메뉴 건너뛰기




Volumn 283, Issue 1, 2016, Pages 39-53

Regulation of Met1-linked polyubiquitin signalling by the deubiquitinase OTULIN

Author keywords

deubiquitinase; LUBAC; Met1 linked; NF B; OTULIN; signalling; substrate assisted catalysis; ubiquitin

Indexed keywords

CASPASE RECRUITMENT DOMAIN PROTEIN 15; DEUBIQUITINASE; GLUTAMIC ACID; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LINEAR UBIQUITIN CHAIN ASSEMBLY COMPLEX; MET1 LINKED POLYUBIQUITIN; OTULIN PROTEIN; POLYUBIQUITIN; PROTEIN P97; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; DNA (CYTOSINE 5) METHYLTRANSFERASE; GUMBY PROTEIN, HUMAN; PROTEINASE;

EID: 84957729036     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.13547     Document Type: Review
Times cited : (26)

References (99)
  • 3
    • 33749346301 scopus 로고    scopus 로고
    • Modification of proteins by ubiquitin and ubiquitin-like proteins
    • Kerscher O, Felberbaum R, &, Hochstrasser M, (2006) Modification of proteins by ubiquitin and ubiquitin-like proteins. Annu Rev Cell Dev Biol 22, 159-180.
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 159-180
    • Kerscher, O.1    Felberbaum, R.2    Hochstrasser, M.3
  • 4
    • 84861783400 scopus 로고    scopus 로고
    • Ubiquitin-binding proteins: Decoders of ubiquitin-mediated cellular functions
    • Husnjak K, &, Dikic I, (2012) Ubiquitin-binding proteins: decoders of ubiquitin-mediated cellular functions. Annu Rev Biochem 81, 291-322.
    • (2012) Annu Rev Biochem , vol.81 , pp. 291-322
    • Husnjak, K.1    Dikic, I.2
  • 6
    • 84937640135 scopus 로고    scopus 로고
    • The demographics of the ubiquitin system
    • Clague MJ, Heride C, &, Urbé S, (2015) The demographics of the ubiquitin system. Trends Cell Biol 25, 417-426.
    • (2015) Trends Cell Biol , vol.25 , pp. 417-426
    • Clague, M.J.1    Heride, C.2    Urbé, S.3
  • 7
    • 84864222562 scopus 로고    scopus 로고
    • Atypical ubiquitylation - The unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages
    • Kulathu Y, &, Komander D, (2012) Atypical ubiquitylation-the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages. Nat Rev Mol Cell Biol 13, 508-523.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 508-523
    • Kulathu, Y.1    Komander, D.2
  • 8
    • 79955620198 scopus 로고    scopus 로고
    • Constructing and decoding unconventional ubiquitin chains
    • Behrends C, &, Harper JW, (2011) Constructing and decoding unconventional ubiquitin chains. Nat Struct Mol Biol 18, 520-528.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 520-528
    • Behrends, C.1    Harper, J.W.2
  • 10
    • 84862248877 scopus 로고    scopus 로고
    • LUBAC, a novel ubiquitin ligase for linear ubiquitination, is crucial for inflammation and immune responses
    • Tokunaga F, &, Iwai K, (2012) LUBAC, a novel ubiquitin ligase for linear ubiquitination, is crucial for inflammation and immune responses. Microbes Infect 14, 563-572.
    • (2012) Microbes Infect , vol.14 , pp. 563-572
    • Tokunaga, F.1    Iwai, K.2
  • 11
    • 79957949190 scopus 로고    scopus 로고
    • UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids
    • Wenzel DM, Lissounov A, Brzovic PS, &, Klevit RE, (2011) UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 474, 105-108.
    • (2011) Nature , vol.474 , pp. 105-108
    • Wenzel, D.M.1    Lissounov, A.2    Brzovic, P.S.3    Klevit, R.E.4
  • 12
    • 84867096523 scopus 로고    scopus 로고
    • The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING-IBR-RING domain and the unique LDD extension
    • Smit JJ, Monteferrario D, Noordermeer SM, van Dijk WJ, van der Reijden BA, &, Sixma TK, (2012) The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING-IBR-RING domain and the unique LDD extension. EMBO J 31, 3833-3844.
