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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:

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

Showing 1-25 of 47 citing articles:

ADP-Ribosylation, a Multifaceted Posttranslational Modification Involved in the Control of Cell Physiology in Health and Disease
Bernhard Lüscher, Mareike Bütepage, Laura Eckei, et al.
Chemical Reviews (2017) Vol. 118, Iss. 3, pp. 1092-1136
Closed Access | Times Cited: 224
Serine is the major residue for ADP-ribosylation upon DNA damage
Luca Palazzo, Orsolya Leidecker, Evgeniia Prokhorova, et al.
eLife (2018) Vol. 7
Open Access | Times Cited: 207
Serine ADP-ribosylation reversal by the hydrolase ARH3
Pietro Fontana, Juán José Bonfiglio, Luca Palazzo, et al.
eLife (2017) Vol. 6
Open Access | Times Cited: 165
Emerging roles of eraser enzymes in the dynamic control of protein ADP-ribosylation
Julia O’Sullivan, Maria Tedim Ferreira, Jean‐Philippe Gagné, et al.
Nature Communications (2019) Vol. 10, Iss. 1
Open Access | Times Cited: 141
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
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
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
HPF1 and nucleosomes mediate a dramatic switch in activity of PARP1 from polymerase to hydrolase
Johannes Rudolph, Genevieve Roberts, Uma M. Muthurajan, et al.
eLife (2021) Vol. 10
Open Access | Times Cited: 60
MSFragger-Labile: A Flexible Method to Improve Labile PTM Analysis in Proteomics
Daniel A. Polasky, Daniel Geiszler, Fengchao Yu, et al.
Molecular & Cellular Proteomics (2023) Vol. 22, Iss. 5, pp. 100538-100538
Open Access | Times Cited: 26
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
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
Pathogen hijacks programmed cell death signaling by arginine ADPR-deacylization of caspases
Ting Peng, Xinyuan Tao, Zhujun Xia, et al.
Molecular Cell (2022) Vol. 82, Iss. 10, pp. 1806-1820.e8
Open Access | Times Cited: 30
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
The multifaceted role of PARP1 in RNA biogenesis
Rebekah Eleazer, Yvonne Fondufe‐Mittendorf
Wiley Interdisciplinary Reviews - RNA (2020) Vol. 12, Iss. 2
Open Access | Times Cited: 41
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
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
Targeting dePARylation for cancer therapy
Muzaffer Ahmad Kassab, Lily Yu, Xiaochun Yu
Cell & Bioscience (2020) Vol. 10, Iss. 1
Open Access | Times Cited: 30
Avoid the trap: Targeting PARP1 beyond human malignancy
Chiho Kim, Chuo Chen, Yonghao Yu
Cell chemical biology (2021) Vol. 28, Iss. 4, pp. 456-462
Open Access | Times Cited: 26
The beauty of ADP-ribosylation: versatility in every link and organelle
Victória Chaves Ribeiro, Jennifer Wirtz, Orsolya Leidecker
BIOspektrum (2025) Vol. 31, Iss. 3, pp. 258-261
Open Access
Poly(ADP-Ribosylation) in Age-Related Neurological Disease
Leeanne McGurk, Olivia M. Rifai, Nancy M. Bonini
Trends in Genetics (2019) Vol. 35, Iss. 8, pp. 601-613
Open Access | Times Cited: 28
Gas-Phase Fragmentation of ADP-Ribosylated Peptides: Arginine-Specific Side-Chain Losses and Their Implication in Database Searches
Peter Gehrig, Kathrin Nowak, Christian Panse, et al.
Journal of the American Society for Mass Spectrometry (2020) Vol. 32, Iss. 1, pp. 157-168
Closed Access | Times Cited: 27
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: 11
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
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