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:

Linear ubiquitination signals in adaptive immune responses
Fumiyo Ikeda
Immunological Reviews (2015) Vol. 266, Iss. 1, pp. 222-236
Open Access | Times Cited: 70

Showing 1-25 of 70 citing articles:

The role of JAK-STAT signaling pathway and its regulators in the fate of T helper cells
Farhad Seif, Majid Khoshmirsafa, Hossein Aazami, et al.
Cell Communication and Signaling (2017) Vol. 15, Iss. 1
Open Access | Times Cited: 689

Cell Type-Specific Roles of NF-κB Linking Inflammation and Thrombosis
Marion Mußbacher, Manuel Salzmann, Christine Brostjan, et al.
Frontiers in Immunology (2019) Vol. 10
Open Access | Times Cited: 484

NF-κB in monocytes and macrophages – an inflammatory master regulator in multitalented immune cells
Marion Mußbacher, Martina Derler, José Basílio, et al.
Frontiers in Immunology (2023) Vol. 14
Open Access | Times Cited: 125

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

RING-Between-RING E3 Ligases: Emerging Themes amid the Variations
Katja K. Dove, Rachel E. Klevit
Journal of Molecular Biology (2017) Vol. 429, Iss. 22, pp. 3363-3375
Open Access | Times Cited: 130

Cell Death Pathways: a Novel Therapeutic Approach for Neuroscientists
Gerwyn Morris, Adam J. Walker, Michael Berk, et al.
Molecular Neurobiology (2017) Vol. 55, Iss. 7, pp. 5767-5786
Open Access | Times Cited: 125

Ubiquitin enzymes in the regulation of immune responses
Petra Ebner, Gijs A. Versteeg, Fumiyo Ikeda
Critical Reviews in Biochemistry and Molecular Biology (2017) Vol. 52, Iss. 4, pp. 425-460
Open Access | Times Cited: 123

The linear ubiquitin chain assembly complex regulates TRAIL‐induced gene activation and cell death
Élodie Lafont, Chahrazade Kantari‐Mimoun, Peter Dráber, et al.
The EMBO Journal (2017) Vol. 36, Iss. 9, pp. 1147-1166
Open Access | Times Cited: 104

Negative Regulators of JAK/STAT Signaling in Rheumatoid Arthritis and Osteoarthritis
Charles J. Malemud
International Journal of Molecular Sciences (2017) Vol. 18, Iss. 3, pp. 484-484
Open Access | Times Cited: 101

Linear ubiquitin chains: enzymes, mechanisms and biology
Katrin Rittinger, Fumiyo Ikeda
Open Biology (2017) Vol. 7, Iss. 4, pp. 170026-170026
Open Access | Times Cited: 94

Non-proteolytic ubiquitylation in cellular signaling and human disease
Yongrong Liao, Izabela Sumara, Evanthia Pangou
Communications Biology (2022) Vol. 5, Iss. 1
Open Access | Times Cited: 40

An Overview of Pathways of Regulated Necrosis in Acute Kidney Injury
Jesper Kers, Jaklien C. Leemans, Andreas Linkermann
Seminars in Nephrology (2016) Vol. 36, Iss. 3, pp. 139-152
Closed Access | Times Cited: 71

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

New Look of EBV LMP1 Signaling Landscape
Ling Wang, Shunbin Ning
Cancers (2021) Vol. 13, Iss. 21, pp. 5451-5451
Open Access | Times Cited: 47

NEMO reshapes the α-Synuclein aggregate interface and acts as an autophagy adapter by co-condensation with p62
Nikolas Furthmann, Verian Bader, Lena Angersbach, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 21

Structural Insights into SHARPIN-Mediated Activation of HOIP for the Linear Ubiquitin Chain Assembly
Jianping Liu, Yingli Wang, Yukang Gong, et al.
Cell Reports (2017) Vol. 21, Iss. 1, pp. 27-36
Open Access | Times Cited: 49

Linear ubiquitination by LUBEL has a role in Drosophila heat stress response
Tomoko Asaoka, Jorge Almagro, Christine Ehrhardt, et al.
EMBO Reports (2016) Vol. 17, Iss. 11, pp. 1624-1640
Open Access | Times Cited: 39

Linear ubiquitin chain‐binding domains
Lilian M. Fennell, Simin Rahighi, Fumiyo Ikeda
FEBS Journal (2018) Vol. 285, Iss. 15, pp. 2746-2761
Open Access | Times Cited: 37

The Linear ubiquitin chain assembly complex acts as a liver tumor suppressor and inhibits hepatocyte apoptosis and hepatitis
Yutaka Shimizu, Nieves Peltzer, Alexandra Sevko, et al.
Hepatology (2017) Vol. 65, Iss. 6, pp. 1963-1978
Open Access | Times Cited: 36

The E3 ubiquitin ligases HOIP and cIAP1 are recruited to the TNFR2 signaling complex and mediate TNFR2-induced canonical NF-κB signaling
Alice Borghi, Mira Haegman, Roman Fischer, et al.
Biochemical Pharmacology (2018) Vol. 153, pp. 292-298
Closed Access | Times Cited: 33

Deubiquitinating Enzymes and Bone Remodeling
Yuchen Guo, Shiwen Zhang, Quan Yuan
Stem Cells International (2018) Vol. 2018, pp. 1-9
Open Access | Times Cited: 33

The Linear Ubiquitin Assembly Complex Modulates Latent Membrane Protein 1 Activation of NF-κB and Interferon Regulatory Factor 7
Ling Wang, Yujia Wang, Juan Zhao, et al.
Journal of Virology (2016) Vol. 91, Iss. 4
Open Access | Times Cited: 32

Ubiquitin-based modifications in endothelial cell–cell contact and inflammation
Jisca Majolée, Igor Kovačević, Peter L. Hordijk
Journal of Cell Science (2019) Vol. 132, Iss. 17
Open Access | Times Cited: 29

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