    • (2012) EMBO J , vol.31 , pp. 3833-3844
    • Smit, J.J.1    Monteferrario, D.2    Noordermeer, S.M.3    Van Dijk, W.J.4    Van Der Reijden, B.A.5    Sixma, T.K.6
  • 17
    • 84867062977 scopus 로고    scopus 로고
    • A20 inhibits LUBAC-mediated NF-κB activation by binding linear polyubiquitin chains via its zinc finger 7
    • Verhelst K, Carpentier I, Kreike M, Meloni L, Verstrepen L, Kensche T, Dikic I, &, Beyaert R, (2012) A20 inhibits LUBAC-mediated NF-κB activation by binding linear polyubiquitin chains via its zinc finger 7. EMBO J 31, 3845-3855.
    • (2012) EMBO J , vol.31 , pp. 3845-3855
    • Verhelst, K.1    Carpentier, I.2    Kreike, M.3    Meloni, L.4    Verstrepen, L.5    Kensche, T.6    Dikic, I.7    Beyaert, R.8
  • 19
    • 84855517985 scopus 로고    scopus 로고
    • Specific recognition of linear ubiquitin chains by the Npl4 zinc finger (NZF) domain of the HOIL-1L subunit of the linear ubiquitin chain assembly complex
    • Sato Y, Fujita H, Yoshikawa A, Yamashita M, Yamagata A, Kaiser SE, Iwai K, &, Fukai S, (2011) Specific recognition of linear ubiquitin chains by the Npl4 zinc finger (NZF) domain of the HOIL-1L subunit of the linear ubiquitin chain assembly complex. Proc Natl Acad Sci 108, 20520-20525.
    • (2011) Proc Natl Acad Sci , vol.108 , pp. 20520-20525
    • Sato, Y.1    Fujita, H.2    Yoshikawa, A.3    Yamashita, M.4    Yamagata, A.5    Kaiser, S.E.6    Iwai, K.7    Fukai, S.8
  • 21
    • 71149105333 scopus 로고    scopus 로고
    • Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction
    • Haas TL, Emmerich CH, Gerlach B, Schmukle AC, Cordier SM, Rieser E, Feltham R, Vince J, Warnken U, Wenger T, et al,. (2009) Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction. Mol Cell 36, 831-844.
    • (2009) Mol Cell , vol.36 , pp. 831-844
    • Haas, T.L.1    Emmerich, C.H.2    Gerlach, B.3    Schmukle, A.C.4    Cordier, S.M.5    Rieser, E.6    Feltham, R.7    Vince, J.8    Warnken, U.9    Wenger, T.10
  • 27
    • 84905036773 scopus 로고    scopus 로고
    • Linear ubiquitin chains: NF-κB signalling, cell death and beyond
    • Iwai K, Fujita H, &, Sasaki Y, (2014) Linear ubiquitin chains: NF-κB signalling, cell death and beyond. Nat Rev Mol Cell Biol 15, 503-508.
    • (2014) Nat Rev Mol Cell Biol , vol.15 , pp. 503-508
    • Iwai, K.1    Fujita, H.2    Sasaki, Y.3
  • 28
    • 84912041074 scopus 로고    scopus 로고
    • Met1-linked ubiquitination in immune signalling
    • Fiil BK, &, Gyrd-Hansen M, (2014) Met1-linked ubiquitination in immune signalling. FEBS J 281, 4337-4350.
    • (2014) FEBS J , vol.281 , pp. 4337-4350
    • Fiil, B.K.1    Gyrd-Hansen, M.2
  • 32
    • 1342304089 scopus 로고    scopus 로고
    • Solution conformation of Lys63-linked di-ubiquitin chain provides clues to functional diversity of polyubiquitin signaling
    • Varadan R, Assfalg M, Haririnia A, Raasi S, Pickart C, &, Fushman D, (2004) Solution conformation of Lys63-linked di-ubiquitin chain provides clues to functional diversity of polyubiquitin signaling. J Biol Chem 279, 7055-7063.
