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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:

The linear ubiquitin chain assembly complex (LUBAC) generates heterotypic ubiquitin chains
Alan Rodriguez Carvajal, Irina Grishkovskaya, Carlos Gómez-Díaz, et al.
eLife (2021) Vol. 10
Open Access | Times Cited: 48

Showing 1-25 of 48 citing articles:

HOIL‐1 ubiquitin ligase activity targets unbranched glucosaccharides and is required to prevent polyglucosan accumulation
Ian R. Kelsall, Elisha H. McCrory, Yingqi Xu, et al.
The EMBO Journal (2022) Vol. 41, Iss. 8
Open Access | Times Cited: 95
Ubiquitin—A structural perspective
Rashmi Agrata, David Komander
Molecular Cell (2025) Vol. 85, Iss. 2, pp. 323-346
Closed Access | Times Cited: 2
Assembly and function of branched ubiquitin chains
SriDurgaDevi Kolla, Mengchen Ye, Kevin G. Mark, et al.
Trends in Biochemical Sciences (2022) Vol. 47, Iss. 9, pp. 759-771
Open Access | Times Cited: 63
A new dawn beyond lysine ubiquitination
Daniel R. Squair, Satpal Virdee
Nature Chemical Biology (2022) Vol. 18, Iss. 8, pp. 802-811
Closed Access | Times Cited: 60
Non-lysine ubiquitylation: Doing things differently
Ian R. Kelsall
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 44
The unifying catalytic mechanism of the RING-between-RING E3 ubiquitin ligase family
Xiangyi S. Wang, Thomas R. Cotton, Sarah J. Trevelyan, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 40
The emerging roles of non-canonical ubiquitination in proteostasis and beyond
Yoshino Akizuki, Stephanie Kaypee, Fumiaki Ohtake, et al.
The Journal of Cell Biology (2024) Vol. 223, Iss. 5
Open Access | Times Cited: 10
Ubiquitination of non-protein substrates
Jun-Ichi Sakamaki, Noboru Mizushima
Trends in Cell Biology (2023) Vol. 33, Iss. 11, pp. 991-1003
Open Access | Times Cited: 20
Glycogen synthase downregulation rescues the amylopectinosis of murine RBCK1 deficiency
Silvia Nitschke, Mitchell A. Sullivan, Sharmistha Mitra, et al.
Brain (2022) Vol. 145, Iss. 7, pp. 2361-2377
Open Access | Times Cited: 20
Combinatorial ubiquitin code degrades deubiquitylation-protected substrates
Mai Morita, Miyu Takao, Honoka Tokuhisa, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access
The RBR E3 ubiquitin ligase HOIL-1 can ubiquitinate diverse non-protein substrates in vitro
Xiangyi S. Wang, Jenny Jiou, Anthony Cerra, et al.
Life Science Alliance (2025) Vol. 8, Iss. 6, pp. e202503243-e202503243
Open Access
Primary disorders of polyubiquitination: Dual roles in autoinflammation and immunodeficiency
András N. Spaan, Bertrand Boisson, Seth L. Masters
The Journal of Experimental Medicine (2025) Vol. 222, Iss. 5
Closed Access
The NF-κB Pharmacopeia: Novel Strategies to Subdue an Intractable Target
Daniela Verzella, Jessica Cornice, Paola Arboretto, et al.
Biomedicines (2022) Vol. 10, Iss. 9, pp. 2233-2233
Open Access | Times Cited: 17
Structural basis for ubiquitylation by HOIL-1
Qilong Wu, Marios G. Koliopoulos, Katrin Rittinger, et al.
Frontiers in Molecular Biosciences (2023) Vol. 9
Open Access | Times Cited: 8
HOIL‐1‐catalysed, ester‐linked ubiquitylation restricts IL‐18 signaling in cytotoxic T cells but promotes TLR signalling in macrophages
Tsvetana Petrova, Jiazhen Zhang, Sambit K. Nanda, et al.
FEBS Journal (2021) Vol. 288, Iss. 20, pp. 5909-5924
Open Access | Times Cited: 20
Deubiquitinases in cell death and inflammation
Kim Newton, Alexander D. Gitlin
Biochemical Journal (2022) Vol. 479, Iss. 10, pp. 1103-1119
Open Access | Times Cited: 13
Novel biochemical, structural, and systems insights into inflammatory signaling revealed by contextual interaction proteomics
Rodolfo Ciuffa, Federico Uliana, Jonathan Mannion, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 40
Open Access | Times Cited: 13
From seeds to trees: how E2 enzymes grow ubiquitin chains
A.J. Middleton, Catherine L. Day
Biochemical Society Transactions (2023) Vol. 51, Iss. 1, pp. 353-362
Open Access | Times Cited: 7
Protein and nonprotein targets of ubiquitin modification
Fumiyo Ikeda
AJP Cell Physiology (2023) Vol. 324, Iss. 5, pp. C1053-C1060
Closed Access | Times Cited: 7
Catalysis of non-canonical protein ubiquitylation by the ARIH1 ubiquitin ligase
Nicholas Purser, Ishita Tripathi‐Giesgen, Jerry Li, et al.
Biochemical Journal (2023) Vol. 480, Iss. 22, pp. 1817-1831
Open Access | Times Cited: 7
Deciphering non-canonical ubiquitin signaling: biology and methodology
Nila van Overbeek, Tim Aguirre, Gerbrand J. van der Heden van Noort, et al.
Frontiers in Molecular Biosciences (2024) Vol. 10
Open Access | Times Cited: 2
Linear ubiquitination in immune and neurodegenerative diseases, and beyond
Fuminori Tokunaga, Fumiyo Ikeda
Biochemical Society Transactions (2022) Vol. 50, Iss. 2, pp. 799-811
Closed Access | Times Cited: 12
Identification of ester-linked ubiquitylation sites during TLR7 signalling increases the number of inter-ubiquitin linkages from 8 to 12
Elisha H. McCrory, Vyacheslav Akimov, Philip Cohen, et al.
Biochemical Journal (2022) Vol. 479, Iss. 23, pp. 2419-2431
Open Access | Times Cited: 12
Secondary interactions in ubiquitin-binding domains achieve linkage or substrate specificity
Martin A. Michel, Simon R. Scutts, David Komander
Cell Reports (2024) Vol. 43, Iss. 8, pp. 114545-114545
Closed Access | Times Cited: 2
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