SHARPIN is a component of the NF-κB-activating linear ubiquitin chain assembly complex

Shared Principles in NF-κB Signaling

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Nuclear factor-κB in cancer development and progression

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Regulation and Function of NF-κB Transcription Factors in the Immune System

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Complementation Cloning of NEMO, a Component of the IκB Kinase Complex Essential for NF-κB Activation

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Involvement of linear polyubiquitylation of NEMO in NF-κB activation

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A ubiquitin ligase complex assembles linear polyubiquitin chains

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Recruitment of the Linear Ubiquitin Chain Assembly Complex Stabilizes the TNF-R1 Signaling Complex and Is Required for TNF-Mediated Gene Induction

Haas, T. L., Emmerich, C. H., Gerlach, B., Schmukle, A. C., Cordier, S. M., Rieser, E., Feltham, R., Vince, J. E., Warnken, U. H., Wenger, T., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.10.013 · Cited by 797

Ubiquitylation in innate and adaptive immunity

Bhoj, V. G., & Chen, Z. J. (2009) · Nature · doi:10.1038/nature07959 · Cited by 632

Distinct Roles in Lymphoid Organogenesis for Lymphotoxins α and β Revealed in Lymphotoxin β–Deficient Mice

Koni, P. A., Sacca, R. E., Lawton, P., Browning, J. L., Ruddle, N. H., & Flavell, R. A. (1997) · Immunity · doi:10.1016/s1074-7613(00)80292-7 · Cited by 589

A novel X-linked disorder of immune deficiency and hypohidrotic ectodermal dysplasia is allelic to incontinentia pigmenti and due to mutations in IKK-gamma (NEMO)

Zonana, J., Elder, M. E., Schneider, L. C., Orlow, S. J., Moss, C., Golabi, M., Shapira, S. K., Farndon, P. A., Wara, D. W., Emmal, S. A., et al. (2000) · The American Journal of Human Genetics · doi:10.1086/316914 · Cited by 521

Regulation of Linear Ubiquitin Chain Assembly Complex by Caspase-Mediated Cleavage of RNF31

Joo, D., Tang, Y., Blonska, M., Jin, J., Zhao, X., & Lin, X. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00474-16 · Cited by 20

Survival of mature T cells depends on signaling through HOIP

Okamura, K., Kitamura, A., Sasaki, Y., Chung, D. H., Kagami, S., Iwaï, K., & Yasutomo, K. (2016) · Scientific Reports · doi:10.1038/srep36135 · Cited by 17

SHARPIN stabilizes β-catenin through a linear ubiquitination-independent manner to support gastric tumorigenesis

Zhang, L., Liu, Q., Liu, K., Qin, Z., Zhu, G.-X., Shen, L., Zhang, N., Liu, B.-Y., Che, L., Li, J.-Y., et al. (2020) · Gastric Cancer · doi:10.1007/s10120-020-01138-5 · Cited by 18

Sex-Specific Linear Polyubiquitination Is a Critical Regulator of Contextual Fear Memory Formation

Musaus, M., Farrell, K., Navabpour, S., Ray, W. K., Helm, R. F., & Jarome, T. J. (2021) · Frontiers in Behavioral Neuroscience · doi:10.3389/fnbeh.2021.709392 · Cited by 18

M1‐linked ubiquitination facilitates NF‐κB activation and survival during sterile inflammation

Aalto, A. L., Martínez‐Chacón, G., Kietz, C., Tsyganova, N., Kreutzer, J., Kallio, P. J., Broemer, M., & Meinander, A. (2022) · FEBS Journal · doi:10.1111/febs.16425 · Cited by 19

Integrin beta 1 inhibition alleviates the chronic hyperproliferative dermatitis phenotype of SHARPIN-deficient mice

Peuhu, E., Salomaa, S. I., Franceschi, N. D., Potter, C. S., Sundberg, J. P., & Pouwels, J. (2017) · PLoS ONE · doi:10.1371/journal.pone.0186628 · Cited by 16