    • (2004) J Biol Chem , vol.279 , pp. 7055-7063
    • Varadan, R.1    Assfalg, M.2    Haririnia, A.3    Raasi, S.4    Pickart, C.5    Fushman, D.6
  • 33
    • 71449095149 scopus 로고    scopus 로고
    • Two-sided ubiquitin binding explains specificity of the TAB 2 NZF domain
    • Kulathu Y, Akutsu M, Bremm A, Hofmann K, &, Komander D, (2009) Two-sided ubiquitin binding explains specificity of the TAB 2 NZF domain. Nat Struct Mol Biol 16, 1328-1330.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 1328-1330
    • Kulathu, Y.1    Akutsu, M.2    Bremm, A.3    Hofmann, K.4    Komander, D.5
  • 37
    • 39549106692 scopus 로고    scopus 로고
    • The structure of the CYLD USP domain explains its specificity for Lys63-linked polyubiquitin and reveals a B box module
    • Komander D, Lord CJ, Scheel H, Swift S, Hofmann K, Ashworth A, &, Barford D, (2008) The structure of the CYLD USP domain explains its specificity for Lys63-linked polyubiquitin and reveals a B box module. Mol Cell 29, 451-464.
    • (2008) Mol Cell , vol.29 , pp. 451-464
    • Komander, D.1    Lord, C.J.2    Scheel, H.3    Swift, S.4    Hofmann, K.5    Ashworth, A.6    Barford, D.7
  • 39
    • 30744460935 scopus 로고    scopus 로고
    • A genetic screen for mutations that affect cranial nerve development in the mouse
    • Mar L, Rivkin E, Kim DY, Yu JY, &, Cordes SP, (2005) A genetic screen for mutations that affect cranial nerve development in the mouse. J Neurosci 25, 11787-11795.
    • (2005) J Neurosci , vol.25 , pp. 11787-11795
    • Mar, L.1    Rivkin, E.2    Kim, D.Y.3    Yu, J.Y.4    Cordes, S.P.5
  • 40
    • 84891804220 scopus 로고    scopus 로고
    • MEROPS: The database of proteolytic enzymes, their substrates and inhibitors
    • Rawlings ND, Waller M, Barrett AJ, &, Bateman A, (2014) MEROPS: the database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res 42, D503-D509.
    • (2014) Nucleic Acids Res , vol.42 , pp. D503-D509
    • Rawlings, N.D.1    Waller, M.2    Barrett, A.J.3    Bateman, A.4
  • 41
    • 0037184947 scopus 로고    scopus 로고
    • Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde
    • Hu M, Li P, Li M, Li W, Yao T, Wu J-W, Gu W, Cohen RE, &, Shi Y, (2002) Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Cell 111, 1041-1054.
    • (2002) Cell , vol.111 , pp. 1041-1054
    • Hu, M.1    Li, P.2    Li, M.3    Li, W.4    Yao, T.5    Wu, J.-W.6    Gu, W.7    Cohen, R.E.8    Shi, Y.9
  • 43
    • 84862806447 scopus 로고    scopus 로고
    • The mechanism of OTUB1-mediated inhibition of ubiquitination
    • Wiener R, Zhang X, Wang T, &, Wolberger C, (2012) The mechanism of OTUB1-mediated inhibition of ubiquitination. Nature 483, 618-622.
    • (2012) Nature , vol.483 , pp. 618-622
    • Wiener, R.1    Zhang, X.2    Wang, T.3    Wolberger, C.4
  • 45
    • 79952290609 scopus 로고    scopus 로고
    • The mechanism of linkage-specific ubiquitin chain elongation by a single-subunit E2
    • Wickliffe KE, Lorenz S, Wemmer DE, Kuriyan J, &, Rape M, (2011) The mechanism of linkage-specific ubiquitin chain elongation by a single-subunit E2. Cell 144, 769-781.
