메뉴 건너뛰기




Volumn 376, Issue 2, 2008, Pages 526-540

Molecular Basis for the Unique Deubiquitinating Activity of the NF-κB Inhibitor A20

Author keywords

A20; crystal structure; deubiquitination; DUB; TRAF6

Indexed keywords

I KAPPA B; INTERLEUKIN 1; LYSINE; NUCLEAR FACTOR KAPPA B INHIBITOR A20; TOLL LIKE RECEPTOR; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 38549146936     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.11.092     Document Type: Article
Times cited : (139)

References (66)
  • 1
    • 0030026698 scopus 로고    scopus 로고
    • A20 zinc finger protein inhibits TNF and IL-1 signaling
    • Jaattela M., Mouritzen H., Elling F., and Bastholm L. A20 zinc finger protein inhibits TNF and IL-1 signaling. J. Immunol. 156 (1996) 1166-1173
    • (1996) J. Immunol. , vol.156 , pp. 1166-1173
    • Jaattela, M.1    Mouritzen, H.2    Elling, F.3    Bastholm, L.4
  • 3
    • 0030909714 scopus 로고    scopus 로고
    • Adenovirus-mediated gene transfer of A20 renders endothelial cells resistant to activation: a means of evaluating the role of endothelial cell activation in xenograft rejection
    • Ferran C., Stroka D.M., Badrichani A.Z., Cooper J.T., and Bach F.H. Adenovirus-mediated gene transfer of A20 renders endothelial cells resistant to activation: a means of evaluating the role of endothelial cell activation in xenograft rejection. Transplant. Proc. 29 (1997) 879-880
    • (1997) Transplant. Proc. , vol.29 , pp. 879-880
    • Ferran, C.1    Stroka, D.M.2    Badrichani, A.Z.3    Cooper, J.T.4    Bach, F.H.5
  • 4
    • 0032745109 scopus 로고    scopus 로고
    • A20 inhibits cytokine-induced apoptosis and nuclear factor kappaB-dependent gene activation in islets
    • Grey S.T., Arvelo M.B., Hasenkamp W., Bach F.H., and Ferran C. A20 inhibits cytokine-induced apoptosis and nuclear factor kappaB-dependent gene activation in islets. J. Exp. Med. 190 (1999) 1135-1146
    • (1999) J. Exp. Med. , vol.190 , pp. 1135-1146
    • Grey, S.T.1    Arvelo, M.B.2    Hasenkamp, W.3    Bach, F.H.4    Ferran, C.5
  • 5
    • 0034668204 scopus 로고    scopus 로고
    • A20 and A20-binding proteins as cellular inhibitors of nuclear factor-kappa B-dependent gene expression and apoptosis
    • Beyaert R., Heyninck K., and Van Huffel S. A20 and A20-binding proteins as cellular inhibitors of nuclear factor-kappa B-dependent gene expression and apoptosis. Biochem. Pharmacol. 60 (2000) 1143-1151
    • (2000) Biochem. Pharmacol. , vol.60 , pp. 1143-1151
    • Beyaert, R.1    Heyninck, K.2    Van Huffel, S.3
  • 6
    • 0037418749 scopus 로고    scopus 로고
    • Regulation of Toll-like receptor 4 signalling by A20 zinc finger protein
    • O'Reilly S.M., and Moynagh P.N. Regulation of Toll-like receptor 4 signalling by A20 zinc finger protein. Biochem. Biophys. Res. Commun. 303 (2003) 586-593
    • (2003) Biochem. Biophys. Res. Commun. , vol.303 , pp. 586-593
    • O'Reilly, S.M.1    Moynagh, P.N.2
  • 7
    • 0025271844 scopus 로고
    • Tumor necrosis factor-alpha induction of novel gene products in human endothelial cells including a macrophage-specific chemotaxin
