메뉴 건너뛰기




Volumn 19, Issue 18, 2013, Pages 3263-3275

When ubiquitin meets NF-κB: A trove for anti-cancer drug development

Author keywords

Cancer; NF B; Therapeutics; Ubiquitin

Indexed keywords

ANTINEOPLASTIC AGENT; AT 406; BIRINAPANT; BORTEZOMIB; CARFILZOMIB; DELANZOMIB; GDC 0152; GDC 0917; HGS 1029; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1; IXAZOMIB CITRATE; LCL 161; MLN 9074; MYELOID DIFFERENTIATION FACTOR 88; ONY 0912; OPROZOMIB; PEVONEDISTAT; PHOSPHOTRANSFERASE; PROTEASOME; RG 7112; SALINOSPORAMIDE A; SERDEMETAN; T LYMPHOCYTE RECEPTOR; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84878875514     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/1381612811319180010     Document Type: Article
Times cited : (23)

References (164)
  • 1
    • 0018772190 scopus 로고
    • Resolution of the ATP-dependent proteolytic system from reticulocytes: A component that interacts with ATP
    • Hershko A, Ciechanover A, Rose IA. Resolution of the ATP-dependent proteolytic system from reticulocytes: a component that interacts with ATP. Proc Natl Acad Sci USA 1979; 76: 3107-10.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 3107-3110
    • Hershko, A.1    Ciechanover, A.2    Rose, I.A.3
  • 2
    • 0022481133 scopus 로고
    • Multiple nuclear factors interact with the immunoglobulin enhancer sequences
    • Sen R, Baltimore D. Multiple nuclear factors interact with the immunoglobulin enhancer sequences. Cell 1986; 46: 705-16.
    • (1986) Cell , vol.46 , pp. 705-716
    • Sen, R.1    Baltimore, D.2
  • 3
    • 1542344435 scopus 로고    scopus 로고
    • Proteasomes and their kin: Proteases in the machine age
    • Pickart CM, Cohen RE. Proteasomes and their kin: proteases in the machine age. Nat Rev Mol Cell Biol 2004; 5: 177-87.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 177-187
    • Pickart, C.M.1    Cohen, R.E.2
  • 4
    • 11244309014 scopus 로고    scopus 로고
    • Proteolysis: From the lysosome to ubiquitin and the proteasome
    • Ciechanover A. Proteolysis: from the lysosome to ubiquitin and the proteasome. Nat Rev Mol Cell Biol 2005; 6: 79-87.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 79-87
    • Ciechanover, A.1
  • 5
    • 59649086030 scopus 로고    scopus 로고
    • Nonproteolytic Functions of Ubiquitin in Cell Signaling
    • Chen ZJ, Sun LJ. Nonproteolytic Functions of Ubiquitin in Cell Signaling. Mol Cell 2009; 33: 275-286.
    • (2009) Mol Cell , vol.33 , pp. 275-286
    • Chen, Z.J.1    Sun, L.J.2
  • 6
    • 78650824534 scopus 로고    scopus 로고
    • Ubiquitin-like protein conjugation and the ubiquitin-proteasome system as drug targets
    • Bedford L, Lowe J, Dick LR, Mayer RJ, Brownell JE. Ubiquitin-like protein conjugation and the ubiquitin-proteasome system as drug targets. Nat Rev Drug Discov 2011; 10: 29-46.
    • (2011) Nat Rev Drug Discov , vol.10 , pp. 29-46
    • Bedford, L.1    Lowe, J.2    Dick, L.R.3    Mayer, R.J.4    Brownell, J.E.5
  • 7
    • 84856641109 scopus 로고    scopus 로고
    • NF-κB, the first quarter-century: Remarkable progress and outstanding questions
    • Hayden MS, Ghosh S. NF-κB, the first quarter-century: remarkable progress and outstanding questions. Genes Dev 2012; 26: 203-34.
    • (2012) Genes Dev , vol.26 , pp. 203-234
    • Hayden, M.S.1    Ghosh, S.2
  • 9
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-kappaB signaling
    • Hayden MS, Ghosh S. Shared principles in NF-kappaB signaling. Cell 2008; 132: 344-62.
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 10
    • 23144449789 scopus 로고    scopus 로고
    • Ubiquitin signalling in the NF-kappaB pathway
    • Chen ZJ. Ubiquitin signalling in the NF-kappaB pathway. Nat Cell Biol 2005; 7: 758-65.
    • (2005) Nat Cell Biol , vol.7 , pp. 758-765
    • Chen, Z.J.1
  • 11
    • 67650744586 scopus 로고    scopus 로고
    • The Role of Ubiquitin in NF-kB Regulatory Pathways
    • Skaug B, Jiang X, Chen ZJ. The Role of Ubiquitin in NF-kB Regulatory Pathways. Annu Rev Biochem 2009; 78: 769-96.
    • (2009) Annu Rev Biochem , vol.78 , pp. 769-796
    • Skaug, B.1    Jiang, X.2    Chen, Z.J.3
  • 12
    • 84864222562 scopus 로고    scopus 로고
    • Atypical ubiquitylation - the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages
    • Kulathu Y, Komander D. Atypical ubiquitylation - the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages. Nat Rev Mol Cell Biol 2012; 13: 508-23.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 508-523
    • Kulathu, Y.1    Komander, D.2
  • 13
    • 84862761186 scopus 로고    scopus 로고
    • Diverse ubiquitin signaling in NF-κB activation
    • Iwai K. Diverse ubiquitin signaling in NF-κB activation. Trends cell biol 2012; 22: 355-64.
    • (2012) Trends Cell Biol , vol.22 , pp. 355-364
    • Iwai, K.1
  • 15
    • 2442437350 scopus 로고
    • Isolation of a polypeptide that has lymphocyte-differentiating properties and is probably represented universally in living cells
    • Goldstein G, Scheid M, Hammerling U, Schlesinger DH, Niall HD, Boyse EA. Isolation of a polypeptide that has lymphocyte-differentiating properties and is probably represented universally in living cells. Proc Natl Acad Sci USA 1975; 72: 11-5.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 11-15
    • Goldstein, G.1    Scheid, M.2    Hammerling, U.3    Schlesinger, D.H.4    Niall, H.D.5    Boyse, E.A.6
  • 16
    • 0018187738 scopus 로고
    • A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes
    • Ciechanover A, Hod Y, Hershko A. A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes. Biochem Biophys Res Commun 1978; 81: 1100-5.
    • (1978) Biochem Biophys Res Commun , vol.81 , pp. 1100-1105
    • Ciechanover, A.1    Hod, Y.2    Hershko, A.3
  • 17
    • 0141987892 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of p21 via N-terminal ubiquitinylation
    • Bloom J, Amador V, Bartolini F, DeMartino G, Pagano M. Proteasome-mediated degradation of p21 via N-terminal ubiquitinylation. Cell 2003; 115: 71-82.
    • (2003) Cell , vol.115 , pp. 71-82
    • Bloom, J.1    Amador, V.2    Bartolini, F.3    Demartino, G.4    Pagano, M.5
  • 18
    • 1442323729 scopus 로고    scopus 로고
    • N-terminal ubiquitination: More protein substrates join in
    • Ciechanover A, Ben-Saadon R. N-terminal ubiquitination: more protein substrates join in. Trends in cell biology 2004; 14: 103-6.
    • (2004) Trends In Cell Biology , vol.14 , pp. 103-106
    • Ciechanover, A.1    Ben-Saadon, R.2
  • 19
    • 33750219981 scopus 로고    scopus 로고
    • A ubiquitin ligase complex assembles linear polyubiquitin chains
    • Kirisako T, Kamei K, Murata S, et al. A ubiquitin ligase complex assembles linear polyubiquitin chains. EMBO J 2006; 25: 4877-87.
    • (2006) EMBO J , vol.25 , pp. 4877-4887
    • Kirisako, T.1    Kamei, K.2    Murata, S.3
  • 20
    • 67650064603 scopus 로고    scopus 로고
    • Linear polyubiquitination: A new regulator of NF-[kappa]B activation
    • Iwai K, Tokunaga F. Linear polyubiquitination: a new regulator of NF-[kappa]B activation. EMBO Rep 2009; 10: 706-13.
    • (2009) EMBO Rep , vol.10 , pp. 706-713
    • Iwai, K.1    Tokunaga, F.2
  • 21
    • 2542501657 scopus 로고    scopus 로고
    • Ubiquitin ligases and the immune response
    • Liu YC. Ubiquitin ligases and the immune response. Annu Rev Immuno 2004; 22: 81-127.
    • (2004) Annu Rev Immuno , vol.22 , pp. 81-127
    • Liu, Y.C.1
  • 22
    • 80052069445 scopus 로고    scopus 로고
    • RINGs of good and evil: RING finger ubiquitin ligases at the crossroads of tumour suppression and oncogenesis
    • Lipkowitz S, Weissman AM. RINGs of good and evil: RING finger ubiquitin ligases at the crossroads of tumour suppression and oncogenesis. Nat Rev Cancer 2011; 11: 629-43.
    • (2011) Nat Rev Cancer , vol.11 , pp. 629-643
    • Lipkowitz, S.1    Weissman, A.M.2
  • 24
    • 44349122993 scopus 로고    scopus 로고
    • Deregulated proteolysis by the F-box proteins SKP2 and [beta]-TrCP: Tipping the scales of cancer
    • Frescas D, Pagano M. Deregulated proteolysis by the F-box proteins SKP2 and [beta]-TrCP: tipping the scales of cancer. Nat Rev Cancer 2008; 8: 438-49.