    • (2011) Cell , vol.144 , pp. 769-781
    • Wickliffe, K.E.1    Lorenz, S.2    Wemmer, D.E.3    Kuriyan, J.4    Rape, M.5
  • 46
    • 84903125623 scopus 로고    scopus 로고
    • Structure of a RING E3 trapped in action reveals ligation mechanism for the ubiquitin-like protein NEDD8
    • Scott DC, Sviderskiy VO, Monda JK, Lydeard JR, Cho SE, Harper JW, &, Schulman BA, (2014) Structure of a RING E3 trapped in action reveals ligation mechanism for the ubiquitin-like protein NEDD8. Cell 157, 1671-1684.
    • (2014) Cell , vol.157 , pp. 1671-1684
    • Scott, D.C.1    Sviderskiy, V.O.2    Monda, J.K.3    Lydeard, J.R.4    Cho, S.E.5    Harper, J.W.6    Schulman, B.A.7
  • 49
    • 84875912087 scopus 로고    scopus 로고
    • Reversible inactivation of deubiquitinases by reactive oxygen species in vitro and in cells
    • Lee J-G, Baek K, Soetandyo N, &, Ye Y, (2013) Reversible inactivation of deubiquitinases by reactive oxygen species in vitro and in cells. Nat Commun 4, 1568.
    • (2013) Nat Commun , vol.4 , pp. 1568
    • Lee, J.-G.1    Baek, K.2    Soetandyo, N.3    Ye, Y.4
  • 50
    • 49649083115 scopus 로고    scopus 로고
    • Hydrogen peroxide prolongs nuclear localization of NF-kappaB in activated cells by suppressing negative regulatory mechanisms
    • Enesa K, Ito K, Luong LA, Thorbjornsen I, Phua C, To Y, Dean J, Haskard DO, Boyle J, Adcock I, et al,. (2008) Hydrogen peroxide prolongs nuclear localization of NF-kappaB in activated cells by suppressing negative regulatory mechanisms. J Biol Chem 283, 18582-18590.
    • (2008) J Biol Chem , vol.283 , pp. 18582-18590
    • Enesa, K.1    Ito, K.2    Luong, L.A.3    Thorbjornsen, I.4    Phua, C.5    To, Y.6    Dean, J.7    Haskard, D.O.8    Boyle, J.9    Adcock, I.10
  • 52
    • 84858124845 scopus 로고    scopus 로고
    • Generation and physiological roles of linear ubiquitin chains
    • Walczak H, Iwai K, &, Dikic I, (2012) Generation and physiological roles of linear ubiquitin chains. BMC Biol 10, 23.
    • (2012) BMC Biol , vol.10 , pp. 23
    • Walczak, H.1    Iwai, K.2    Dikic, I.3
  • 53
    • 4444376712 scopus 로고    scopus 로고
    • Signaling to NF-kappaB
    • Hayden MS, &, Ghosh S, (2004) Signaling to NF-kappaB. Genes Dev 18, 2195-2224.
    • (2004) Genes Dev , vol.18 , pp. 2195-2224
    • Hayden, M.S.1    Ghosh, S.2
  • 54
    • 2342464085 scopus 로고    scopus 로고
    • The two NF-kappaB activation pathways and their role in innate and adaptive immunity
    • Bonizzi G, &, Karin M, (2004) The two NF-kappaB activation pathways and their role in innate and adaptive immunity. Trends Immunol 25, 280-288.
    • (2004) Trends Immunol , vol.25 , pp. 280-288
    • Bonizzi, G.1    Karin, M.2
  • 55
    • 67650724069 scopus 로고    scopus 로고
    • Regulation and function of NF-kappaB transcription factors in the immune system
    • Vallabhapurapu S, &, Karin M, (2009) Regulation and function of NF-kappaB transcription factors in the immune system. Annu Rev Immunol 27, 693-733.
