| http://purl.uniprot.org/citations/32403254 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/32403254 | http://www.w3.org/2000/01/rdf-schema#comment | "The linear ubiquitin chain assembly complex (LUBAC) is a ubiquitin ligase composed of the Heme-oxidized IRP2 ubiquitin ligase-1L (HOIL-1L), HOIL-1L-interacting protein (HOIP), and Shank-associated RH domain interactor (SHARPIN) subunits. LUBAC specifically generates the N-terminal Met1-linked linear ubiquitin chain and regulates acquired and innate immune responses, such as the canonical nuclear factor-κB (NF-κB) and interferon antiviral pathways. Deubiquitinating enzymes, OTULIN and CYLD, physiologically bind to HOIP and control its function by hydrolyzing the linear ubiquitin chain. Moreover, proteins containing linear ubiquitin-specific binding domains, such as NF-κB-essential modulator (NEMO), optineurin, A20-binding inhibitors of NF-κB (ABINs), and A20, modulate the functions of LUBAC, and the dysregulation of the LUBAC-mediated linear ubiquitination pathway induces cancer and inflammatory, autoimmune, and neurodegenerative diseases. Therefore, inhibitors of LUBAC would be valuable to facilitate investigations of the molecular and cellular bases for LUBAC-mediated linear ubiquitination and signal transduction, and for potential therapeutic purposes. We identified and characterized α,β-unsaturated carbonyl-containing chemicals, named HOIPINs (HOIP inhibitors), as LUBAC inhibitors. We summarize recent advances in elucidations of the pathophysiological functions of LUBAC-mediated linear ubiquitination and identifications of its regulators, toward the development of LUBAC inhibitors."xsd:string |
| http://purl.uniprot.org/citations/32403254 | http://purl.org/dc/terms/identifier | "doi:10.3390/ijms21093381"xsd:string |
| http://purl.uniprot.org/citations/32403254 | http://purl.uniprot.org/core/author | "Ito H."xsd:string |
| http://purl.uniprot.org/citations/32403254 | http://purl.uniprot.org/core/author | "Sato Y."xsd:string |
| http://purl.uniprot.org/citations/32403254 | http://purl.uniprot.org/core/author | "Tokunaga F."xsd:string |
| http://purl.uniprot.org/citations/32403254 | http://purl.uniprot.org/core/author | "Oikawa D."xsd:string |
| http://purl.uniprot.org/citations/32403254 | http://purl.uniprot.org/core/date | "2020"xsd:gYear |
| http://purl.uniprot.org/citations/32403254 | http://purl.uniprot.org/core/name | "Int J Mol Sci"xsd:string |
| http://purl.uniprot.org/citations/32403254 | http://purl.uniprot.org/core/pages | "E3381"xsd:string |
| http://purl.uniprot.org/citations/32403254 | http://purl.uniprot.org/core/title | "Linear Ubiquitin Code: Its Writer, Erasers, Decoders, Inhibitors, and Implications in Disorders."xsd:string |
| http://purl.uniprot.org/citations/32403254 | http://purl.uniprot.org/core/volume | "21"xsd:string |
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