메뉴 건너뛰기




Volumn 27, Issue 11, 2005, Pages 1147-1157

TRIM/RBCC, a novel class of 'single protein RING finger' E3 ubiquitin ligases

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN RBCC; PROTEIN TRIM; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 30444452500     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.20304     Document Type: Review
Times cited : (579)

References (106)
  • 1
    • 0035083772 scopus 로고    scopus 로고
    • Two B or not two B? Overview of the rapidly expanding B-box family of proteins
    • Torok M, Etkin LD. 2001. Two B or not two B? Overview of the rapidly expanding B-box family of proteins. Differentiation 67:63-71.
    • (2001) Differentiation , vol.67 , pp. 63-71
    • Torok, M.1    Etkin, L.D.2
  • 2
    • 17744371839 scopus 로고    scopus 로고
    • The tripartite motif family identifies cell compartments
    • Reymond A, Meroni G, Fantozzi A, Merla G, Cairo S, et al. 2001. The tripartite motif family identifies cell compartments. Embo J 20:2140-2151.
    • (2001) Embo J , vol.20 , pp. 2140-2151
    • Reymond, A.1    Meroni, G.2    Fantozzi, A.3    Merla, G.4    Cairo, S.5
  • 3
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A. 2002. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 82:373-428.
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 4
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • Hicke L, Dunn R. 2003. Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu Rev Cell Dev Biol 19:141-172.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 5
    • 0038362292 scopus 로고    scopus 로고
    • When ubiquitin meets ubiquitin receptors: A signaling connection
    • Di Fiore PP, Polo S, Hofmann K. 2003. When ubiquitin meets ubiquitin receptors: a signaling connection. Nat Rev Mol Cell Biol 4:491-497.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 491-497
    • Di Fiore, P.P.1    Polo, S.2    Hofmann, K.3
  • 6
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • Weissman AM. 2001. Themes and variations on ubiquitylation. Nat Rev Mol Cell Biol 2:169-178.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 7
    • 0038434056 scopus 로고    scopus 로고
    • A superfamily of protein tags: Ubiquitin, SUMO and related modifiers
    • Schwartz DC, Hochstrasser M. 2003. A superfamily of protein tags: ubiquitin, SUMO and related modifiers. Trends Biochem Sci 28:321-328.
    • (2003) Trends Biochem Sci , vol.28 , pp. 321-328
    • Schwartz, D.C.1    Hochstrasser, M.2
  • 8
    • 0027239790 scopus 로고
    • The RING finger. A novel protein sequence motif related to the zinc finger
    • Freemont PS. 1993. The RING finger. A novel protein sequence motif related to the zinc finger. Ann N Y Acad Sci 684:174-192.
    • (1993) Ann N Y Acad Sci , vol.684 , pp. 174-192
    • Freemont, P.S.1
  • 9
    • 0028181750 scopus 로고
    • Structure of the C3HC4 domain by 1H-nuclear magnetic resonance spectroscopy. A new structural class of zinc-finger
    • Barlow PN, Luisi B, Milner A, Elliott M, Everett R. 1994. Structure of the C3HC4 domain by 1H-nuclear magnetic resonance spectroscopy. A new structural class of zinc-finger. J Mol Biol 237:201-211.
    • (1994) J Mol Biol , vol.237 , pp. 201-211
    • Barlow, P.N.1    Luisi, B.2    Milner, A.3    Elliott, M.4    Everett, R.5
  • 10
    • 0028932963 scopus 로고
    • The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML
    • Borden KL, Boddy MN, Lally J, O'Reilly NJ, Martin S, et al. 1995. The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML. Embo J 14:1532-1541.
    • (1995) Embo J , vol.14 , pp. 1532-1541
    • Borden, K.L.1    Boddy, M.N.2    Lally, J.3    O'Reilly, N.J.4    Martin, S.5
  • 11
    • 0033961923 scopus 로고    scopus 로고
    • RING for destruction?
    • Freemont PS. 2000. RING for destruction? Curr Biol 10:R84-87.
    • (2000) Curr Biol , vol.10
    • Freemont, P.S.1
  • 12
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: Mediators of ubiquitin ligase activity
    • Joazeiro CA, Weissman AM. 2000. RING finger proteins: mediators of ubiquitin ligase activity. Cell 102:549-552.
    • (2000) Cell , vol.102 , pp. 549-552
    • Joazeiro, C.A.1    Weissman, A.M.2
  • 13
    • 0027422113 scopus 로고
    • Characterisation of a novel cysteine/histidine-rich metal binding domain from Xenopus nuclear factor XNF7
    • Borden KL, Martin SR, O'Reilly NJ, Lally JM, Reddy BA, et al. 1993. Characterisation of a novel cysteine/histidine-rich metal binding domain from Xenopus nuclear factor XNF7. FEBS Lett 335:255-260.
    • (1993) FEBS Lett , vol.335 , pp. 255-260
    • Borden, K.L.1    Martin, S.R.2    O'Reilly, N.J.3    Lally, J.M.4    Reddy, B.A.5
  • 14
    • 0028844506 scopus 로고
    • Novel topology of a zinc-binding domain from a protein involved in regulating early Xenopus development
    • Borden KL, Lally JM, Martin SR, O'Reilly NJ, Etkin LD, et al. 1995. Novel topology of a zinc-binding domain from a protein involved in regulating early Xenopus development. Embo J 14:5947-5956.