Simultaneous Detection of Distinct Ubiquitin Chain Topologies by 19F NMR

Shekhawat, S. S., Pham, G. H., Prabakaran, J., & Strieter, E. R. (2014) · ACS Chemical Biology · doi:10.1021/cb500589c · Cited by 16

Keratinocyte-specific deletion of SHARPIN induces atopic dermatitis-like inflammation in mice

Sundberg, J. P., Pratt, C. H., Goodwin, L. O., Silva, K. A., Kennedy, V. E., Potter, C. S., Dunham, A. D., Sundberg, B. A., & HogenEsch, H. (2020) · PLoS ONE · doi:10.1371/journal.pone.0235295 · Cited by 17

Site‐specific ubiquitination of the E3 ligase HOIP regulates apoptosis and immune signaling

Fennell, L. M., Diaz, C. G., Deszcz, L., Kavirayani, A. M., Hoffmann, D., Yanagitani, K., Schleiffer, A., Mechtler, K., Hagelkrüys, A., Penninger, J. M., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2019103303 · Cited by 17

Immune dysregulation in SHARPIN-deficient mice is dependent on CYLD-mediated cell death

Ang, R. L., Chan, M., Legarda, D., Sundberg, J. P., Sun, S., Gillespie, V., Chun, N. H., Heeger, P. S., Xiong, H., Lira, S. A., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2001602118 · Cited by 16

The evolving world of ubiquitin: transformed polyubiquitin chains

Morimoto, D., & Shirakawa, M. (2016) · BioMolecular Concepts · doi:10.1515/bmc-2016-0009 · Cited by 14

How Is the Fidelity of Proteins Ensured in Terms of Both Quality and Quantity at the Endoplasmic Reticulum? Mechanistic Insights into E3 Ubiquitin Ligases

Kang, J. A., & Jeon, Y. J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22042078 · Cited by 15

New Insights into the Role of Ubiquitin Networks in the Regulation of Antiapoptosis Pathways

Asaoka, T., & Ikeda, F. (2015) · International review of cytology · doi:10.1016/bs.ircmb.2015.05.003 · Cited by 15

Molecular finds of pressure ulcer: A bioinformatics approach in pressure ulcer

Santos, E. M., Farias, L. C., Santos, S. H. S., de Paula, A. M. B., Silva, C. S. D. O. E., & Guimarães, A. L. S. (2017) · Journal of Tissue Viability · doi:10.1016/j.jtv.2017.01.002 · Cited by 16

Cellular and Mathematical Analyses of LUBAC Involvement in T Cell Receptor-Mediated NF-κB Activation Pathway

Oikawa, D., Hatanaka, N., Suzuki, T., & Tokunaga, F. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.601926 · Cited by 15

Linear Ubiquitination of RIPK1 on Lys612 Regulates Systemic Inflammation via Preventing Cell Death

Tu, H., Tang, Y., Zhang, J., Cheng, L., Joo, D., Zhao, X., & Lin, X. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2100299 · Cited by 16

Ripoptocide – A Spark for Inflammation

Ang, R. L., Chan, M., & Ting, A. T. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00163 · Cited by 15

The Sharpin interactome reveals a role for Sharpin in lamellipodium formation via the Arp2/3 complex

Khan, M. H., Salomaa, S. I., Jacquemet, G., Butt, U., Miihkinen, M., Deguchi, T., Kremneva, E., Lappalainen, P., Humphries, M. J., & Pouwels, J. (2017) · Journal of Cell Science · doi:10.1242/jcs.200329 · Cited by 14

68Ga-DOTA-E[c(RGDfK)]2 PET Imaging of SHARPIN-Regulated Integrin Activity in Mice

Viitanen, R., Peuhu, E., Autio, A. K., Liljenbäck, H., Mattila, E., Metsälä, O., Käkelä, M., Saanijoki, T., Dijkgraaf, I., Jalkanen, S., et al. (2019) · Journal of Nuclear Medicine · doi:10.2967/jnumed.118.222026 · Cited by 14

Loss of Function of the Mouse Sharpin Gene Results in Peyer’s Patch Regression

Seymour, R. E., Shirley, B., HogenEsch, H., Shultz, L. D., & Sundberg, J. P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055224 · Cited by 15

