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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:

Preserving ester-linked modifications reveals glutamate and aspartate mono-ADP-ribosylation by PARP1 and its reversal by PARG
Edoardo José Longarini, Ivan Matić
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 12

Showing 12 citing articles:

C(sp3)–H Carboxylation via Carbene/Photoredox Cooperative Catalysis
Cullen R. Schull, Jing Cao, Sophia R. Mitton-Fry, et al.
ACS Catalysis (2025) Vol. 15, Iss. 2, pp. 1287-1293
Closed Access
PARP12-mediated ADP-ribosylation contributes to breast cancer cell fate by regulating AKT activation and DNA-damage response
Anupama Pavithran, Maria Matarese, Barbara Morone, et al.
Cellular and Molecular Life Sciences (2025) Vol. 82, Iss. 1
Open Access
Ubiquitin is directly linked via an ester to protein-conjugated mono-ADP-ribose
Daniel S. Bejan, Rachel E. Lacoursiere, Jonathan N. Pruneda, et al.
The EMBO Journal (2025)
Open Access
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: 4
Regulation of PARP1/2 and the tankyrases: emerging parallels
Matthew Jessop, Benjamin J. Broadway, Katy Miller, et al.
Biochemical Journal (2024) Vol. 481, Iss. 17, pp. 1097-1123
Open Access | Times Cited: 1
Reversal of tyrosine-linked ADP-ribosylation by ARH3 and PARG
J.G.M. Rack, Jim Voorneveld, Edoardo José Longarini, et al.
Journal of Biological Chemistry (2024), pp. 107838-107838
Open Access | Times Cited: 1
Discovery of ester-linked ubiquitylation of PARP10 mono-ADP-ribosylation in cells: a dual post-translational modification on Glu/Asp side chains
Daniel S. Bejan, Rachel E. Lacoursiere, Jonathan N. Pruneda, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Closed Access
PARP14 mediated SQSTM1/p62 cysteine ADP-ribosylation is counteracted by the SARS-CoV-2 macrodomain
David Kubon, Deena M. Leslie Pedrioli, Michael O. Hottiger
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Closed Access
Mono‐ADP‐ribosylation of peptides: an overview of synthetic and chemoenzymatic methodologies
Hugo Minnee, Jeroen D. C. Codée, Dmitri V. Filippov
ChemBioChem (2024)
Open Access
Single-nucleosome imaging reveals principles of transient multiscale chromatin unfolding triggered by histone ADP-ribosylation at DNA lesions
Fabiola García Fernández, Catherine Chapuis, J.H. Park, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
An ADPRS variant disrupts ARH3 stability and subcellular localization in children with neurodegeneration and respiratory failure
Maxwell Bannister, Sarah J. Bray, Anjali Aggarwal, et al.
Human Genetics and Genomics Advances (2024) Vol. 6, Iss. 1, pp. 100386-100386
Open Access
Suppression of ADP-ribosylation reversal triggers cell vulnerability to alkylating agents
Rocco Caggiano, Evgeniia Prokhorova, Lena Duma, et al.
Neoplasia (2024) Vol. 59, pp. 101092-101092
Closed Access
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