    • (1995) Embo J , vol.14 , pp. 5947-5956
    • Borden, K.L.1    Lally, J.M.2    Martin, S.R.3    O'Reilly, N.J.4    Etkin, L.D.5
  • 15
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • Lupas A. 1996. Coiled coils: new structures and new functions. Trends in Biochemical Sciences 21:375-382.
    • (1996) Trends in Biochemical Sciences , vol.21 , pp. 375-382
    • Lupas, A.1
  • 16
    • 0031773260 scopus 로고    scopus 로고
    • B30.2-like domain proteins: Update and new insights into a rapidly expanding family of proteins
    • Henry J, Mather IH, McDermott MF, Pontarotti P. 1998. B30.2-like domain proteins: update and new insights into a rapidly expanding family of proteins. Mol Biol Evol 15:1696-1705.
    • (1998) Mol Biol Evol , vol.15 , pp. 1696-1705
    • Henry, J.1    Mather, I.H.2    McDermott, M.F.3    Pontarotti, P.4
  • 17
    • 0032410209 scopus 로고    scopus 로고
    • A novel repeat domain that is often associated with RING finger and B- box motifs
    • Slack FJ, Ruvkun G. 1998. A novel repeat domain that is often associated with RING finger and B- box motifs. Trends Biochem Sci 23:474-475.
    • (1998) Trends Biochem Sci , vol.23 , pp. 474-475
    • Slack, F.J.1    Ruvkun, G.2
  • 18
    • 0036311183 scopus 로고    scopus 로고
    • Hetero-oligomerization among the TIF family of RBCC/TRIM domain-containing nuclear cofactors: A potential mechanism for regulating the switch between coactivation and corepression
    • Peng H, Feldman I, Rauscher FJ 3rd. 2002. Hetero-oligomerization among the TIF family of RBCC/TRIM domain-containing nuclear cofactors: a potential mechanism for regulating the switch between coactivation and corepression. J Mol Biol 320:629-644.
    • (2002) J Mol Biol , vol.320 , pp. 629-644
    • Peng, H.1    Feldman, I.2    Rauscher III, F.J.3
  • 19
    • 0037216934 scopus 로고    scopus 로고
    • Cluster of TRIM genes in the human MHC class I region sharing the B30.2 domain
    • Meyer M, Gaudieri S, Rhodes DA, Trowsdale J. 2003. Cluster of TRIM genes in the human MHC class I region sharing the B30.2 domain. Tissue Antigens 61:63-71.
    • (2003) Tissue Antigens , vol.61 , pp. 63-71
    • Meyer, M.1    Gaudieri, S.2    Rhodes, D.3    Trowsdale, J.4
  • 20
    • 0034308251 scopus 로고    scopus 로고
    • The lore of the RINGs: Substrate recognition and catalysis by ubiquitin ligases
    • Jackson PK, Eldridge AG, Freed E, Furstenthal L, Hsu JY, et al. 2000. The lore of the RINGs: substrate recognition and catalysis by ubiquitin ligases. Trends Cell Biol 10:429-439.
    • (2000) Trends Cell Biol , vol.10 , pp. 429-439
    • Jackson, P.K.1    Eldridge, A.G.2    Freed, E.3    Furstenthal, L.4    Hsu, J.Y.5
  • 21
    • 9744227183 scopus 로고    scopus 로고
    • Ubiquitin: Structures, functions, mechanisms
    • Pickart CM, Eddins MJ. 2004. Ubiquitin: structures, functions, mechanisms. Biochim Biophys Acta 1695:55-72.
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 55-72
    • Pickart, C.M.1    Eddins, M.J.2
  • 22
    • 0037142070 scopus 로고    scopus 로고
    • Efp targets 14-3-3 sigma for proteolysis and promotes breast tumour growth
    • Urano T, Saito T, Tsukui T, Fujita M, Hosoi T, et al. 2002. Efp targets 14-3-3 sigma for proteolysis and promotes breast tumour growth. Nature 417:871-875.
    • (2002) Nature , vol.417 , pp. 871-875
    • Urano, T.1    Saito, T.2    Tsukui, T.3    Fujita, M.4    Hosoi, T.5
  • 23
    • 0035184651 scopus 로고    scopus 로고
    • MID1, mutated in Opitz syndrome, encodes an ubiquitin ligase that targets phosphatase 2A for degradation
    • Trockenbacher A, Suckow V, Foerster J, Winter J, Krauss S, et al. 2001. MID1, mutated in Opitz syndrome, encodes an ubiquitin ligase that targets phosphatase 2A for degradation. Nat Genet 29:287-294.
    • (2001) Nat Genet , vol.29 , pp. 287-294
    • Trockenbacher, A.1    Suckow, V.2    Foerster, J.3    Winter, J.4    Krauss, S.5
  • 24
    • 0035811068 scopus 로고    scopus 로고
    • Phosphorylation and microtubule association of the Opitz syndrome protein mid-1 is regulated by protein phosphatase 2A via binding to the regulatory subunit alpha 4
    • Liu J, Prickett TD, Elliott E, Meroni G, Brautigan DL. 2001. Phosphorylation and microtubule association of the Opitz syndrome protein mid-1 is regulated by protein phosphatase 2A via binding to the regulatory subunit alpha 4. Proc Natl Acad Sci USA 98:6650-6655.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6650-6655
    • Liu, J.1    Prickett, T.D.2    Elliott, E.3    Meroni, G.4    Brautigan, D.L.5
  • 25
    • 17044365440 scopus 로고    scopus 로고
    • Germ-layer specification and control of cell growth by Ectodermin, a Smad4 ubiquitin ligase
    • Dupont S, Zacchigna L, Cordenonsi M, Soligo S, Adorno M, et al. 2005. Germ-layer specification and control of cell growth by Ectodermin, a Smad4 ubiquitin ligase. Cell 121:87-99.
