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:

Molecular basis for DarT ADP-ribosylation of a DNA base
M. Schuller, Rachel E. Butler, A. Ariza, et al.
Nature (2021) Vol. 596, Iss. 7873, pp. 597-602
Closed Access | Times Cited: 58

Showing 1-25 of 58 citing articles:

Toxin-Antitoxin Systems as Phage Defense Elements
Michele LeRoux, Michael T. Laub
Annual Review of Microbiology (2022) Vol. 76, Iss. 1, pp. 21-43
Closed Access | Times Cited: 143

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

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

The CD38 glycohydrolase and the NAD sink: implications for pathological conditions
Julianna D. Zeidler, Kelly A. Hogan, Guillermo Agorrody, et al.
AJP Cell Physiology (2022) Vol. 322, Iss. 3, pp. C521-C545
Open Access | Times Cited: 49

Modular antibodies reveal DNA damage-induced mono-ADP-ribosylation as a second wave of PARP1 signaling
Edoardo José Longarini, Helen Dauben, Carolina Locatelli, et al.
Molecular Cell (2023) Vol. 83, Iss. 10, pp. 1743-1760.e11
Open Access | Times Cited: 38

PARP14 is a PARP with both ADP-ribosyl transferase and hydrolase activities
N Mimica Dukic, Øyvind Strømland, Jonas D. Elsborg, et al.
Science Advances (2023) Vol. 9, Iss. 37
Open Access | Times Cited: 38

Molecular basis for the reversible ADP-ribosylation of guanosine bases
M. Schuller, Roberto Raggiaschi, Petra Mikolčević, et al.
Molecular Cell (2023) Vol. 83, Iss. 13, pp. 2303-2315.e6
Open Access | Times Cited: 28

DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on nucleic acids
Kang Zhu, Marcin J. Suskiewicz, Chatrin Chatrin, et al.
Nucleic Acids Research (2023) Vol. 52, Iss. 2, pp. 801-815
Open Access | Times Cited: 24

Retron-Eco1 assembles NAD+-hydrolyzing filaments that provide immunity against bacteriophages
Arturo Carabias, Sarah Camara-Wilpert, Mario Rodríguez Mestre, et al.
Molecular Cell (2024) Vol. 84, Iss. 11, pp. 2185-2202.e12
Closed Access | Times Cited: 13

Mechanism of phage sensing and restriction by toxin-antitoxin-chaperone systems
Toomas Mets, Tatsuaki Kurata, Karin Ernits, et al.
Cell Host & Microbe (2024) Vol. 32, Iss. 7, pp. 1059-1073.e8
Open Access | Times Cited: 13

In silico characterization of defense system hotspots in Acinetobacter spp.
Wen‐Jing Yi, Ning Zhu, Zhenwei Peng, et al.
Communications Biology (2025) Vol. 8, Iss. 1
Open Access | Times Cited: 1

Phages carry orphan antitoxin-like enzymes to neutralize the DarTG1 toxin-antitoxin defense system
Anna Johannesman, Leila C. Awasthi, Nico A Carlson, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 1

β-NAD as a building block in natural product biosynthesis
Lena Barra, Takayoshi Awakawa, Kohei Shirai, et al.
Nature (2021) Vol. 600, Iss. 7890, pp. 754-758
Closed Access | Times Cited: 50

An ADP-ribosyltransferase toxin kills bacterial cells by modifying structured non-coding RNAs
Nathan P. Bullen, David Sychantha, Stephanie S. Thang, et al.
Molecular Cell (2022) Vol. 82, Iss. 18, pp. 3484-3498.e11
Open Access | Times Cited: 38

Legionella metaeffector MavL reverses ubiquitin ADP-ribosylation via a conserved arginine-specific macrodomain
Zhengrui Zhang, Jiaqi Fu, J.G.M. Rack, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 6

Beyond protein modification: the rise of non-canonical ADP-ribosylation
M. Schuller, Ivan Ahel
Biochemical Journal (2022) Vol. 479, Iss. 4, pp. 463-477
Open Access | Times Cited: 27

Deregulated DNA ADP-ribosylation impairs telomere replication
Anne R. Wondisford, Junyeop Lee, Robert Lu, et al.
Nature Structural & Molecular Biology (2024) Vol. 31, Iss. 5, pp. 791-800
Open Access | Times Cited: 5

TARG1 protects against toxic DNA ADP-ribosylation
Callum Tromans‐Coia, Andrea Sanchi, Giuliana Katharina Moeller, et al.
Nucleic Acids Research (2021) Vol. 49, Iss. 18, pp. 10477-10492
Open Access | Times Cited: 29

Mammalian N1-adenosine PARylation is a reversible DNA modification
Michael U. Musheev, Lars Schomacher, Amitava Basu, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 22

DarT-mediated mtDNA damage induces dynamic reorganization and selective segregation of mitochondria
Nitish Dua, Akshaya Seshadri, Anjana Badrinarayanan
The Journal of Cell Biology (2022) Vol. 221, Iss. 10
Open Access | Times Cited: 19

Specificity of DNA ADP-Ribosylation Reversal by NADARs
Bara Cihlova, Yang Lu, Andreja Mikoč, et al.
Toxins (2024) Vol. 16, Iss. 5, pp. 208-208
Open Access | Times Cited: 4

Discovery of reversing enzymes for RNA ADP-ribosylation reveals a possible defence module against toxic attack
Yang Lu, M. Schuller, Nathan P. Bullen, et al.
Nucleic Acids Research (2025) Vol. 53, Iss. 4
Open Access

Simultaneous ultrasensitive ADP and ATP quantification based on CRISPR/Cas12a integrated ZIF-90@Ag3AuS2@Fe3O4 nanocomposites
Yingwen Wang, Dun Zhang, Yan Zeng, et al.
Biosensors and Bioelectronics (2022) Vol. 218, pp. 114784-114784
Closed Access | Times Cited: 18

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