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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:

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

Showing 51-75 of 129 citing articles:

Switch-like compaction of poly(ADP-ribose) upon cation binding
Mohsen Badiee, Adam Kenet, Laura R. Ganser, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 19
Open Access | Times Cited: 13
Coarse-Grained Modeling of Liquid–Liquid Phase Separation in Cells: Challenges and Opportunities
Shaokang Shi, Zhao Li, Zhong‐Yuan Lu
The Journal of Physical Chemistry Letters (2024) Vol. 15, Iss. 28, pp. 7280-7287
Closed Access | Times Cited: 5
PARP enzyme de novo synthesis of protein-free poly(ADP-ribose)
Marie-France Langelier, Manija Mirhasan, Karine Gilbert, et al.
Molecular Cell (2024)
Closed Access | Times Cited: 5
PARPs’ impact on base excision DNA repair
Olga I. Lavrik
DNA repair (2020) Vol. 93, pp. 102911-102911
Closed Access | Times Cited: 35
Uncovering the Invisible: Mono-ADP-ribosylation Moved into the Spotlight
Ann-Katrin Hopp, Michael O. Hottiger
Cells (2021) Vol. 10, Iss. 3, pp. 680-680
Open Access | Times Cited: 28
14-3-3 Proteins are Potential Regulators of Liquid–Liquid Phase Separation
Xianlong Huang, Zhiwen Zheng, Yixin Wu, et al.
Cell Biochemistry and Biophysics (2022) Vol. 80, Iss. 2, pp. 277-293
Open Access | Times Cited: 22
Repair Foci as Liquid Phase Separation: Evidence and Limitations
Judith Miné-Hattab, Siyu Liu, Angela Taddei
Genes (2022) Vol. 13, Iss. 10, pp. 1846-1846
Open Access | Times Cited: 19
Influence of chain length and branching on poly(ADP-ribose)–protein interactions
Tobias Löffler, Annika Krüger, Peyman Zirak, et al.
Nucleic Acids Research (2023) Vol. 51, Iss. 2, pp. 536-552
Open Access | Times Cited: 11
Mesoscale molecular assembly is favored by the active, crowded cytoplasm
Tong Shu, Gaurav Mitra, Jonathan Alberts, et al.
PRX Life (2024) Vol. 2, Iss. 3
Open Access | Times Cited: 4
Cation-induced intramolecular coil-to-globule transition in poly(ADP-ribose)
Tong Wang, Kush Coshic, Mohsen Badiee, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 4
Regulation of stress granule maturation and dynamics by poly(ADP-ribose) interaction with PARP13
Shang-Jung Cheng, Temitope Gafaar, Jijin R. A. Kuttiyatveetil, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
Insight into the function of the Golgi membrane protein GOLM1 in cholangiocytes through interactomic analysis
Meghana Nagaraj, Emmagouni Sharath Kumar Goud, Vaishali Chaurasiya, et al.
FEBS Letters (2025)
Closed Access
dELTA-MS: A Mass Spectrometry-Based Proteomics Approach for Identifying ADP-Ribosylation Sites and Forms
Isabel Uribe, Emily Zahn, Richard Searfoss, et al.
Journal of Proteome Research (2025)
Closed Access
Interferon-induced PARP14-mediated ADP-ribosylation in p62 bodies requires the ubiquitin-proteasome system
Rameez Raja, Banhi Biswas, Rachy Abraham, et al.
The EMBO Journal (2025)
Open Access
A pH-Centric Model of Nucleolar Activity and Regulation
Diego Detrés, Adriana Camacho-Badillo, Eliezer Calo
Journal of Molecular Biology (2025), pp. 169136-169136
Closed Access
Adenosine diphosphate-ribosylation greatly affects proteins function: a focus on neurodegenerative diseases
Chaowen Huang, Hong Xiao, Yang Yang, et al.
Frontiers in Aging Neuroscience (2025) Vol. 17
Open Access
Biochemical Timekeeping Via Reentrant Phase Transitions
Bede Portz, James Shorter
Journal of Molecular Biology (2020) Vol. 433, Iss. 12, pp. 166794-166794
Open Access | Times Cited: 31
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
PARP1 condensates differentially partition DNA repair proteins and enhance DNA ligation
Christopher Chin Sang, Gaelen Moore, Maria Tereshchenko, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 3
PARG is essential for Polθ-mediated DNA end-joining by removing repressive poly-ADP-ribose marks
Umeshkumar Vekariya, Leonid Minakhin, Gurushankar Chandramouly, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 3
Divalent and multivalent cations control liquid-like assembly of poly(ADP-ribosyl)ated PARP1 into multimolecular associates in vitro
Maria V. Sukhanova, Rashid O. Anarbaev, Ekaterina A. Maltseva, et al.
Communications Biology (2024) Vol. 7, Iss. 1
Open Access | Times Cited: 3
Phase Separation of FUS with Poly(ADP-ribosyl)ated PARP1 Is Controlled by Polyamines, Divalent Metal Cations, and Poly(ADP-ribose) Structure
Maria V. Sukhanova, Rashid O. Anarbaev, Konstantin N. Naumenko, et al.
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 22, pp. 12445-12445
Open Access | Times Cited: 3
SERBP1 interacts with PARP1 and is present in PARylation-dependent protein complexes regulating splicing, cell division, and ribosome biogenesis
Kira Breunig, Xiufen Lei, Mauro Montalbano, et al.
(2025)
Open Access
Emerging connections: Poly(ADP-ribose), FET proteins and RNA in the regulation of DNA damage condensates
Silvia Lombardi, Mara Zilocchi, Roland Nicsanu, et al.
DNA repair (2025), pp. 103846-103846
Open Access
Mechanisms governing PARP expression, localization, and activity in cells
Daniel J. Sanderson, Michael S. Cohen
Critical Reviews in Biochemistry and Molecular Biology (2020) Vol. 55, Iss. 6, pp. 541-554
Closed Access | Times Cited: 27

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