    • Dixit V.M., Green S., Sarma V., Holzman L.B., Wolf F.W., O'Rourke K., et al. Tumor necrosis factor-alpha induction of novel gene products in human endothelial cells including a macrophage-specific chemotaxin. J. Biol. Chem. 265 (1990) 2973-2978
    • (1990) J. Biol. Chem. , vol.265 , pp. 2973-2978
    • Dixit, V.M.1    Green, S.2    Sarma, V.3    Holzman, L.B.4    Wolf, F.W.5    O'Rourke, K.6
  • 8
    • 0025179989 scopus 로고
    • The A20 cDNA induced by tumor necrosis factor alpha encodes a novel type of zinc finger protein
    • Opipari Jr. A.W., Boguski M.S., and Dixit V.M. The A20 cDNA induced by tumor necrosis factor alpha encodes a novel type of zinc finger protein. J. Biol. Chem. 265 (1990) 14705-14708
    • (1990) J. Biol. Chem. , vol.265 , pp. 14705-14708
    • Opipari Jr., A.W.1    Boguski, M.S.2    Dixit, V.M.3
  • 9
    • 0026699666 scopus 로고
    • Transcriptional activation of the tumor necrosis factor alpha-inducible zinc finger protein, A20, is mediated by kappa B elements
    • Krikos A., Laherty C.D., and Dixit V.M. Transcriptional activation of the tumor necrosis factor alpha-inducible zinc finger protein, A20, is mediated by kappa B elements. J. Biol. Chem. 267 (1992) 17971-17976
    • (1992) J. Biol. Chem. , vol.267 , pp. 17971-17976
    • Krikos, A.1    Laherty, C.D.2    Dixit, V.M.3
  • 10
    • 0026465540 scopus 로고
    • The Epstein-Barr virus LMP1 gene product induces A20 zinc finger protein expression by activating nuclear factor kappa B
    • Laherty C.D., Hu H.M., Opipari A.W., Wang F., and Dixit V.M. The Epstein-Barr virus LMP1 gene product induces A20 zinc finger protein expression by activating nuclear factor kappa B. J. Biol. Chem. 267 (1992) 24157-24160
    • (1992) J. Biol. Chem. , vol.267 , pp. 24157-24160
    • Laherty, C.D.1    Hu, H.M.2    Opipari, A.W.3    Wang, F.4    Dixit, V.M.5
  • 11
    • 0027456337 scopus 로고
    • Human T cell leukemia virus type I Tax and phorbol 12-myristate 13-acetate induce expression of the A20 zinc finger protein by distinct mechanisms involving nuclear factor kappa B
    • Laherty C.D., Perkins N.D., and Dixit V.M. Human T cell leukemia virus type I Tax and phorbol 12-myristate 13-acetate induce expression of the A20 zinc finger protein by distinct mechanisms involving nuclear factor kappa B. J. Biol. Chem. 268 (1993) 5032-5039
    • (1993) J. Biol. Chem. , vol.268 , pp. 5032-5039
    • Laherty, C.D.1    Perkins, N.D.2    Dixit, V.M.3
  • 12
    • 0028850937 scopus 로고
    • Lymphoid expression and regulation of A20, an inhibitor of programmed cell death
    • Tewari M., Wolf F.W., Seldin M.F., Shea O.'K.S., Dixit V.M., and Turka L.A. Lymphoid expression and regulation of A20, an inhibitor of programmed cell death. J. Immunol. 154 (1995) 1699-1706
    • (1995) J. Immunol. , vol.154 , pp. 1699-1706
    • Tewari, M.1    Wolf, F.W.2    Seldin, M.F.3    Shea, O.'K.S.4    Dixit, V.M.5    Turka, L.A.6
  • 13
    • 0029073035 scopus 로고
    • Activation of the B-cell surface receptor CD40 induces A20, a novel zinc finger protein that inhibits apoptosis
    • Sarma V., Lin Z., Clark L., Rust B.M., Tewari M., Noelle R.J., and Dixit V.M. Activation of the B-cell surface receptor CD40 induces A20, a novel zinc finger protein that inhibits apoptosis. J. Biol. Chem. 270 (1995) 12343-12346