Estrogen receptor-α, RBCK1, and protein kinase C β 1 cooperate to regulate estrogen receptor-α gene expression

Gustafsson, N., Heldring, N., & Dahlman‐Wright, K. (2012) · Journal of Molecular Endocrinology · doi:10.1530/jme-12-0073 · Cited by 14

Reduced SHARPIN and LUBAC Formation May Contribute to CCl4- or Acetaminophen-Induced Liver Cirrhosis in Mice

Yamamotoya, T., Nakatsu, Y., Matsunaga, Y., Fukushima, T., Yamazaki, H., Kaneko, S., Fujishiro, M., Kikuchi, T., Kushiyama, A., Tokunaga, F., et al. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18020326 · Cited by 14

Crucial Role of Linear Ubiquitin Chain Assembly Complex–Mediated Inhibition of Programmed Cell Death in TLR4-Mediated B Cell Responses and B1b Cell Development

Sasaki, Y., & Iwaï, K. (2018) · The Journal of Immunology · doi:10.4049/jimmunol.1701526 · Cited by 14

Modifications in Biomacromolecules

Zhan, X., & Jabbari, A. (2022) · Biochemistry · doi:10.5772/intechopen.97318 · Cited by 13

Legionella pneumophila-mediated host posttranslational modifications

Yang, Y., Mei, L., Chen, J., Chen, X., Wang, Z., Liu, L., & Yang, A. (2023) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjad032 · Cited by 14

Direct inhibition of NF-κB activation by peptide targeting the NOA ubiquitin binding domain of NEMO

Chiaravalli, J., Fontan, É., Fsihi, H., Coïc, Y., Baleux, F., Véron, M., & Agou, F. (2011) · Biochemical Pharmacology · doi:10.1016/j.bcp.2011.07.083 · Cited by 13

Elevation of SHARPIN Protein Levels in Prostate Adenocarcinomas Promotes Metastasis and Impairs Patient Survivals

Huang, H. W., Du, T., Zhang, Y., Lai, Y., Li, K., Fan, X., Zhu, D., Lin, T., Xu, K., Huang, J., et al. (2017) · The Prostate · doi:10.1002/pros.23302 · Cited by 13

Dysregulation of Cell Death in Human Chronic InflammationPreprint

Li, Y., Klein, C., & Kotlarz, D. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a037036 · Cited by 15

Glycobiology of cellular expiry: Decrypting the role of glycan-lectin regulatory complex and therapeutic strategies focusing on cancer

Das, A. K., Ghosh, N., Mandal, A., & Sil, P. C. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115367 · Cited by 13

IFN-γ or IFN-α Ameliorates Chronic Proliferative Dermatitis by Inducing Expression of Linear Ubiquitin Chain Assembly Complex

Tamiya, H., Terao, M., Takiuchi, T., Nakahara, M., Sasaki, Y., Katayama, I., Yoshikawa, H., & Iwaï, K. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1302308 · Cited by 12

SHARPIN: Role in Finding NEMO and in Amyloid-Beta Clearance and Degradation (ABCD) Pathway in Alzheimer’s Disease?

Krishnan, D., Menon, R. N., & Gopala, S. (2021) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-020-01023-w · Cited by 12

Crosstalk Between NDP52 and LUBAC in Innate Immune Responses, Cell Death, and Xenophagy

Miyashita, H., Oikawa, D., Terawaki, S., Kabata, D., Shintani, A., & Tokunaga, F. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.635475 · Cited by 14

Langerhans cells are an essential cellular intermediary in chronic dermatitis

Anderton, H., Chopin, M., Dawson, C. A., Nutt, S. L., Whitehead, L. W., Silke, N., Lalaoui, N., & Silke, J. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110922 · Cited by 12

Structural basis for ubiquitylation by HOIL-1

Wu, Q., Koliopoulos, M. G., Rittinger, K., & Stieglitz, B. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.1098144 · Cited by 10

Differential protein-protein interactions underlie signaling mediated by the TCR and a 4-1BB domain–containing CAR

