메뉴 건너뛰기




Volumn 48, Issue 2, 2013, Pages 89-97

The role of allostery in the ubiquitin-proteasome system

Author keywords

Allosteric; Allostery; Degradation; Molecular machine; Ubiquitin

Indexed keywords

PROTEASOME; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3;

EID: 84875591188     PISSN: 10409238     EISSN: 15497798     Source Type: Journal    
DOI: 10.3109/10409238.2012.742856     Document Type: Review
Times cited : (28)

References (89)
  • 1
    • 0038449224 scopus 로고    scopus 로고
    • Otubains: A new family of cysteine proteases in the ubiquitin pathway
    • Balakirev MY, Tcherniuk SO, Jaquinod M, et al. (2003). Otubains: a new family of cysteine proteases in the ubiquitin pathway. EMBO Rep 4:517-22
    • (2003) EMBO Rep , vol.4 , pp. 517-522
    • Balakirev, M.Y.1    Tcherniuk, S.O.2    Jaquinod, M.3
  • 2
    • 59649104242 scopus 로고    scopus 로고
    • Polyubiquitin substrates allosterically activate their own degradation by the 26S proteasome
    • Bech-Otschir D, Helfrich A, Enenkel C, et al. (2009). Polyubiquitin substrates allosterically activate their own degradation by the 26S proteasome. Nat Struct Mol Biol 16:219-25
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 219-225
    • Bech-Otschir, D.1    Helfrich, A.2    Enenkel, C.3
  • 3
    • 0036177128 scopus 로고    scopus 로고
    • Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1
    • Bernier-Villamor V, Sampson DA, Matunis MJ, et al. (2002). Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1. Cell 108:345-56
    • (2002) Cell , vol.108 , pp. 345-356
    • Bernier-Villamor, V.1    Sampson, D.A.2    Matunis, M.J.3
  • 4
    • 33644850903 scopus 로고    scopus 로고
    • A UbcH5/ ubiquitin noncovalent complex is required for processive BRCA1- directed ubiquitination
    • Brzovic PS, Lissounov A, Christensen DE, et al. (2006). A UbcH5/ ubiquitin noncovalent complex is required for processive BRCA1- directed ubiquitination. Mol Cell 21:873-80
    • (2006) Mol Cell , vol.21 , pp. 873-880
    • Brzovic, P.S.1    Lissounov, A.2    Christensen, D.E.3
  • 5
    • 36549014181 scopus 로고    scopus 로고
    • Taking it step by step: Mechanistic insights from structural studies of ubiquitin/ubiquitin-like protein modification pathways
    • Capili AD, Lima CD. (2007). Taking it step by step: mechanistic insights from structural studies of ubiquitin/ubiquitin-like protein modification pathways. Curr Opin Struct Biol 17:726-35
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 726-735
    • Capili, A.D.1    Lima, C.D.2
  • 6
    • 84863115494 scopus 로고    scopus 로고
    • Behind the curtain: Cellular mechanisms for allosteric modulation of calcium-sensing receptors
    • Cavanaugh A, Huang Y, Breitwieser GE. (2012). Behind the curtain: cellular mechanisms for allosteric modulation of calcium-sensing receptors. Brit J Pharmacol 165:1670-7
    • (2012) Brit J Pharmacol , vol.165 , pp. 1670-1677
    • Cavanaugh, A.1    Huang, Y.2    Breitwieser, G.E.3
  • 7
    • 79959656754 scopus 로고    scopus 로고
    • An allosteric inhibitor of the human Cdc34 ubiquitin-conjugating enzyme
    • Ceccarelli DF, Tang X, Pelletier B, et al. (2011). An allosteric inhibitor of the human Cdc34 ubiquitin-conjugating enzyme. Cell 145:1075-87
    • (2011) Cell , vol.145 , pp. 1075-1087
    • Ceccarelli, D.F.1    Tang, X.2    Pelletier, B.3
  • 8
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg
    • Ciechanover A, Brundin P. (2003). The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Neuron 40:427-46
    • (2003) Neuron , vol.40 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 9
    • 45749091661 scopus 로고    scopus 로고
    • The CK2 phosphorylation of catalytic domain of Cdc34 modulates its activity at the G1 to S transition in Saccharomyces cerevisiae
    • Coccetti P, Tripodi F, Tedeschi G, et al. (2008). The CK2 phosphorylation of catalytic domain of Cdc34 modulates its activity at the G1 to S transition in Saccharomyces cerevisiae. Cell Cycle 7:1391-401
    • (2008) Cell Cycle , vol.7 , pp. 1391-1401
    • Coccetti, P.1    Tripodi, F.2    Tedeschi, G.3
  • 10
    • 53149123284 scopus 로고    scopus 로고
    • Structure of the human 26S proteasome: Subunit radial displacements open the gate into the proteolytic core
