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

Shared Principles in NF-κB Signaling

Hayden, M. S., & Ghosh, S. (2008) · Cell · doi:10.1016/j.cell.2008.01.020 · Cited by 4,954

Nuclear factor-κB in cancer development and progression

Karin, M. (2006) · Nature · doi:10.1038/nature04870 · Cited by 3,519

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

Vallabhapurapu, S., & Karin, M. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132641 · Cited by 2,635

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

Yamaoka, S., Courtois, G., Chable-Bessia, C., Whiteside, S. T., Weil, R., Agou, F., Kirk, H., Kay, R. J., & Israël, A. (1998) · Cell · doi:10.1016/s0092-8674(00)81466-x · Cited by 1,077

Involvement of linear polyubiquitylation of NEMO in NF-κB activation

Tokunaga, F., Sakata, S., Saeki, Y., Satomi, Y., Kirisako, T., Kamei, K., Nakagawa, T., Kato, M., Murata, S., Yamaoka, S., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1821 · Cited by 960

A ubiquitin ligase complex assembles linear polyubiquitin chains

Kirisako, T., Kamei, K., Murata, S., Kato, M., Fukumoto, H., Kanie, M., Sano, S., Tokunaga, F., Tanaka, K., & Iwaï, K. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601360 · Cited by 803

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

Expression, solubility monitoring, and purification of the co-folded LUBAC LTM domain by structure-guided tandem folding in autoinducing cultures

Walinda, E., Morimoto, D., Sorada, T., Iwaï, K., & Sugase, K. (2021) · Protein Expression and Purification · doi:10.1016/j.pep.2021.105953 · Cited by 5

Functional Significance of the E3 Ubiquitin Ligases in Disease and Therapeutics

Dongdem, J. T., & Wezena, C. A. (2021) · Biochemistry · doi:10.5772/intechopen.100534 · Cited by 5

A Polymorphism in the Gene Encoding Heat Shock Factor 1 (HSF1) Increases the Risk of Type 2 Diabetes: A Pilot Study Supports a Role for Impaired Protein Folding in Disease Pathogenesis

Klyosova, E. Y., Azarova, I. E., & Polonikov, A. (2022) · Life · doi:10.3390/life12111936 · Cited by 6

Aberrant expression and high‑frequency mutations of SHARPIN in nonmelanoma skin cancer

Zheng, Y., Yang, Y., Wang, J., & Liang, Y. (2019) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2019.7261 · Cited by 5

SHARPIN regulates cell proliferation of cutaneous basal cell carcinoma via inactivation of the transcriptional factors GLI2 and c‑JUN

Yang, Y., Liang, Y., Zheng, Y., Tang, L., Zhou, S., & Zhu, J. (2020) · Molecular Medicine Reports · doi:10.3892/mmr.2020.10981 · Cited by 5

Effects of removing a highly conserved disulfide bond in ubiquitin-associated domain of human HOIP on biochemical characteristics

Ma, W., Lu, Y., Zuo, Y., Wang, C., & Liu, J. (2021) · Protein Expression and Purification · doi:10.1016/j.pep.2021.106005 · Cited by 5

Cysteine-rich zinc finger proteins and the nuclear factor kappa-B pathway

Stoltzfus, A. T., & Michel, S. L. J. (2024) · Frontiers in Chemical Biology · doi:10.3389/fchbi.2024.1503390 · Cited by 4

Shared interactions of six neurotropic viruses with 38 human proteins: a computational and literature-based exploration of viral interactions and hijacking of human proteins in neuropsychiatric disorders

Ozer, E. A., Keskin, A., Berrak, Y. H., Cankara, F., Can, F., Özdemir, Y., Keskin, Ö., Gürsoy, A., & Eser, H. Y. (2025) · Discover Mental Health · doi:10.1007/s44192-025-00128-2 · Cited by 4

Primary disorders of polyubiquitination: Dual roles in autoinflammation and immunodeficiency

Spaan, A. N., Boisson, B., & Masters, S. L. (2025) · The Journal of Experimental Medicine · doi:10.1084/jem.20241047 · Cited by 4

Monogenic disorders of the TNF signalling pathway

Lalaoui, N., & Masters, S. L. (2025) · Nature Reviews Rheumatology · doi:10.1038/s41584-025-01327-5 · Cited by 6

Immunoblot Analysis of Linear Polyubiquitination of NEMO

Sasaki, Y., Fujita, H., Nakai, M., & Iwaï, K. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2422-6_17 · Cited by 4