    • (2008) Nat Rev Cancer , vol.8 , pp. 438-449
    • Frescas, D.1    Pagano, M.2
  • 25
    • 28344456279 scopus 로고    scopus 로고
    • A Genomic and Functional Inventory of Deubiquitinating Enzymes
    • Nijman SMB, Luna-Vargas MPA, Velds A, et al. A Genomic and Functional Inventory of Deubiquitinating Enzymes. Cell 2005; 123: 773-86.
    • (2005) Cell , vol.123 , pp. 773-786
    • Nijman, S.M.B.1    Luna-Vargas, M.P.A.2    Velds, A.3
  • 26
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: Structure and function of the deubiquitinases
    • Komander D, Clague MJ, Urbe S. Breaking the chains: structure and function of the deubiquitinases. Nat Rev Mol Cell Biol 2009; 10: 550-63.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbe, S.3
  • 27
    • 67649634849 scopus 로고    scopus 로고
    • Defining the Human Deubiquitinating Enzyme Interaction Landscape
    • Sowa ME, Bennett EJ, Gygi SP, Harper JW. Defining the Human Deubiquitinating Enzyme Interaction Landscape. Cell 2009; 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
  • 28
    • 83555168176 scopus 로고    scopus 로고
    • Roles of ubiquitin signaling in transcription regulation
    • Hammond-Martel I, Yu H, Affar EB. Roles of ubiquitin signaling in transcription regulation. Cell Signal 2012; 24: 410-21.
    • (2012) Cell Signal , vol.24 , pp. 410-421
    • Hammond-Martel, I.1    Yu, H.2    Affar, E.B.3
  • 29
    • 34249066085 scopus 로고    scopus 로고
    • PCNA, the Maestro of the Replication Fork
    • Moldovan G-L, Pfander B, Jentsch S. PCNA, the Maestro of the Replication Fork. Cell 2007; 129: 665-79.
    • (2007) Cell , vol.129 , pp. 665-679
    • Moldovan, G.-L.1    Pfander, B.2    Jentsch, S.3
  • 30
    • 63649144413 scopus 로고    scopus 로고
    • Principles of ubiquitin and SUMO modifications in DNA repair
    • Bergink S, Jentsch S. Principles of ubiquitin and SUMO modifications in DNA repair. Nature 2009; 458: 461-7.
    • (2009) Nature , vol.458 , pp. 461-467
    • Bergink, S.1    Jentsch, S.2
  • 31
    • 0348134742 scopus 로고    scopus 로고
    • Mono-versus polyubiquitination: Differential control of p53 fate by Mdm2
    • Li M, Brooks CL, Wu-Baer F, Chen D, Baer R, Gu W. Mono-versus polyubiquitination: differential control of p53 fate by Mdm2. Science 2003; 302: 1972-5.
    • (2003) Science , vol.302 , pp. 1972-1975
    • Li, M.1    Brooks, C.L.2    Wu-Baer, F.3    Chen, D.4    Baer, R.5    Gu, W.6
  • 32
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • Hicke L, Dunn R. Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu Rev Cell Dev Biol 2003; 19: 141-72.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 33
    • 0036922992 scopus 로고    scopus 로고
    • Structural Properties of Polyubiquitin Chains in Solution
    • Varadan R, Walker O, Pickart C, Fushman D. Structural Properties of Polyubiquitin Chains in Solution. J Mol Biol 2002; 324: 637-47.
    • (2002) J Mol Biol , vol.324 , pp. 637-647
    • Varadan, R.1    Walker, O.2    Pickart, C.3    Fushman, D.4
  • 35
    • 79955620198 scopus 로고    scopus 로고
    • Constructing and decoding unconventional ubiquitin chains
    • Behrends C, Harper JW. Constructing and decoding unconventional ubiquitin chains. Nat Struct Mol Biol 2011; 18: 520-8.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 520-528
    • Behrends, C.1    Harper, J.W.2
  • 36
    • 78650300883 scopus 로고    scopus 로고
    • c-IAP1 and UbcH5 promote K11-linked polyubiquitination of RIP1 in TNF signalling
    • Dynek JN, Goncharov T, Dueber EC, et al. c-IAP1 and UbcH5 promote K11-linked polyubiquitination of RIP1 in TNF signalling. EMBO J 2010; 29: 4198-209.
    • (2010) EMBO J , vol.29 , pp. 4198-4209
    • Dynek, J.N.1    Goncharov, T.2    Dueber, E.C.3
  • 37
    • 44649101850 scopus 로고    scopus 로고
    • Atypical ubiquitin chains: New molecular signals
    • Ikeda F, Dikic I. Atypical ubiquitin chains: new molecular signals. EMBO Rep 2008; 9: 536-42.
    • (2008) EMBO Rep , vol.9 , pp. 536-542
    • Ikeda, F.1    Dikic, I.2
  • 38
    • 0031897632 scopus 로고    scopus 로고
    • NF-kappa B and Rel proteins: Evolutionarily conserved mediators of immune responses
    • Ghosh S, May MJ, Kopp EB. NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses. Annu Rev Immunol 1998; 16: 225-60.
    • (1998) Annu Rev Immunol , vol.16 , pp. 225-260
    • Ghosh, S.1    May, M.J.2    Kopp, E.B.3
  • 39
    • 33645971047 scopus 로고    scopus 로고
    • Good cop, bad cop: The different faces of NF-kappaB
    • Perkins ND, Gilmore TD. Good cop, bad cop: the different faces of NF-kappaB. Cell Death Differ 2006; 13: 759-72.
    • (2006) Cell Death Differ , vol.13 , pp. 759-772
    • Perkins, N.D.1    Gilmore, T.D.2
  • 40
    • 67650724069 scopus 로고    scopus 로고
    • Regulation and Function of NF-kappaB Transcription Factors in the Immune System
    • Vallabhapurapu S, Karin M. Regulation and Function of NF-kappaB Transcription Factors in the Immune System. Annu Rev Immuno 2009; 27: 693-733.
    • (2009) Annu Rev Immuno , vol.27 , pp. 693-733
    • Vallabhapurapu, S.1    Karin, M.2
  • 41
    • 4444376712 scopus 로고    scopus 로고
    • Signaling to NF-kappaB
    • Hayden MS, Ghosh S. Signaling to NF-kappaB. Genes Dev 2004; 18: 2195-224.
    • (2004) Genes Dev , vol.18 , pp. 2195-2224
    • Hayden, M.S.1    Ghosh, S.2
  • 42
    • 84858722471 scopus 로고    scopus 로고
    • DNA damage-dependent NF-kappaB activation: NEMO turns nuclear signaling inside out
    • McCool KW, Miyamoto S. DNA damage-dependent NF-kappaB activation: NEMO turns nuclear signaling inside out. Immunol Rev 2012; 246: 311-26.
    • (2012) Immunol Rev , vol.246 , pp. 311-326
    • McCool, K.W.1    Miyamoto, S.2
  • 43
    • 35448960010 scopus 로고    scopus 로고
    • Many faces of NF-kappaB signaling induced by genotoxic stress
    • Wu ZH, Miyamoto S. Many faces of NF-kappaB signaling induced by genotoxic stress. J Mol Med 2007; 85: 1187-1202.
    • (2007) J Mol Med , vol.85 , pp. 1187-1202
    • Wu, Z.H.1    Miyamoto, S.2
  • 44
    • 0027980321 scopus 로고
    • The ubiquitinproteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB
    • Palombella VJ, Rando OJ, Goldberg AL, Maniatis T. The ubiquitinproteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB. Cell 1994; 78: 773-85.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 45
    • 17944401842 scopus 로고    scopus 로고
    • Identification of the receptor component of the IkappaBalpha-ubiquitin ligase
    • Yaron A, Hatzubai A, Davis M, et al. Identification of the receptor component of the IkappaBalpha-ubiquitin ligase. Nature 1998; 396: 590-4.
    • (1998) Nature , vol.396 , pp. 590-594
    • Yaron, A.1    Hatzubai, A.2    Davis, M.3
  • 46
  • 47
    • 0029146930 scopus 로고
    • Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway
    • Chen Z, Hagler J, Palombella VJ, et al. Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway. Genes Dev 1995; 9: 1586-97.
    • (1995) Genes Dev , vol.9 , pp. 1586-1597
    • Chen, Z.1    Hagler, J.2    Palombella, V.J.3
  • 48
    • 0347624589 scopus 로고    scopus 로고
    • Dual effects of IkappaB kinase beta-mediated phosphorylation on p105 Fate: SCF(beta-TrCP)-dependent degradation and SCF(beta-TrCP)-independent processing
    • Cohen S, Achbert-Weiner H, Ciechanover A. Dual effects of IkappaB kinase beta-mediated phosphorylation on p105 Fate: SCF(beta-TrCP)-dependent degradation and SCF(beta-TrCP)-independent processing. Mol Cell Biol 2004; 24: 475-86.
    • (2004) Mol Cell Biol , vol.24 , pp. 475-486
    • Cohen, S.1    Achbert-Weiner, H.2    Ciechanover, A.3
  • 49
    • 33646548968 scopus 로고    scopus 로고
    • The 20S proteasome processes NF-kappaB1 p105 into p50 in a translation-independent manner
    • Moorthy AK, Savinova OV, Ho JQ, Wang VY, Vu D, Ghosh G. The 20S proteasome processes NF-kappaB1 p105 into p50 in a translation-independent manner. EMBO J 2006; 25: 1945-56.