    • da Fonseca PC, Morris EP. (2008). Structure of the human 26S proteasome: subunit radial displacements open the gate into the proteolytic core. J Biol Chem 283:23305-14
    • (2008) J Biol Chem , vol.283 , pp. 23305-23314
    • Da Fonseca, P.C.1    Morris, E.P.2
  • 11
    • 67449110736 scopus 로고    scopus 로고
    • Allosteric activation of E2- RING finger-mediated ubiquitylation by a structurally defined specific E2-binding region of gp78
    • Das R, Mariano J, Tsai YC, et al. (2009). Allosteric activation of E2- RING finger-mediated ubiquitylation by a structurally defined specific E2-binding region of gp78. Mol Cell 34:674-85
    • (2009) Mol Cell , vol.34 , pp. 674-685
    • Das, R.1    Mariano, J.2    Tsai, Y.C.3
  • 12
    • 84856708226 scopus 로고    scopus 로고
    • Structural basis for autoinhibition and phosphorylation-dependent activation of c-Cbl
    • Dou H, Buetow L, Hock A, et al. (2012a). Structural basis for autoinhibition and phosphorylation-dependent activation of c-Cbl. Nat Struct Mol Biol 19:184-92
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 184-192
    • Dou, H.1    Buetow, L.2    Hock, A.3
  • 13
    • 84866124869 scopus 로고    scopus 로고
    • BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer
    • Dou H, Buetow L, Sibbet GJ, et al. (2012b). BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nat Struct Mol Biol 19:876-83
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 876-883
    • Dou, H.1    Buetow, L.2    Sibbet, G.J.3
  • 14
    • 50449108516 scopus 로고    scopus 로고
    • Structural insights into NEDD8 activation of cullin-RING ligases: Conformational control of conjugation
    • Duda DM, Borg LA, Scott DC, et al. (2008). Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation. Cell 134:995-1006
    • (2008) Cell , vol.134 , pp. 995-1006
    • Duda, D.M.1    Borg, L.A.2    Scott, D.C.3
  • 15
    • 79953068658 scopus 로고    scopus 로고
    • Structural regulation of cullin-RING ubiquitin ligase complexes
    • Duda DM, Scott DC, Calabrese MF, et al. (2011). Structural regulation of cullin-RING ubiquitin ligase complexes. Curr Opin Struct Biol 21:257-64
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 257-264
    • Duda, D.M.1    Scott, D.C.2    Calabrese, M.F.3
  • 16
    • 0034955239 scopus 로고    scopus 로고
    • Deubiquitination step in the endocytic pathway of yeast plasma membrane proteins: Crucial role of Doa4p ubiquitin isopeptidase
    • Dupre S, Haguenauer-Tsapis R. (2001). Deubiquitination step in the endocytic pathway of yeast plasma membrane proteins: crucial role of Doa4p ubiquitin isopeptidase. Mol Cellular Biol 21:4482-94
    • (2001) Mol Cellular Biol , vol.21 , pp. 4482-4494
    • Dupre, S.1    Haguenauer-Tsapis, R.2
  • 17
    • 0033553857 scopus 로고    scopus 로고
    • A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae
    • Fisk HA, Yaffe MP. (1999). A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae. J Cell Biol 145:1199-208
    • (1999) J Cell Biol , vol.145 , pp. 1199-1208
    • Fisk, H.A.1    Yaffe, M.P.2
  • 18
    • 80054836161 scopus 로고    scopus 로고
    • Atomic force microscopy of proteasome assemblies
    • Gaczynska M, Osmulski PA. (2011). Atomic force microscopy of proteasome assemblies. Methods Mol Biol 736:117-32
    • (2011) Methods Mol Biol , vol.736 , pp. 117-132
    • Gaczynska, M.1    Osmulski, P.A.2
  • 19
    • 0042848726 scopus 로고    scopus 로고
    • Proline- and argininerich peptides constitute a novel class of allosteric inhibitors of proteasome activity
    • Gaczynska M, Osmulski PA, Gao Y, et al. (2003). Proline- and argininerich peptides constitute a novel class of allosteric inhibitors of proteasome activity. Biochemistry 42:8663-70
    • (2003) Biochemistry , vol.42 , pp. 8663-8670
    • Gaczynska, M.1    Osmulski, P.A.2    Gao, Y.3
  • 20
    • 47649125643 scopus 로고    scopus 로고
    • Allosteric regulation and catalysis emerge via a common route
    • Goodey NM, Benkovic SJ. (2008). Allosteric regulation and catalysis emerge via a common route. Nat Chem Biol 4:474-82
    • (2008) Nat Chem Biol , vol.4 , pp. 474-482
    • Goodey, N.M.1    Benkovic, S.J.2
  • 21
    • 6344219895 scopus 로고    scopus 로고
    • Is allostery an intrinsic property of all dynamic proteins?