Characterisation of HOIP RBR E3 ligase conformational dynamics using integrative modelling

Kausas, M., Esposito, D., Rittinger, K., & Fraternali, F. (2022) · Scientific Reports · doi:10.1038/s41598-022-18890-6 · Cited by 4

TSG101 Physically Interacts with Linear Ubiquitin Chain Assembly Complex (LUBAC) and Upregulates the TNFα-Induced NF-κB Activation

Kim, E., Cho, H., Lee, G., Baek, H., Lee, I., & Choi, E. (2023) · Molecules and Cells · doi:10.14348/molcells.2023.0026 · Cited by 4

LUBAC and ABIN-1 Modulate TRAIL-Based NF-κB Induction in Human Embryonic Kidney 293 Cells

Dörn, S., Schoergenhofer, C., Krainer, M., Müller, M., & Jilma, B. (2018) · BioResearch open access · doi:10.1089/biores.2018.0006 · Cited by 4

Shank‑associated RH domain‑interacting protein expression is upregulated in entodermal and mesodermal cancer or downregulated in ectodermal malignancy

Liang, Y., Chen, B., Liu, F., Wang, J., Yang, Y., Zheng, Y., & Tan, S. (2018) · Oncology Letters · doi:10.3892/ol.2018.9514 · Cited by 4

NOD ‐Like Receptors

Arnold, C. M., Kienes, I., Sowa, A. S., & Kufer, T. A. (2018) · Wiley eBooks · doi:10.1002/9780470015902.a0026236 · Cited by 4

Discovery of DTX3L inhibitors through a homogeneous FRET-based assay that monitors formation and removal of poly-ubiquitin chains

Vela‐Rodríguez, C., Scarpulla, I., Ashok, Y., & Lehtiö, L. (2023) · SLAS DISCOVERY · doi:10.1016/j.slasd.2023.08.005 · Cited by 3

Human Viral Oncoproteins and Ubiquitin–Proteasome System

Atani, Z. R., Hosseini, S. S., Goudarzi, H., & Faghihloo, E. (2024) · Global Medical Genetics · doi:10.1055/s-0044-1790210 · Cited by 3

NMR resonance assignments of the NZF domain of mouse HOIL-1L free and bound to linear di-ubiquitin

Ishii, N., Walinda, E., Iwakawa, N., Morimoto, D., Iwaï, K., Sugase, K., & Shirakawa, M. (2018) · Biomolecular NMR Assignments · doi:10.1007/s12104-018-09868-5 · Cited by 3

OTULIN and Muller’s morphs

Spaan, A. N. (2024) · The Journal of Experimental Medicine · doi:10.1084/jem.20240418 · Cited by 3

IAPs and Necroptotic Cell Death

Silke, J., & Vaux, D. L. (2014) · Springer eBooks · doi:10.1007/978-1-4614-8220-8_4 · Cited by 3

Crystallization of SHARPIN using an automated two-dimensional grid screen for optimization

Stieglitz, B., Rittinger, K., & Haire, L. F. (2012) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309112022208 · Cited by 3

Deficiency of the E3 Ubiquitin Ligase RBCK1 Causes Diffuse Brain Polyglucosan Accumulation and NeurodegenerationPreprint

Sullivan, M. A., Nitschké, F., Chown, E. E., DiGiovanni, L. F., Chown, M., Perri, A. M., Mitra, S., Zhao, X., Ackerley, C. A., Israelian, L., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/277392 · Cited by 3

BATF3-dependent induction of IL-27 in B cells bridges the innate and adaptive stages of the antibody responsePreprint

Yan, H. M., Wang, R., Wang, J., Wu, S., Fernandez, M., Rivera, C. E., Cervantes, C., Moroney, J. B., Li, X.-D., Zhang, N., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.06.26.117010 · Cited by 3

Linear ubiquitination at damaged lysosomes induces local NF-κB activation and controls cell survivalPreprint

Zein, L., Dietrich, M., Balta, D., Bader, V., Scheuer, C., Zellner, S., Weinelt, N., Vandrey, J., Mari, M. C., Behrends, C., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.10.06.560832 · Cited by 3

HOIL1 mediates MDA5 activation through ubiquitination of LGP2Preprint

Cheng, D., Zhu, J., Liu, G., Gack, M. U., & MacDuff, D. A. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.04.02.587772 · Cited by 3

Solution structure of the HOIL-1L NZF domain reveals a conformational switch regulating linear ubiquitin affinity