    • (2006) EMBO J , vol.25 , pp. 1945-1956
    • Moorthy, A.K.1    Savinova, O.V.2    Ho, J.Q.3    Wang, V.Y.4    Vu, D.5    Ghosh, G.6
  • 50
    • 33846475712 scopus 로고    scopus 로고
    • COMMD1 promotes the ubiquitination of NF-[kappa]B subunits through a cullin-containing ubiquitin ligase
    • Maine GN, Mao X, Komarck CM, Burstein E. COMMD1 promotes the ubiquitination of NF-[kappa]B subunits through a cullin-containing ubiquitin ligase. EMBO J 2007; 26: 436-47.
    • (2007) EMBO J , vol.26 , pp. 436-447
    • Maine, G.N.1    Mao, X.2    Komarck, C.M.3    Burstein, E.4
  • 51
    • 0347955360 scopus 로고    scopus 로고
    • Regulation of NF-κB Signaling by Pin1-Dependent Prolyl Isomerization and Ubiquitin-Mediated Proteolysis of p65/RelA
    • Ryo A, Suizu F, Yoshida Y, et al. Regulation of NF-κB Signaling by Pin1-Dependent Prolyl Isomerization and Ubiquitin-Mediated Proteolysis of p65/RelA. Mol Cell 2003; 12: 1413-26.
    • (2003) Mol Cell , vol.12 , pp. 1413-1426
    • Ryo, A.1    Suizu, F.2    Yoshida, Y.3
  • 52
    • 34249066486 scopus 로고    scopus 로고
    • PDLIM2-mediated termination of transcription factor NF-[kappa]B activation by intranuclear sequestration and degradation of the p65 subunit
    • Tanaka T, Grusby MJ, Kaisho T. PDLIM2-mediated termination of transcription factor NF-[kappa]B activation by intranuclear sequestration and degradation of the p65 subunit. Nat Immunol 2007; 8: 584-91.
    • (2007) Nat Immunol , vol.8 , pp. 584-591
    • Tanaka, T.1    Grusby, M.J.2    Kaisho, T.3
  • 53
    • 34547815755 scopus 로고    scopus 로고
    • Negative Regulation of Toll-Like Receptor Signaling by NF-{kappa}B p50 Ubiquitination Blockade
    • In: ed
    • Carmody RJ, Ruan Q, Palmer S, Hilliard B, Chen YH. Negative Regulation of Toll-Like Receptor Signaling by NF-{kappa}B p50 Ubiquitination Blockade. In: ed.^eds., Science 2007; pp. 675-8.
    • (2007) Science , pp. 675-678
    • Carmody, R.J.1    Ruan, Q.2    Palmer, S.3    Hilliard, B.4    Chen, Y.H.5
  • 54
    • 0030004897 scopus 로고    scopus 로고
    • Site-specific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity
    • Chen ZJ, Parent L, Maniatis T. Site-specific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity. Cell 1996; 84: 853-62.
    • (1996) Cell , vol.84 , pp. 853-862
    • Chen, Z.J.1    Parent, L.2    Maniatis, T.3
  • 55
    • 0037204948 scopus 로고    scopus 로고
    • TNF-R1 signaling: A beautiful pathway
    • Chen G, Goeddel DV. TNF-R1 signaling: a beautiful pathway. Science 2002; 296: 1634-5.
    • (2002) Science , vol.296 , pp. 1634-1635
    • Chen, G.1    Goeddel, D.V.2
  • 56
    • 70449424269 scopus 로고    scopus 로고
    • Structural Basis for the Lack of E2 Interaction in the RING Domain of TRAF2
    • Yin Q, Lamothe B, Darnay BG, Wu H. Structural Basis for the Lack of E2 Interaction in the RING Domain of TRAF2. Biochemistry 2009; 48: 10558-67.
    • (2009) Biochemistry , vol.48 , pp. 10558-10567
    • Yin, Q.1    Lamothe, B.2    Darnay, B.G.3    Wu, H.4
  • 57
    • 77953923379 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate is a missing cofactor for the E3 ubiquitin ligase TRAF2
    • Alvarez SE, Harikumar KB, Hait NC, et al. Sphingosine-1-phosphate is a missing cofactor for the E3 ubiquitin ligase TRAF2. Nature 2010; 465: 1084-1088.
    • (2010) Nature , vol.465 , pp. 1084-1088
    • Alvarez, S.E.1    Harikumar, K.B.2    Hait, N.C.3
  • 58
    • 33646034316 scopus 로고    scopus 로고
    • Activation of IKK by TNF[alpha] Requires Site-Specific Ubiquitination of RIP1 and Polyubiquitin Binding by NEMO
    • Ea CK, Deng L, Xia ZP, Pineda G, Chen ZJ. Activation of IKK by TNF[alpha] Requires Site-Specific Ubiquitination of RIP1 and Polyubiquitin Binding by NEMO. Mol Cell 2006; 22: 245-57.
    • (2006) Mol Cell , vol.22 , pp. 245-257
    • Ea, C.K.1    Deng, L.2    Xia, Z.P.3    Pineda, G.4    Chen, Z.J.5
  • 59
    • 33645703930 scopus 로고    scopus 로고
    • Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation
    • Wu CJ, Conze DB, Li T, Srinivasula SM, Ashwell JD. Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-kappaB activation. Nat Cell Biol 2006; 8: 398-406.
    • (2006) Nat Cell Biol , vol.8 , pp. 398-406
    • Wu, C.J.1    Conze, D.B.2    Li, T.3    Srinivasula, S.M.4    Ashwell, J.D.5
  • 60
    • 4344712350 scopus 로고    scopus 로고
    • TAB2 and TAB3 activate the NF-kappaB pathway through binding to polyubiquitin chains
    • Kanayama A, Seth RB, Sun L, et al. TAB2 and TAB3 activate the NF-kappaB pathway through binding to polyubiquitin chains. Mol Cell 2004; 15: 535-48.
    • (2004) Mol Cell , vol.15 , pp. 535-548
    • Kanayama, A.1    Seth, R.B.2    Sun, L.3
  • 61
    • 61649103747 scopus 로고    scopus 로고
    • Structural basis for recognition of diubiquitins by NEMO
    • Lo YC, Lin SC, Rospigliosi CC, et al. Structural basis for recognition of diubiquitins by NEMO. Mol Cell 2009; 33: 602-15.
    • (2009) Mol Cell , vol.33 , pp. 602-615
    • Lo, Y.C.1    Lin, S.C.2    Rospigliosi, C.C.3
  • 62
    • 0141621240 scopus 로고    scopus 로고
    • A Role for NF-kB Essential Modifier/IkB Kinase-gamma (NEMO/IKKgamma) Ubiquitination in the Activation of the IkB Kinase Complex by Tumor Necrosis Factor-a
    • Tang ED, Wang CY, Xiong Y, Guan KL. A Role for NF-kB Essential Modifier/IkB Kinase-gamma (NEMO/IKKgamma) Ubiquitination in the Activation of the IkB Kinase Complex by Tumor Necrosis Factor-a. J Biol Chem 2003; 278: 37297-305.
    • (2003) J Biol Chem , vol.278 , pp. 37297-37305
    • Tang, E.D.1    Wang, C.Y.2    Xiong, Y.3    Guan, K.L.4
  • 63
    • 59649103156 scopus 로고    scopus 로고
    • Involvement of linear polyubiquitylation of NEMO in NF-kappaB activation
    • Tokunaga F, Sakata S, Saeki Y, et al. Involvement of linear polyubiquitylation of NEMO in NF-kappaB activation. Nat Cell Biol 2009; 11: 123-32.
    • (2009) Nat Cell Biol , vol.11 , pp. 123-132
    • Tokunaga, F.1    Sakata, S.2    Saeki, Y.3
  • 64
    • 84858725584 scopus 로고    scopus 로고
    • Regulation of NF-kappaB by deubi-quitinases
    • Harhaj EW, Dixit VM. Regulation of NF-kappaB by deubi-quitinases. Immunol Rev 2012; 246: 107-24.
    • (2012) Immunol Rev , vol.246 , pp. 107-124
    • Harhaj, E.W.1    Dixit, V.M.2
  • 65
    • 39549106692 scopus 로고    scopus 로고
    • The Structure of the CYLD USP Domain Explains Its Specificity for Lys63-Linked Poly-ubiquitin and Reveals a B Box Module
    • Komander D, Lord CJ, Scheel H, et al. The Structure of the CYLD USP Domain Explains Its Specificity for Lys63-Linked Poly-ubiquitin and Reveals a B Box Module. Mol Cell 2008; 29: 451-64.
    • (2008) Mol Cell , vol.29 , pp. 451-464
    • Komander, D.1    Lord, C.J.2    Scheel, H.3
  • 66
    • 0041967054 scopus 로고    scopus 로고
    • The tumour suppressor CYLD negatively regulates NF-[kappa]B signalling by deubiquitination
    • Kovalenko A, Chable-Bessia C, Cantarella G, Israel A, Wallach D, Courtois G. The tumour suppressor CYLD negatively regulates NF-[kappa]B signalling by deubiquitination. Nature 2003; 424: 801-5.
    • (2003) Nature , vol.424 , pp. 801-805
    • Kovalenko, A.1    Chable-Bessia, C.2    Cantarella, G.3    Israel, A.4    Wallach, D.5    Courtois, G.6
  • 67
    • 3943054838 scopus 로고    scopus 로고
    • De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling
    • Wertz IE, O'Rourke KM, Zhou H, et al. De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling. Nature 2004; 430: 694-9.
