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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:

The Promise of Proteomics for the Study of ADP-Ribosylation
Casey M. Daniels, Shao-En Ong, Anthony K. L. Leung
Molecular Cell (2015) Vol. 58, Iss. 6, pp. 911-924
Open Access | Times Cited: 193

Showing 1-25 of 193 citing articles:

PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes
Rebecca Gupte, Ziying Liu, W. Lee Kraus
Genes & Development (2017) Vol. 31, Iss. 2, pp. 101-126
Open Access | Times Cited: 618
Biology of Poly(ADP-Ribose) Polymerases: The Factotums of Cell Maintenance
Péter Bai
Molecular Cell (2015) Vol. 58, Iss. 6, pp. 947-958
Open Access | Times Cited: 415
Poly(ADP-ribosyl)ation by PARP1: reaction mechanism and regulatory proteins
Elizaveta E. Alemasova, Olga I. Lavrik
Nucleic Acids Research (2019) Vol. 47, Iss. 8, pp. 3811-3827
Open Access | Times Cited: 387
Chemical genetic discovery of PARP targets reveals a role for PARP-1 in transcription elongation
Bryan A. Gibson, Yajie Zhang, Hong Jiang, et al.
Science (2016) Vol. 353, Iss. 6294, pp. 45-50
Open Access | Times Cited: 341
Phase Separation: Linking Cellular Compartmentalization to Disease
Adriano Aguzzi, Matthias Altmeyer
Trends in Cell Biology (2016) Vol. 26, Iss. 7, pp. 547-558
Closed Access | Times Cited: 321
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
Phosphoribosylation of Ubiquitin Promotes Serine Ubiquitination and Impairs Conventional Ubiquitination
Sagar Bhogaraju, Sissy Kalayil, Yaobin Liu, et al.
Cell (2016) Vol. 167, Iss. 6, pp. 1636-1649.e13
Open Access | Times Cited: 281
Insights into the biogenesis, function, and regulation of ADP-ribosylation
Michael S. Cohen, Paul Chang
Nature Chemical Biology (2018) Vol. 14, Iss. 3, pp. 236-243
Open Access | Times Cited: 272
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: 238
Readers of poly(ADP-ribose): designed to be fit for purpose
Federico Teloni, Matthias Altmeyer
Nucleic Acids Research (2015) Vol. 44, Iss. 3, pp. 993-1006
Open Access | Times Cited: 226
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: 223
Serine is a new target residue for endogenous ADP-ribosylation on histones
Orsolya Leidecker, Juán José Bonfiglio, Thomas Colby, et al.
Nature Chemical Biology (2016) Vol. 12, Iss. 12, pp. 998-1000
Open Access | Times Cited: 219
Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue
Rita Martello, Mario Leutert, Stephanie Jungmichel, et al.
Nature Communications (2016) Vol. 7, Iss. 1
Open Access | Times Cited: 212
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
ADP-ribosylhydrolase activity of Chikungunya virus macrodomain is critical for virus replication and virulence
Robert Lyle McPherson, Rachy Abraham, Easwaran Sreekumar, et al.
Proceedings of the National Academy of Sciences (2017) Vol. 114, Iss. 7, pp. 1666-1671
Open Access | Times Cited: 176
Multi-omics approaches for biomarker discovery in early ovarian cancer diagnosis
Yinan Xiao, Meiyu Bi, Hongyan Guo, et al.
EBioMedicine (2022) Vol. 79, pp. 104001-104001
Open Access | Times Cited: 122
PARPs and ADP-Ribosylation: 50 Years … and Counting
W. Lee Kraus
Molecular Cell (2015) Vol. 58, Iss. 6, pp. 902-910
Open Access | Times Cited: 166
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
Viral Macro Domains Reverse Protein ADP-Ribosylation
Changqing Li, Yannick Debing, Gytis Jankevicius, et al.
Journal of Virology (2016) Vol. 90, Iss. 19, pp. 8478-8486
Open Access | Times Cited: 158
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
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
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: 129
PARPs and ADP-ribosylation in RNA biology: from RNA expression and processing to protein translation and proteostasis
Dae-Seok Kim, Sridevi Challa, Aarin Jones, et al.
Genes & Development (2020) Vol. 34, Iss. 5-6, pp. 302-320
Open Access | Times Cited: 122
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
Use of poly ADP-ribose polymerase [PARP] inhibitors in cancer cells bearing DDR defects: the rationale for their inclusion in the clinic
Aniello Cerrato, Francesco Morra, Angela Celetti
Journal of Experimental & Clinical Cancer Research (2016) Vol. 35, Iss. 1
Open Access | Times Cited: 112
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