Ritmeester-Loy, S. A., Draper, I. H., Bueter, E., Lautz, J. D., Zhang-Wong, Y., Gustafson, J. A., Wilson, A. L., Lin, C., Gafken, P. R., Jensen, M. C., et al. (2024) · Science Signaling · doi:10.1126/scisignal.add4671 · Cited by 14

SIPL1 enhances the proliferation, attachment, and migration of CHO cells by inhibiting PTEN function

Melo, J. D., Wu, V., He, L., Yan, J., & Tang, D. (2014) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2014.1840 · Cited by 12

Selective monitoring of ubiquitin signals with genetically encoded ubiquitin chain–specific sensors

van Wijk, S. J. L., Fiškin, E., & Đikić, I. (2013) · Nature Protocols · doi:10.1038/nprot.2013.089 · Cited by 12

The Role of Ubiquitination in Regulation of Innate Immune Signaling

Zohaib, A., Duan, X., Zhu, B., Ye, J., Wan, S., Chen, H., Liu, X., & Cao, S. (2016) · Current Issues in Molecular Biology · doi:10.21775/cimb.018.001 · Cited by 12

Angiogenesis in the skin of SHARPIN-deficient mice with chronic proliferative dermatitis

HogenEsch, H., Sola, M., Stearns, T. M., Silva, K. A., Kennedy, V. E., & Sundberg, J. P. (2016) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2016.05.015 · Cited by 12

Atypical ubiquitination of proteins

Бунеева, О. А., & Medvedev, A. E. (2016) · Biomeditsinskaya Khimiya · doi:10.18097/pbmc20166205496 · Cited by 12

LUBAC Suppresses IL-21-Induced Apoptosis in CD40-Activated Murine B Cells and Promotes Germinal Center B Cell Survival and the T-Dependent Antibody Response

Wang, J., Li, T., Zan, H., Rivera, C. E., Yan, H. M., & Xu, Z. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.658048 · Cited by 12

IAPs, TNF, inflammation and Jürg TSCHOPP; a personal perspective

Silke, J., & Vince, J. E. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.166 · Cited by 12

LUBAC promotes angiogenesis and lung tumorigenesis by ubiquitinating and antagonizing autophagic degradation of HIF1α

Jin, Y. H., Peng, Y., Xu, J., Yuan, Y., Yang, N., Zhang, Z., Xu, L., Li, L., Xiong, Y., Sun, D., et al. (2024) · Oncogenesis · doi:10.1038/s41389-024-00508-3 · Cited by 12

The RBR E3 ubiquitin ligase HOIL-1 can ubiquitinate diverse non-protein substrates in vitro

Wang, X. S., Jiou, J., Cerra, A., Cobbold, S. A., Jochem, M., Mak, K. H. T., Corcilius, L., Silke, J., Payne, R. J., Goddard‐Borger, E. D., et al. (2025) · Life Science Alliance · doi:10.26508/lsa.202503243 · Cited by 11

The LUBAC participates in Lysophosphatidic Acid-induced NF-κB Activation

Douanne, T., Chapelier, S., Rottapel, R. K., Gavard, J., & Bidère, N. (2020) · Cellular Immunology · doi:10.1016/j.cellimm.2020.104133 · Cited by 11

Structural basis for the simultaneous recognition of NEMO and acceptor ubiquitin by the HOIP NZF1 domain

Rahighi, S., Iyer, M., Oveisi, H., Nasser, S., & Duong, V. (2022) · Scientific Reports · doi:10.1038/s41598-022-16193-4 · Cited by 10

Role of linear ubiquitination in inflammatory responses and tissue homeostasis

Sasaki, K., & Iwaï, K. (2022) · International Immunology · doi:10.1093/intimm/dxac047 · Cited by 14

Signatures derived from increase in SHARPIN gene copy number are associated with poor prognosis in patients with breast cancer

Ojo, D., Seliman, M., & Tang, D. (2017) · BBA Clinical · doi:10.1016/j.bbacli.2017.07.004 · Cited by 11

Tumor necrosis factor-driven cell death in donor organ as a barrier to immunological tolerance

Ang, R. L., & Ting, A. T. (2018) · Current Opinion in Organ Transplantation · doi:10.1097/mot.0000000000000599 · Cited by 12

