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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 HOIL-1L ligase modulates immune signalling and cell death via monoubiquitination of LUBAC
Yasuhiro Fuseya, Hiroaki Fujita, Minsoo Kim, et al.
Nature Cell Biology (2020) Vol. 22, Iss. 6, pp. 663-673
Open Access | Times Cited: 80

Showing 1-25 of 80 citing articles:

The mechanisms and roles of selective autophagy in mammals
Jose Norberto S. Vargas, Maho Hamasaki, Tsuyoshi Kawabata, et al.
Nature Reviews Molecular Cell Biology (2022) Vol. 24, Iss. 3, pp. 167-185
Closed Access | Times Cited: 558
Ubiquitination in the regulation of inflammatory cell death and cancer
Peter E. Cockram, Matthias Kist, Sumit Prakash, et al.
Cell Death and Differentiation (2021) Vol. 28, Iss. 2, pp. 591-605
Open Access | Times Cited: 310
E3 ubiquitin ligases: styles, structures and functions
Quan Yang, Jinyao Zhao, Dan Chen, et al.
Molecular Biomedicine (2021) Vol. 2, Iss. 1
Open Access | Times Cited: 219
Eosinophil extracellular traps drive asthma progression through neuro-immune signals
Yiwen Lu, Yi-Jiao Huang, Li Jiang, et al.
Nature Cell Biology (2021) Vol. 23, Iss. 10, pp. 1060-1072
Closed Access | Times Cited: 78
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
Physiological functions of ULK1/2
Gautam Pareek, Mondira Kundu
Journal of Molecular Biology (2024) Vol. 436, Iss. 15, pp. 168472-168472
Open Access | Times Cited: 9
Biallelic human SHARPIN loss of function induces autoinflammation and immunodeficiency
Hirotsugu Oda, Kalpana Manthiram, Pallavi Pimpale Chavan, et al.
Nature Immunology (2024) Vol. 25, Iss. 5, pp. 764-777
Closed Access | Times Cited: 8
Chain reactions: molecular mechanisms of RBR ubiquitin ligases
Thomas R. Cotton, Bernhard C. Lechtenberg
Biochemical Society Transactions (2020) Vol. 48, Iss. 4, pp. 1737-1750
Open Access | Times Cited: 57
The Met1-linked ubiquitin machinery in inflammation and infection
Berthe Katrine Fiil, Mads Gyrd‐Hansen
Cell Death and Differentiation (2021) Vol. 28, Iss. 2, pp. 557-569
Open Access | Times Cited: 52
ABL1-dependent OTULIN phosphorylation promotes genotoxic Wnt/β-catenin activation to enhance drug resistance in breast cancers
Wei Wang, Mingqi Li, Suriyan Ponnusamy, et al.
Nature Communications (2020) Vol. 11, Iss. 1
Open Access | Times Cited: 51
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
OTULIN in NF-κB signaling, cell death, and disease
Lien Verboom, Esther Hoste, Geert Loo
Trends in Immunology (2021) Vol. 42, Iss. 7, pp. 590-603
Closed Access | Times Cited: 43
RING domains act as both substrate and enzyme in a catalytic arrangement to drive self-anchored ubiquitination
L. Kiss, Dean Clift, Nadine Renner, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 41
HOIP modulates the stability of GPx4 by linear ubiquitination
Kangyun Dong, Ran Wei, Taijie Jin, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 44
Open Access | Times Cited: 32
The mechanism of linear ubiquitination in regulating cell death and correlative diseases
Liyuan Gao, Wei Zhang, Xiao Hui Shi, et al.
Cell Death and Disease (2023) Vol. 14, Iss. 10
Open Access | Times Cited: 19
Dominant negative OTULIN-related autoinflammatory syndrome
Sophia Davidson, Y. Shibata, Sophie Collard, et al.
The Journal of Experimental Medicine (2024) Vol. 221, Iss. 6
Open Access | Times Cited: 6
Mechanisms orchestrating the enzymatic activity and cellular functions of deubiquitinases
Benjamin Estavoyer, Clémence Messmer, Mohamed Echbicheb, et al.
Journal of Biological Chemistry (2022) Vol. 298, Iss. 8, pp. 102198-102198
Open Access | Times Cited: 24
Exploiting E3 ubiquitin ligases to reeducate the tumor microenvironment for cancer therapy
Xian-Miao Li, Zhenyu Zhao, Yu Xiao, et al.
Experimental Hematology and Oncology (2023) Vol. 12, Iss. 1
Open Access | Times Cited: 14
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
LUBAC-mediated linear ubiquitination in tissue homeostasis and disease
Katsuhiro Sasaki, Kazuhiro Iwaï
The Journal of Biochemistry (2023) Vol. 174, Iss. 2, pp. 99-107
Open Access | Times Cited: 12
A de novo dominant-negative variant is associated with OTULIN-related autoinflammatory syndrome
Y. Takeda, M. Ueki, Junpei Matsuhiro, et al.
The Journal of Experimental Medicine (2024) Vol. 221, Iss. 6
Open Access | Times Cited: 4
Host Immunity and Intracellular Bacteria Evasion Mechanisms: Enhancing Host-Directed Therapies with Drug Delivery Systems
Jiayang Cai, Han Zhou, Mingwei Liu, et al.
International Journal of Antimicrobial Agents (2025), pp. 107492-107492
Closed 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
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