Walinda, E., Sugase, K., Ishii, N., Shirakawa, M., Iwaï, K., & Morimoto, D. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105165 · Cited by 2

Synergistic involvement of the NZF domains of the LUBAC accessory subunits HOIL-1L and SHARPIN in the regulation of LUBAC function

Toda, Y., Fujita, H., Mino, K., Koyama, T., Matsuoka, S., Kaizuka, T., Agawa, M., Matsumoto, S., Idei, A., Nishikori, M., et al. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-07199-z · Cited by 2

Mechanisms, regulation and clinical relevance of necroptosis

Yang, Y., Jiao, H., & Xu, D. (2026) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-026-01002-x · Cited by 2

IAP Proteins and Their Therapeutic Potential

Vucic, D. (2013) · Springer eBooks · doi:10.1007/978-1-4614-9302-0_5 · Cited by 2

Biochemical and functional characterization of the N-terminal ubiquitin-like domain of human SHARPIN

Ma, W., Lu, Y., Qi, J., Zuo, Y., Wang, C., Zheng, X., & Liu, J. (2021) · Protein Expression and Purification · doi:10.1016/j.pep.2021.106042 · Cited by 2

Linear ubiquitination‐induced necrotic tumor remodeling elicits immune evasion

Sasaki, K., Hayamizu, Y., Murakami, R., Toi, M., & Iwaï, K. (2023) · FEBS Letters · doi:10.1002/1873-3468.14623 · Cited by 2

An interaction between OTULIN and SCRIB uncovers roles for linear ubiquitination in planar cell polarity

Almeida, S. M., Ivantsiv, S., Niibori, R., Dunham, W. H., Green, B. A., Zhao, L., Gingras, A., & Cordes, S. P. (2023) · Disease Models & Mechanisms · doi:10.1242/dmm.049762 · Cited by 2

CRISPR/Cas9-mediated knock-in cells of the late-onset Alzheimer’s disease-risk variant, SHARPIN G186R, reveal reduced NF-κB pathway and accelerated Aβ secretion

Asanomi, Y., Kimura, T., Shimoda, N., Shigemizu, D., Niida, S., & Ozaki, K. (2024) · Journal of Human Genetics · doi:10.1038/s10038-024-01224-x · Cited by 3

Comparative analysis of meningeal transcriptomes in birds: Potential pathways of resilience to repeated impacts

Beatty, A. E., Barnes‐Tompkins, T. M., Long, K. M., & Tobiansky, D. J. (2024) · The Anatomical Record · doi:10.1002/ar.25583 · Cited by 2

Linear ubiquitin chain induces apoptosis and inhibits tumor growth

Qin, Z., Jiang, W., Wang, G., Sun, Y., & Xiao, W. (2017) · APOPTOSIS · doi:10.1007/s10495-017-1433-8 · Cited by 2

Identification and molecular analysis of RNF31 Q622H germline polymorphism

Nakazawa, S., Mamiya, R., Kawabata‐Iwakawa, R., Oikawa, D., Kaira, K., Tokunaga, F., Nobusawa, S., Sato, Y., Sasaki, A., Yajima, T., et al. (2022) · Oncology Letters · doi:10.3892/ol.2022.13514 · Cited by 3

Linear Ubiquitination Mediates EGFR-Induced NF-kB Pathway and Tumor DevelopmentPreprint

Hua, F., Hap, W., Wang, L., & Li, S. (2021) · Preprints.org · doi:10.20944/preprints202109.0394.v1 · Cited by 2

Species-specific LUBAC-mediated M1 ubiquitination regulates necroptosis by segregating the cellular distribution and fate of activated MLKLPreprint

Weinelt, N., Wächtershäuser, K. N., Smith, S. M., Andrieux, G., Das, T., Jeiler, B., Roedig, J., Feist, L., Rotter, B., Boerries, M., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.12.08.519265 · Cited by 2

STK4 inhibits the E3 activity of HOIP by phosphorylating its allosteric ubiquitin-binding site

Wang, Y., Zhou, X., Lin, Z., Huang, Y., Zhang, Y., Liu, H., Zhou, Y., Liu, J., & Pan, L. (2025) · Cell Discovery · doi:10.1038/s41421-025-00824-x · Cited by 1

Vinburnine Sensitizes Radiotherapy Efficacy in Nasopharyngeal Carcinoma by Triggering Pyroptosis and Immune Responses via Activation of EDAR‐NFκB Pathway