    • (2005) Cell , vol.121 , pp. 87-99
    • Dupont, S.1    Zacchigna, L.2    Cordenonsi, M.3    Soligo, S.4    Adorno, M.5
  • 26
    • 0037020175 scopus 로고    scopus 로고
    • TRIM8/GERP RING finger protein interacts with SOCS-1
    • Toniato E, Chen XP, Losman J, Flati V, Donahue L, et al. 2002. TRIM8/GERP RING finger protein interacts with SOCS-1. J Biol Chem 277:37315-37322.
    • (2002) J Biol Chem , vol.277 , pp. 37315-37322
    • Toniato, E.1    Chen, X.P.2    Losman, J.3    Flati, V.4    Donahue, L.5
  • 27
    • 0037363692 scopus 로고    scopus 로고
    • A tripartite motif protein TRIM11 binds and destabilizes Humanin, a neuroprotective peptide against Alzheimer's disease-relevant insults
    • Niikura T, Hashimoto Y, Tajima H, Ishizaka M, Yamagishi Y, et al. 2003. A tripartite motif protein TRIM11 binds and destabilizes Humanin, a neuroprotective peptide against Alzheimer's disease-relevant insults. Eur J Neurosci 17:1150-1158.
    • (2003) Eur J Neurosci , vol.17 , pp. 1150-1158
    • Niikura, T.1    Hashimoto, Y.2    Tajima, H.3    Ishizaka, M.4    Yamagishi, Y.5
  • 28
    • 0036544533 scopus 로고    scopus 로고
    • Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1
    • McElhinny AS, Kakinuma K, Sorimachi H, Labeit S, Gregorio CC. 2002. Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1. J Cell Biol 157:125-136.
    • (2002) J Cell Biol , vol.157 , pp. 125-136
    • McElhinny, A.S.1    Kakinuma, K.2    Sorimachi, H.3    Labeit, S.4    Gregorio, C.C.5
  • 29
    • 0035941020 scopus 로고    scopus 로고
    • Identification of ubiquitin ligases required for skeletal muscle atrophy
    • Bodine SC, Latres E, Baumhueter S, Lai VK, Nunez L, et al. 2001. Identification of ubiquitin ligases required for skeletal muscle atrophy. Science 294:1704-1708.
    • (2001) Science , vol.294 , pp. 1704-1708
    • Bodine, S.C.1    Latres, E.2    Baumhueter, S.3    Lai, V.K.4    Nunez, L.5
  • 30
    • 0038148965 scopus 로고    scopus 로고
    • BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta
    • Xu L, Yang L, Moitra PK, Hashimoto K, Rallabhandi P, et al. 2003. BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta. Exp Cell Res 288:84-93.
    • (2003) Exp Cell Res , vol.288 , pp. 84-93
    • Xu, L.1    Yang, L.2    Moitra, P.K.3    Hashimoto, K.4    Rallabhandi, P.5
  • 31
    • 0036453682 scopus 로고    scopus 로고
    • RING finger, B-box, and coiled-coil (RBCC) protein expression in branchial epithelial cells of Japanese eel, Anguilla japonica
    • Miyamoto K, Nakamura N, Kashiwagi M, Honda S, Kato A, et al. 2002. RING finger, B-box, and coiled-coil (RBCC) protein expression in branchial epithelial cells of Japanese eel, Anguilla japonica. Eur J Biochem 269:6152-6161.
    • (2002) Eur J Biochem , vol.269 , pp. 6152-6161
    • Miyamoto, K.1    Nakamura, N.2    Kashiwagi, M.3    Honda, S.4    Kato, A.5
  • 32
    • 10744221161 scopus 로고    scopus 로고
    • RING protein Trim32 associated with skin carcinogenesis has anti-apoptotic and E3-ubiquitin ligase properties
    • Horn EJ, Albor A, Liu Y, El-Hizawi S, Vanderbeek GE, et al. 2004. RING protein Trim32 associated with skin carcinogenesis has anti-apoptotic and E3-ubiquitin ligase properties. Carcinogenesis 25:157-167.
    • (2004) Carcinogenesis , vol.25 , pp. 157-167
    • Horn, E.J.1    Albor, A.2    Liu, Y.3    El-Hizawi, S.4    Vanderbeek, G.E.5
  • 33
    • 0033613222 scopus 로고    scopus 로고
    • RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination
    • Lorick KL, Jensen JP, Fang S, Ong AM, Hatakeyama S, et al. 1999. RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination. Proc Natl Acad Sci USA 96:11364-11369.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11364-11369
    • Lorick, K.L.1    Jensen, J.P.2    Fang, S.3    Ong, A.M.4    Hatakeyama, S.5
  • 34
    • 0034682718 scopus 로고    scopus 로고
    • Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases
    • Zheng N, Wang P, Jeffrey PD, Pavletich NP. 2000. Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell 102:533-539.