    • (2004) Nature , vol.430 , pp. 694-699
    • Wertz, I.E.1    O'Rourke, K.M.2    Zhou, H.3
  • 68
    • 81355150892 scopus 로고    scopus 로고
    • Direct, Noncatalytic Mechanism of IKK Inhibition by A20
    • Skaug B, Chen J, Du F, He J, Ma A, Chen Zhijian J. Direct, Noncatalytic Mechanism of IKK Inhibition by A20. Mol Cell 2011; 44: 559-71.
    • (2011) Mol Cell , vol.44 , pp. 559-571
    • Skaug, B.1    Chen, J.2    Du, F.3    He, J.4    Ma, A.5    Chen, Z.J.6
  • 69
    • 69949093459 scopus 로고    scopus 로고
    • Direct activation of protein kinases by unanchored polyubiquitin chains
    • Xia ZP, Sun L, Chen X, et al. Direct activation of protein kinases by unanchored polyubiquitin chains. Nature 2009; 461: 114-9.
    • (2009) Nature , vol.461 , pp. 114-119
    • Xia, Z.P.1    Sun, L.2    Chen, X.3
  • 70
    • 77951708374 scopus 로고    scopus 로고
    • Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity
    • Zeng W, Sun L, Jiang X, et al. Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity. Cell 2010; 141: 315-30.
    • (2010) Cell , vol.141 , pp. 315-330
    • Zeng, W.1    Sun, L.2    Jiang, X.3
  • 71
    • 70350015537 scopus 로고    scopus 로고
    • A ubiquitin replacement strategy in human cells reveals distinct mechanisms of IKK activation by TNFalpha and IL-1beta
    • Xu M, Skaug B, Zeng W, Chen ZJ. A ubiquitin replacement strategy in human cells reveals distinct mechanisms of IKK activation by TNFalpha and IL-1beta. Mol Cell 2009; 36: 302-14.
    • (2009) Mol Cell , vol.36 , pp. 302-314
    • Xu, M.1    Skaug, B.2    Zeng, W.3    Chen, Z.J.4
  • 72
    • 79953240109 scopus 로고    scopus 로고
    • Linear ubiquitination prevents inflammation and regulates immune signalling
    • Gerlach B, Cordier SM, Schmukle AC, et al. Linear ubiquitination prevents inflammation and regulates immune signalling. Nature 2011; 471: 591-6.
    • (2011) Nature , vol.471 , pp. 591-596
    • Gerlach, B.1    Cordier, S.M.2    Schmukle, A.C.3
  • 73
    • 79956300649 scopus 로고    scopus 로고
    • Toll-like Receptors and Their Crosstalk with Other Innate Receptors in Infection and Immunity
    • Kawai T, Akira S. Toll-like Receptors and Their Crosstalk with Other Innate Receptors in Infection and Immunity. Immunity 2011; 34: 637-50.
    • (2011) Immunity , vol.34 , pp. 637-650
    • Kawai, T.1    Akira, S.2
  • 74
    • 70349472923 scopus 로고    scopus 로고
    • Peli1 facilitates TRIF-dependent Toll-like receptor signaling and proinflammatory cytokine production
    • Chang M, Jin W, Sun S-C. Peli1 facilitates TRIF-dependent Toll-like receptor signaling and proinflammatory cytokine production. Nat Immunol 2009; 10: 1089-95.
    • (2009) Nat Immunol , vol.10 , pp. 1089-1095
    • Chang, M.1    Jin, W.2    Sun, S.-C.3
  • 75
    • 74049136127 scopus 로고    scopus 로고
    • Different modes of ubiquitination of the adaptor TRAF3 selectively activate the expression of type I interferons and proinflammatory cytokines
    • Tseng P-H, Matsuzawa A, Zhang W, Mino T, Vignali DAA, Karin M. Different modes of ubiquitination of the adaptor TRAF3 selectively activate the expression of type I interferons and proinflammatory cytokines. Nat Immunol 2010; 11: 70-5.
    • (2010) Nat Immunol , vol.11 , pp. 70-75
    • Tseng, P.-H.1    Matsuzawa, A.2    Zhang, W.3    Mino, T.4    Vignali, D.A.A.5    Karin, M.6
  • 76
    • 15944410614 scopus 로고    scopus 로고
    • PDK1 Nucleates T Cell Receptor-Induced Signaling Complex for NF-κB Activation
    • Lee K-Y, D'Acquisto F, Hayden MS, Shim J-H, Ghosh S. PDK1 Nucleates T Cell Receptor-Induced Signaling Complex for NF-κB Activation. Science 2005; 308: 114-8.
    • (2005) Science , vol.308 , pp. 114-118
    • Lee, K.-Y.1    D'Acquisto, F.2    Hayden, M.S.3    Shim, J.-H.4    Ghosh, S.5
  • 77
    • 0036707520 scopus 로고    scopus 로고
    • A requirement for CARMA1 in TCR-induced NF-kappa B activation
    • Wang D, You Y, Case SM, et al. A requirement for CARMA1 in TCR-induced NF-kappa B activation. Nature immunology 2002; 3: 830-5.
    • (2002) Nature Immunology , vol.3 , pp. 830-835
    • Wang, D.1    You, Y.2    Case, S.M.3
  • 78
    • 2342629277 scopus 로고    scopus 로고
    • The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes
    • Sun L, Deng L, Ea CK, Xia ZP, Chen ZJ. The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes. Mol Cell 2004; 14: 289-301.
    • (2004) Mol Cell , vol.14 , pp. 289-301
    • Sun, L.1    Deng, L.2    Ea, C.K.3    Xia, Z.P.4    Chen, Z.J.5
  • 79
    • 84863338304 scopus 로고    scopus 로고
    • Ubiquitination in signaling to and activation of IKK
    • Chen ZJ. Ubiquitination in signaling to and activation of IKK. Immunol Rev 2012; 246: 95-106.
    • (2012) Immunol Rev , vol.246 , pp. 95-106
    • Chen, Z.J.1
  • 80
    • 84862976890 scopus 로고    scopus 로고
    • Selective Autophagy of the Adaptor Protein Bcl10 Modulates T Cell Receptor Activation of NF-κB
    • Paul S, Kashyap Anuj K, Jia W, He YW, Schaefer Brian C. Selective Autophagy of the Adaptor Protein Bcl10 Modulates T Cell Receptor Activation of NF-κB. Immunity 2012; 36: 947-58.
    • (2012) Immunity , vol.36 , pp. 947-958
    • Paul, S.1    Kashyap, A.K.2    Jia, W.3    He, Y.W.4    Schaefer, B.C.5
  • 81
    • 1942453854 scopus 로고    scopus 로고
    • Degradation of Bcl10 Induced by T-Cell Activation Negatively Regulates NF-κB Signaling
    • Scharschmidt E, Wegener E, Heissmeyer V, Rao A, Krappmann D. Degradation of Bcl10 Induced by T-Cell Activation Negatively Regulates NF-κB Signaling. Mol Cell Biol 2004; 24: 3860-73.
    • (2004) Mol Cell Biol , vol.24 , pp. 3860-3873
    • Scharschmidt, E.1    Wegener, E.2    Heissmeyer, V.3    Rao, A.4    Krappmann, D.5
  • 82
    • 78751554067 scopus 로고    scopus 로고
    • Signals from the Nucleus: Activation of NF-{kappa}B by Cytosolic ATM in the DNA Damage Response
    • Hadian K, Krappmann D. Signals from the Nucleus: Activation of NF-{kappa}B by Cytosolic ATM in the DNA Damage Response. Sci. Signal. 2011; 4: pe2.
    • (2011) Sci. Signal , vol.4
    • Hadian, K.1    Krappmann, D.2
  • 83
    • 78650873024 scopus 로고    scopus 로고
    • Nuclear initiated NF-[kappa]B signaling: NEMO and ATM Take Center Stage
    • Miyamoto S. Nuclear initiated NF-[kappa]B signaling: NEMO and ATM take center stage. Cell Res 2011; 21: 116-30.
    • (2011) Cell Res , vol.21 , pp. 116-130
    • Miyamoto, S.1
  • 84
    • 0344305376 scopus 로고    scopus 로고
    • Sequential modification of NEMO/IKKgamma by SUMO-1 and ubiquitin mediates NF-kappaB activation by genotoxic stress
    • Huang TT, Wuerzberger-Davis SM, Wu ZH, Miyamoto S. Sequential modification of NEMO/IKKgamma by SUMO-1 and ubiquitin mediates NF-kappaB activation by genotoxic stress. Cell 2003; 115: 565-76.
    • (2003) Cell , vol.115 , pp. 565-576
    • Huang, T.T.1    Wuerzberger-Davis, S.M.2    Wu, Z.H.3    Miyamoto, S.4
  • 85
    • 33748188499 scopus 로고    scopus 로고
    • PIASy mediates NEMO sumoylation and NF-kappaB activation in response to genotoxic stress
    • Mabb AM, Wuerzberger-Davis SM, Miyamoto S. PIASy mediates NEMO sumoylation and NF-kappaB activation in response to genotoxic stress. Nat Cell Biol 2006; 8: 986-93.