Shank‑associated RH domain interactor signaling in tumorigenesis (Review)

Zeng, C., Xiong, D., Zhang, K., & Yao, J. (2020) · Oncology Letters · doi:10.3892/ol.2020.11850 · Cited by 11

Platelet SHARPIN regulates platelet adhesion and inflammatory responses through associations with αIIbβ3 and LUBAC

Kasirer‐Friede, A., Peuhu, E., Ivaska, J., & Shattil, S. J. (2022) · Blood Advances · doi:10.1182/bloodadvances.2021005611 · Cited by 12

RING‐between‐RINGs—keeping the safety on loaded guns

Dove, K. K., & Klevit, R. E. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.260 · Cited by 11

A role of SIPL1/SHARPIN in promoting resistance to hormone therapy in breast cancer

Ojo, D., Wu, Y., Bane, A. L., & Tang, D. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.12.018 · Cited by 11

Blockade of TNF receptor superfamily 1 (TNFR1)–dependent and TNFR1-independent cell death is crucial for normal epidermal differentiation

Piao, X., Miura, R., Miyake, S., Komazawa‐Sakon, S., Koike, M., Shindo, R., Takeda, J., Hasegawa, A., Abe, R., Nishiyama, C., et al. (2018) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2018.02.043 · Cited by 12

SHARPIN is a novel gene of colorectal cancer that promotes tumor growth potentially via inhibition of p53 expression

Nakano, Y., Masuda, T., Sakamoto, T., Tanaka, N., Tobo, T., Hashimoto, M., Tatsumi, T., Saito, H., Takahashi, J., Koike, K., et al. (2024) · International Journal of Oncology · doi:10.3892/ijo.2024.5701 · Cited by 10

Serine 165 phosphorylation of SHARPIN regulates the activation of NF-κB

Thys, A., Trillet, K., Rosińska, S., Gayraud, A., Douanne, T., Danger, Y., Renaud, C. C. N., Antigny, L., Lavigne, R., Pineau, C., et al. (2021) · iScience · doi:10.1016/j.isci.2020.101939 · Cited by 10

Ubiquitin: Structure and Function

Dongdem, J. T., Dawson, S. P., & Layfield, R. (2024) · Biochemistry · doi:10.5772/intechopen.112091 · Cited by 10

Dual roles for LUBAC signaling in thymic epithelial cell development and survival

Jain, R., Zhao, K., Sheridan, J. M., Heinlein, M., Kupresanin, F., Abeysekera, W., Hall, C. M., Rickard, J. A., Bouillet, P., Walczak, H., et al. (2021) · Cell Death and Differentiation · doi:10.1038/s41418-021-00850-8 · Cited by 10

Structures, functions, and inhibitors of LUBAC and its related diseases

Ning, S., Luo, L., Yu, B., Mai, D., & Wang, F. (2022) · Journal of Leukocyte Biology · doi:10.1002/jlb.3mr0222-508r · Cited by 11

Advances in the Structural and Physiological Functions of SHARPIN

Yu, B., Wang, F., & Wang, Y. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.858505 · Cited by 10

Linear ubiquitination mediates coronavirus NSP14-induced NF-κB activation

Hua, F., Hao, W., Wang, L., Song, K., Hasan, A., Wu, Y., Li, K., Lin, Z., Sun, Y., & Li, S. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01949-4 · Cited by 10

SHARPIN Enhances Ferroptosis in Synovial Sarcoma Cells via NF-κB- and PRMT5-Mediated PGC1α Reduction

Tamiya, H., Urushihara, N., Shizuma, K., Ogawa, H., Nakai, S., Wakamatsu, T., Takenaka, S., & Kakunaga, S. (2023) · Cancers · doi:10.3390/cancers15133484 · Cited by 9

TLRs Go Linear – On the Ubiquitin Edge

Zinngrebe, J., & Walczak, H. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.02.003 · Cited by 9

“Toll-free” pathways for production of type I interferons

Wang, L., & Ning, S. (2017) · AIMS Allergy and Immunology · doi:10.3934/allergy.2017.3.143 · Cited by 9