    • Gunasekaran K, Ma B, Nussinov R. (2004). Is allostery an intrinsic property of all dynamic proteins? Proteins 57:433-43
    • (2004) Proteins , vol.57 , pp. 433-443
    • Gunasekaran, K.1    Berhow, M.A.2    Nussinov, R.3
  • 22
    • 0347987907 scopus 로고    scopus 로고
    • The ubiquitin- proteasome system in cardiovascular diseases - A hypothesis extended
    • Herrmann J, Ciechanover A, Lerman LO, et al. (2004). The ubiquitin- proteasome system in cardiovascular diseases - a hypothesis extended. Cardiovasc Res 61:11-21
    • (2004) Cardiovasc Res , vol.61 , pp. 11-21
    • Herrmann, J.1    Ciechanover, A.2    Lerman, L.O.3
  • 23
    • 23944523369 scopus 로고    scopus 로고
    • Early work on the ubiquitin proteasome system, an interview with Avram Hershko. Interview by CDD
    • Hershko A. (2005). Early work on the ubiquitin proteasome system, an interview with Avram Hershko. Interview by CDD. Cell Death Differ 12:1158-61
    • (2005) Cell Death Differ , vol.12 , pp. 1158-1161
    • Hershko, A.1
  • 24
    • 0033525582 scopus 로고    scopus 로고
    • Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair
    • Hofmann RM, Pickart CM. (1999). Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. Cell 96:645-53
    • (1999) Cell , vol.96 , pp. 645-653
    • Hofmann, R.M.1    Pickart, C.M.2
  • 25
    • 33846548206 scopus 로고    scopus 로고
    • Basis for a ubiquitinlike protein thioester switch toggling E1-E2 affinity
    • Huang DT, Hunt HW, Zhuang M, et al. (2007). Basis for a ubiquitinlike protein thioester switch toggling E1-E2 affinity. Nature 445:394-8
    • (2007) Nature , vol.445 , pp. 394-398
    • Huang, D.T.1    Hunt, H.W.2    Zhuang, M.3
  • 26
    • 13244249669 scopus 로고    scopus 로고
    • Structural basis for recruitment of Ubc12 by an E2 binding domain in NEDD8's E1
    • Huang DT, Paydar A, Zhuang M, et al. (2005). Structural basis for recruitment of Ubc12 by an E2 binding domain in NEDD8's E1. Mol Cell 17:341-50
    • (2005) Mol Cell , vol.17 , pp. 341-350
    • Huang, D.T.1    Paydar, A.2    Zhuang, M.3
  • 27
    • 70350359679 scopus 로고    scopus 로고
    • CRL4s: The CUL4-RING E3 ubiquitin ligases
    • Jackson S, Xiong Y. (2009). CRL4s: the CUL4-RING E3 ubiquitin ligases. Trends Biochem Sci 34:562-70
    • (2009) Trends Biochem Sci , vol.34 , pp. 562-570
    • Jackson, S.1    Xiong, Y.2
  • 29
    • 79951672720 scopus 로고    scopus 로고
    • Alternative allosteric mechanisms can regulate the substrate and E2 in SUMO conjugation
    • Karaca E, Tozluoglu M, Nussinov R, Haliloglu T. (2011). Alternative allosteric mechanisms can regulate the substrate and E2 in SUMO conjugation. J. Mol Biol 406:620-30
    • (2011) J. Mol Biol , vol.406 , pp. 620-630
    • Karaca, E.1    Tozluoglu, M.2    Nussinov, R.3    Haliloglu, T.4
  • 30
    • 79551666466 scopus 로고    scopus 로고
    • N-terminal domain of human Hsp90 triggers binding to the cochaperone p23
    • Karagoz GE, Duarte AM, Ippel H, et al. (2011). N-terminal domain of human Hsp90 triggers binding to the cochaperone p23. Proc Natl Acad Sci USA 108:580-5
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 580-585
    • Karagoz, G.E.1    Duarte, A.M.2    Ippel, H.3
  • 31
    • 84857497773 scopus 로고    scopus 로고
    • Biased signalling and allosteric machines: New vistas and challenges for drug discovery
    • Kenakin TP. (2012). Biased signalling and allosteric machines: new vistas and challenges for drug discovery. Brit J Pharmacol 165:1659-69
    • (2012) Brit J Pharmacol , vol.165 , pp. 1659-1669
    • Kenakin, T.P.1
  • 32
    • 14044259999 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in HIV replication: Potential targets for antiretroviral therapy
    • Klinger PP, Schubert U. (2005). The ubiquitin-proteasome system in HIV replication: potential targets for antiretroviral therapy. Expert Rev Anti-infective Therapy 3:61-79
    • (2005) Expert Rev Anti-infective Therapy , vol.3 , pp. 61-79
    • Klinger, P.P.1    Schubert, U.2
  • 33