Chen, J., Liu, N., Tao, Q., Wu, J., Huang, J., Lü, C., Li, Q., Shen, L., Chen, X., & Peng, C. (2025) · Advanced Science · doi:10.1002/advs.202506139 · Cited by 1

Receptor-Interacting Protein Kinase 1 (RIPK1): A Potential Therapeutic Target in Ischemic Stroke

Liu, Z., Xu, F., Wang, Z., Zhang, Y., Zhao, Y., & Fang, W. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-05661-x · Cited by 1

Ubiquitin beyond the proteome: lipids, glycans, metabolites, nucleic acids, and an expanding molecular landscape

Endo, A., & Yoshida, Y. (2026) · Biochemical Society Transactions · doi:10.1042/bst20260081 · Cited by 1

Pyoderma gangrenosum caused by the molecular uncoupling of OTULIN catalytic activity and LUBAC binding

Swaminathan, B., Gil, H. M., Bhattad, S., Janardhanan, J., Baltodano, G. M., Mariskanish, C., Basaria, S., Choi, J. M., Liu, Q., Scheepmaker, L. M., et al. (2026) · Nature Immunology · doi:10.1038/s41590-026-02568-6 · Cited by 1

Synthesis and Analysis of Linear Ubiquitin Chains

Iwaï, K. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-474-2_16 · Cited by 2

Apoptosis

Wible, D. J., & Bratton, S. B. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.65424-7 · Cited by 1

Linear Polyubiquitination: A Crucial Regulator of NF-κB Activation

Iwaï, K. (2015) · Springer eBooks · doi:10.1007/978-4-431-55651-0_4 · Cited by 1

Apoptosis: the extrinsic pathway

Teng, X., & Hardwick, J. M. (2013) · Cambridge University Press eBooks · doi:10.1017/cbo9781139046947.031 · Cited by 1

Immunoblot Analysis of the Regulation of TNF Receptor Family-Induced NF-κB Signaling by c-IAP Proteins

Varfolomeev, E. E., Goncharov, T., & Vucic, D. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1669-7_7 · Cited by 1

2011: Signaling Breakthroughs of the Year

Adler, E. M. (2012) · Science Signaling · doi:10.1126/scisignal.2002787 · Cited by 1

The role of ripk1 in tnf-induced cell death in intestinal epithelial cells

Garcia‐Carbonell, R. (2017) · Dipòsit Digital de la Universitat de Barcelona (Universitat de Barcelona) · Cited by 1

Excess Met1-ubiquitination leads to solid aggregate formationPreprint

Kaypee, S., Miyasaka, M., NAKAJIMA, T., Nishimura, H., Sakamaki, J.-I., Komatsu, M., & Ikeda, F. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.20.700516 · Cited by 1

The binding of OTULIN restrains LUBAC activity to prevent TNF-driven immunopathologyPreprint

Lyu, W., Fiil, B. K., Rizk, J., Kjær, M., Sauerland, M. B., Ma, B., Jessen, M., Damgaard, R. B., & Gyrd‐Hansen, M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.27.708452 · Cited by 1

SHARPIN serine 146 phosphorylation mediates ARP2/3 interaction, cancer cell invasion and metastasis

Butt, U., Khan, M. H., Pouwels, J., & Westermarck, J. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.21.477220 · Cited by 6

Molecular Mechanism of Ubiquitin-Dependent Traffic

Maspero, E., Wollscheid, H.-P., & Polo, S. (2013) · Springer eBooks · doi:10.1007/978-1-4614-6528-7_10

Characterization of phosphorylation-dependent interactions involving neurofibromin 2 (NF2, merlin) isoforms and the Parkinson protein 7 (PARK7, DJ1)

Worseck, J. M. (2012) · edoc Publication server (Humboldt University of Berlin) · doi:10.18452/16533

New Tools for Ubiquitin Signaling

Keusekotten, K., & Komander, D. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.02.032

TAB3 in B Cell Activation via MAPKs Polyubiquitin-Binding Proteins TAB2 and Essential Roles of K63-Linked

Mino, T., Akira, S., Takeuchi, O., Ori, D., Kato, H., Sanjo, H., & Tartey, S. (2013)

Regulation of Death Receptor-Induced Necroptosis by Ubiquitination

Darding, M., & Walczak, H. (2014) · Springer eBooks · doi:10.1007/978-1-4614-8220-8_5