    • (2000) Cell , vol.102 , pp. 533-539
    • Zheng, N.1    Wang, P.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 35
    • 0034602922 scopus 로고    scopus 로고
    • Reconstitution of the KRAB-KAP-1 repressor complex: A model system for defining the molecular anatomy of RING-B box-coiled-coil domain-mediated protein-protein interactions
    • Peng H, Begg GE, Schultz DC, Friedman JR, Jensen DE, et al. 2000. Reconstitution of the KRAB-KAP-1 repressor complex: a model system for defining the molecular anatomy of RING-B box-coiled-coil domain-mediated protein-protein interactions. J Mol Biol 295:1139-1162.
    • (2000) J Mol Biol , vol.295 , pp. 1139-1162
    • Peng, H.1    Begg, G.E.2    Schultz, D.C.3    Friedman, J.R.4    Jensen, D.E.5
  • 36
    • 7344248065 scopus 로고    scopus 로고
    • Cooperation between the RING + B1-B2 and coiled-coil domains of PML is necessary for its effects on cell survival
    • Fagioli M, Alcalay M, Tomassoni L, Ferrucci PF, Mencarelli A, et al. 1998. Cooperation between the RING + B1-B2 and coiled-coil domains of PML is necessary for its effects on cell survival. Oncogene 16:2905-2913.
    • (1998) Oncogene , vol.16 , pp. 2905-2913
    • Fagioli, M.1    Alcalay, M.2    Tomassoni, L.3    Ferrucci, P.F.4    Mencarelli, A.5
  • 37
    • 0043092246 scopus 로고    scopus 로고
    • Cloning and characterization of a novel RING-B-box-coiled-coil protein with apoptotic function
    • Kimura F, Suzu S, Nakamura Y, Nakata Y, Yamada M, et al. 2003. Cloning and characterization of a novel RING-B-box-coiled-coil protein with apoptotic function. J Biol Chem 278:25046-25054.
    • (2003) J Biol Chem , vol.278 , pp. 25046-25054
    • Kimura, F.1    Suzu, S.2    Nakamura, Y.3    Nakata, Y.4    Yamada, M.5
  • 38
    • 0030751654 scopus 로고    scopus 로고
    • Involvement of the rfp tripartite motif in protein-protein interactions and subcellular distribution
    • Cao T, Borden KL, Freemont PS, Etkin LD. 1997. Involvement of the rfp tripartite motif in protein-protein interactions and subcellular distribution. J Cell Sci 110:1563-1571.
    • (1997) J Cell Sci , vol.110 , pp. 1563-1571
    • Cao, T.1    Borden, K.L.2    Freemont, P.S.3    Etkin, L.D.4
  • 39
    • 0037458011 scopus 로고    scopus 로고
    • RFPL4 interacts with oocyte proteins of the ubiquitin-proteasome degradation pathway
    • Suzumori N, Burns KH, Yan W, Matzuk MM. 2003. RFPL4 interacts with oocyte proteins of the ubiquitin-proteasome degradation pathway. Proc Natl Acad Sci USA 100:550-555.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 550-555
    • Suzumori, N.1    Burns, K.H.2    Yan, W.3    Matzuk, M.M.4
  • 40
    • 0036279167 scopus 로고    scopus 로고
    • The PHD domain of MEKK1 acts as an E3 ubiquitin ligase and mediates ubiquitination and degradation of ERK1/2
    • Lu Z, Xu S, Joazeiro C, Cobb MH, Hunter T. 2002. The PHD domain of MEKK1 acts as an E3 ubiquitin ligase and mediates ubiquitination and degradation of ERK1/2. Mol Cell 9:945-956.
    • (2002) Mol Cell , vol.9 , pp. 945-956
    • Lu, Z.1    Xu, S.2    Joazeiro, C.3    Cobb, M.H.4    Hunter, T.5
  • 41
    • 0032231606 scopus 로고    scopus 로고
    • Structure, organization, and dynamics of promyelocytic leukemia protein nuclear bodies
    • Hodges M, Tissot C, Howe K, Grimwade D, Freemont PS. 1998. Structure, organization, and dynamics of promyelocytic leukemia protein nuclear bodies. Am J Hum Genet 63:297-304.
    • (1998) Am J Hum Genet , vol.63 , pp. 297-304
    • Hodges, M.1    Tissot, C.2    Howe, K.3    Grimwade, D.4    Freemont, P.S.5
  • 42
    • 0031800796 scopus 로고    scopus 로고
    • Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML
    • Cao T, Duprez E, Borden KL, Freemont PS, Etkin LD. 1998. Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML. J Cell Sci 111:1319-1329.
    • (1998) J Cell Sci , vol.111 , pp. 1319-1329
    • Cao, T.1    Duprez, E.2    Borden, K.L.3    Freemont, P.S.4    Etkin, L.D.5
  • 43
    • 2342654045 scopus 로고    scopus 로고
    • MID1 and MID2 homo- and heterodimerise to tether the rapamycin- sensitive PP2A regulatory subunit, Alpha 4, to microtubules: Implications for the clinical variability of X-linked Opitz GBBB syndrome and other developmental disorders
    • Short KM, Hopwood B, Yi Z, Cox TC. 2002. MID1 and MID2 homo- and heterodimerise to tether the rapamycin- sensitive PP2A regulatory subunit, Alpha 4, to microtubules: implications for the clinical variability of X-linked Opitz GBBB syndrome and other developmental disorders. BMC Cell Biol 3:1.