    • (2006) Nat Cell Biol , vol.8 , pp. 986-993
    • Mabb, A.M.1    Wuerzberger-Davis, S.M.2    Miyamoto, S.3
  • 86
    • 28944447430 scopus 로고    scopus 로고
    • PIDD mediates NF-kappaB activation in response to DNA damage
    • Janssens S, Tinel A, Lippens S, Tschopp J. PIDD mediates NF-kappaB activation in response to DNA damage. Cell 2005; 123: 1079-92.
    • (2005) Cell , vol.123 , pp. 1079-1092
    • Janssens, S.1    Tinel, A.2    Lippens, S.3    Tschopp, J.4
  • 87
    • 70449102637 scopus 로고    scopus 로고
    • A Nuclear Poly(ADP-Ribose)-Dependent Signalosome Confers DNA Damage-Induced IkB Kinase Activation
    • Stilmann M, Hinz M, Arslan SC, Zimmer A, Schreiber V, Scheidereit C. A Nuclear Poly(ADP-Ribose)-Dependent Signalosome Confers DNA Damage-Induced IkB Kinase Activation. Mol Cell 2009; 36: 365-78.
    • (2009) Mol Cell , vol.36 , pp. 365-378
    • Stilmann, M.1    Hinz, M.2    Arslan, S.C.3    Zimmer, A.4    Schreiber, V.5    Scheidereit, C.6
  • 88
    • 33644538632 scopus 로고    scopus 로고
    • Molecular linkage between the kinase ATM and NF-kappaB signaling in response to genotoxic stimuli
    • Wu ZH, Shi Y, Tibbetts RS, Miyamoto S. Molecular linkage between the kinase ATM and NF-kappaB signaling in response to genotoxic stimuli. Science 2006; 311: 1141-6.
    • (2006) Science , vol.311 , pp. 1141-1146
    • Wu, Z.H.1    Shi, Y.2    Tibbetts, R.S.3    Miyamoto, S.4
  • 89
    • 77957374335 scopus 로고    scopus 로고
    • ATM-and NEMO-Dependent ELKS Ubiquitination Coordinates TAK1-Mediated IKK Activation in response to Genotoxic Stress
    • Wu ZH, Wong ET, Shi Y, et al. ATM-and NEMO-Dependent ELKS Ubiquitination Coordinates TAK1-Mediated IKK Activation in response to Genotoxic Stress. Mol Cell 2010; 40: 75-86.
    • (2010) Mol Cell , vol.40 , pp. 75-86
    • Wu, Z.H.1    Wong, E.T.2    Shi, Y.3
  • 90
    • 77957333810 scopus 로고    scopus 로고
    • A Cytoplasmic ATM-TRAF6-cIAP1 Module Links Nuclear DNA Damage Signaling to Ubiquitin-Mediated NF-kappaB Activation
    • Hinz M, Stilmann M, Arslan SC, Khanna KK, Dittmar G, Scheidereit C. A Cytoplasmic ATM-TRAF6-cIAP1 Module Links Nuclear DNA Damage Signaling to Ubiquitin-Mediated NF-kappaB Activation. Mol Cell 2010; 40: 63-74.
    • (2010) Mol Cell , vol.40 , pp. 63-74
    • Hinz, M.1    Stilmann, M.2    Arslan, S.C.3    Khanna, K.K.4    Dittmar, G.5    Scheidereit, C.6
  • 92
    • 79953239980 scopus 로고    scopus 로고
    • SHARPIN forms a linear ubiquitin ligase complex regulating NF-[kgr]B activity and apoptosis
    • Ikeda F, Deribe YL, Skanland SS, et al. SHARPIN forms a linear ubiquitin ligase complex regulating NF-[kgr]B activity and apoptosis. Nature 2011; 471: 637-41.
    • (2011) Nature , vol.471 , pp. 637-641
    • Ikeda, F.1    Deribe, Y.L.2    Skanland, S.S.3
  • 93
    • 79953237668 scopus 로고    scopus 로고
    • SHARPIN is a component of the NF-kB-activating linear ubiquitin chain assembly complex
    • Tokunaga F, Nakagawa T, Nakahara M, et al. SHARPIN is a component of the NF-kB-activating linear ubiquitin chain assembly complex. Nature 2011; 471: 633-6.
    • (2011) Nature , vol.471 , pp. 633-636
    • Tokunaga, F.1    Nakagawa, T.2    Nakahara, M.3
  • 94
    • 84858113865 scopus 로고    scopus 로고
    • No one can whistle a symphony alone-how different ubiquitin linkages cooperate to orchestrate NF-kappaB activity
    • Schmukle AC, Walczak H. No one can whistle a symphony alone-how different ubiquitin linkages cooperate to orchestrate NF-kappaB activity. J Cell Sci 2012; 125: 549-59.
    • (2012) J Cell Sci , vol.125 , pp. 549-559
    • Schmukle, A.C.1    Walczak, H.2
  • 95
    • 33750497452 scopus 로고    scopus 로고
    • Mutual regulation of conventional protein kinase C and a ubiquitin ligase complex
    • Nakamura M, Tokunaga F, Sakata S-I, Iwai K. Mutual regulation of conventional protein kinase C and a ubiquitin ligase complex. Biochem Biophys Res Commun 2006; 351: 340-7.
    • (2006) Biochem Biophys Res Commun , vol.351 , pp. 340-347
    • Nakamura, M.1    Tokunaga, F.2    Sakata, S.-I.3    Iwai, K.4
  • 96
    • 79251550124 scopus 로고    scopus 로고
    • Linear Ubiquitin Assembly Complex Negatively Regulates RIG-I-and TRIM25-Mediated Type I Interferon Induction
    • Inn KS, Gack MU, Tokunaga F, et al. Linear Ubiquitin Assembly Complex Negatively Regulates RIG-I-and TRIM25-Mediated Type I Interferon Induction. Mol Cell 2011; 41: 354-65.
    • (2011) Mol Cell , vol.41 , pp. 354-365
    • Inn, K.S.1    Gack, M.U.2    Tokunaga, F.3
  • 97
    • 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, et al. Recruitment of the Linear Ubiquitin Chain Assembly Complex Stabilizes the TNF-R1 Signaling Complex and is Required for TNF-Mediated Gene Induction. Mol Cell 2009; 36: 831-44.
    • (2009) Mol Cell , vol.36 , pp. 831-844
    • Haas, T.L.1    Emmerich, C.H.2    Gerlach, B.3
  • 98
    • 62549155321 scopus 로고    scopus 로고
    • Specific recognition of linear ubiquitin chains by NEMO is important for NF-kappaB activation
    • Rahighi S, Ikeda F, Kawasaki M, et al. Specific recognition of linear ubiquitin chains by NEMO is important for NF-kappaB activation. Cell 2009; 136: 1098-109.
    • (2009) Cell , vol.136 , pp. 1098-1109
    • Rahighi, S.1    Ikeda, F.2    Kawasaki, M.3
  • 99
    • 80052692078 scopus 로고    scopus 로고
    • LUBAC regulates NF-[kappa]B activation upon genotoxic stress by promoting linear ubiquitination of NEMO
    • Niu J, Shi Y, Iwai K, Wu Z-H. LUBAC regulates NF-[kappa]B activation upon genotoxic stress by promoting linear ubiquitination of NEMO. EMBO J 2011; 30: 3741-53.
    • (2011) EMBO J , vol.30 , pp. 3741-3753
    • Niu, J.1    Shi, Y.2    Iwai, K.3    Wu, Z.-H.4
  • 100
    • 84863115198 scopus 로고    scopus 로고
    • Intrinsic antiviral immunity
    • Yan N, Chen ZJ. Intrinsic antiviral immunity. Nat Immunol 2012; 13: 214-222.
    • (2012) Nat Immunol , vol.13 , pp. 214-222
    • Yan, N.1    Chen, Z.J.2
  • 101
    • 34247341367 scopus 로고    scopus 로고
    • TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity
    • Gack MU, Shin YC, Joo CH, et al. TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity. Nature 2007; 446: 916-20.
    • (2007) Nature , vol.446 , pp. 916-920
    • Gack, M.U.1    Shin, Y.C.2    Joo, C.H.3
  • 103
    • 30044437123 scopus 로고    scopus 로고
    • Site-specific Monoubiquitination of I B Kinase IKK Regulates Its Phosphorylation and Persistent Activation
    • Carter RS, Pennington KN, Arrate P, Oltz EM, Ballard DW. Site-specific Monoubiquitination of I B Kinase IKK Regulates Its Phosphorylation and Persistent Activation. J Biol Chem 2005; 280: 43272-9.
    • (2005) J Biol Chem , vol.280 , pp. 43272-43279
    • Carter, R.S.1    Pennington, K.N.2    Arrate, P.3    Oltz, E.M.4    Ballard, D.W.5
  • 104
    • 84862852850 scopus 로고    scopus 로고
    • Monoubiquitination of nuclear RelA negatively regulates NF-kappaB activity independent of proteasomal degradation
    • Hochrainer K, Racchumi G, Zhang S, Iadecola C, Anrather J. Monoubiquitination of nuclear RelA negatively regulates NF-kappaB activity independent of proteasomal degradation. Cell Mol Life Sci 2012; 69: 2057-73.
    • (2012) Cell Mol Life Sci , vol.69 , pp. 2057-2073
    • Hochrainer, K.1    Racchumi, G.2    Zhang, S.3    Iadecola, C.4    Anrather, J.5
  • 105
    • 43049162227 scopus 로고    scopus 로고
    • Mechanism of Ubiquitin-Chain Formation by the Human Anaphase-Promoting Complex
    • Jin L, Williamson A, Banerjee S, Philipp I, Rape M. Mechanism of Ubiquitin-Chain Formation by the Human Anaphase-Promoting Complex. Cell 2008; 133: 653-65.