Structural bases of the assembly, recognition and disassembly of linear ubiquitin chain

Liu, J., & Pan, L. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.07.003 · Cited by 8

Regulation of ERα Stability and Estrogen Signaling in Breast Cancer by HOIL-1

Ding, J., & Kuang, P. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.664689 · Cited by 10

Genetic deletion and pharmacologic inhibition of E3 ubiquitin ligase HOIP impairs the propagation of myeloid leukemia

Jimbo, K., Hattori, A., Koide, S., Ito, T., Sasaki, K., Iwaï, K., Nannya, Y., Iwama, A., Tojo, A., & Konuma, T. (2022) · Leukemia · doi:10.1038/s41375-022-01750-7 · Cited by 9

Ubiquitination and autophagy in host–pathogen interactions: from immune surveillance to therapeutic targeting

Mello-Vieira, J., & Đikić, I. (2026) · Nature reviews. Immunology · doi:10.1038/s41577-025-01239-1 · Cited by 10

Die Lys48‐verknüpfte Polyubiquitinkette als proteasomales Signal: kein Einzelkind mehr

Kravtsova‐Ivantsiv, Y., Sommer, T., & Ciechanover, A. J. (2012) · Angewandte Chemie · doi:10.1002/ange.201205656 · Cited by 8

The ubiquitin ligase HOIL-1L regulates immune responses by interacting with linear ubiquitin chains

Diaz, C. G., Jonsson, G., Schodl, K., Deszcz, L., Bestehorn, A., Eislmayr, K., Almagro, J., Kavirayani, A. M., Seida, M., Fennell, L. M., et al. (2021) · iScience · doi:10.1016/j.isci.2021.103241 · Cited by 7

Emerging Roles of Non-proteolytic Ubiquitination in Tumorigenesis

Yin, X., Liu, Q., Liu, F., Tian, X., Yan, T., Han, J., & Jiang, S. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.944460 · Cited by 8

Mechanisms underlying linear ubiquitination and implications in tumorigenesis and drug discovery

Li, J., Liu, S., & Li, S. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01239-5 · Cited by 8

Germline Polymorphisms in RNF31 Regulate Linear Ubiquitination and Oncogenic Signaling

Grumati, P., & Đikić, I. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-14-0177 · Cited by 8

Sharpin Controls Osteogenic Differentiation of Mesenchymal Bone Marrow Cells

Jeschke, A., Catalá-Lehnen, P., Sieber, S., Bickert, T., Schweizer, M., Koehne, T., Wintges, K., Marshall, R. P., Mautner, A., Duchstein, L., et al. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1402392 · Cited by 8

Human LUBAC deficiency leads to autoinflammation and immunodeficiency by dysregulation in TNF-mediated cell deathPreprint

Oda, H., Manthiram, K., Chavan, P. P., Nakabo, S., Kuehn, H. S., Beck, D. B., Chae, J. J., Nehrebecky, M. E., Ombrello, A. K., Romeo, T., et al. (2022) · medRxiv · doi:10.1101/2022.11.09.22281431 · Cited by 8

Insights into non-proteinaceous ubiquitination

Dearlove, E. L., & Huang, D. T. C. (2025) · Biochemical Society Transactions · doi:10.1042/bst20253029 · Cited by 8

Linear ubiquitination prevents lipodystrophy and obesity-associated metabolic syndrome

Hildebrandt, X., Veli, Ö., Hyoubi, A., Zinngrebe, J., Abdallah, A. T., Rodefeld, J., Hoffmann, A., Gardeweg, L., Kaya, Ö., Wagner, E., et al. (2025) · Science Advances · doi:10.1126/sciadv.adw2539 · Cited by 7

Skin immunity and inflammation: cellular interactions and communication

Narayanan, D., Sim, S.-L., & Kumari, S. (2025) · Clinical & Translational Immunology · doi:10.1002/cti2.70053 · Cited by 10

N-acetylcysteine combined with insulin attenuates myocardial injury in canines with type 1 diabetes mellitus by modulating TNF-α-mediated apoptotic pathways and affecting linear ubiquitination