    • (2002) BMC Cell Biol , vol.3 , pp. 1
    • Short, K.M.1    Hopwood, B.2    Yi, Z.3    Cox, T.C.4
  • 44
    • 0032721510 scopus 로고    scopus 로고
    • A RA-dependent, tumour-growth suppressive transcription complex is the target of the PML-RARalpha and T18 oncoproteins
    • Zhong S, Delva L, Rachez C, Cenciarelli C, Gandini D, et al. 1999. A RA-dependent, tumour-growth suppressive transcription complex is the target of the PML-RARalpha and T18 oncoproteins. Nat Genet 23:287-295.
    • (1999) Nat Genet , vol.23 , pp. 287-295
    • Zhong, S.1    Delva, L.2    Rachez, C.3    Cenciarelli, C.4    Gandini, D.5
  • 45
    • 1242272073 scopus 로고    scopus 로고
    • The coiled-coil domain is the structural determinant for mammalian homologues of Drosophila Sina-mediated degradation of promyelocytic leukemia protein and other tripartite motif proteins by the proteasome
    • Fanelli M, Fantozzi A, De Luca P, Caprodossi S, Matsuzawa S, et al. 2004. The coiled-coil domain is the structural determinant for mammalian homologues of Drosophila Sina-mediated degradation of promyelocytic leukemia protein and other tripartite motif proteins by the proteasome. J Biol Chem 279:5374-5379.
    • (2004) J Biol Chem , vol.279 , pp. 5374-5379
    • Fanelli, M.1    Fantozzi, A.2    De Luca, P.3    Caprodossi, S.4    Matsuzawa, S.5
  • 46
    • 0037376172 scopus 로고    scopus 로고
    • Ubiquitin: Not just for proteasomes anymore
    • Aguilar RC, Wendland B. 2003. Ubiquitin: not just for proteasomes anymore. Curr Opin Cell Biol 15:184-190.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 184-190
    • Aguilar, R.C.1    Wendland, B.2
  • 47
    • 4444301185 scopus 로고    scopus 로고
    • SUMO and ubiquitin in the nucleus: Different functions, similar mechanisms?
    • Gill G. 2004. SUMO and ubiquitin in the nucleus: different functions, similar mechanisms? Genes Dev 18:2046-2059.
    • (2004) Genes Dev , vol.18 , pp. 2046-2059
    • Gill, G.1
  • 48
    • 0035969125 scopus 로고    scopus 로고
    • PML protein isoforms and the RBCC/TRIM motif
    • Jensen K, Shiels C, Freemont PS. 2001. PML protein isoforms and the RBCC/TRIM motif. Oncogene 20:7223-7233.
    • (2001) Oncogene , vol.20 , pp. 7223-7233
    • Jensen, K.1    Shiels, C.2    Freemont, P.S.3
  • 49
    • 0035969104 scopus 로고    scopus 로고
    • PML interaction with p53 and its role in apoptosis and replicative senescence
    • Pearson M, Pelicci PG. 2001. PML interaction with p53 and its role in apoptosis and replicative senescence. Oncogene 20:7250-7256.
    • (2001) Oncogene , vol.20 , pp. 7250-7256
    • Pearson, M.1    Pelicci, P.G.2
  • 50
    • 0035969102 scopus 로고    scopus 로고
    • SUMO: Of branched proteins and nuclear bodies
    • Seeler JS, Dejean A. 2001. SUMO: of branched proteins and nuclear bodies. Oncogene 20:7243-7249.
    • (2001) Oncogene , vol.20 , pp. 7243-7249
    • Seeler, J.S.1    Dejean, A.2
  • 51
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: A history of modification
    • Hay RT. 2005. SUMO: a history of modification. Mol Cell 18:1-12.
    • (2005) Mol Cell , vol.18 , pp. 1-12
    • Hay, R.T.1
  • 53
    • 0033034749 scopus 로고    scopus 로고
    • SUMO-1 modification of the acute promyelocytic leukaemia protein PML: Implications for nuclear localisation
    • Duprez E, Saurin AJ, Desterro JM, Lallemand-Breitenbach V, Howe K, et al. 1999. SUMO-1 modification of the acute promyelocytic leukaemia protein PML: implications for nuclear localisation. J Cell Sci 112:381-393.
    • (1999) J Cell Sci , vol.112 , pp. 381-393
    • Duprez, E.1    Saurin, A.J.2    Desterro, J.M.3    Lallemand-Breitenbach, V.4    Howe, K.5
  • 54
    • 0029736651 scopus 로고    scopus 로고
    • PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia
    • Boddy MN, Howe K, Etkin LD, Solomon E, Freemont PS. 1996. PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia. Oncogene 13:971-982.
    • (1996) Oncogene , vol.13 , pp. 971-982
    • Boddy, M.N.1    Howe, K.2    Etkin, L.D.3    Solomon, E.4    Freemont, P.S.5
  • 55
    • 0032721540 scopus 로고    scopus 로고
    • PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1
    • Ishov AM, Sotnikov AG, Negorev D, Vladimirova OV, Neff N, et al. 1999. PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1. J Cell Biol 147:221-234.
