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:

Roles of linear ubiquitinylation, a crucial regulator of NF‐κB and cell death, in the immune system
Katsuhiro Sasaki, Kazuhiro Iwaï
Immunological Reviews (2015) Vol. 266, Iss. 1, pp. 175-189
Open Access | Times Cited: 108

Showing 1-25 of 108 citing articles:

30 Years of NF-κB: A Blossoming of Relevance to Human Pathobiology
Qian Zhang, Michael J. Lenardo, David Baltimore
Cell (2017) Vol. 168, Iss. 1-2, pp. 37-57
Open Access | Times Cited: 1656

TRIM Family Proteins: Roles in Autophagy, Immunity, and Carcinogenesis
Shigetsugu Hatakeyama
Trends in Biochemical Sciences (2017) Vol. 42, Iss. 4, pp. 297-311
Closed Access | Times Cited: 748

The Ubiquitin Code in the Ubiquitin-Proteasome System and Autophagy
Yong Tae Kwon, Aaron Ciechanover
Trends in Biochemical Sciences (2017) Vol. 42, Iss. 11, pp. 873-886
Closed Access | Times Cited: 669

Toll-Like Receptor Signaling and Its Role in Cell-Mediated Immunity
Tianhao Duan, Yang Du, Changsheng Xing, et al.
Frontiers in Immunology (2022) Vol. 13
Open Access | Times Cited: 491

The Nuclear Factor Kappa B (NF-kB) signaling in cancer development and immune diseases
Mohammad Reza Zinatizadeh, Bettina Schock, Ghanbar Mahmoodi Chalbatani, et al.
Genes & Diseases (2020) Vol. 8, Iss. 3, pp. 287-297
Open Access | Times Cited: 365

The family of the interleukin‐1 receptors
Diana Boraschi, Paola Italiani, Sabrina Weil, et al.
Immunological Reviews (2017) Vol. 281, Iss. 1, pp. 197-232
Closed Access | Times Cited: 318

Proteolytic Cleavage—Mechanisms, Function, and “Omic” Approaches for a Near-Ubiquitous Posttranslational Modification
Théo Klein, Ulrich Eckhard, Antoine Dufour, et al.
Chemical Reviews (2017) Vol. 118, Iss. 3, pp. 1137-1168
Closed Access | Times Cited: 180

Structure of a HOIP/E2~ubiquitin complex reveals RBR E3 ligase mechanism and regulation
Bernhard C. Lechtenberg, Akhil Rajput, Ruslan Sanishvili, et al.
Nature (2016) Vol. 529, Iss. 7587, pp. 546-550
Open Access | Times Cited: 179

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: 96

SNIPERs—Hijacking IAP activity to induce protein degradation
Mikihiko Naito, Nobumichi Ohoka, Norihito Shibata
Drug Discovery Today Technologies (2019) Vol. 31, pp. 35-42
Open Access | Times Cited: 135

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

Linear ubiquitination is involved in the pathogenesis of optineurin-associated amyotrophic lateral sclerosis
Seshiru Nakazawa, Daisuke Oikawa, Ryohei Ishii, et al.
Nature Communications (2016) Vol. 7, Iss. 1
Open Access | Times Cited: 124

The Met1-Linked Ubiquitin Machinery: Emerging Themes of (De)regulation
Matouš Hrdinka, Mads Gyrd‐Hansen
Molecular Cell (2017) Vol. 68, Iss. 2, pp. 265-280
Open Access | Times Cited: 119

Fragment-Based Covalent Ligand Screening Enables Rapid Discovery of Inhibitors for the RBR E3 Ubiquitin Ligase HOIP
Henrik Johansson, Yi‐Chun Isabella Tsai, Ken G. M. Fantom, et al.
Journal of the American Chemical Society (2019) Vol. 141, Iss. 6, pp. 2703-2712
Open Access | Times Cited: 111

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

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

LUBAC prevents lethal dermatitis by inhibiting cell death induced by TNF, TRAIL and CD95L
Lucia Taraborrelli, Nieves Peltzer, Antonella Montinaro, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 93

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

Targeting ubiquitin signaling for cancer immunotherapy
Xiaofei Zhou, Shao‐Cong Sun
Signal Transduction and Targeted Therapy (2021) Vol. 6, Iss. 1
Open Access | Times Cited: 60

Holding All the CARDs: How MALT1 Controls CARMA/CARD-Dependent Signaling
Mélanie Juilland, Margot Thome
Frontiers in Immunology (2018) Vol. 9
Open Access | Times Cited: 79

Regulation of inflammasomes by ubiquitination
Joseph S. Bednash, Rama K. Mallampalli
Cellular and Molecular Immunology (2016) Vol. 13, Iss. 6, pp. 722-728
Open Access | Times Cited: 77

LUBAC and OTULIN regulate autophagy initiation and maturation by mediating the linear ubiquitination and the stabilization of ATG13
Yuanyuan Chu, Yingjin Kang, Cong Yan, et al.
Autophagy (2020) Vol. 17, Iss. 7, pp. 1684-1699
Open Access | Times Cited: 64

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

Met1-linked ubiquitin signalling in health and disease: inflammation, immunity, cancer, and beyond
Akhee Sabiha Jahan, Camilla Reiter Elbæk, Rune Busk Damgaard
Cell Death and Differentiation (2021) Vol. 28, Iss. 2, pp. 473-492
Open Access | Times Cited: 43

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