    • (2009) Annu Rev Immunol , vol.27 , pp. 693-733
    • Vallabhapurapu, S.1    Karin, M.2
  • 56
    • 84856641109 scopus 로고    scopus 로고
    • NF-κB, the first quarter-century: Remarkable progress and outstanding questions
    • Hayden MS, &, Ghosh S, (2012) NF-κB, the first quarter-century: remarkable progress and outstanding questions. Genes Dev 26, 203-234.
    • (2012) Genes Dev , vol.26 , pp. 203-234
    • Hayden, M.S.1    Ghosh, S.2
  • 58
    • 4143080425 scopus 로고    scopus 로고
    • AMSH is an endosome-associated ubiquitin isopeptidase
    • McCullough J, Clague MJ, &, Urbé S, (2004) AMSH is an endosome-associated ubiquitin isopeptidase. J Cell Biol 166, 487-492.
    • (2004) J Cell Biol , vol.166 , pp. 487-492
    • McCullough, J.1    Clague, M.J.2    Urbé, S.3
  • 59
    • 84925949741 scopus 로고    scopus 로고
    • Deubiquitinase-based analysis of ubiquitin chain architecture using Ubiquitin Chain Restriction (UbiCRest)
    • Hospenthal MK, Mevissen TET, &, Komander D, (2015) Deubiquitinase-based analysis of ubiquitin chain architecture using Ubiquitin Chain Restriction (UbiCRest). Nat Protoc 10, 349-361.
    • (2015) Nat Protoc , vol.10 , pp. 349-361
    • Hospenthal, M.K.1    Mevissen, T.E.T.2    Komander, D.3
  • 66
    • 84895822094 scopus 로고    scopus 로고
    • Mechanism underlying IκB Kinase activation mediated by the linear ubiquitin chain assembly complex
    • Fujita H, Rahighi S, Akita M, Kato R, Sasaki Y, Wakatsuki S, &, Iwai K, (2014) Mechanism underlying IκB Kinase activation mediated by the linear ubiquitin chain assembly complex. Mol Cell Biol 34, 1322-1335.
    • (2014) Mol Cell Biol , vol.34 , pp. 1322-1335
    • Fujita, H.1    Rahighi, S.2    Akita, M.3    Kato, R.4    Sasaki, Y.5    Wakatsuki, S.6    Iwai, K.7
  • 67
    • 84856474838 scopus 로고    scopus 로고
    • Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system
    • Meyer H, Bug M, &, Bremer S, (2012) Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system. Nat Cell Biol 14, 117-123.
    • (2012) Nat Cell Biol , vol.14 , pp. 117-123
    • Meyer, H.1    Bug, M.2    Bremer, S.3
  • 68
    • 33748752425 scopus 로고    scopus 로고
    • The PUB domain functions as a p97 binding module in human peptide N-glycanase
    • Allen MD, Buchberger A, &, Bycroft M, (2006) The PUB domain functions as a p97 binding module in human peptide N-glycanase. J Biol Chem 281, 25502-25508.
    • (2006) J Biol Chem , vol.281 , pp. 25502-25508
    • Allen, M.D.1    Buchberger, A.2    Bycroft, M.3
  • 69
    • 34547419767 scopus 로고    scopus 로고
    • Studies on peptide:N-glycanase-p97 interaction suggest that p97 phosphorylation modulates endoplasmic reticulum-associated degradation
    • Zhao G, Zhou X, Wang L, Li G, Schindelin H, &, Lennarz WJ, (2007) Studies on peptide:N-glycanase-p97 interaction suggest that p97 phosphorylation modulates endoplasmic reticulum-associated degradation. Proc Natl Acad Sci USA 104, 8785-8790.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 8785-8790
    • Zhao, G.1    Zhou, X.2    Wang, L.3    Li, G.4    Schindelin, H.5    Lennarz, W.J.6
  • 73
    • 84892448171 scopus 로고    scopus 로고
    • The p97-UFD1L-NPL4 protein complex mediates cytokine-induced I&kgr;Bα proteolysis
    • Li JM, Wu H, Zhang W, Blackburn MR, &, Jin J, (2014) The p97-UFD1L-NPL4 protein complex mediates cytokine-induced I&kgr;Bα proteolysis. Mol Cell Biol 34, 335-347.