    • (1995) J. Biol. Chem. , vol.270 , pp. 12343-12346
    • Sarma, V.1    Lin, Z.2    Clark, L.3    Rust, B.M.4    Tewari, M.5    Noelle, R.J.6    Dixit, V.M.7
  • 14
    • 0032531994 scopus 로고    scopus 로고
    • Lipopolysaccharide induces the antiapoptotic molecules, A1 and A20, in microvascular endothelial cells
    • Hu X., Yee E., Harlan J.M., Wong F., and Karsan A. Lipopolysaccharide induces the antiapoptotic molecules, A1 and A20, in microvascular endothelial cells. Blood 92 (1998) 2759-2765
    • (1998) Blood , vol.92 , pp. 2759-2765
    • Hu, X.1    Yee, E.2    Harlan, J.M.3    Wong, F.4    Karsan, A.5
  • 15
    • 0041998173 scopus 로고    scopus 로고
    • Differential expression and function of A20 and TRAF1 in Hodgkin lymphoma and anaplastic large cell lymphoma and their induction by CD30 stimulation
    • Durkop H., Hirsch B., Hahn C., Foss H.D., and Stein H. Differential expression and function of A20 and TRAF1 in Hodgkin lymphoma and anaplastic large cell lymphoma and their induction by CD30 stimulation. J. Pathol. 200 (2003) 229-239
    • (2003) J. Pathol. , vol.200 , pp. 229-239
    • Durkop, H.1    Hirsch, B.2    Hahn, C.3    Foss, H.D.4    Stein, H.5
  • 16
    • 0034730713 scopus 로고    scopus 로고
    • Failure to regulate TNF-induced NF-kappaB and cell death responses in A20-deficient mice
    • Lee E.G., Boone D.L., Chai S., Libby S.L., Chien M., Lodolce J.P., and Ma A. Failure to regulate TNF-induced NF-kappaB and cell death responses in A20-deficient mice. Science 289 (2000) 2350-2354
    • (2000) Science , vol.289 , pp. 2350-2354
    • Lee, E.G.1    Boone, D.L.2    Chai, S.3    Libby, S.L.4    Chien, M.5    Lodolce, J.P.6    Ma, A.7
  • 17
    • 5444223519 scopus 로고    scopus 로고
    • The ubiquitin-modifying enzyme A20 is required for termination of Toll-like receptor responses
    • Boone D.L., Turer E.E., Lee E.G., Ahmad R.C., Wheeler M.T., Tsui C., et al. The ubiquitin-modifying enzyme A20 is required for termination of Toll-like receptor responses. Nat. Immunol. 5 (2004) 1052-1060
    • (2004) Nat. Immunol. , vol.5 , pp. 1052-1060
    • Boone, D.L.1    Turer, E.E.2    Lee, E.G.3    Ahmad, R.C.4    Wheeler, M.T.5    Tsui, C.6
  • 18
    • 33644850482 scopus 로고    scopus 로고
    • Negative regulation of the retinoic acid-inducible gene I-induced antiviral state by the ubiquitin-editing protein A20
    • Lin R., Yang L., Nakhaei P., Sun Q., Sharif-E. Askari I., and Julkunen J. Negative regulation of the retinoic acid-inducible gene I-induced antiviral state by the ubiquitin-editing protein A20. J. Biol. Chem. 281 (2006) 2095-2103
    • (2006) J. Biol. Chem. , vol.281 , pp. 2095-2103
    • Lin, R.1    Yang, L.2    Nakhaei, P.3    Sun, Q.4    Sharif-E. Askari, I.5    Julkunen, J.6
  • 19
    • 4944251748 scopus 로고    scopus 로고
    • A20 is a potent inhibitor of TLR3- and Sendai virus-induced activation of NF-kappaB and ISRE and IFN-beta promoter
    • Wang Y.Y., Li L., Han K.J., Zhai Z., and Shu H.B. A20 is a potent inhibitor of TLR3- and Sendai virus-induced activation of NF-kappaB and ISRE and IFN-beta promoter. FEBS Lett. 576 (2004) 86-90
    • (2004) FEBS Lett. , vol.576 , pp. 86-90
    • Wang, Y.Y.1    Li, L.2    Han, K.J.3    Zhai, Z.4    Shu, H.B.5