    • (1999) J Cell Biol , vol.147 , pp. 221-234
    • Ishov, A.M.1    Sotnikov, A.G.2    Negorev, D.3    Vladimirova, O.V.4    Neff, N.5
  • 56
    • 0033570892 scopus 로고    scopus 로고
    • Activation of p53 by conjugation to the ubiquitin-like protein SUMO-1
    • Gostissa M, Hengstermann A, Fogal V, Sandy P, Schwarz SE, et al. 1999. Activation of p53 by conjugation to the ubiquitin-like protein SUMO-1. Embo J 18:6462-6471.
    • (1999) Embo J , vol.18 , pp. 6462-6471
    • Gostissa, M.1    Hengstermann, A.2    Fogal, V.3    Sandy, P.4    Schwarz, S.E.5
  • 57
    • 0035968313 scopus 로고    scopus 로고
    • A novel human striated muscle RING zinc finger protein, SMRZ, interacts with SMTSb via its RING domain
    • Dai KS, Liew CC. 2001. A novel human striated muscle RING zinc finger protein, SMRZ, interacts with SMTSb via its RING domain. J Biol Chem 276:23992-23999.
    • (2001) J Biol Chem , vol.276 , pp. 23992-23999
    • Dai, K.S.1    Liew, C.C.2
  • 58
    • 0037123605 scopus 로고    scopus 로고
    • Emerging roles of ubiquitin in transcription regulation
    • Conaway RC, Brower CS, Conaway JW. 2002. Emerging roles of ubiquitin in transcription regulation. Science 296:1254-1258.
    • (2002) Science , vol.296 , pp. 1254-1258
    • Conaway, R.C.1    Brower, C.S.2    Conaway, J.W.3
  • 59
    • 0029841744 scopus 로고    scopus 로고
    • A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors
    • Le Douarin B, Nielsen AL, Garnier JM, lchinose H, Jeanmougin F, et al. 1996. A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors. Embo J 15:6701-6715.
    • (1996) Embo J , vol.15 , pp. 6701-6715
    • Le Douarin, B.1    Nielsen, A.L.2    Garnier, J.M.3    Lchinose, H.4    Jeanmougin, F.5
  • 60
    • 0034671552 scopus 로고    scopus 로고
    • RET finger protein is a transcriptional represser and interacts with enhancer of polycomb that has dual transcriptional functions
    • Shimono Y, Murakami H, Hasegawa Y, Takahashi M. 2000. RET finger protein is a transcriptional represser and interacts with enhancer of polycomb that has dual transcriptional functions. J Biol Chem 275:39411-39419.
    • (2000) J Biol Chem , vol.275 , pp. 39411-39419
    • Shimono, Y.1    Murakami, H.2    Hasegawa, Y.3    Takahashi, M.4
  • 61
    • 0036235857 scopus 로고    scopus 로고
    • The TRIM37 gene encodes a peroxisomal RING-B-box-coiled-coil protein: Classification of mulibrey nanism as a new peroxisomal disorder
    • Kallijarvi J, Avela K, Lipsanen-Nyman M, Ulmanen I, Lehesjoki AE. 2002. The TRIM37 gene encodes a peroxisomal RING-B-box-coiled-coil protein: classification of mulibrey nanism as a new peroxisomal disorder. Am J Hum Genet 70:1215-12128.
    • (2002) Am J Hum Genet , vol.70 , pp. 1215-12128
    • Kallijarvi, J.1    Avela, K.2    Lipsanen-Nyman, M.3    Ulmanen, I.4    Lehesjoki, A.E.5
  • 62
    • 0032555120 scopus 로고    scopus 로고
    • Localization of ADP-ribosylation factor domain protein 1 (ARD1) in lysosomes and Golgi apparatus
    • Vitale N, Horiba K, Ferrans VJ, Moss J, Vaughan M. 1998. Localization of ADP-ribosylation factor domain protein 1 (ARD1) in lysosomes and Golgi apparatus. Proc Natl Acad Sci USA 95:8613-8618.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 8613-8618
    • Vitale, N.1    Horiba, K.2    Ferrans, V.J.3    Moss, J.4    Vaughan, M.5
  • 63
    • 0035798541 scopus 로고    scopus 로고
    • Spring, a novel RING finger protein that regulates synaptic vesicle exocytosis
    • Li Y, Chin LS, Weigel C, Li L. 2001. Spring, a novel RING finger protein that regulates synaptic vesicle exocytosis. J Biol Chem 276:40824-40833.
    • (2001) J Biol Chem , vol.276 , pp. 40824-40833
    • Li, Y.1    Chin, L.S.2    Weigel, C.3    Li, L.4
  • 64
    • 16944365777 scopus 로고    scopus 로고
    • Opitz G/BBB syndrome, a defect of midline development, is due to mutations in a new RING finger gene on Xp22
    • Quaderi NA, Schweiger S, Gaudenz K, Franco B, Rugarli EI, et al. 1997. Opitz G/BBB syndrome, a defect of midline development, is due to mutations in a new RING finger gene on Xp22. Nature Genetics 17:285-291.
    • (1997) Nature Genetics , vol.17 , pp. 285-291
    • Quaderi, N.A.1    Schweiger, S.2    Gaudenz, K.3    Franco, B.4    Rugarli, E.I.5
  • 65
    • 0032854670 scopus 로고    scopus 로고
    • Functional characterization of the Opitz syndrome gene product (midin): Evidence for homodimerization and association with microtubules throughout the cell cycle
    • Cainarca S, Messali S, Ballabio A, Meroni G. 1999. Functional characterization of the Opitz syndrome gene product (midin): evidence for homodimerization and association with microtubules throughout the cell cycle. Hum Mol Genet 8:1387-1396.
