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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:

Nuclear ADP-Ribosylation and Its Role in Chromatin Plasticity, Cell Differentiation, and Epigenetics
Michael O. Hottiger
Annual Review of Biochemistry (2015) Vol. 84, Iss. 1, pp. 227-263
Open Access | Times Cited: 216

Showing 1-25 of 216 citing articles:

Laying a trap to kill cancer cells: PARP inhibitors and their mechanisms of action
Yves Pommier, Mark J. O’Connor, Johann S. de Bono
Science Translational Medicine (2016) Vol. 8, Iss. 362
Closed Access | Times Cited: 652
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
Poly(ADP-Ribose) Prevents Pathological Phase Separation of TDP-43 by Promoting Liquid Demixing and Stress Granule Localization
Leeanne McGurk, Edward Gomes, Lin Guo, et al.
Molecular Cell (2018) Vol. 71, Iss. 5, pp. 703-717.e9
Open Access | Times Cited: 375
Born to run: control of transcription elongation by RNA polymerase II
Fei Chen, Edwin R. Smith, Ali Shilatifard
Nature Reviews Molecular Cell Biology (2018) Vol. 19, Iss. 7, pp. 464-478
Open Access | Times Cited: 363
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
Inside HDACs with more selective HDAC inhibitors
Joëlle Roche, Philìppe Bertrand
European Journal of Medicinal Chemistry (2016) Vol. 121, pp. 451-483
Closed Access | Times Cited: 294
Functions of PARylation in DNA Damage Repair Pathways
Huiting Wei, Xiaochun Yu
Genomics Proteomics & Bioinformatics (2016) Vol. 14, Iss. 3, pp. 131-139
Open Access | Times Cited: 263
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
The role of poly ADP-ribosylation in the first wave of DNA damage response
Chao Liu, Aditi Vyas, Muzaffer Ahmad Kassab, et al.
Nucleic Acids Research (2017) Vol. 45, Iss. 14, pp. 8129-8141
Open Access | Times Cited: 198
Ubiquitin Modification by the E3 Ligase/ADP-Ribosyltransferase Dtx3L/Parp9
Chunsong Yang, Kasey Jividen, Adam Spencer, et al.
Molecular Cell (2017) Vol. 66, Iss. 4, pp. 503-516.e5
Open Access | Times Cited: 191
The impact of PARPs and ADP-ribosylation on inflammation and host–pathogen interactions
Anthony R. Fehr, Sasha A. Singh, Catherine M. Kerr, et al.
Genes & Development (2020) Vol. 34, Iss. 5-6, pp. 341-359
Open Access | Times Cited: 188
Epigenome Editing: State of the Art, Concepts, and Perspectives
Goran Kungulovski, Albert Jeltsch
Trends in Genetics (2015) Vol. 32, Iss. 2, pp. 101-113
Closed Access | Times Cited: 185
PARP1 and PARP2 stabilise replication forks at base excision repair intermediates through Fbh1-dependent Rad51 regulation
George E. Ronson, Ann Liza Piberger, Martin R. Higgs, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 179
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
Oxidative Metabolism Drives Immortalization of Neural Stem Cells during Tumorigenesis
François Bonnay, Ana Veloso, Victoria Steinmann, et al.
Cell (2020) Vol. 182, Iss. 6, pp. 1490-1507.e19
Open Access | Times Cited: 148
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
The conserved macrodomains of the non-structural proteins of Chikungunya virus and other pathogenic positive strand RNA viruses function as mono-ADP-ribosylhydrolases
Laura Eckei, Sarah Krieg, Mareike Bütepage, et al.
Scientific Reports (2017) Vol. 7, Iss. 1
Open Access | Times Cited: 134
The Enigmatic Function of PARP1: From PARylation Activity to PAR Readers
Tatiana Kamaletdinova, Zahra Fanaei‐Kahrani, Zhao‐Qi Wang
Cells (2019) Vol. 8, Iss. 12, pp. 1625-1625
Open Access | Times Cited: 133
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
Catalytic-Independent Functions of PARP-1 Determine Sox2 Pioneer Activity at Intractable Genomic Loci
Ziying Liu, W. Lee Kraus
Molecular Cell (2017) Vol. 65, Iss. 4, pp. 589-603.e9
Open Access | Times Cited: 116
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
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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