  • 21
    • 4444376712 scopus 로고    scopus 로고
    • Signaling to NF-kappaB
    • Hayden M.S., and Ghosh S. Signaling to NF-kappaB. Genes Dev. 18 (2004) 2195-2224
    • (2004) Genes Dev. , vol.18 , pp. 2195-2224
    • Hayden, M.S.1    Ghosh, S.2
  • 22
    • 0032939356 scopus 로고    scopus 로고
    • The cytokine-inducible zinc finger protein A20 inhibits IL-1-induced NF-kappaB activation at the level of TRAF6
    • Heyninck K., and Beyaert R. The cytokine-inducible zinc finger protein A20 inhibits IL-1-induced NF-kappaB activation at the level of TRAF6. FEBS Lett. 442 (1999) 147-150
    • (1999) FEBS Lett. , vol.442 , pp. 147-150
    • Heyninck, K.1    Beyaert, R.2
  • 23
    • 0033612571 scopus 로고    scopus 로고
    • The zinc finger protein A20 inhibits TNF-induced NF-kappaB-dependent gene expression by interfering with an RIP- or TRAF2-mediated transactivation signal and directly binds to a novel NF-kappaB-inhibiting protein ABIN
    • Heyninck K., De Valck D., Vanden Berghe W., Van Criekinge W., Contreras R., Fiers W., et al. The zinc finger protein A20 inhibits TNF-induced NF-kappaB-dependent gene expression by interfering with an RIP- or TRAF2-mediated transactivation signal and directly binds to a novel NF-kappaB-inhibiting protein ABIN. J. Cell Biol. 145 (1999) 1471-1482
    • (1999) J. Cell Biol. , vol.145 , pp. 1471-1482
    • Heyninck, K.1    De Valck, D.2    Vanden Berghe, W.3    Van Criekinge, W.4    Contreras, R.5    Fiers, W.6
  • 24
    • 3943054838 scopus 로고    scopus 로고
    • De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling
    • Wertz I.E., O'Rourke K.M., Zhou H., Eby M., Aravind L., Seshagiri S., et al. De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling. Nature 430 (2004) 694-699
    • (2004) Nature , vol.430 , pp. 694-699
    • Wertz, I.E.1    O'Rourke, K.M.2    Zhou, H.3    Eby, M.4    Aravind, L.5    Seshagiri, S.6
  • 25
    • 0033712615 scopus 로고    scopus 로고
    • Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKgamma) upon receptor stimulation
    • Zhang S.Q., Kovalenko A., Cantarella G., and Wallach D. Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKgamma) upon receptor stimulation. Immunity 12 (2000) 301-311
    • (2000) Immunity , vol.12 , pp. 301-311
    • Zhang, S.Q.1    Kovalenko, A.2    Cantarella, G.3    Wallach, D.4
  • 26
    • 23144449789 scopus 로고    scopus 로고
    • Ubiquitin signalling in the NF-kappaB pathway
    • Chen Z.J. Ubiquitin signalling in the NF-kappaB pathway. Nat. Cell Biol. 7 (2005) 758-765
    • (2005) Nat. Cell Biol. , vol.7 , pp. 758-765
    • Chen, Z.J.1
  • 27
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • Deng L., Wang C., Spencer E., Yang L., Braun A., You J., et al. Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 103 (2000) 351-361
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1    Wang, C.2    Spencer, E.3    Yang, L.4    Braun, A.5    You, J.6
  • 29
    • 33947506493 scopus 로고    scopus 로고
    • Site-specific Lys-63-linked tumor necrosis factor receptor-associated factor 6 auto-ubiquitination is a critical determinant of I kappa B kinase activation