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: Structure and function of the deubiquitinases
    • Komander D, Clague MJ, Urbe S. (2009). Breaking the chains: structure and function of the deubiquitinases. Nat Rev Mol Cell Biol 10:550-63
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbe, S.3
  • 34
    • 0033970020 scopus 로고    scopus 로고
    • Folding and binding cascades: Dynamic landscapes and population shifts
    • Kumar S, Ma B, Tsai, CJ, et al. (2000). Folding and binding cascades: dynamic landscapes and population shifts. Protein Sci: Publ Protein Soc 9:10-19
    • (2000) Protein Sci: Publ Protein Soc , vol.9 , pp. 10-19
    • Kumar, S.1    Berhow, M.A.2    Tsai, C.J.3
  • 35
    • 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 AD, et al. (2007). 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 282:4102-12
    • (2007) J Biol Chem , vol.282 , pp. 4102-4112
    • Lamothe, B.1    Besse, A.2    Campos, A.D.3
  • 36
    • 84856976866 scopus 로고    scopus 로고
    • Complete subunit architecture of the proteasome regulatory particle
    • Lander GC, Estrin E, Matyskiela ME, et al. (2012). Complete subunit architecture of the proteasome regulatory particle. Nature 482:186- 91
    • (2012) Nature , vol.482 , pp. 186-191
    • Lander, G.C.1    Estrin, E.2    Matyskiela, M.E.3
  • 37
    • 84857134729 scopus 로고    scopus 로고
    • Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach
    • Lasker K, Forster F, Bohn S, et al. (2012). Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach. Proc Natl Acad Sci USA 109:380-7
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 380-387
    • Lasker, K.1    Forster, F.2    Bohn, S.3
  • 38
  • 39
    • 0033970878 scopus 로고    scopus 로고
    • PR39, a peptide regulator of angiogenesis
    • Li J, Post M, Volk R, et al. (2000). PR39, a peptide regulator of angiogenesis. Nat Med 6:49-55
    • (2000) Nat Med , vol.6 , pp. 49-55
    • Li, J.1    Post, M.2    Volk, R.3
  • 40
    • 62649096662 scopus 로고    scopus 로고
    • Mechanistic insights into active siteassociated polyubiquitination by the ubiquitin-conjugating enzyme Ube2g2
    • Li W, Tu D, Li L, et al. (2009). Mechanistic insights into active siteassociated polyubiquitination by the ubiquitin-conjugating enzyme Ube2g2. Proc Natl Acad Sci USA 106:3722-7
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 3722-3727
    • Li, W.1    Tu, D.2    Li, L.3
  • 41
    • 38949190032 scopus 로고    scopus 로고
    • Allosteric effects in the marginally stable von Hippel-Lindau tumor suppressor protein and allostery-based rescue mutant design
    • Liu J, Nussinov R. (2008). Allosteric effects in the marginally stable von Hippel-Lindau tumor suppressor protein and allostery-based rescue mutant design. Proc Natl Acad Sci USA 105:901-6
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 901-906
    • Liu, J.1    Nussinov, R.2
  • 42
    • 73549086113 scopus 로고    scopus 로고
    • The mechanism of ubiquitination in the cullin-RING E3 ligase machinery: Conformational control of substrate orientation
    • Liu J, Nussinov R. (2009). The mechanism of ubiquitination in the cullin-RING E3 ligase machinery: conformational control of substrate orientation. PLoS Comput Biol 5:e1000527
    • (2009) PLoS Comput Biol , vol.5
    • Liu, J.1    Nussinov, R.2
  • 43
    • 77649272268 scopus 로고    scopus 로고
    • Molecular dynamics reveal the essential role of linker motions in the function of cullin-RING E3 ligases
    • Liu J, Nussinov R. (2010a). Molecular dynamics reveal the essential role of linker motions in the function of cullin-RING E3 ligases. J Mol Biol 396:1508-23
    • (2010) J Mol Biol , vol.396 , pp. 1508-1523
    • Liu, J.1    Nussinov, R.2
  • 44
    • 77955682724 scopus 로고    scopus 로고
    • Rbx1 flexible linker facilitates cullin-RING ligase function before neddylation and after deneddylation
    • Liu J, Nussinov R. (2010b). Rbx1 flexible linker facilitates cullin-RING ligase function before neddylation and after deneddylation. Biophys J 99:736-44