    • (2014) Mol Cell Biol , vol.34 , pp. 335-347
    • Li, J.M.1    Wu, H.2    Zhang, W.3    Blackburn, M.R.4    Jin, J.5
  • 74
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa ME, Bennett EJ, Gygi SP, &, Harper JW, (2009) Defining the human deubiquitinating enzyme interaction landscape. Cell 138, 389-403.
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 75
    • 1842421376 scopus 로고    scopus 로고
    • A dynamic role of HAUSP in the p53-Mdm2 pathway
    • Li M, Brooks CL, Kon N, &, Gu W, (2004) A dynamic role of HAUSP in the p53-Mdm2 pathway. Mol Cell 13, 879-886.
    • (2004) Mol Cell , vol.13 , pp. 879-886
    • Li, M.1    Brooks, C.L.2    Kon, N.3    Gu, W.4
  • 76
    • 84871111938 scopus 로고    scopus 로고
    • Direct and indirect control of mitogen-activated protein kinase pathway-associated components, BRAP/IMP E3 ubiquitin ligase and CRAF/RAF1 kinase, by the deubiquitylating enzyme USP15
    • Hayes SD, Liu H, MacDonald E, Sanderson CM, Coulson JM, Clague MJ, &, Urbé S, (2012) Direct and indirect control of mitogen-activated protein kinase pathway-associated components, BRAP/IMP E3 ubiquitin ligase and CRAF/RAF1 kinase, by the deubiquitylating enzyme USP15. J Biol Chem 287, 43007-43018.
    • (2012) J Biol Chem , vol.287 , pp. 43007-43018
    • Hayes, S.D.1    Liu, H.2    MacDonald, E.3    Sanderson, C.M.4    Coulson, J.M.5    Clague, M.J.6    Urbé, S.7
  • 77
    • 84908028504 scopus 로고    scopus 로고
    • Ubiquitin-specific protease 19 regulates the stability of the E3 ubiquitin ligase MARCH6
    • Nakamura N, Harada K, Kato M, &, Hirose S, (2014) Ubiquitin-specific protease 19 regulates the stability of the E3 ubiquitin ligase MARCH6. Exp Cell Res 328, 207-216.
    • (2014) Exp Cell Res , vol.328 , pp. 207-216
    • Nakamura, N.1    Harada, K.2    Kato, M.3    Hirose, S.4
  • 81
    • 77951622671 scopus 로고    scopus 로고
    • A20: From ubiquitin editing to tumour suppression
    • Hymowitz SG, &, Wertz IE, (2010) A20: from ubiquitin editing to tumour suppression. Nat Rev Cancer 10, 332-341.
    • (2010) Nat Rev Cancer , vol.10 , pp. 332-341
    • Hymowitz, S.G.1    Wertz, I.E.2
  • 84
    • 61949220270 scopus 로고    scopus 로고
    • The ubiquitin-editing enzyme A20 requires RNF11 to downregulate NF-kappaB signalling
    • Shembade N, Parvatiyar K, Harhaj NS, &, Harhaj EW, (2009) The ubiquitin-editing enzyme A20 requires RNF11 to downregulate NF-kappaB signalling. EMBO J 28, 513-522.
    • (2009) EMBO J , vol.28 , pp. 513-522
    • Shembade, N.1    Parvatiyar, K.2    Harhaj, N.S.3    Harhaj, E.W.4
  • 85
    • 77649225756 scopus 로고    scopus 로고
    • Inhibition of NF-{kappa}B signaling by A20 through disruption of ubiquitin enzyme complexes
    • Shembade N, Ma A, &, Harhaj EW, (2010) Inhibition of NF-{kappa}B signaling by A20 through disruption of ubiquitin enzyme complexes. Science 327, 1135-1139.