    • (2008) Cell , vol.133 , pp. 653-665
    • Jin, L.1    Williamson, A.2    Banerjee, S.3    Philipp, I.4    Rape, M.5
  • 106
    • 63049125531 scopus 로고    scopus 로고
    • Quantitative Proteomics Reveals the Function of Unconventional Ubiquitin Chains in Proteasomal Degradation
    • Xu P, Duong DM, Seyfried NT, et al. Quantitative Proteomics Reveals the Function of Unconventional Ubiquitin Chains in Proteasomal Degradation. Cell 2009; 137: 133-45.
    • (2009) Cell , vol.137 , pp. 133-145
    • Xu, P.1    Duong, D.M.2    Seyfried, N.T.3
  • 107
    • 77954953473 scopus 로고    scopus 로고
    • K33-Linked Polyubiquitination of T Cell Receptor-Regulates Proteolysis-Independent T Cell Signaling
    • Huang H, Jeon MS, Liao L, et al. K33-Linked Polyubiquitination of T Cell Receptor-Regulates Proteolysis-Independent T Cell Signaling. Immunity 2010; 33: 60-70.
    • (2010) Immunity , vol.33 , pp. 60-70
    • Huang, H.1    Jeon, M.S.2    Liao, L.3
  • 108
    • 77957677615 scopus 로고    scopus 로고
    • Polyubiquitin conjugation to NEMO by triparite motif protein 23 (TRIM23) is critical in antiviral defense
    • Arimoto K-I, Funami K, Saeki Y, et al. Polyubiquitin conjugation to NEMO by triparite motif protein 23 (TRIM23) is critical in antiviral defense. Proc Natl Acad Sci USA 2010; 107: 15856-61.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 15856-15861
    • Arimoto, K.-I.1    Funami, K.2    Saeki, Y.3
  • 109
    • 33645999706 scopus 로고    scopus 로고
    • NF-kappaB and IKK as therapeutic targets in cancer
    • Kim HJ, Hawke N, Baldwin AS. NF-kappaB and IKK as therapeutic targets in cancer. Cell Death Differ 2006; 13: 738-47.
    • (2006) Cell Death Differ , vol.13 , pp. 738-747
    • Kim, H.J.1    Hawke, N.2    Baldwin, A.S.3
  • 110
    • 84856213846 scopus 로고    scopus 로고
    • The diverse and complex roles of NF-κB subunits in cancer
    • Perkins ND. The diverse and complex roles of NF-κB subunits in cancer. Nat Rev Cancer 2012; 12: 121-32.
    • (2012) Nat Rev Cancer , vol.12 , pp. 121-132
    • Perkins, N.D.1
  • 112
    • 25844459154 scopus 로고    scopus 로고
    • NF-kappaB: Linking inflammation and immunity to cancer development and progression
    • Karin M, Greten FR. NF-kappaB: linking inflammation and immunity to cancer development and progression. Nat Rev Immunol 2005; 5: 749-59.
    • (2005) Nat Rev Immunol , vol.5 , pp. 749-759
    • Karin, M.1    Greten, F.R.2
  • 113
    • 32944474237 scopus 로고    scopus 로고
    • Innate Immunity Gone Awry: Linking Microbial Infections to Chronic Inflammation and Cancer
    • Karin M, Lawrence T, Nizet V. Innate Immunity Gone Awry: Linking Microbial Infections to Chronic Inflammation and Cancer. Cell 2006; 124: 823-35.
    • (2006) Cell , vol.124 , pp. 823-835
    • Karin, M.1    Lawrence, T.2    Nizet, V.3
  • 114
    • 0035137882 scopus 로고    scopus 로고
    • Control of oncogenesis and cancer therapy resistance by the transcription factor NF-kappaB
    • Baldwin AS. Control of oncogenesis and cancer therapy resistance by the transcription factor NF-kappaB. J Clin Invest 2001; 107: 241-6.
    • (2001) J Clin Invest , vol.107 , pp. 241-246
    • Baldwin, A.S.1
  • 115
    • 16844366650 scopus 로고    scopus 로고
    • Nuclear factor-kappaB inhibitors as sensitizers to anticancer drugs
    • Nakanishi C, Toi M. Nuclear factor-kappaB inhibitors as sensitizers to anticancer drugs. Nat Rev Cancer 2005; 5: 297-309.
    • (2005) Nat Rev Cancer , vol.5 , pp. 297-309
    • Nakanishi, C.1    Toi, M.2
  • 116
    • 79952284127 scopus 로고    scopus 로고
    • Hallmarks of Cancer: The Next Generation
    • Hanahan D, Weinberg Robert A. Hallmarks of Cancer: The Next Generation. Cell 2011; 144: 646-74.
    • (2011) Cell , vol.144 , pp. 646-674
    • Hanahan, D.1    Weinberg, R.A.2
  • 117
    • 58149202128 scopus 로고    scopus 로고
    • Is NF-[kappa]B a good target for cancer therapy? Hopes and pitfalls
    • Baud V, Karin M. Is NF-[kappa]B a good target for cancer therapy? Hopes and pitfalls. Nat Rev Drug Discov 2009; 8: 33-40.
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 33-40
    • Baud, V.1    Karin, M.2
  • 118
    • 61449182121 scopus 로고    scopus 로고
    • Principles of Cancer Therapy: Oncogene and Non-oncogene Addiction
    • Luo J, Solimini NL, Elledge SJ. Principles of Cancer Therapy: Oncogene and Non-oncogene Addiction. Cell 2009; 136: 823-37.
    • (2009) Cell , vol.136 , pp. 823-837
    • Luo, J.1    Solimini, N.L.2    Elledge, S.J.3
  • 119
    • 70549105793 scopus 로고    scopus 로고
    • Control of cell growth by the SCF and APC/C ubiquitin ligases
    • Skaar JR, Pagano M. Control of cell growth by the SCF and APC/C ubiquitin ligases. Curr Opin Cell Biol 2009; 21: 816-24.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 816-824
    • Skaar, J.R.1    Pagano, M.2
  • 120
    • 75149189204 scopus 로고    scopus 로고
    • BRCA1 and its toolbox for the maintenance of genome integrity
    • Huen MS, Sy SM, Chen J. BRCA1 and its toolbox for the maintenance of genome integrity. Nat Rev Mol Cell Biol 2010; 11: 138-48.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 138-148
    • Huen, M.S.1    Sy, S.M.2    Chen, J.3
  • 121
    • 72149119542 scopus 로고    scopus 로고
    • How the fanconi anemia pathway guards the genome
    • Moldovan GL, D'Andrea AD. How the fanconi anemia pathway guards the genome. Annu Rev Genet 2009; 43: 223-49.
    • (2009) Annu Rev Genet , vol.43 , pp. 223-249
    • Moldovan, G.L.1    D'Andrea, A.D.2
  • 122
    • 77449155637 scopus 로고    scopus 로고
    • The multiple levels of regulation by p53 ubiquitination
    • Lee JT, Gu W. The multiple levels of regulation by p53 ubiquitination. Cell Death Differ 2010; 17: 86-92.
    • (2010) Cell Death Differ , vol.17 , pp. 86-92
    • Lee, J.T.1    Gu, W.2
  • 123
    • 0027954044 scopus 로고
    • Mutations of the VHL tumour suppressor gene in renal carcinoma
    • Gnarra JR, Tory K, Weng Y, et al. Mutations of the VHL tumour suppressor gene in renal carcinoma. Nat genet 1994; 7: 85-90.
    • (1994) Nat Genet , vol.7 , pp. 85-90
    • Gnarra, J.R.1    Tory, K.2    Weng, Y.3
  • 124
    • 84855447125 scopus 로고    scopus 로고
    • FBXO11 targets BCL6 for degradation and is inactivated in diffuse large B-cell lymphomas
    • Duan S, Cermak L, Pagan JK, et al. FBXO11 targets BCL6 for degradation and is inactivated in diffuse large B-cell lymphomas. Nature 2012; 481: 90-3.
    • (2012) Nature , vol.481 , pp. 90-93
    • Duan, S.1    Cermak, L.2    Pagan, J.K.3
  • 125
    • 2342667387 scopus 로고    scopus 로고
    • The development of proteasome inhibitors as anticancer drugs
    • Adams J. The development of proteasome inhibitors as anticancer drugs. Cancer Cell 2004; 5: 417-21.
    • (2004) Cancer Cell , vol.5 , pp. 417-421
    • Adams, J.1
  • 127
    • 52449135431 scopus 로고    scopus 로고
    • Bortezomib-Resistant Nuclear Factor-B Activity in Multiple Myeloma Cells
    • Markovina S, Callander NS, O'Connor SL, et al. Bortezomib-Resistant Nuclear Factor-B Activity in Multiple Myeloma Cells. Mol Cancer Res 2008; 6: 1356-64.
    • (2008) Mol Cancer Res , vol.6 , pp. 1356-1364
    • Markovina, S.1    Callander, N.S.2    O'Connor, S.L.3
  • 128
    • 70349243697 scopus 로고    scopus 로고
    • Bortezomib induces canonical nuclear factor-B activation in multiple myeloma cells
    • Hideshima T, Ikeda H, Chauhan D, et al. Bortezomib induces canonical nuclear factor-B activation in multiple myeloma cells. Blood 2009; 114: 1046-52.