    • Lamothe B., Besse A., Campos A.D., Webster W.K., Wu H., and Darnay B.G. Site-specific Lys-63-linked tumor necrosis factor receptor-associated factor 6 auto-ubiquitination is a critical determinant of I kappa B kinase activation. J. Biol. Chem. 282 (2007) 4102-4112
    • (2007) J. Biol. Chem. , vol.282 , pp. 4102-4112
    • Lamothe, B.1    Besse, A.2    Campos, A.D.3    Webster, W.K.4    Wu, H.5    Darnay, B.G.6
  • 30
    • 0033580466 scopus 로고    scopus 로고
    • The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase cascade in the IL-1 signalling pathway
    • Ninomiya-Tsuji J., Kishimoto K., Hiyama A., Inoue J., Cao Z., and Matsumoto K. The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase cascade in the IL-1 signalling pathway. Nature 398 (1999) 252-256
    • (1999) Nature , vol.398 , pp. 252-256
    • Ninomiya-Tsuji, J.1    Kishimoto, K.2    Hiyama, A.3    Inoue, J.4    Cao, Z.5    Matsumoto, K.6
  • 31
    • 0035793610 scopus 로고    scopus 로고
    • The MAPK kinase kinase TAK1 plays a central role in coupling the interleukin-1 receptor to both transcriptional and RNA-targeted mechanisms of gene regulation
    • Holtmann H., Enninga J., Kalble S., Thiefes A., Dorrie A., Broemer M., et al. The MAPK kinase kinase TAK1 plays a central role in coupling the interleukin-1 receptor to both transcriptional and RNA-targeted mechanisms of gene regulation. J. Biol. Chem. 276 (2001) 3508-3516
    • (2001) J. Biol. Chem. , vol.276 , pp. 3508-3516
    • Holtmann, H.1    Enninga, J.2    Kalble, S.3    Thiefes, A.4    Dorrie, A.5    Broemer, M.6
  • 32
    • 0033952268 scopus 로고    scopus 로고
    • TAK1 mediates an activation signal from toll-like receptor(s) to nuclear factor-kappaB in lipopolysaccharide-stimulated macrophages
    • Irie T., Muta T., and Takeshige K. TAK1 mediates an activation signal from toll-like receptor(s) to nuclear factor-kappaB in lipopolysaccharide-stimulated macrophages. FEBS Lett. 467 (2000) 160-164
    • (2000) FEBS Lett. , vol.467 , pp. 160-164
    • Irie, T.1    Muta, T.2    Takeshige, K.3
  • 33
    • 0033669743 scopus 로고    scopus 로고
    • TAK1 regulates multiple protein kinase cascades activated by bacterial lipopolysaccharide
    • Lee J., Mira-Arbibe L., and Ulevitch R.J. TAK1 regulates multiple protein kinase cascades activated by bacterial lipopolysaccharide. J. Leukocyte Biol. 68 (2000) 909-915
    • (2000) J. Leukocyte Biol. , vol.68 , pp. 909-915
    • Lee, J.1    Mira-Arbibe, L.2    Ulevitch, R.J.3
  • 34
    • 0038714270 scopus 로고    scopus 로고
    • Poly(I-C)-induced Toll-like receptor 3 (TLR3)-mediated activation of NFkappa B and MAP kinase is through an interleukin-1 receptor-associated kinase (IRAK)-independent pathway employing the signaling components TLR3-TRAF6-TAK1-TAB2-PKR
    • Jiang Z., Zamanian-Daryoush M., Nie H., Silva A.M., Williams B.R., and Li X. Poly(I-C)-induced Toll-like receptor 3 (TLR3)-mediated activation of NFkappa B and MAP kinase is through an interleukin-1 receptor-associated kinase (IRAK)-independent pathway employing the signaling components TLR3-TRAF6-TAK1-TAB2-PKR. J. Biol. Chem. 278 (2003) 16713-16719
    • (2003) J. Biol. Chem. , vol.278 , pp. 16713-16719
    • Jiang, Z.1    Zamanian-Daryoush, M.2    Nie, H.3    Silva, A.M.4    Williams, B.R.5    Li, X.6