Regulation of NF-κB Pathway by Linkage-Specific Ubiquitin-Binding Domains

Sato, Y. (2015) · Springer eBooks · doi:10.1007/978-4-431-55561-2_10

Ubiquitination-Mediated NF-κB Regulation in Inflammatory Response

Tokunaga, F. (2015) · Springer eBooks · doi:10.1007/978-4-431-55561-2_12 · Cited by 1

Key Roles of Ubiquitination and Phosphorylation in RIG-I/MAVS Viral Sensing Pathway

Liu, S. (2013)

The Role of TRAF1 in Signaling Downstream of 4-1BB on CD8 T Cells

McPherson, A. J. (2013) · TSpace (University of Toronto)

Proteasomal Degradation of Soluble, Misfolded Proteins

Seneci, P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800186-8.00003-1

Holding RIPK1 on the Ubiquitin Leash in TNFR1

Peltzer, S., Darding, M., & Walczak, H. (2016)

The Role of TNFR Family Members GITR and CD30 on CD8 T Cell Responses

Snell, L. M. (2013) · TSpace (University of Toronto)

IAPs and Resistance to Death Receptors in Cancer

Dubrez, L., & Fulda, S. (2017) · Resistance to targeted anti-cancer therapeutics · doi:10.1007/978-3-319-56805-8_3

OPTN translocates to an ATG9A-positive compartment to regulate innate immune signalling and cytokine secretionPreprint

O’Loughlin, T. A., Kruppa, A. J., Ribeiro, A. L. R., Edgar, J. R., Ghannam, A., Smith, A. M., & Buß, F. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/744672

A role for SHARPIN in platelet linear protein ubiquitination and functionPreprint

Moore, S., Zhao, X., Mallah, S., Poole, A. W., Mundell, S. J., Hutchinson, J. L., & Hers, I. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.01.13.426403

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

Diaz, C. G., Jonsson, G., Schodl, K., Deszcz, L., Bestehorn, A., Eislmayr, K., Almagro, J., Kavirayani, A., Fennell, L. M., Hagelkruys, A., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.13.439587

M1-linked ubiquitination facilitates NF-κB activation during sterile inflammationPreprint

Aalto, A. L., Martínez‐Chacón, G., Tsyganova, N., Kreutzer, J., Kallio, P. J., Broemer, M., & Meinander, A. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.03.446895

Mathematical Simulation of Linear Ubiquitination in T Cell Receptor-Mediated NF-κB Activation Pathway

Oikawa, D., Hatanaka, N., Suzuki, T., & Tokunaga, F. (2021) · Springer proceedings in mathematics & statistics · doi:10.1007/978-981-16-4866-3_14

Regulación de la señalización del ABA mediante mecanismos que controlan vida media y actividad de los receptores PYR/PYL

López, M. A. F. (2021) · RiuNet (Universitat Politècnica de València) · doi:10.4995/thesis/10251/172364

Sterilita da asciutta in risaia

Moletti, M. (2003) · Informatore agrario

Tumor Necrosis Factor

Chu, W. (2014) · Springer eBooks · doi:10.1007/978-3-642-27841-9_6040-8

TIR Signaling Pathway Deficiency, HOIL1 Deficiency

Fung, S., & Turvey, S. E. (2020) · Springer eBooks · doi:10.1007/978-1-4614-8678-7_48

TIR Signaling Pathway Deficiency, HOIL1 Deficiency

Fung, S., & Turvey, S. E. (2018) · Springer eBooks · doi:10.1007/978-1-4614-9209-2_48-1

Tumor Necrosis Factor

Chu, W. (2017) · Springer eBooks · doi:10.1007/978-3-662-46875-3_6040

State-dependent protein-protein interactions mediating 4-1BB CAR SignalingPreprint

Ritmeester-Loy, S. A., Lautz, J. D., Zhang-Wong, Y., Gustafson, J. A., Wilson, A. L., Lin, C., Gafken, P. R., Jensen, M. C., Orentas, R. J., & Smith, S. E. P. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.07.495180

Regulation of NF-κB Signaling by Regulatory Ubiquitination: Specific Pathways and A20

De, A. (2015) · Springer theses · doi:10.1007/978-3-319-14965-3_2

Analyzing Functional Interactions of Designed Peptides by NMR Spectroscopy

Choi, W. (2023) · Chapman University Digital Commons (Chapman University) · doi:10.36837/chapman.000507

Mind bomb 2 limits inflammatory dermatitis in Sharpin mutant mice independently of cell death

Simpson, D. S., Anderton, H., Yousef, J. M., Vaibhav, V., Cobbold, S. A., Bandala‐Sanchez, E., Kueh, A. J., Dagley, L. F., Herold, M. J., Silke, J., et al. (2023) · PNAS Nexus · doi:10.1093/pnasnexus/pgad438

