Hope for Treating Aging and Age-Related Conditions
Jingjing Li, Wei-Dong Sun, Xiaojuan Zhu, et al.
Metabolites (2024) Vol. 14, Iss. 6, pp. 343-343
Open Access | Times Cited: 5
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
Androgen signaling uses a writer and a reader of ADP-ribosylation to regulate protein complex assembly
Chunsong Yang, Kasey Jividen, Teddy Kamata, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 29

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