    • (2009) Blood , vol.114 , pp. 1046-1052
    • Hideshima, T.1    Ikeda, H.2    Chauhan, D.3
  • 129
    • 0037441760 scopus 로고    scopus 로고
    • Molecular mechanisms mediating antimyeloma activity of proteasome inhibitor PS-341
    • Hideshima T, Mitsiades C, Akiyama M, et al. Molecular mechanisms mediating antimyeloma activity of proteasome inhibitor PS-341. Blood 2003; 101: 1530-4.
    • (2003) Blood , vol.101 , pp. 1530-1534
    • Hideshima, T.1    Mitsiades, C.2    Akiyama, M.3
  • 130
    • 1642486367 scopus 로고    scopus 로고
    • Proteasome inhibitor PS-341 induces growth arrest and apoptosis of non-small cell lung cancer cells via the JNK/c-Jun/AP-1 signaling
    • Yang Y, Ikezoe T, Saito T, Kobayashi M, Koeffler HP, Taguchi H. Proteasome inhibitor PS-341 induces growth arrest and apoptosis of non-small cell lung cancer cells via the JNK/c-Jun/AP-1 signaling. Cancer sci 2004; 95: 176-80.
    • (2004) Cancer Sci , vol.95 , pp. 176-180
    • Yang, Y.1    Ikezoe, T.2    Saito, T.3    Kobayashi, M.4    Koeffler, H.P.5    Taguchi, H.6
  • 131
    • 34447116376 scopus 로고    scopus 로고
    • Antitumor activity of PR-171, a novel irreversible inhibitor of the proteasome
    • Demo SD, Kirk CJ, Aujay MA, et al. Antitumor activity of PR-171, a novel irreversible inhibitor of the proteasome. Cancer Res 2007; 67: 6383-91.
    • (2007) Cancer Res , vol.67 , pp. 6383-6391
    • Demo, S.D.1    Kirk, C.J.2    Aujay, M.A.3
  • 132
    • 36148944490 scopus 로고    scopus 로고
    • Potent activity of carfilzomib, a novel, irreversible inhibitor of the ubiquitin-proteasome pathway, against preclinical models of multiple myeloma
    • Kuhn DJ, Chen Q, Voorhees PM, et al. Potent activity of carfilzomib, a novel, irreversible inhibitor of the ubiquitin-proteasome pathway, against preclinical models of multiple myeloma. Blood 2007; 110: 3281-90.
    • (2007) Blood , vol.110 , pp. 3281-3290
    • Kuhn, D.J.1    Chen, Q.2    Voorhees, P.M.3
  • 133
    • 64749098830 scopus 로고    scopus 로고
    • An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer
    • Soucy TA, Smith PG, Milhollen MA, et al. An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer. Nature 2009; 458: 732-6.
    • (2009) Nature , vol.458 , pp. 732-736
    • Soucy, T.A.1    Smith, P.G.2    Milhollen, M.A.3
  • 134
    • 79751469547 scopus 로고    scopus 로고
    • NEDD8 Pathways in Cancer, Sine Quibus Non
    • Watson IR, Irwin MS, Ohh M. NEDD8 Pathways in Cancer, Sine Quibus Non. Cancer Cell 2011; 19: 168-76.
    • (2011) Cancer Cell , vol.19 , pp. 168-176
    • Watson, I.R.1    Irwin, M.S.2    Ohh, M.3
  • 135
    • 67349256160 scopus 로고    scopus 로고
    • Ubiquitin-like protein activation by E1 enzymes: The apex for downstream signalling pathways
    • Schulman BA, Wade Harper J. Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways. Nat Rev Mol Cell Biol 2009; 10: 319-31.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 319-331
    • Schulman, B.A.1    Wade, H.J.2
  • 136
    • 50449108516 scopus 로고    scopus 로고
    • Structural Insights into NEDD8 Activation of Cullin-RING Ligases: Conformational Control of Conjugation
    • Duda DM, Borg LA, Scott DC, Hunt HW, Hammel M, Schulman BA. Structural Insights into NEDD8 Activation of Cullin-RING Ligases: Conformational Control of Conjugation. Cell 2008; 134: 995-1006.
    • (2008) Cell , vol.134 , pp. 995-1006
    • Duda, D.M.1    Borg, L.A.2    Scott, D.C.3    Hunt, H.W.4    Hammel, M.5    Schulman, B.A.6
  • 137
    • 50449110781 scopus 로고    scopus 로고
    • Autoinhibitory regulation of SCF-mediated ubiquitination by human cullin 1's C-terminal tail
    • Yamoah K, Oashi T, Sarikas A, Gazdoiu S, Osman R, Pan ZQ. Autoinhibitory regulation of SCF-mediated ubiquitination by human cullin 1's C-terminal tail. Proc Natl Acad Sci USA 2008; 105: 12230-5.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 12230-12235
    • Yamoah, K.1    Oashi, T.2    Sarikas, A.3    Gazdoiu, S.4    Osman, R.5    Pan, Z.Q.6
  • 138
    • 73649110303 scopus 로고    scopus 로고
    • Substrate-Assisted Inhibition of Ubiquitin-like Protein-Activating Enzymes: The NEDD8 E1 Inhibitor MLN4924 Forms a NEDD8-AMP Mimetic In Situ
    • Brownell JE, Sintchak MD, Gavin JM, et al. Substrate-Assisted Inhibition of Ubiquitin-like Protein-Activating Enzymes: The NEDD8 E1 Inhibitor MLN4924 Forms a NEDD8-AMP Mimetic In Situ. Mol Cell 2010; 37: 102-11.
    • (2010) Mol Cell , vol.37 , pp. 102-111
    • Brownell, J.E.1    Sintchak, M.D.2    Gavin, J.M.3
  • 139
    • 77952558703 scopus 로고    scopus 로고
    • Inhibition of NEDD8-activating enzyme: A novel approach for the treatment of acute myeloid leukemia
    • Swords RT, Kelly KR, Smith PG, et al. Inhibition of NEDD8-activating enzyme: A novel approach for the treatment of acute myeloid leukemia. Blood 2010; 115: 3796-800.
    • (2010) Blood , vol.115 , pp. 3796-3800
    • Swords, R.T.1    Kelly, K.R.2    Smith, P.G.3
  • 140
    • 77956578834 scopus 로고    scopus 로고
    • MLN4924, a NEDD8-activating enzyme inhibitor, is active in diffuse large B-cell lymphoma models: Rationale for treatment of NF-κB-dependent lymphoma
    • Milhollen MA, Traore T, Adams-Duffy J, et al. MLN4924, a NEDD8-activating enzyme inhibitor, is active in diffuse large B-cell lymphoma models: rationale for treatment of NF-κB-dependent lymphoma. Blood 2010; 116: 1515-23.
    • (2010) Blood , vol.116 , pp. 1515-1523
    • Milhollen, M.A.1    Traore, T.2    Adams-Duffy, J.3
  • 141
    • 84876857315 scopus 로고    scopus 로고
    • WEE1 accumulation and deregulation of S-phase proteins mediate MLN4924 potent inhibitory effect on Ewing sarcoma cells
    • Mackintosh C, Garcia-Dominguez DJ, Ordonez JL, et al. WEE1 accumulation and deregulation of S-phase proteins mediate MLN4924 potent inhibitory effect on Ewing sarcoma cells. Oncogene 2012.
    • (2012) Oncogene
    • Mackintosh, C.1    Garcia-Dominguez, D.J.2    Ordonez, J.L.3
  • 142
    • 84863568271 scopus 로고    scopus 로고
    • The Nedd8-Activating Enzyme Inhibitor MLN4924 Induces Autophagy and Apoptosis to Suppress Liver Cancer Cell Growth
    • Luo Z, Yu G, Lee HW, et al. The Nedd8-Activating Enzyme Inhibitor MLN4924 Induces Autophagy and Apoptosis to Suppress Liver Cancer Cell Growth. Cancer Res 2012; 72: 3360-71.
    • (2012) Cancer Res , vol.72 , pp. 3360-3371
    • Luo, Z.1    Yu, G.2    Lee, H.W.3
  • 143
    • 84855411991 scopus 로고    scopus 로고
    • Radiosensitization of Human Pancreatic Cancer Cells by MLN4924, an Investigational NEDD8-Activating Enzyme Inhibitor
    • Wei D, Li H, Yu J, et al. Radiosensitization of Human Pancreatic Cancer Cells by MLN4924, an Investigational NEDD8-Activating Enzyme Inhibitor. Cancer Res 2012; 72: 282-93.
    • (2012) Cancer Res , vol.72 , pp. 282-293
    • Wei, D.1    Li, H.2    Yu, J.3
  • 144
    • 84863338311 scopus 로고    scopus 로고
    • Treatment-Emergent Mutations in NAE Confer Resistance to the NEDD8-Activating Enzyme Inhibitor MLN4924
    • Milhollen Michael A, Thomas Michael P, Narayanan U, et al. Treatment-Emergent Mutations in NAE Confer Resistance to the NEDD8-Activating Enzyme Inhibitor MLN4924. Cancer Cell 2012; 21: 388-401.
    • (2012) Cancer Cell , vol.21 , pp. 388-401
    • Milhollen, M.A.1    Thomas, M.P.2    Narayanan, U.3
  • 145
    • 35148886143 scopus 로고    scopus 로고
    • Inhibitors of Ubiquitin-Activating Enzyme (E1), a New Class of Potential Cancer Therapeutics
    • Yang Y, Kitagaki J, Dai RM, et al. Inhibitors of Ubiquitin-Activating Enzyme (E1), a New Class of Potential Cancer Therapeutics. Cancer Res 2007; 67: 9472-81.