Huang, J., Pang, X., Zhang, X., Qiu, W., Zhang, X., Wang, R., Xie, W., Bai, Y., Zhou, S., Liao, J., et al. (2023) · Translational research · doi:10.1016/j.trsl.2023.07.003 · Cited by 7

Genetic Regulation of Cell Death: Insights from Autoinflammatory Diseases

Oda, H., Annibaldi, A., Kastner, D. L., & Aksentijevich, I. A. (2025) · Annual Review of Immunology · doi:10.1146/annurev-immunol-090222-105848 · Cited by 10

SHARPIN overexpression promotes TAK1 expression and activates JNKs and NF‐κB pathway in Mycosis Fungoides

Chen, B., Zheng, Y., Zhu, J., & Liang, Y. (2019) · Experimental Dermatology · doi:10.1111/exd.14026 · Cited by 7

Global Screening of LUBAC and OTULIN Interacting Proteins by Human Proteome Microarray

Zhou, L., Ge, Y., Fu, Y., Wu, B., Zhang, Y., Li, L., Cui, C., Wang, S., & Zhang, L. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.686395 · Cited by 7

MyD88-Dependent Signaling Is Required for HOIP Deficiency–Induced Autoinflammation

Wu, X. G., Tang, Y., Zhang, S., Zhao, X., & Lin, X. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2100173 · Cited by 8

The role of atypical ubiquitination in cell regulation

Бунеева, О. А., & Medvedev, A. E. (2017) · Biochemistry (Moscow) Supplement Series B Biomedical Chemistry · doi:10.1134/s1990750817010024 · Cited by 7

SHARPIN Negatively Associates with TRAF2-Mediated NFκB Activation

Liang, Y. (2011) · PLoS ONE · doi:10.1371/journal.pone.0021696 · Cited by 7

HOIL-1-catalysed ubiquitylation of unbranched glucosaccharides and its activation by ubiquitin oligomersPreprint

Kelsall, I. R., McCrory, E. H., Xu, Y., Scudamore, C. L., Nanda, S. K., Mancebo‐Gamella, P., Wood, N. T., Knebel, A., Matthews, S., & Cohen, P. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.09.10.459791 · Cited by 7

SHARPIN S146 phosphorylation mediates ARP2/3 interaction, cancer cell invasion and metastasis

Butt, U., Khan, M. H., Pouwels, J., & Westermarck, J. (2022) · Journal of Cell Science · doi:10.1242/jcs.260627 · Cited by 6

Novel genotypes, phenotypes, and triggers in humans with OTULIN haploinsufficiency

van der Linden, T. J., Arts, R. J. W., Biggs, C. M., Habibi, L., Batlle-Masó, L., van Laarhoven, A., Scheepmaker, L. M., Yousefi, P., Raccio, A. C. G., Alizadeh, Z., et al. (2025) · Journal of Human Immunity · doi:10.70962/jhi.20250018 · Cited by 6

M1-linked ubiquitination by LUBAC regulates AMPK signalling and the response to energetic stress

Elbæk, C. R., Gradinaru, S., Dahlström, A. M., Frueh, A., Jahan, A. S., Cuenco, J., Aalto, A. L., Rizk, J., Hawley, S. A., Franks, S. N. J., et al. (2026) · Cell Death and Differentiation · doi:10.1038/s41418-026-01675-z · Cited by 8

Spata2L Suppresses TLR4 Signaling by Promoting CYLD-Mediated Deubiquitination of TRAF6 and TAK1

Zhang, Z., Zhang, S., Jiang, X., Wu, D., Du, Y., & Yang, X. (2022) · Biochemistry (Moscow) · doi:10.1134/s0006297922090085 · Cited by 6

Systematic HOIP interactome profiling reveals critical roles of linear ubiquitination in tissue homeostasis

Fu, Y., Li, L., Zhang, X., Deng, Z., Wu, Y. H., Chen, W., Liu, Y., He, S., Wang, J., Xie, Y., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-47289-2 · Cited by 6

Linear polyubiquitylation of Gli protein regulates its protein stability and facilitates tumor growth in colorectal cancer