  • 35
    • 0036150184 scopus 로고    scopus 로고
    • Receptor activator of NF-kappaB ligand (RANKL) activates TAK1 mitogen-activated protein kinase kinase kinase through a signaling complex containing RANK, TAB2, and TRAF6
    • Mizukami J., Takaesu G., Akatsuka H., Sakurai H., Ninomiya-Tsuji J., Matsumoto K., and Sakurai N. Receptor activator of NF-kappaB ligand (RANKL) activates TAK1 mitogen-activated protein kinase kinase kinase through a signaling complex containing RANK, TAB2, and TRAF6. Mol. Cell Biol. 22 (2002) 992-1000
    • (2002) Mol. Cell Biol. , vol.22 , pp. 992-1000
    • Mizukami, J.1    Takaesu, G.2    Akatsuka, H.3    Sakurai, H.4    Ninomiya-Tsuji, J.5    Matsumoto, K.6    Sakurai, N.7
  • 36
    • 0029940355 scopus 로고    scopus 로고
    • TAB1: an activator of the TAK1 MAPKKK in TGF-beta signal transduction
    • Shibuya H., Yamaguchi K., Shirakabe K., Tonegawa A., Gotoh Y., Ueno N., et al. TAB1: an activator of the TAK1 MAPKKK in TGF-beta signal transduction. Science 272 (1996) 1179-1182
    • (1996) Science , vol.272 , pp. 1179-1182
    • Shibuya, H.1    Yamaguchi, K.2    Shirakabe, K.3    Tonegawa, A.4    Gotoh, Y.5    Ueno, N.6
  • 37
    • 0033634977 scopus 로고    scopus 로고
    • TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway
    • Takaesu G., Kishida S., Hiyama A., Yamaguchi K., Shibuya H., Irie K., et al. TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway. Mol. Cell 5 (2000) 649-658
    • (2000) Mol. Cell , vol.5 , pp. 649-658
    • Takaesu, G.1    Kishida, S.2    Hiyama, A.3    Yamaguchi, K.4    Shibuya, H.5    Irie, K.6
  • 39
    • 1542314841 scopus 로고    scopus 로고
    • TAB3, a new binding partner of the protein kinase TAK1
    • Cheung P.C., Nebreda A.R., and Cohen P. TAB3, a new binding partner of the protein kinase TAK1. Biochem. J. 378 (2004) 27-34
    • (2004) Biochem. J. , vol.378 , pp. 27-34
    • Cheung, P.C.1    Nebreda, A.R.2    Cohen, P.3
  • 42
    • 4344712350 scopus 로고    scopus 로고
    • TAB2 and TAB3 activate the NF-kappaB pathway through binding to polyubiquitin chains
    • Kanayama A., Seth R.B., Sun L., Ea C.K., Hong M., Shaito A., et al. TAB2 and TAB3 activate the NF-kappaB pathway through binding to polyubiquitin chains. Mol. Cell 15 (2004) 535-548
    • (2004) Mol. Cell , vol.15 , pp. 535-548
    • Kanayama, A.1    Seth, R.B.2    Sun, L.3    Ea, C.K.4    Hong, M.5    Shaito, A.6
  • 43
    • 11844251985 scopus 로고    scopus 로고
    • A20 inhibits NF-kappaB activation by dual ubiquitin-editing functions
    • Heyninck K., and Beyaert R. A20 inhibits NF-kappaB activation by dual ubiquitin-editing functions. Trends Biochem. Sci. 30 (2005) 1-4
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 1-4
    • Heyninck, K.1    Beyaert, R.2
  • 44
    • 1642423503 scopus 로고    scopus 로고
    • Zinc-finger protein A20, a regulator of inflammation and cell survival, has de-ubiquitinating activity
    • Evans P.C., Ovaa H., Hamon M., Kilshaw P.J., Hamm S., Bauer S., et al. Zinc-finger protein A20, a regulator of inflammation and cell survival, has de-ubiquitinating activity. Biochem. J. 378 (2004) 727-734
    • (2004) Biochem. J. , vol.378 , pp. 727-734