    • (2010) Biophys J , vol.99 , pp. 736-744
    • Liu, J.1    Nussinov, R.2
  • 45
    • 81755171430 scopus 로고    scopus 로고
    • Flexible cullins in cullin-RING E3 ligases allosterically regulate ubiquitination
    • Liu J, Nussinov R. (2011). Flexible cullins in cullin-RING E3 ligases allosterically regulate ubiquitination. J Biol Chem 286:40934-42
    • (2011) J Biol Chem , vol.286 , pp. 40934-40942
    • Liu, J.1    Nussinov, R.2
  • 47
    • 0032824805 scopus 로고    scopus 로고
    • Folding funnels and binding mechanisms
    • Ma B, Kumar S, Tsai CJ, et al. (1999). Folding funnels and binding mechanisms. Protein Eng 12:713-20
    • (1999) Protein Eng , vol.12 , pp. 713-720
    • Berhow, M.A.1    Kumar, S.2    Tsai, C.J.3
  • 48
    • 79960189344 scopus 로고    scopus 로고
    • Dynamic allostery: Linkers are not merely flexible
    • Ma B, Tsai CJ, Haliloglu T, et al. (2011). Dynamic allostery: linkers are not merely flexible. Structure 19:907-17
    • (2011) Structure , vol.19 , pp. 907-917
    • Berhow, M.A.1    Tsai, C.J.2    Haliloglu, T.3
  • 49
    • 23044506681 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and its role in cancer
    • Mani A, Gelmann EP. (2005). The ubiquitin-proteasome pathway and its role in cancer. J Clin Oncol: OJ Amer Soc Clin Oncol 23:4776-89
    • (2005) J Clin Oncol: OJ Amer Soc Clin Oncol , vol.23 , pp. 4776-4789
    • Mani, A.1    Gelmann, E.P.2
  • 50
    • 62549083952 scopus 로고    scopus 로고
    • Clioquinol inhibits the proteasome and displays preclinical activity in leukemia and myeloma
    • Mao X, Li X, Sprangers R, et al. (2009). Clioquinol inhibits the proteasome and displays preclinical activity in leukemia and myeloma. Leukemia: OJ Leukemia Soc Amer Leukemia Res Fund UK 23:585-90
    • (2009) Leukemia: OJ Leukemia Soc Amer Leukemia Res Fund UK , vol.23 , pp. 585-590
    • Mao, X.1    Li, X.2    Sprangers, R.3
  • 51
    • 33745674468 scopus 로고    scopus 로고
    • Drug discovery in the ubiquitin- proteasome system
    • Nalepa G, Rolfe M, Harper JW. (2006). Drug discovery in the ubiquitin- proteasome system. Nat Rev Drug Discov 5:596-613
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 596-613
    • Nalepa, G.1    Rolfe, M.2    Harper, J.W.3
  • 52
    • 81755184126 scopus 로고    scopus 로고
    • Allo-network drugs: Harnessing allostery in cellular networks
    • Nussinov R, Tsai CJ, Csermely P. (2011). Allo-network drugs: harnessing allostery in cellular networks. Trends Pharmacol Sci 32:686-93
    • (2011) Trends Pharmacol Sci , vol.32 , pp. 686-693
    • Nussinov, R.1    Tsai, C.J.2    Csermely, P.3
  • 53
    • 84866597525 scopus 로고    scopus 로고
    • Allosteric post-translational modification codes
    • Nussinov R, Tsai CJ, Xin F, et al. (2012). Allosteric post-translational modification codes. Trends Biochem Sci 37:447-55
    • (2012) Trends Biochem Sci , vol.37 , pp. 447-455
    • Nussinov, R.1    Tsai, C.J.2    Xin, F.3
  • 54
    • 23044505285 scopus 로고    scopus 로고
    • Regulation of Smurf2 ubiquitin ligase activity by anchoring the E2 to the HECT domain
    • Ogunjimi AA, Briant DJ, Pece-Barbara N, et al. (2005). Regulation of Smurf2 ubiquitin ligase activity by anchoring the E2 to the HECT domain. Mol Cell 19:297-308
    • (2005) Mol Cell , vol.19 , pp. 297-308
    • Ogunjimi, A.A.1    Briant, D.J.2    Pece-Barbara, N.3
  • 55
    • 77954513389 scopus 로고    scopus 로고
    • An allosteric inhibitor of substrate recognition by the SCF(Cdc4) ubiquitin ligase
    • Orlicky S, Tang X, Neduva V, et al. (2010). An allosteric inhibitor of substrate recognition by the SCF(Cdc4) ubiquitin ligase. Nat Biotechnol 28:733-7
    • (2010) Nat Biotechnol , vol.28 , pp. 733-737
    • Orlicky, S.1    Tang, X.2    Neduva, V.3
  • 56
    • 30044437590 scopus 로고    scopus 로고
    • Mechanistic insight into the allosteric activation of a ubiquitin-conjugating enzyme by RING-type ubiquitin ligases
    • Ozkan E, Yu H, Deisenhofer J. (2005). Mechanistic insight into the allosteric activation of a ubiquitin-conjugating enzyme by RING-type ubiquitin ligases. Proc Natl Acad Sci USA 102:18890-5