Cheng, J., Xu, L., Xuan, Y., Zhou, F., Huang, A., Zeng, S., Wang, H., Wang, Y., Zhan, Y., Yan, X., et al. (2024) · Cell Death Discovery · doi:10.1038/s41420-024-02147-4 · Cited by 6

Matrine promotes colorectal cancer apoptosis by downregulating shank-associated RH domain interactor expression

Zhou, Y.-C., Wang, Q.-Q., Zhou, G.-Y.-J., Yin, T., Zhao, D.-Y., Sun, X., Tan, C., Zhou, L., & Yao, S. (2024) · World Journal of Gastrointestinal Oncology · doi:10.4251/wjgo.v16.i12.4700 · Cited by 7

Characterization of SHARPIN knockout Syrian hamsters developed using CRISPR /Cas9 system

Miao, J., Lan, T., Guo, H., Wang, J., Zhang, G., Wang, Z., Yang, P., Li, H., Zhang, C., Wang, Y., et al. (2022) · Animal Models and Experimental Medicine · doi:10.1002/ame2.12265 · Cited by 6

Mechanistic insights into the enzymatic activity of E3 ligase HOIL-1L and its regulation by the linear ubiquitin chain binding

Xu, X., Wang, Y., Zhang, Y., Wang, Y., Yin, Y., Peng, C., Gong, X., Li, M., Zhang, Y., Zhang, M., et al. (2023) · Science Advances · doi:10.1126/sciadv.adi4599 · Cited by 4

The good, the bad, and the modified: CYLD’s post-translational tale

Macé, Y., Bidère, N., & Douanne, T. (2025) · Frontiers in Cell Death · doi:10.3389/fceld.2025.1583221 · Cited by 5

CYLD-TRAF6 interaction promotes ADP-heptose-induced NF-κB signaling in H. pylori infection

Lim, M. C. C., Maubach, G., & Naumann, M. (2025) · EMBO Reports · doi:10.1038/s44319-025-00480-y · Cited by 5

Junctional adhesion molecule C limits glioblastoma stem-like cell invasion by regulating integrin adhesion at the endothelial interface

Rosińska, S., André‐Grégoire, G., Kerhervé, M., Trillet, K., Fugio, L. B., Merlet, L., Roux, Q., Gall, M. L., Salnot, V., Faurobert, E., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116194 · Cited by 6

Parkin promotes cell survival via linear ubiquitination

Fiškin, E., & Đikić, I. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.70 · Cited by 5

Ubiquitin-Dependent Regulation of Treg Function and Plasticity

Dong, Y. W., & Pan, F. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-6407-9_4 · Cited by 5

SHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis

Ikeda, F., Deribe, Y. L., Skånland, S. S., Stieglitz, B., Grabbe, C., Franz-Wachtel, M., van Wijk, S. J. L., Goswami, P., Nagy, V., Terzic, J., et al. (2011) · Nature · doi:10.1038/nature09814 · Cited by 745

Serine 165 phosphorylation of SHARPIN regulates the activation of NF-κB

Thys, A., Trillet, K., Rosińska, S., Gayraud, A., Douanne, T., Danger, Y., Renaud, C. C. N., Antigny, L., Lavigne, R., Pineau, C., et al. (2021) · iScience · doi:10.1016/j.isci.2020.101939 · Cited by 10

Linear ubiquitination prevents inflammation and regulates immune signalling

Gerlach, B., Cordier, S. M., Schmukle, A. C., Emmerich, C. H., Rieser, E., Haas, T. L., Webb, A. I., Rickard, J. A., Anderton, H., Wong, W. W.-L., et al. (2011) · Nature · doi:10.1038/nature09816 · Cited by 940

Linear polyubiquitin chains

Iwaï, K. (2011) · Cell Cycle · doi:10.4161/cc.10.18.17437 · Cited by 32

LUBAC, a novel ubiquitin ligase for linear ubiquitination, is crucial for inflammation and immune responses

Tokunaga, F., & Iwaï, K. (2012) · Microbes and Infection · doi:10.1016/j.micinf.2012.01.011 · Cited by 92