    • (2007) Cancer Res , vol.67 , pp. 9472-9481
    • Yang, Y.1    Kitagaki, J.2    Dai, R.M.3
  • 146
    • 77950421253 scopus 로고    scopus 로고
    • The ubiquitin-activating enzyme E1 as a therapeutic target for the treatment of leukemia and multiple myeloma
    • Xu GW, Ali M, Wood TE, et al. The ubiquitin-activating enzyme E1 as a therapeutic target for the treatment of leukemia and multiple myeloma. Blood 2010; 115: 2251-9.
    • (2010) Blood , vol.115 , pp. 2251-2259
    • Xu, G.W.1    Ali, M.2    Wood, T.E.3
  • 147
    • 59149101898 scopus 로고    scopus 로고
    • Nitric oxide prodrug JS-K inhibits ubiquitin E1 and kills tumor cells retaining wild-type p53
    • Kitagaki J, Yang Y, Saavedra JE, Colburn NH, Keefer LK, Perantoni AO. Nitric oxide prodrug JS-K inhibits ubiquitin E1 and kills tumor cells retaining wild-type p53. Oncogene 2008; 28: 619-24.
    • (2008) Oncogene , vol.28 , pp. 619-624
    • Kitagaki, J.1    Yang, Y.2    Saavedra, J.E.3    Colburn, N.H.4    Keefer, L.K.5    Perantoni, A.O.6
  • 148
    • 84865415118 scopus 로고    scopus 로고
    • Inhibition of proliferation and survival of diffuse large B-cell lymphoma cells by a small-molecule inhibitor of the ubiquitin-conjugating enzyme Ubc13-Uev1A
    • Pulvino M, Liang Y, Oleksyn D, et al. Inhibition of proliferation and survival of diffuse large B-cell lymphoma cells by a small-molecule inhibitor of the ubiquitin-conjugating enzyme Ubc13-Uev1A. Blood 2012.
    • (2012) Blood
    • Pulvino, M.1    Liang, Y.2    Oleksyn, D.3
  • 149
    • 0037435012 scopus 로고    scopus 로고
    • Alterations of anaphase-promoting complex genes in human colon cancer cells
    • Wang Q, Moyret-Lalle C, Couzon F, et al. Alterations of anaphase-promoting complex genes in human colon cancer cells. Oncogene 2003; 22: 1486-90.
    • (2003) Oncogene , vol.22 , pp. 1486-1490
    • Wang, Q.1    Moyret-Lalle, C.2    Couzon, F.3
  • 150
    • 84555196106 scopus 로고    scopus 로고
    • BRCA1 and BRCA2: Different roles in a common pathway of genome protection
    • Roy R, Chun J, Powell SN. BRCA1 and BRCA2: different roles in a common pathway of genome protection. Nat Rev Cancer 2012; 12: 68-78.
    • (2012) Nat Rev Cancer , vol.12 , pp. 68-78
    • Roy, R.1    Chun, J.2    Powell, S.N.3
  • 151
    • 77449101168 scopus 로고    scopus 로고
    • Mdm2-mediated ubiquitylation: P53 and beyond
    • Marine JC, Lozano G. Mdm2-mediated ubiquitylation: p53 and beyond. Cell Death Differ 2009; 17: 93-102.
    • (2009) Cell Death Differ , vol.17 , pp. 93-102
    • Marine, J.C.1    Lozano, G.2
  • 152
    • 11144315535 scopus 로고    scopus 로고
    • Small molecule RITA binds to p53, blocks p53-HDM-2 interaction and activates p53 function in tumors
    • Issaeva N, Bozko P, Enge M, et al. Small molecule RITA binds to p53, blocks p53-HDM-2 interaction and activates p53 function in tumors. Nat Med 2004; 10: 1321-8.
    • (2004) Nat Med , vol.10 , pp. 1321-1328
    • Issaeva, N.1    Bozko, P.2    Enge, M.3
  • 153
    • 10744221485 scopus 로고    scopus 로고
    • In vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
    • Vassilev LT, Vu BT, Graves B, et al. In vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2. Science 2004; 303: 844-8.
    • (2004) Science , vol.303 , pp. 844-848
    • Vassilev, L.T.1    Vu, B.T.2    Graves, B.3
  • 154
    • 44149121239 scopus 로고    scopus 로고
    • The inherent instability of mutant p53 is alleviated by Mdm2 or p16INK4a loss
    • Terzian T, Suh YA, Iwakuma T, et al. The inherent instability of mutant p53 is alleviated by Mdm2 or p16INK4a loss. Genes Dev 2008; 22: 1337-44.
    • (2008) Genes Dev , vol.22 , pp. 1337-1344
    • Terzian, T.1    Suh, Y.A.2    Iwakuma, T.3
  • 155
    • 36048982462 scopus 로고    scopus 로고
    • Smac Mimetics and TNF: A Dangerous Liaison?
    • Wu H, Tschopp J, Lin SC. Smac Mimetics and TNF: A Dangerous Liaison? Cell 2007; 131: 655-8.
    • (2007) Cell , vol.131 , pp. 655-658
    • Wu, H.1    Tschopp, J.2    Lin, S.C.3
  • 156
    • 84856495152 scopus 로고    scopus 로고
    • Targeting IAP proteins for therapeutic intervention in cancer
    • Fulda S, Vucic D. Targeting IAP proteins for therapeutic intervention in cancer. Nat Rev Drug Discov 2012; 11: 109-24.
    • (2012) Nat Rev Drug Discov , vol.11 , pp. 109-124
    • Fulda, S.1    Vucic, D.2
  • 157
  • 158
    • 36148954336 scopus 로고    scopus 로고
    • IAP Antagonists Target cIAP1 to Induce TNF-Dependent Apoptosis
    • Vince JE, Wong WWL, Khan N, et al. IAP Antagonists Target cIAP1 to Induce TNF-Dependent Apoptosis. Cell 2007; 131: 682-93.
    • (2007) Cell , vol.131 , pp. 682-693
    • Vince, J.E.1    Wong, W.W.L.2    Khan, N.3
  • 159
    • 36048999753 scopus 로고    scopus 로고
    • IAP Antagonists Induce Autoubiquitination of c-IAPs, NF-κB Activation, and TNF-Dependent Apoptosis
    • Varfolomeev E, Blankenship JW, Wayson SM, et al. IAP Antagonists Induce Autoubiquitination of c-IAPs, NF-κB Activation, and TNF-Dependent Apoptosis. Cell 2007; 131: 669-81.
    • (2007) Cell , vol.131 , pp. 669-681
    • Varfolomeev, E.1    Blankenship, J.W.2    Wayson, S.M.3
  • 160
    • 35948994157 scopus 로고    scopus 로고
    • Autocrine TNF Signaling Renders Human Cancer Cells Susceptible to Smac-Mimetic-Induced Apoptosis
    • Petersen SL, Wang L, Yalcin-Chin A, et al. Autocrine TNF Signaling Renders Human Cancer Cells Susceptible to Smac-Mimetic-Induced Apoptosis. Cancer Cell 2007; 12: 445-56.
    • (2007) Cancer Cell , vol.12 , pp. 445-456
    • Petersen, S.L.1    Wang, L.2    Yalcin-Chin, A.3
  • 161
    • 79955759159 scopus 로고    scopus 로고
    • Smac Mimetics Activate the E3 Ligase Activity of cIAP1 Protein by Promoting RING Domain Dimerization
    • Feltham R, Bettjeman B, Budhidarmo R, et al. Smac Mimetics Activate the E3 Ligase Activity of cIAP1 Protein by Promoting RING Domain Dimerization. J Biol Chem 2011; 286: 17015-28.
    • (2011) J Biol Chem , vol.286 , pp. 17015-17028
    • Feltham, R.1    Bettjeman, B.2    Budhidarmo, R.3
  • 162
    • 79953197650 scopus 로고    scopus 로고
    • Polyubiquitin Linkage Profiles in Three Models of Proteolytic Stress Suggest the Etiology of Alzheimer Disease
    • Dammer EB, Na CH, Xu P, et al. Polyubiquitin Linkage Profiles in Three Models of Proteolytic Stress Suggest the Etiology of Alzheimer Disease. J Biol Chem 2011; 286: 10457-65.
    • (2011) J Biol Chem , vol.286 , pp. 10457-10465
    • Dammer, E.B.1    Na, C.H.2    Xu, P.3
  • 163
    • 84866718513 scopus 로고    scopus 로고
    • Cell-Selective Inhibition of NF-κB Signaling Improves Therapeutic Index in a Melanoma Chemotherapy Model
    • Enzler T, Sano Y, Choo MK, et al. Cell-Selective Inhibition of NF-κB Signaling Improves Therapeutic Index in a Melanoma Chemotherapy Model. Cancer Discovery 2011; 1: 496-507.
    • (2011) Cancer Discovery , vol.1 , pp. 496-507
    • Enzler, T.1    Sano, Y.2    Choo, M.K.3
  • 164
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8Åresolution
    • Vijay-Kumar S, Bugg CE, Cook WJ. Structure of ubiquitin refined at 1.8Åresolution. J Mol Biol 1987; 194: 531-44.
    • (1987) J Mol Biol , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.