    • (1999) Hum Mol Genet , vol.8 , pp. 1387-1396
    • Cainarca, S.1    Messali, S.2    Ballabio, A.3    Meroni, G.4
  • 67
    • 0034696939 scopus 로고    scopus 로고
    • Efp as a primary estrogen-responsive gene in human breast cancer
    • Ikeda K, Orimo A, Higashi Y, Muramatsu M, lnoue S. 2000. Efp as a primary estrogen-responsive gene in human breast cancer. FEBS Lett 472:9-13.
    • (2000) FEBS Lett , vol.472 , pp. 9-13
    • Ikeda, K.1    Orimo, A.2    Higashi, Y.3    Muramatsu, M.4    Lnoue, S.5
  • 68
    • 0036179479 scopus 로고    scopus 로고
    • Limb-girdle muscular dystrophy type 2H associated with mutation in TRIM32, a putative E3-ubiquitin-ligase gene
    • Frosk P, Weiler T, Nylen E, Sudha T, Greenberg CR, et al. 2002. Limb-girdle muscular dystrophy type 2H associated with mutation in TRIM32, a putative E3-ubiquitin-ligase gene. Am J Hum Genet 70:663-672.
    • (2002) Am J Hum Genet , vol.70 , pp. 663-672
    • Frosk, P.1    Weiler, T.2    Nylen, E.3    Sudha, T.4    Greenberg, C.R.5
  • 69
    • 0033918327 scopus 로고    scopus 로고
    • Gene encoding a new RING-B-box-coiled-coil protein is mutated in mulibrey nanism
    • Avela K, Lipsanen-Nyman M, ldanheimo N, Seemanova E, Rosengren S, et al. 2000. Gene encoding a new RING-B-box-coiled-coil protein is mutated in mulibrey nanism [In Process Citation]. Nat Genet 25:298-301.
    • (2000) Nat Genet , vol.25 , pp. 298-301
    • Avela, K.1    Lipsanen-Nyman, M.2    Ldanheimo, N.3    Seemanova, E.4    Rosengren, S.5
  • 70
    • 0030745449 scopus 로고    scopus 로고
    • Ancient missense mutations in a new member of the RoRet gene family are likely to cause familial Mediterranean fever
    • FMF International Consortium. 1997. Ancient missense mutations in a new member of the RoRet gene family are likely to cause familial Mediterranean fever. Cell 90:797-807.
    • (1997) Cell , vol.90 , pp. 797-807
  • 71
    • 16944365196 scopus 로고    scopus 로고
    • A candidate gene for familial Mediterranean fever
    • FMF Franch Consortium. 1997. A candidate gene for familial Mediterranean fever. Nat Genet 17:25-31.
    • (1997) Nat Genet , vol.17 , pp. 25-31
  • 73
    • 0034829948 scopus 로고    scopus 로고
    • SS-56, a novel cellular target of autoantibody responses in Sjogren syndrome and systemic lupus erythematosus
    • Billaut-Mulot O, Cocude C, Kolesnitchenko V, Truong MJ, Chan EK, et al. 2001. SS-56, a novel cellular target of autoantibody responses in Sjogren syndrome and systemic lupus erythematosus. J Clin Invest 108:861-869.
    • (2001) J Clin Invest , vol.108 , pp. 861-869
    • Billaut-Mulot, O.1    Cocude, C.2    Kolesnitchenko, V.3    Truong, M.J.4    Chan, E.K.5
  • 74
    • 0025875679 scopus 로고
    • The PML-RAR alpha fusion mRNA generated by the t(15:17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR
    • de The H, Lavau C, Marchio A, Chomienne C, Degos L, et al. 1991. The PML-RAR alpha fusion mRNA generated by the t(15:17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR. Cell 66:675-684.
    • (1991) Cell , vol.66 , pp. 675-684
    • De The, H.1    Lavau, C.2    Marchio, A.3    Chomienne, C.4    Degos, L.5
  • 75
    • 0023875393 scopus 로고
    • Developmentally regulated expression of a human "finger"- containing gene encoded by the 5′ half of the ret transforming gene
    • Takahashi M, Inaguma Y, Hiai H, Hirose F. 1988. Developmentally regulated expression of a human "finger"-containing gene encoded by the 5′ half of the ret transforming gene. Mol Cell Biol 8:1853-1856.
    • (1988) Mol Cell Biol , vol.8 , pp. 1853-1856
    • Takahashi, M.1    Inaguma, Y.2    Hiai, H.3    Hirose, F.4
  • 76
    • 0033615042 scopus 로고    scopus 로고
    • The transcription coactivator HTIF1 and a related protein are fused to the RET receptor tyrosine kinase in childhood papillary thyroid carcinomas
    • Klugbauer S, Rabes HM. 1999. The transcription coactivator HTIF1 and a related protein are fused to the RET receptor tyrosine kinase in childhood papillary thyroid carcinomas. Oncogene 18:4388-4393.
    • (1999) Oncogene , vol.18 , pp. 4388-4393
    • Klugbauer, S.1    Rabes, H.M.2
  • 77
    • 0029030016 scopus 로고
    • The N-terminal part of TIF1, a putative mediator of the ligand- dependent activation function (AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T18
    • Le Douarin B, Zechel C, Garnier JM, Lutz Y, Tora L, et al. 1995. The N-terminal part of TIF1, a putative mediator of the ligand- dependent activation function (AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T18. Embo J 14:2020-2033.