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 18890-18895
    • Ozkan, E.1    Yu, H.2    Deisenhofer, J.3
  • 57
    • 75149141847 scopus 로고    scopus 로고
    • Mechanisms of transcription factor selectivity
    • Pan Y, Tsai CJ, Ma B, et al. (2010). Mechanisms of transcription factor selectivity. Trends Genet 26:75-83
    • (2010) Trends Genet , vol.26 , pp. 75-83
    • Pan, Y.1    Tsai, C.J.2    Berhow, M.A.3
  • 58
    • 84864021794 scopus 로고    scopus 로고
    • Loop 7 of e2 enzymes: An ancestral conserved functional motif involved in the e2-mediated steps of the ubiquitination cascade
    • Papaleo E, Casiraghi N, Arrigoni A, et al. (2012). Loop 7 of e2 enzymes: an ancestral conserved functional motif involved in the e2-mediated steps of the ubiquitination cascade. PloS One 7:e40786
    • (2012) PloS One , vol.7
    • Papaleo, E.1    Casiraghi, N.2    Arrigoni, A.3
  • 59
    • 79958155322 scopus 로고    scopus 로고
    • An acidic loop and cognate phosphorylation sites define a molecular switch that modulates ubiquitin charging activity in Cdc34-like enzymes
    • Papaleo E, Ranzani V, Tripodi F, et al. (2011). An acidic loop and cognate phosphorylation sites define a molecular switch that modulates ubiquitin charging activity in Cdc34-like enzymes. PLoS Comput Biol 7:e1002056
    • (2011) PLoS Comput Biol , vol.7
    • Papaleo, E.1    Ranzani, V.2    Tripodi, F.3
  • 60
    • 84856023509 scopus 로고    scopus 로고
    • The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcomplexes together
    • Pathare GR, Nagy I, Bohn S, et al. (2012). The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcomplexes together. Proc Natl Acad Sci USA 109:149-54
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 149-154
    • Pathare, G.R.1    Nagy, I.2    Bohn, S.3
  • 61
    • 58149159907 scopus 로고    scopus 로고
    • Dysfunction of the ubiquitin-proteasome system in multiple disease conditions: Therapeutic approaches
    • Paul S. (2008). Dysfunction of the ubiquitin-proteasome system in multiple disease conditions: therapeutic approaches. BioEssays: News Rev Mol Cellular Dev Biol 30:1172-84
    • (2008) BioEssays: News Rev Mol Cellular Dev Biol , vol.30 , pp. 1172-1184
    • Paul, S.1
  • 62
    • 0034253590 scopus 로고    scopus 로고
    • Ubiquitin biology: An old dog learns an old trick
    • Pickart CM. (2000). Ubiquitin biology: an old dog learns an old trick. Nat Cell Biol i2:E139-41
    • (2000) Nat Cell Biol i2
    • Pickart, C.M.1
  • 63
    • 84866858702 scopus 로고    scopus 로고
    • Structure of an E3:E2 approximately Ub complex reveals an allosteric mechanism shared among RING/U-box ligases
    • Pruneda JN, Littlefield PJ, Soss SE, et al. (2012). Structure of an E3:E2 approximately Ub complex reveals an allosteric mechanism shared among RING/U-box ligases. Mol Cell 47:933-42
    • (2012) Mol Cell , vol.47 , pp. 933-942
    • Pruneda, J.N.1    Littlefield, P.J.2    Soss, S.E.3
  • 64
    • 20444384040 scopus 로고    scopus 로고
    • Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex
    • Reverter D, Lima CD. (2005). Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex. Nature 435:687-92
    • (2005) Nature , vol.435 , pp. 687-692
    • Reverter, D.1    Lima, C.D.2
  • 65
    • 27144530248 scopus 로고    scopus 로고
    • Towards a proteome-scale map of the human protein-protein interaction network
    • Rual JF,Venkatesan K, HaoT, et al. (2005). Towards a proteome-scale map of the human protein-protein interaction network. Nature 437:1173-8
    • (2005) Nature , vol.437 , pp. 1173-1178
    • Haot, K.1    Venkatesan, K.2
  • 66
    • 79960208716 scopus 로고    scopus 로고
    • Novel proteasome inhibitors to overcome bortezomib resistance
    • Ruschak AM, Slassi M, Kay LE, et al. (2011). Novel proteasome inhibitors to overcome bortezomib resistance. J Natl Cancer Inst 103:1007-17
    • (2011) J Natl Cancer Inst , vol.103 , pp. 1007-1017