    • Evans, P.C.1    Ovaa, H.2    Hamon, M.3    Kilshaw, P.J.4    Hamm, S.5    Bauer, S.6
  • 45
    • 0035370106 scopus 로고    scopus 로고
    • Functional redundancy of the zinc fingers of A20 for inhibition of NF-kappaB activation and protein-protein interactions
    • Klinkenberg M., Van Huffel S., Heyninck K., and Beyaert R. Functional redundancy of the zinc fingers of A20 for inhibition of NF-kappaB activation and protein-protein interactions. FEBS Lett. 498 (2001) 93-97
    • (2001) FEBS Lett. , vol.498 , pp. 93-97
    • Klinkenberg, M.1    Van Huffel, S.2    Heyninck, K.3    Beyaert, R.4
  • 46
    • 9644268864 scopus 로고    scopus 로고
    • Mechanism and function of deubiquitinating enzymes
    • Amerik A.Y., and Hochstrasser M. Mechanism and function of deubiquitinating enzymes. Biochim. Biophys. Acta 1695 (2004) 189-207
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 189-207
    • Amerik, A.Y.1    Hochstrasser, M.2
  • 48
    • 0033974998 scopus 로고    scopus 로고
    • A novel superfamily of predicted cysteine proteases from eukaryotes, viruses and Chlamydia pneumoniae
    • Makarova K.S., Aravind L., and Koonin E.V. A novel superfamily of predicted cysteine proteases from eukaryotes, viruses and Chlamydia pneumoniae. Trends Biochem. Sci. 25 (2000) 50-52
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 50-52
    • Makarova, K.S.1    Aravind, L.2    Koonin, E.V.3
  • 49
    • 0031059039 scopus 로고    scopus 로고
    • Detecting and overcoming crystal twinning
    • Yeates T.O. Detecting and overcoming crystal twinning. Methods Enzymol. 276 (1997) 344-358
    • (1997) Methods Enzymol. , vol.276 , pp. 344-358
    • Yeates, T.O.1
  • 50
    • 0346432075 scopus 로고    scopus 로고
    • Structure of superoxide dismutase from Pyrobaculum aerophilum presents a challenging case in molecular replacement with multiple molecules, pseudo-symmetry and twinning
    • Lee S., Sawaya M.R., and Eisenberg D. Structure of superoxide dismutase from Pyrobaculum aerophilum presents a challenging case in molecular replacement with multiple molecules, pseudo-symmetry and twinning. Acta Crystallogr. Sect. D 59 (2003) 2191-2199
    • (2003) Acta Crystallogr. Sect. D , vol.59 , pp. 2191-2199
    • Lee, S.1    Sawaya, M.R.2    Eisenberg, D.3
  • 52
    • 0033565867 scopus 로고    scopus 로고
    • Structural basis for the specificity of ubiquitin C-terminal hydrolases
    • Johnston S.C., Riddle S.M., Cohen R.E., and Hill C.P. Structural basis for the specificity of ubiquitin C-terminal hydrolases. EMBO J. 18 (1999) 3877-3887
    • (1999) EMBO J. , vol.18 , pp. 3877-3887
    • Johnston, S.C.1    Riddle, S.M.2    Cohen, R.E.3    Hill, C.P.4
  • 53
  • 54
    • 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., et al. Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde. Cell 111 (2002) 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
  • 55
    • 27744516748 scopus 로고    scopus 로고
    • Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14
    • Hu M., Li P., Song L., Jeffrey P.D., Chenova T.A., Wilkinson K.D., et al. Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14. EMBO J. 24 (2005) 3747-3756
    • (2005) EMBO J. , vol.24 , pp. 3747-3756
    • Hu, M.1    Li, P.2    Song, L.3    Jeffrey, P.D.4    Chenova, T.A.5    Wilkinson, K.D.6
