
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 in immunity
Yutaka Shimizu, Lucia Taraborrelli, Henning Walczak
Immunological Reviews (2015) Vol. 266, Iss. 1, pp. 190-207
Open Access | Times Cited: 139
Yutaka Shimizu, Lucia Taraborrelli, Henning Walczak
Immunological Reviews (2015) Vol. 266, Iss. 1, pp. 190-207
Open Access | Times Cited: 139
Showing 1-25 of 139 citing articles:
Ubiquitin chain diversity at a glance
Masato Akutsu, Ivan Đikić, Anja Bremm
Journal of Cell Science (2016) Vol. 129, Iss. 5, pp. 875-880
Open Access | Times Cited: 494
Masato Akutsu, Ivan Đikić, Anja Bremm
Journal of Cell Science (2016) Vol. 129, Iss. 5, pp. 875-880
Open Access | Times Cited: 494
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
Tianhao Duan, Yang Du, Changsheng Xing, et al.
Frontiers in Immunology (2022) Vol. 13
Open Access | Times Cited: 491
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: 490
Marion Mußbacher, Manuel Salzmann, Christine Brostjan, et al.
Frontiers in Immunology (2019) Vol. 10
Open Access | Times Cited: 490
Ubiquitin signaling in immune responses
Hongbo Hu, Shao‐Cong Sun
Cell Research (2016) Vol. 26, Iss. 4, pp. 457-483
Open Access | Times Cited: 417
Hongbo Hu, Shao‐Cong Sun
Cell Research (2016) Vol. 26, Iss. 4, pp. 457-483
Open Access | Times Cited: 417
NF-κB: At the Borders of Autoimmunity and Inflammation
Laura Barnabei, Emmanuel Laplantine, William Mbongo, et al.
Frontiers in Immunology (2021) Vol. 12
Open Access | Times Cited: 402
Laura Barnabei, Emmanuel Laplantine, William Mbongo, et al.
Frontiers in Immunology (2021) Vol. 12
Open Access | Times Cited: 402
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
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
LUBAC-Recruited CYLD and A20 Regulate Gene Activation and Cell Death by Exerting Opposing Effects on Linear Ubiquitin in Signaling Complexes
Peter Dráber, Sebastian Kupka, Matthias Reichert, et al.
Cell Reports (2015) Vol. 13, Iss. 10, pp. 2258-2272
Open Access | Times Cited: 266
Peter Dráber, Sebastian Kupka, Matthias Reichert, et al.
Cell Reports (2015) Vol. 13, Iss. 10, pp. 2258-2272
Open Access | Times Cited: 266
TBK1 and IKKε prevent TNF-induced cell death by RIPK1 phosphorylation
Élodie Lafont, Peter Dráber, Eva Rieser, et al.
Nature Cell Biology (2018) Vol. 20, Iss. 12, pp. 1389-1399
Open Access | Times Cited: 240
Élodie Lafont, Peter Dráber, Eva Rieser, et al.
Nature Cell Biology (2018) Vol. 20, Iss. 12, pp. 1389-1399
Open Access | Times Cited: 240
LUBAC is essential for embryogenesis by preventing cell death and enabling haematopoiesis
Nieves Peltzer, Maurice Darding, Antonella Montinaro, et al.
Nature (2018) Vol. 557, Iss. 7703, pp. 112-117
Open Access | Times Cited: 192
Nieves Peltzer, Maurice Darding, Antonella Montinaro, et al.
Nature (2018) Vol. 557, Iss. 7703, pp. 112-117
Open Access | Times Cited: 192
NF-κB Pathway in Autoinflammatory Diseases: Dysregulation of Protein Modifications by Ubiquitin Defines a New Category of Autoinflammatory Diseases
Ivona Aksentijevich, Qing Zhou
Frontiers in Immunology (2017) Vol. 8
Open Access | Times Cited: 191
Ivona Aksentijevich, Qing Zhou
Frontiers in Immunology (2017) Vol. 8
Open Access | Times Cited: 191
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: 181
Théo Klein, Ulrich Eckhard, Antoine Dufour, et al.
Chemical Reviews (2017) Vol. 118, Iss. 3, pp. 1137-1168
Closed Access | Times Cited: 181
Holding RIPK1 on the Ubiquitin Leash in TNFR1 Signaling
Nieves Peltzer, Maurice Darding, Henning Walczak
Trends in Cell Biology (2016) Vol. 26, Iss. 6, pp. 445-461
Open Access | Times Cited: 173
Nieves Peltzer, Maurice Darding, Henning Walczak
Trends in Cell Biology (2016) Vol. 26, Iss. 6, pp. 445-461
Open Access | Times Cited: 173
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
Ian R. Kelsall, Elisha H. McCrory, Yingqi Xu, et al.
