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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:

SUMO-activated target traps (SATTs) enable the identification of a comprehensive E3-specific SUMO proteome
Daniel Salas‐Lloret, Nicolette S. Jansen, Easa Nagamalleswari, et al.
Science Advances (2023) Vol. 9, Iss. 31
Open Access | Times Cited: 12

Showing 12 citing articles:

BioE3 identifies specific substrates of ubiquitin E3 ligases
Orhi Barroso‐Gomila, Laura Merino‐Cacho, Veronica Muratore, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 23
SUMO and the DNA damage response
Jai S. Bhachoo, Alexander J. Garvin
Biochemical Society Transactions (2024) Vol. 52, Iss. 2, pp. 773-792
Open Access | Times Cited: 6
dsRNAi-mediated silencing of PIAS2beta specifically kills anaplastic carcinomas by mitotic catastrophe
Joana S. Rodrigues, Miguel Chenlo, Susana B. Bravo, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 5
BRCA1/BARD1 ubiquitinates PCNA in unperturbed conditions to promote continuous DNA synthesis
Daniel Salas‐Lloret, Néstor García‐Rodríguez, Emily Soto-Hidalgo, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 5
Cullin-RING ligase BioE3 reveals molecular-glue-induced neosubstrates and rewiring of the endogenous Cereblon ubiquitome
Laura Merino‐Cacho, Orhi Barroso‐Gomila, Mónica Pozo-Rodríguez, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2025)
Open Access
Cullin-RING ligase BioE3 reveals molecular-glue-induced neosubstrates and rewiring of the endogenous Cereblon ubiquitome
Laura Merino‐Cacho, Orhi Barroso‐Gomila, Mónica Pozo-Rodríguez, et al.
Cell Communication and Signaling (2025) Vol. 23, Iss. 1
Open Access
SUMO2/3 conjugation of TDP-43 protects against aggregation
Enza Maria Verde, Francesco Antoniani, Laura Mediani, et al.
Science Advances (2025) Vol. 11, Iss. 8
Open Access
Biotin‐Based Strategies to Explore the World of Ubiquitin and Ubiquitin‐Like Modifiers
Laura Merino‐Cacho, Orhi Barroso‐Gomila, Sandra Hernández‐Sánchez, et al.
ChemBioChem (2023) Vol. 25, Iss. 6
Closed Access | Times Cited: 3
SUMOylation differentially regulates SMCHD1 complex formation and function in a genomic context-specific manner
Remko Goossens, Mara S. Tihaya, Iris M. Willemsen, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Structure and methyl-lysine binding selectivity of the HUSH complex subunit MPP8
Nikos Nikolopoulos, Shun-ichiro Oda, Daniil M. Prigozhin, et al.
Journal of Molecular Biology (2024) Vol. 437, Iss. 2, pp. 168890-168890
Open Access
Cajal body formation is regulated by coilin SUMOylation
Sara K. Tucker, Douglas M. McLaurin, Michael D. Hebert
Journal of Cell Science (2024) Vol. 137, Iss. 23
Open Access
Structure and methyl-lysine binding selectivity of the HUSH complex subunit MPP8
Nikos Nikolopoulos, Shun-ichiro Oda, Daniil M. Prigozhin, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
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