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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:

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

Showing 1-25 of 226 citing articles:

The multifaceted roles of PARP1 in DNA repair and chromatin remodelling
Arnab Ray Chaudhuri, André Nussenzweig
Nature Reviews Molecular Cell Biology (2017) Vol. 18, Iss. 10, pp. 610-621
Open Access | Times Cited: 1366
Ubiquitin Ligases: Structure, Function, and Regulation
Ning Zheng, Nitzan Shabek
Annual Review of Biochemistry (2017) Vol. 86, Iss. 1, pp. 129-157
Closed Access | Times Cited: 1207
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
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
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
Phase separation of 53 BP 1 determines liquid‐like behavior of DNA repair compartments
Sinan Kilic, Aleksandra Lezaja, Marco Gatti, et al.
The EMBO Journal (2019) Vol. 38, Iss. 16
Open Access | Times Cited: 369
Properties of Stress Granule and P-Body Proteomes
Ji‐Young Youn, Boris J.A. Dyakov, Jianping Zhang, et al.
Molecular Cell (2019) Vol. 76, Iss. 2, pp. 286-294
Open Access | Times Cited: 361
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
Are aberrant phase transitions a driver of cellular aging?
Simon Alberti, Anthony A. Hyman
BioEssays (2016) Vol. 38, Iss. 10, pp. 959-968
Open Access | Times Cited: 283
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
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
PARP-1 Activation Directs FUS to DNA Damage Sites to Form PARG-Reversible Compartments Enriched in Damaged DNA
Anastasia S. Singatulina, Loïc Hamon, Maria V. Sukhanova, et al.
Cell Reports (2019) Vol. 27, Iss. 6, pp. 1809-1821.e5
Open Access | Times Cited: 191
The expanding universe of PARP1-mediated molecular and therapeutic mechanisms
Dan Huang, W. Lee Kraus
Molecular Cell (2022) Vol. 82, Iss. 12, pp. 2315-2334
Open Access | Times Cited: 158
Liquid–liquid phase separation in tumor biology
Xuhui Tong, Rong Tang, Jin Xu, et al.
Signal Transduction and Targeted Therapy (2022) Vol. 7, Iss. 1
Open Access | Times Cited: 136
Inhibitors of PARP: Number crunching and structure gazing
Johannes Rudolph, Karen Jung, Karolin Luger
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 11
Open Access | Times Cited: 85
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: 72
A New Phase of Networking: The Molecular Composition and Regulatory Dynamics of Mammalian Stress Granules
Seán Millar, Jie Huang, Karl J. Schreiber, et al.
Chemical Reviews (2023) Vol. 123, Iss. 14, pp. 9036-9064
Open Access | Times Cited: 62
PARP14 and PARP9/DTX3L regulate interferon-induced ADP-ribosylation
Pulak Kar, Chatrin Chatrin, N Mimica Dukic, et al.
The EMBO Journal (2024) Vol. 43, Iss. 14, pp. 2929-2953
Open Access | Times Cited: 16
PARP2 mediates branched poly ADP-ribosylation in response to DNA damage
Qian Chen, Muzaffer Ahmad Kassab, Françoise Dantzer, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 147
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
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
Synthetic viability by BRCA2 and PARP1/ARTD1 deficiencies
Xia Ding, Arnab Ray Chaudhuri, Elsa Callén, et al.
Nature Communications (2016) Vol. 7, Iss. 1
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
Structural Insights Into TDP-43 and Effects of Post-translational Modifications
Liberty François‐Moutal, Samantha Perez‐Miller, David D. Scott, et al.
Frontiers in Molecular Neuroscience (2019) Vol. 12
Open Access | Times Cited: 121
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