    • Ruschak, A.M.1    Slassi, M.2    Kay, L.E.3
  • 67
    • 77952773419 scopus 로고    scopus 로고
    • Allosteric regulation of the ubiquitin:NIK and ubiquitin:TRAF3 E3 ligases by the lymphotoxinbeta receptor
    • Sanjo H, Zajonc DM, Braden R, et al. (2010). Allosteric regulation of the ubiquitin:NIK and ubiquitin:TRAF3 E3 ligases by the lymphotoxinbeta receptor. J Biol Chem 285:17148-55
    • (2010) J Biol Chem , vol.285 , pp. 17148-17155
    • Sanjo, H.1    Zajonc, D.M.2    Braden, R.3
  • 68
    • 67349256160 scopus 로고    scopus 로고
    • Ubiquitin-like protein activation by E1 enzymes: The apex for downstream signalling pathways
    • Schulman BA, Harper JW. (2009). Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways. Nat Rev Mol Cell Biol 10:319-31
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 319-331
    • Schulman, B.A.1    Harper, J.W.2
  • 69
    • 50149089376 scopus 로고    scopus 로고
    • Structural dissection of a gating mechanism preventing misactivation of ubiquitin by NEDD8's E1
    • Souphron J, Waddell MB, Paydar A, et al. (2008). Structural dissection of a gating mechanism preventing misactivation of ubiquitin by NEDD8's E1. Biochemistry 47:8961-9
    • (2008) Biochemistry , vol.47 , pp. 8961-8969
    • Souphron, J.1    Waddell, M.B.2    Paydar, A.3
  • 70
    • 0034616943 scopus 로고    scopus 로고
    • Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain
    • Spence J, Gali RR, Dittmar G, et al. (2000). Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain. Cell 102:67-76
    • (2000) Cell , vol.102 , pp. 67-76
    • Spence, J.1    Gali, R.R.2    Dittmar, G.3
  • 71
    • 46049107832 scopus 로고    scopus 로고
    • TROSY-based NMR evidence for a novel class of 20S proteasome inhibitors
    • Sprangers R, Li X, Mao X, et al. (2008). TROSY-based NMR evidence for a novel class of 20S proteasome inhibitors. Biochemistry 47:6727-34
    • (2008) Biochemistry , vol.47 , pp. 6727-6734
    • Sprangers, R.1    Li, X.2    Mao, X.3
  • 72
    • 11444271001 scopus 로고    scopus 로고
    • Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection
    • Tatham MH, Kim S, Jaffray E, et al. (2005). Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection. Nat Struct Mol Biol 12:67-74
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 67-74
    • Tatham, M.H.1    Kim, S.2    Jaffray, E.3
  • 73
    • 78049422341 scopus 로고    scopus 로고
    • A mechanistic view of the role of E3 in sumoylation
    • Tozluoglu M, Karaca E, Nussinov R, et al. (2010). A mechanistic view of the role of E3 in sumoylation. PLoS Comput Biol 6:e1000913.
    • (2010) PLoS Comput Biol , vol.6
    • Tozluoglu, M.1    Karaca, E.2    Nussinov, R.3
  • 74
    • 79959432848 scopus 로고    scopus 로고
    • Entropy-driven mechanism of an E3 ligase
    • Truong K, Su Y, Song J, Chen Y. (2011). Entropy-driven mechanism of an E3 ligase. Biochemistry 50:5757-66
    • (2011) Biochemistry , vol.50 , pp. 5757-5766
    • Truong, K.1    Su, Y.2    Song, J.3    Chen, Y.4
  • 75
    • 60649109828 scopus 로고    scopus 로고
    • Protein allostery, signal transmission and dynamics: A classification scheme of allosteric mechanisms
    • Tsai CJ, Del Sol A, Nussinov R. (2009). Protein allostery, signal transmission and dynamics: a classification scheme of allosteric mechanisms. Mol Biosyst 5:207-16
    • (2009) Mol Biosyst , vol.5 , pp. 207-216
    • Tsai, C.J.1    Del Sol, A.2    Nussinov, R.3
  • 77
    • 0033621104 scopus 로고    scopus 로고
    • Folding and binding cascades: Shifts in energy landscapes
    • Tsai CJ, Ma B, Nussinov R. (1999b). Folding and binding cascades: shifts in energy landscapes. Proc Natl Acad Sci USA 96:9970-2
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9970-9972
    • Tsai, C.J.1    Berhow, M.A.2    Nussinov, R.3
  • 78
    • 80052751115 scopus 로고    scopus 로고
    • Gene-specific transcription activation via long-range allosteric shape-shifting
    • Tsai CJ, Nussinov R. (2011). Gene-specific transcription activation via long-range allosteric shape-shifting. Biochem J 439:15-25