  • 56
    • 33746827805 scopus 로고    scopus 로고
    • Structural basis of ubiquitin recognition by the deubiquitinating protease USP2
    • Renatus M., Parrado S.G., D'Arcy A., Eidhoff U., Gerhartz B., Hassiepen U., et al. Structural basis of ubiquitin recognition by the deubiquitinating protease USP2. Structure 14 (2006) 1293-1302
    • (2006) Structure , vol.14 , pp. 1293-1302
    • Renatus, M.1    Parrado, S.G.2    D'Arcy, A.3    Eidhoff, U.4    Gerhartz, B.5    Hassiepen, U.6
  • 58
    • 0023704385 scopus 로고
    • The role of the otu gene in Drosophila oogenesis
    • King R.C., and Storto P.D. The role of the otu gene in Drosophila oogenesis. Bioessays 8 (1988) 18-24
    • (1988) Bioessays , vol.8 , pp. 18-24
    • King, R.C.1    Storto, P.D.2
  • 60
    • 0000783145 scopus 로고
    • Ubiquitin-aldehyde: a general inhibitor of ubiquitin-recycling processes
    • Hershko A., and Rose I.A. Ubiquitin-aldehyde: a general inhibitor of ubiquitin-recycling processes. Proc. Natl Acad. Sci. USA 84 (1987) 1829-1833
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 1829-1833
    • Hershko, A.1    Rose, I.A.2
  • 62
    • 0023042522 scopus 로고
    • Mechanism of ubiquitin carboxyl-terminal hydrolase. Borohydride and hydroxylamine inactivate in the presence of ubiquitin
    • Pickart C.M., and Rose I.A. Mechanism of ubiquitin carboxyl-terminal hydrolase. Borohydride and hydroxylamine inactivate in the presence of ubiquitin. J. Biol. Chem. 261 (1986) 10210-10217
    • (1986) J. Biol. Chem. , vol.261 , pp. 10210-10217
    • Pickart, C.M.1    Rose, I.A.2
  • 63
    • 0032539582 scopus 로고    scopus 로고
    • Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes
    • Dang L.C., Melandri F.D., and Stein R.L. Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes. Biochemistry 37 (1998) 1868-1879
    • (1998) Biochemistry , vol.37 , pp. 1868-1879
    • Dang, L.C.1    Melandri, F.D.2    Stein, R.L.3
  • 64
    • 33947312840 scopus 로고    scopus 로고
    • Ubiquitylation within signaling pathways in- and outside of inflammation
    • Hochrainer K., and Lipp J. Ubiquitylation within signaling pathways in- and outside of inflammation. Thromb. Haemost. 97 (2007) 370-377
    • (2007) Thromb. Haemost. , vol.97 , pp. 370-377
    • Hochrainer, K.1    Lipp, J.2
  • 65
    • 38149051652 scopus 로고    scopus 로고
    • Structure of the A20 OTU domain and mechanistic insights into deubiquitination
    • Komander D., and Barford D. Structure of the A20 OTU domain and mechanistic insights into deubiquitination. Biochem J. 409 (2008) 77-85
    • (2008) Biochem J. , vol.409 , pp. 77-85
    • Komander, D.1    Barford, D.2
  • 66
    • 0037779022 scopus 로고    scopus 로고
    • A statistic for local intensity differences: robustness to anisotropy and pseudo-centering and utility for detecting twinning
    • Padilla J.E., and Yeates T.O. A statistic for local intensity differences: robustness to anisotropy and pseudo-centering and utility for detecting twinning. Acta Crystallogr. Sect. D 59 (2003) 1124-1130
    • (2003) Acta Crystallogr. Sect. D , vol.59 , pp. 1124-1130
    • Padilla, J.E.1    Yeates, T.O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.