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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:

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: 222

Showing 1-25 of 222 citing articles:

Post-translational regulation of ubiquitin signaling
Lei Song, Zhao‐Qing Luo
The Journal of Cell Biology (2019) Vol. 218, Iss. 6, pp. 1776-1786
Open Access | Times Cited: 270
ADP‐ribosyltransferases, an update on function and nomenclature
Bernhard Lüscher, Ivan Ahel, Matthias Altmeyer, et al.
FEBS Journal (2021) Vol. 289, Iss. 23, pp. 7399-7410
Open Access | Times Cited: 234
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: 206
Targeting protein modifications in metabolic diseases: molecular mechanisms and targeted therapies
Xiumei Wu, Mengyun Xu, M. Geng, et al.
Signal Transduction and Targeted Therapy (2023) Vol. 8, Iss. 1
Open Access | Times Cited: 96
Targeting PARP proteins in acute leukemia: DNA damage response inhibition and therapeutic strategies
Antonella Padella, Andrea Ghelli Luserna di Rorà, Giovanni Marconi, et al.
Journal of Hematology & Oncology (2022) Vol. 15, Iss. 1
Open Access | Times Cited: 69
ADP-ribosylation from molecular mechanisms to therapeutic implications
Marcin J. Suskiewicz, Evgeniia Prokhorova, J.G.M. Rack, et al.
Cell (2023) Vol. 186, Iss. 21, pp. 4475-4495
Open Access | Times Cited: 68
Design, Synthesis, and Structure–Activity Relationship of Novel Pyridazinone-Based PARP7/HDACs Dual Inhibitors for Elucidating the Relationship between Antitumor Immunity and HDACs Inhibition
Ji‐Long Duan, Chenchen Wang, Yinghui Yuan, et al.
Journal of Medicinal Chemistry (2024) Vol. 67, Iss. 6, pp. 4950-4976
Closed Access | Times Cited: 32
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: 139
Post-translational modifications of Hsp70 family proteins: Expanding the chaperone code
Nitika Nitika, Corey M. Porter, Andrew W. Truman, et al.
Journal of Biological Chemistry (2020) Vol. 295, Iss. 31, pp. 10689-10708
Open Access | Times Cited: 136
Poly(ADP-ribose): A Dynamic Trigger for Biomolecular Condensate Formation
Anthony K. L. Leung
Trends in Cell Biology (2020) Vol. 30, Iss. 5, pp. 370-383
Open Access | Times Cited: 127
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: 103
Impaired albumin function: a novel potential indicator for liver function damage?
Lejia Sun, Huanhuan Yin, Meixi Liu, et al.
Annals of Medicine (2019) Vol. 51, Iss. 7-8, pp. 333-344
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
Nuclear poly(ADP-ribose) activity is a therapeutic target in amyotrophic lateral sclerosis
Leeanne McGurk, Jelena Mojsilovic‐Petrovic, Vivianna M. Van Deerlin, et al.
Acta Neuropathologica Communications (2018) Vol. 6, Iss. 1
Open Access | Times Cited: 97
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
Regulation of Glucose Metabolism by NAD+ and ADP-Ribosylation
Ann-Katrin Hopp, Patrick Grüter, Michael O. Hottiger
Cells (2019) Vol. 8, Iss. 8, pp. 890-890
Open Access | Times Cited: 89
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: 89
Visfatin: A Possible Role in Cardiovasculo-Metabolic Disorders
Ali Dakroub, Suzanne A. Nasser, Nour K. Younis, et al.
Cells (2020) Vol. 9, Iss. 11, pp. 2444-2444
Open Access | Times Cited: 87
ADP-ribosylation of DNA and RNA
Joséphine Groslambert, Evgeniia Prokhorova, Ivan Ahel
DNA repair (2021) Vol. 105, pp. 103144-103144
Open Access | Times Cited: 79
Viral macrodomains: a structural and evolutionary assessment of the pharmacological potential
J.G.M. Rack, Valentina Zorzini, Zihan Zhu, et al.
Open Biology (2020) Vol. 10, Iss. 11
Open Access | Times Cited: 76
Metabolism and the Epigenome: A Dynamic Relationship
Spencer A. Haws, Cassandra M. Leech, John M. Denu
Trends in Biochemical Sciences (2020) Vol. 45, Iss. 9, pp. 731-747
Open Access | Times Cited: 70
ADP-ribosylation of RNA and DNA: fromin vitrocharacterization toin vivofunction
Lisa Weixler, Katja Schäringer, Jeffrey Momoh, et al.
Nucleic Acids Research (2021) Vol. 49, Iss. 7, pp. 3634-3650
Open Access | Times Cited: 67
Identifying Poly(ADP-ribose)-Binding Proteins with Photoaffinity-Based Proteomics
Morgan Dasovich, Morgan Q. Beckett, Scott Bailey, et al.
Journal of the American Chemical Society (2021) Vol. 143, Iss. 8, pp. 3037-3042
Open Access | Times Cited: 61
The CD38 glycohydrolase and the NAD sink: implications for pathological conditions
Julianna D. Zeidler, Kelly A. Hogan, Guillermo Agorrody, et al.
AJP Cell Physiology (2022) Vol. 322, Iss. 3, pp. C521-C545
Open Access | Times Cited: 47
PARPs and ADP-ribosylation: Deciphering the complexity with molecular tools
Morgan Dasovich, Anthony K. L. Leung
Molecular Cell (2023) Vol. 83, Iss. 10, pp. 1552-1572
Open Access | Times Cited: 33
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