    • (2011) Biochem J , vol.439 , pp. 15-25
    • Tsai, C.J.1    Nussinov, R.2
  • 79
    • 0034213352 scopus 로고    scopus 로고
    • Peptides accelerate their uptake by activating a ubiquitin-dependent proteolytic pathway
    • Turner GC, Du F, Varshavsky A. (2000). Peptides accelerate their uptake by activating a ubiquitin-dependent proteolytic pathway. Nature 405:579-83
    • (2000) Nature , vol.405 , pp. 579-583
    • Turner, G.C.1    Du, F.2    Varshavsky, A.3
  • 80
    • 0034600851 scopus 로고    scopus 로고
    • Two RING finger proteins mediate cooperation between ubiquitin- conjugating enzymes in DNA repair
    • Ulrich HD, Jentsch S. (2000). Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair. EMBO J 19:3388-97
    • (2000) EMBO J , vol.19 , pp. 3388-3397
    • Ulrich, H.D.1    Jentsch, S.2
  • 81
    • 79960683356 scopus 로고    scopus 로고
    • The N-end rule pathway and regulation by proteolysis
    • Varshavsky A. (2011). The N-end rule pathway and regulation by proteolysis. Protein Sci: Publ Protein Soc 20:1298-1345
    • (2011) Protein Sci: Publ Protein Soc , vol.20 , pp. 1298-1345
    • Varshavsky, A.1
  • 82
    • 34250011799 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system and its role in inflammatory and autoimmune diseases
    • Wang J, Maldonado MA. (2006). The ubiquitin-proteasome system and its role in inflammatory and autoimmune diseases. Cell Mol Immunol 3:255-61
    • (2006) Cell Mol Immunol , vol.3 , pp. 255-261
    • Wang, J.1    Maldonado, M.A.2
  • 83
    • 67649983106 scopus 로고    scopus 로고
    • (G2) Bringing an E2 to E3
    • Wang J, Schulman BA. (2009). (G2)Bringing an E2 to E3. Structure 17:916-7
    • (2009) Structure , vol.17 , pp. 916-917
    • Wang, J.1    Schulman, B.A.2
  • 84
    • 84858135252 scopus 로고    scopus 로고
    • Following Ariadne's thread: A new perspective on RBR ubiquitin ligases
    • Wenzel DM, Klevit RE. (2012). Following Ariadne's thread: a new perspective on RBR ubiquitin ligases. BMC Biol 10:24
    • (2012) BMC Biol , vol.10 , pp. 24
    • Wenzel, D.M.1    Klevit, R.E.2
  • 85
    • 84862806447 scopus 로고    scopus 로고
    • The mechanism of OTUB1- mediated inhibition of ubiquitination
    • Wiener R, Zhang X, Wang T. (2012). The mechanism of OTUB1- mediated inhibition of ubiquitination. Nature 483:618-22
    • (2012) Nature , vol.483 , pp. 618-622
    • Wiener, R.1    Zhang, X.2    Wang, T.3
  • 86
    • 79953213637 scopus 로고    scopus 로고
    • ''Molecular switches'' on mGluR allosteric ligands that modulate modes of pharmacology
    • Wood MR, Hopkins CR, Brogan JT, et al. (2011). ''Molecular switches'' on mGluR allosteric ligands that modulate modes of pharmacology. Biochemistry 50:2403-10
    • (2011) Biochemistry , vol.50 , pp. 2403-2410
    • Wood, M.R.1    Hopkins, C.R.2    Brogan, J.T.3
  • 87
    • 0033485869 scopus 로고    scopus 로고
    • The E2-E3 interaction in the N-end rule pathway: The RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain
    • Xie Y, Varshavsky A. (1999). The E2-E3 interaction in the N-end rule pathway: the RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain. EMBO J 18:6832-44
    • (1999) EMBO J , vol.18 , pp. 6832-6844
    • Xie, Y.1    Varshavsky, A.2
  • 88
    • 58149295169 scopus 로고    scopus 로고
    • Targeting the ubiquitin-proteasome system for cancer therapy
    • Yang Y, Kitagaki J, Wang H, et al. (2009). Targeting the ubiquitin-proteasome system for cancer therapy. Cancer Sci 100:24-8
    • (2009) Cancer Sci , vol.100 , pp. 24-28
    • Yang, Y.1    Kitagaki, J.2    Wang, H.3
  • 89
    • 18344391432 scopus 로고    scopus 로고
    • Structure of the Cul1- Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex
    • Zheng N, Schulman BA, Song L, et al. (2002). Structure of the Cul1- Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. Nature 416:703-9
    • (2002) Nature , vol.416 , pp. 703-709
    • Zheng, N.1    Schulman, B.A.2    Song, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.