The EMBO Journal (2022) Vol. 41, Iss. 8
Open Access | Times Cited: 96
The E3 ligase HOIL-1 catalyses ester bond formation between ubiquitin and components of the Myddosome in mammalian cells
Ian R. Kelsall, Jiazhen Zhang, Axel Knebel, et al.
Proceedings of the National Academy of Sciences (2019) Vol. 116, Iss. 27, pp. 13293-13298
Open Access | Times Cited: 133
Ian R. Kelsall, Jiazhen Zhang, Axel Knebel, et al.
Proceedings of the National Academy of Sciences (2019) Vol. 116, Iss. 27, pp. 13293-13298
Open Access | Times Cited: 133
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
Katja K. Dove, Rachel E. Klevit
Journal of Molecular Biology (2017) Vol. 429, Iss. 22, pp. 3363-3375
Open Access | Times Cited: 130
Assembly and regulation of ASC specks
Florian Hoß, Juan F. Rodríguez-Alcázar, Eicke Latz
Cellular and Molecular Life Sciences (2016) Vol. 74, Iss. 7, pp. 1211-1229
Open Access | Times Cited: 125
Florian Hoß, Juan F. Rodríguez-Alcázar, Eicke Latz
Cellular and Molecular Life Sciences (2016) Vol. 74, Iss. 7, pp. 1211-1229
Open Access | Times Cited: 125
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
Matouš Hrdinka, Mads Gyrd‐Hansen
Molecular Cell (2017) Vol. 68, Iss. 2, pp. 265-280
Open Access | Times Cited: 119
Recognition of Client Proteins by the Proteasome
Houqing Yu, Andreas Matouschek
Annual Review of Biophysics (2017) Vol. 46, Iss. 1, pp. 149-173
Open Access | Times Cited: 117
Houqing Yu, Andreas Matouschek
Annual Review of Biophysics (2017) Vol. 46, Iss. 1, pp. 149-173
Open Access | Times Cited: 117
Activity‐based probes for the ubiquitin conjugation–deconjugation machinery: new chemistries, new tools, and new insights
David S. Hewings, John A. Flygare, Matthew Bogyo, et al.
FEBS Journal (2017) Vol. 284, Iss. 10, pp. 1555-1576
Open Access | Times Cited: 111
David S. Hewings, John A. Flygare, Matthew Bogyo, et al.
FEBS Journal (2017) Vol. 284, Iss. 10, pp. 1555-1576
Open Access | Times Cited: 111
Conventional and unconventional ubiquitination in plant immunity
Bangjun Zhou, Lirong Zeng
Molecular Plant Pathology (2016) Vol. 18, Iss. 9, pp. 1313-1330
Open Access | Times Cited: 106
Bangjun Zhou, Lirong Zeng
Molecular Plant Pathology (2016) Vol. 18, Iss. 9, pp. 1313-1330
Open Access | Times Cited: 106
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: 105
Élodie Lafont, Chahrazade Kantari‐Mimoun, Peter Dráber, et al.
The EMBO Journal (2017) Vol. 36, Iss. 9, pp. 1147-1166
Open Access | Times Cited: 105
Structure, Dynamics and Function of the 26S Proteasome
Youdong Mao
Sub-cellular biochemistry/Subcellular biochemistry (2020), pp. 1-151
Open Access | Times Cited: 96
Youdong Mao
Sub-cellular biochemistry/Subcellular biochemistry (2020), pp. 1-151
Open Access | Times Cited: 96
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: 95
Katrin Rittinger, Fumiyo Ikeda
Open Biology (2017) Vol. 7, Iss. 4, pp. 170026-170026
Open Access | Times Cited: 95
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
Lucia Taraborrelli, Nieves Peltzer, Antonella Montinaro, et al.
Nature Communications (2018) Vol. 9, Iss. 1
Open Access | Times Cited: 93
Protein phosphatase 2A as a therapeutic target in inflammation and neurodegeneration
Andrew R. Clark, Michael Ohlmeyer
Pharmacology & Therapeutics (2019) Vol. 201, pp. 181-201
Open Access | Times Cited: 83
Andrew R. Clark, Michael Ohlmeyer
Pharmacology & Therapeutics (2019) Vol. 201, pp. 181-201
Open Access | Times Cited: 83