Met1-linked ubiquitination in cell signaling regulation

Guo, Y., Zhao, Y., & Cong, Y. (2024) · Biophysics Reports · doi:10.52601/bpr.2024.230030

Antibody-dependent Intracellular neutralisation by TRIM21 is potentiated by HOIP and linear ubiquitin chainsPreprint

Green, C., Winklhofer, K. F., Fletcher, A. J., James, L. C., Skidmore, J., Duce, J. A., & McEwan, W. A. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.04.02.587719

The Ligands of the Tumor Necrosis Factor Superfamily and Their Receptors

Wajant, H. (2024) · Elsevier eBooks · doi:10.1016/b978-0-128-24465-4.00052-1

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

Wang, X. S., Jiou, J., Cerra, A., Cobbold, S. A., Jochem, M., Mak, K. H. T., Corcilius, L., Payne, R. J., Goddard‐Borger, E. D., Komander, D., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.29.626046

Genome-wide screen based on 2DG activated NLRP3 inflammasome reveals the priming signal of TLR2/4 to IKKβ but not IKKα

Gao, H., Sun, M., Gao, H., Sun, Y., Chen, W., & Dong, N. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.113781

Homozygous OTULIN Variant Linked to OTULIN-Related Autoinflammatory Syndrome with Abscess FormationPreprint

Alkhammash, S., Monecke, T., Moepps, B., Bajaber, D., Untereiner, M., Debatin, K., Walczak, H., Niessing, D., Fischer‐Posovszky, P., & Zinngrebe, J. (2025) · medRxiv · doi:10.1101/2025.03.04.25323351 · Cited by 1

Human inborn errors of type I interferon–independent intrinsic immunity in nonleukocytic cells

Zhang, S., Casanova, J., & Spaan, A. N. (2025) · Current Opinion in Immunology · doi:10.1016/j.coi.2025.102651 · Cited by 1

Apoptosis

Wible, D. J., & Bratton, S. B. (2018) · Elsevier eBooks · doi:10.1016/b978-0-323-95488-4.20017-x

E2 variants for probing E3 ubiquitin ligase activities

Du, J., Andree, G. A., Horn‐Ghetko, D., Stier, L. J., Singh, J., Kostrhon, S., Kiss, L., Mann, M., Sidhu, S. S., & Schulman, B. A. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2524899122

Linear ubiquitination triggers Amph-mediated T-tubule biogenesis

Kawaguchi, K., Hama, Y., Yoshikawa, H., Nishino, K., Morimoto, K., Nakamura, T. S., Koizumi, M., Sakamaki, Y., Abe, K., Kakuta, S., et al. (2026) · Science Advances · doi:10.1126/sciadv.ady4934

Purification and analysis of cell death complexes

Yan, L., & Xu, D. (2026) · Methods in cell biology · doi:10.1016/bs.mcb.2026.02.018

Deubiquitinating enzyme MINDY2 regulates TNF-α-induced cell death by targeting RIPK1

Huang, W., Chen, Y., Chen, D., Liu, Y., Lu, J., Feng, J., Lin, J., & Li, L. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.117134

Organisation et dynamique des protéines d'échafaudage de la postsynapse glutamatergique : implications dans la physio-pathologie de la transmission synaptique.

Moutin, E. (2011) · theses.fr (ABES) · doi:10.70675/05b33070za45dz42c0za7a2z5ae562c649c7

Uncovering ubiquitylation pathways in liver metabolism by a proteomic approach

Magliarelli, H. D. F. (2014) · theses.fr (ABES) · doi:10.70675/0aca726cz3a4bz4a79z8398z0300a98caba3

Le rôle de l’ubiquitination et des endomembranes dans l’activation du facteur de transcription NF-κB

Zemirli, N. (2014) · theses.fr (ABES) · doi:10.70675/098ff617z3ed6z43caz9f51z004f55dce561

Caractérisation de nouveaux inhibiteurs de la kinase RIPK1 et de la nécroptose

Cann, F. L. (2017) · theses.fr (ABES) · doi:10.70675/14750b73za612z432ezbf7cz5b72ea09e2e5

Identification and functional characterization of LACC1 in familial forms of juvenile idiopathic arthritis

Omarjee, O. (2019) · theses.fr (ABES) · doi:10.70675/1b227389z0b09z451cza8adze7187b6b8888

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