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:

Serine ADP-Ribosylation Depends on HPF1
Juán José Bonfiglio, Pietro Fontana, Qi Zhang, et al.
Molecular Cell (2017) Vol. 65, Iss. 5, pp. 932-940.e6
Open Access | Times Cited: 315

Showing 26-50 of 315 citing articles:

ADP‐ribosylation: new facets of an ancient modification
Luca Palazzo, Andreja Mikoč, Ivan Ahel
FEBS Journal (2017) Vol. 284, Iss. 18, pp. 2932-2946
Open Access | Times Cited: 129

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

Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase
Jeannette Abplanalp, Mario Leutert, Emilie Frugier, et al.
Nature Communications (2017) Vol. 8, Iss. 1
Open Access | Times Cited: 116

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

Genetic screens in isogenic mammalian cell lines without single cell cloning
Peter C. DeWeirdt, Annabel K. Sangree, Ruth E. Hanna, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 112

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

Mapping Physiological ADP-Ribosylation Using Activated Ion Electron Transfer Dissociation
Sara C. Buch-Larsen, Ivo A. Hendriks, Jean M. Lodge, et al.
Cell Reports (2020) Vol. 32, Iss. 12, pp. 108176-108176
Open Access | Times Cited: 104

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

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 C-terminal domain of p53 orchestrates the interplay between non-covalent and covalent poly(ADP-ribosyl)ation of p53 by PARP1
Arthur Fischbach, Annika Krüger, Stephanie Hampp, et al.
Nucleic Acids Research (2017) Vol. 46, Iss. 2, pp. 804-822
Open Access | Times Cited: 96

Comprehensive ADP‐ribosylome analysis identifies tyrosine as an ADP‐ribose acceptor site
Deena M. Leslie Pedrioli, Mario Leutert, Vera Bilan, et al.
EMBO Reports (2018) Vol. 19, Iss. 8
Open Access | Times Cited: 92

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

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

Rapid Detection and Signaling of DNA Damage by PARP-1
Nootan Pandey, Ben E. Black
Trends in Biochemical Sciences (2021) Vol. 46, Iss. 9, pp. 744-757
Open Access | Times Cited: 88

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

CARM1 regulates replication fork speed and stress response by stimulating PARP1
Marie‐Michelle Genois, Jean‐Philippe Gagné, Takaaki Yasuhara, et al.
Molecular Cell (2021) Vol. 81, Iss. 4, pp. 784-800.e8
Open Access | Times Cited: 83

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

The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome
Ivo A. Hendriks, Sara C. Buch-Larsen, Evgeniia Prokhorova, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 81

ADP-ribosylation of DNA and RNA
Joséphine Groslambert, Evgeniia Prokhorova, Ivan Ahel
DNA repair (2021) Vol. 105, pp. 103144-103144
Open Access | Times Cited: 80

Real-time monitoring of PARP1-dependent PARylation by ATR-FTIR spectroscopy
Annika Krüger, Alexander Bürkle, Karin Hauser, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 79

Serine-linked PARP1 auto-modification controls PARP inhibitor response
Evgeniia Prokhorova, Florian Zobel, Rebecca Smith, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 77

Clinical PARP inhibitors do not abrogate PARP1 exchange at DNA damage sites in vivo
Zhengping Shao, Brian J. Lee, Élise Rouleau-Turcotte, et al.
Nucleic Acids Research (2020) Vol. 48, Iss. 17, pp. 9694-9709
Open Access | Times Cited: 71

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