    • (2010) Science , vol.327 , pp. 1135-1139
    • Shembade, N.1    Ma, A.2    Harhaj, E.W.3
  • 87
    • 84903726513 scopus 로고    scopus 로고
    • The deubiquitinase activity of A20 is dispensable for NF-κB signaling
    • De A, Dainichi T, Rathinam CV, &, Ghosh S, (2014) The deubiquitinase activity of A20 is dispensable for NF-κB signaling. EMBO Rep 15, 775-783.
    • (2014) EMBO Rep , vol.15 , pp. 775-783
    • De, A.1    Dainichi, T.2    Rathinam, C.V.3    Ghosh, S.4
  • 89
    • 0042467558 scopus 로고    scopus 로고
    • CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members
    • Trompouki E, Hatzivassiliou E, Tsichritzis T, Farmer H, Ashworth A, &, Mosialos G, (2003) CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members. Nature 424, 793-796.
    • (2003) Nature , vol.424 , pp. 793-796
    • Trompouki, E.1    Hatzivassiliou, E.2    Tsichritzis, T.3    Farmer, H.4    Ashworth, A.5    Mosialos, G.6
  • 90
    • 0042467554 scopus 로고    scopus 로고
    • Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-kappaB
    • Brummelkamp TR, Nijman SMB, Dirac AMG, &, Bernards R, (2003) Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-kappaB. Nature 424, 797-801.
    • (2003) Nature , vol.424 , pp. 797-801
    • Brummelkamp, T.R.1    Nijman, S.M.B.2    Dirac, A.M.G.3    Bernards, R.4
  • 91
  • 92
    • 77449150629 scopus 로고    scopus 로고
    • CYLD: A tumor suppressor deubiquitinase regulating NF-kappaB activation and diverse biological processes
    • Sun S-C, (2010) CYLD: a tumor suppressor deubiquitinase regulating NF-kappaB activation and diverse biological processes. Cell Death Differ 17, 25-34.
    • (2010) Cell Death Differ , vol.17 , pp. 25-34
    • Sun, S.-C.1
  • 94
    • 84862907678 scopus 로고    scopus 로고
    • Ubiquitin-specific protease 4 (USP4) targets TRAF2 and TRAF6 for deubiquitination and inhibits TNFα-induced cancer cell migration
    • Xiao N, Li H, Luo J, Wang R, Chen H, Chen J, &, Wang P, (2012) Ubiquitin-specific protease 4 (USP4) targets TRAF2 and TRAF6 for deubiquitination and inhibits TNFα-induced cancer cell migration. Biochem J 441, 979-986.
    • (2012) Biochem J , vol.441 , pp. 979-986
    • Xiao, N.1    Li, H.2    Luo, J.3    Wang, R.4    Chen, H.5    Chen, J.6    Wang, P.7
  • 96
    • 74049114641 scopus 로고    scopus 로고
    • Ubiquitin-specific peptidase 21 inhibits tumor necrosis factor alpha-induced nuclear factor kappaB activation via binding to and deubiquitinating receptor-interacting protein 1
    • Xu G, Tan X, Wang H, Sun W, Shi Y, Burlingame S, Gu X, Cao G, Zhang T, Qin J, et al,. (2010) Ubiquitin-specific peptidase 21 inhibits tumor necrosis factor alpha-induced nuclear factor kappaB activation via binding to and deubiquitinating receptor-interacting protein 1. J Biol Chem 285, 969-978.
    • (2010) J Biol Chem , vol.285 , pp. 969-978
    • Xu, G.1    Tan, X.2    Wang, H.3    Sun, W.4    Shi, Y.5    Burlingame, S.6    Gu, X.7    Cao, G.8    Zhang, T.9    Qin, J.10
  • 99
    • 33646117490 scopus 로고    scopus 로고
    • Functional screening for proapoptotic genes by reverse transfection cell array technology
    • Mannherz O, Mertens D, Hahn M, &, Lichter P, (2006) Functional screening for proapoptotic genes by reverse transfection cell array technology. Genomics 87, 665-672.
    • (2006) Genomics , vol.87 , pp. 665-672
    • Mannherz, O.1    Mertens, D.2    Hahn, M.3    Lichter, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.