Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

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:

ELTA: Enzymatic Labeling of Terminal ADP-Ribose
Yoshinari Ando, Elad Elkayam, Robert Lyle McPherson, et al.
Molecular Cell (2019) Vol. 73, Iss. 4, pp. 845-856.e5
Open Access | Times Cited: 65

Showing 1-25 of 65 citing articles:

The DarTG toxin-antitoxin system provides phage defence by ADP-ribosylating viral DNA
Michele LeRoux, Sriram Srikant, Gabriella I. C. Teodoro, et al.
Nature Microbiology (2022) Vol. 7, Iss. 7, pp. 1028-1040
Open Access | Times Cited: 131
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: 130
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
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: 90
Stress granule formation, disassembly, and composition are regulated by alphavirus ADP-ribosylhydrolase activity
Aravinth Kumar Jayabalan, Srivathsan Adivarahan, Aakash Koppula, et al.
Proceedings of the National Academy of Sciences (2021) Vol. 118, Iss. 6
Open Access | Times Cited: 73
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: 63
Poly(ADP-ribose) drives condensation of FUS via a transient interaction
Kevin Rhine, Morgan Dasovich, Joseph Yoniles, et al.
Molecular Cell (2022) Vol. 82, Iss. 5, pp. 969-985.e11
Open Access | Times Cited: 61
HPF1 and nucleosomes mediate a dramatic switch in activity of PARP1 from polymerase to hydrolase
Johannes Rudolph, Genevieve Roberts, Uma M. Muthurajan, et al.
eLife (2021) Vol. 10
Open Access | Times Cited: 60
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: 34
Flap endonuclease 1 repairs DNA-protein cross-links via ADP-ribosylation–dependent mechanisms
Yilun Sun, Lisa M. Jenkins, Lara H. El Touny, et al.
Science Advances (2025) Vol. 11, Iss. 2
Open Access | Times Cited: 1
PARPs and ADP-ribosylation-mediated biomolecular condensates: determinants, dynamics, and disease implications
Hongrui Liu, Meenakshi Pillai, Anthony K. L. Leung
Trends in Biochemical Sciences (2025)
Closed Access | Times Cited: 1
Both ADP-Ribosyl-Binding and Hydrolase Activities of the Alphavirus nsP3 Macrodomain Affect Neurovirulence in Mice
Rachy Abraham, Robert Lyle McPherson, Morgan Dasovich, et al.
mBio (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 56
MARTs and MARylation in the Cytosol: Biological Functions, Mechanisms of Action, and Therapeutic Potential
Sridevi Challa, MiKayla S Stokes, W. Lee Kraus
Cells (2021) Vol. 10, Iss. 2, pp. 313-313
Open Access | Times Cited: 56
Why structure and chain length matter: on the biological significance underlying the structural heterogeneity of poly(ADP-ribose)
Julia M. Reber, Aswin Mangerich
Nucleic Acids Research (2021) Vol. 49, Iss. 15, pp. 8432-8448
Open Access | Times Cited: 45
PAR recognition by PARP1 regulates DNA‐dependent activities and independently stimulates catalytic activity of PARP1
Waghela Deeksha, Suman Abhishek, Eerappa Rajakumara
FEBS Journal (2023) Vol. 290, Iss. 21, pp. 5098-5113
Open Access | Times Cited: 18
PARP1 condensates differentially partition DNA repair proteins and enhance DNA ligation
Christopher Chin Sang, Gaelen Moore, Maria Tereshchenko, et al.
EMBO Reports (2024)
Closed Access | Times Cited: 8
ADPriboDB 2.0: an updated database of ADP-ribosylated proteins
Vinay Ayyappan, Ricky Wat, Calvin Barber, et al.
Nucleic Acids Research (2020) Vol. 49, Iss. D1, pp. D261-D265
Open Access | Times Cited: 42
A molecular toolbox for ADP-ribosyl binding proteins
Sven T. Sowa, Albert Galera‐Prat, Sarah Wazir, et al.
Cell Reports Methods (2021) Vol. 1, Iss. 8, pp. 100121-100121
Open Access | Times Cited: 33
Mitochondrial PARP1 regulates NAD+-dependent poly ADP-ribosylation of mitochondrial nucleoids
Jong-Hyuk Lee, Mansoor Hussain, Edward W. Kim, et al.
Experimental & Molecular Medicine (2022) Vol. 54, Iss. 12, pp. 2135-2147
Open Access | Times Cited: 24
Regulation of Biomolecular Condensates by Poly(ADP-ribose)
Kevin Rhine, Hana M. Odeh, James Shorter, et al.
Chemical Reviews (2023) Vol. 123, Iss. 14, pp. 9065-9093
Closed Access | Times Cited: 16
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
Poly(ADP-ribose)-dependent ubiquitination and its clinical implications
Christina A. Vivelo, Vinay Ayyappan, Anthony K. L. Leung
Biochemical Pharmacology (2019) Vol. 167, pp. 3-12
Open Access | Times Cited: 40
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
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
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
Page 1 - Next Page

Scroll to top