    • (1995) Embo J , vol.14 , pp. 2020-2033
    • Le Douarin, B.1    Zechel, C.2    Garnier, J.M.3    Lutz, Y.4    Tora, L.5
  • 78
    • 1542288934 scopus 로고    scopus 로고
    • The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys
    • Stremlau M, Owens CM, Perron MJ, Kiessling M, Autissier P, et al. 2004. The cytoplasmic body component TRIM5alpha restricts HIV-1 infection in Old World monkeys. Nature 427:848-853.
    • (2004) Nature , vol.427 , pp. 848-853
    • Stremlau, M.1    Owens, C.M.2    Perron, M.J.3    Kiessling, M.4    Autissier, P.5
  • 79
    • 3242720240 scopus 로고    scopus 로고
    • Trim5alpha protein restricts both HIV-1 and murine leukemia virus
    • Yap MW, Nisole S, Lynch C, Stoye JP. 2004. Trim5alpha protein restricts both HIV-1 and murine leukemia virus. Proc Natl Acad Sci USA 101:10786-10791.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 10786-10791
    • Yap, M.W.1    Nisole, S.2    Lynch, C.3    Stoye, J.P.4
  • 80
    • 0035969127 scopus 로고    scopus 로고
    • Role and fate of PML nuclear bodies in response to interferon and viral infections
    • Regad T, Chelbi-Alix MK. 2001. Role and fate of PML nuclear bodies in response to interferon and viral infections. Oncogene 20:7274-7286.
    • (2001) Oncogene , vol.20 , pp. 7274-7286
    • Regad, T.1    Chelbi-Alix, M.K.2
  • 81
    • 0029015347 scopus 로고
    • Molecular cloning of a new interferon-induced factor that represses human immunodeficiency virus type 1 long terminal repeat expression
    • Tissot C, Mechti N. 1995. Molecular cloning of a new interferon-induced factor that represses human immunodeficiency virus type 1 long terminal repeat expression. J Biol Chem 270:14891-14898.
    • (1995) J Biol Chem , vol.270 , pp. 14891-14898
    • Tissot, C.1    Mechti, N.2
  • 82
    • 0023988517 scopus 로고
    • rpt-1, an intracellular protein from helper/inducer T cells that regulates gene expression of interleukin 2 receptor and human immunodeficiency virus type 1
    • Patarca R, Freeman GJ, Schwartz J, Singh RP, Kong QT, et al. 1988. rpt-1, an intracellular protein from helper/inducer T cells that regulates gene expression of interleukin 2 receptor and human immunodeficiency virus type 1. Proc Natl Acad Sci USA 85:2733-2737.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2733-2737
    • Patarca, R.1    Freeman, G.J.2    Schwartz, J.3    Singh, R.P.4    Kong, Q.T.5
  • 83
    • 0034306769 scopus 로고    scopus 로고
    • Molecular cloning of ring finger protein 21 (RNF21)/interferon-responsive finger protein (ifp1), which possesses two RING-B box-coiled coil domains in tandem
    • Orimo A, Tominaga N, Yoshimura K, Yamauchi Y, Nomura M, et al. 2000. Molecular cloning of ring finger protein 21 (RNF21)/interferon-responsive finger protein (ifp1), which possesses two RING-B box-coiled coil domains in tandem. Genomics 69:143-149.
    • (2000) Genomics , vol.69 , pp. 143-149
    • Orimo, A.1    Tominaga, N.2    Yoshimura, K.3    Yamauchi, Y.4    Nomura, M.5
  • 84
    • 0034973563 scopus 로고    scopus 로고
    • Cytoplasmic recruitment of INI1 and PML on incoming HIV preintegration complexes: Interference with early steps of viral replication
    • Turelli P, Doucas V, Craig E, Mangeat B, Klages N, et al. 2001. Cytoplasmic recruitment of INI1 and PML on incoming HIV preintegration complexes: interference with early steps of viral replication. Mol Cell 7:1245-1254.
    • (2001) Mol Cell , vol.7 , pp. 1245-1254
    • Turelli, P.1    Doucas, V.2    Craig, E.3    Mangeat, B.4    Klages, N.5
  • 85
    • 0035969107 scopus 로고    scopus 로고
    • Cellular proteins localized at and interacting within ND10/PML nuclear bodies/PODs suggest functions of a nuclear depot
    • Negorev D, Maul GG. 2001. Cellular proteins localized at and interacting within ND10/PML nuclear bodies/PODs suggest functions of a nuclear depot. Oncogene 20:7234-7242.
    • (2001) Oncogene , vol.20 , pp. 7234-7242
    • Negorev, D.1    Maul, G.G.2
  • 86
    • 0037169341 scopus 로고    scopus 로고
    • The role of PML in tumor suppression
    • Salomoni P, Pandolfi PP. 2002. The role of PML in tumor suppression. Cell 108:165-170.
    • (2002) Cell , vol.108 , pp. 165-170
    • Salomoni, P.1    Pandolfi, P.P.2
  • 87
    • 0034931896 scopus 로고    scopus 로고
    • Molecular cloning and characterization of neural activity-related RING finger protein (NARF): A new member of the RBCC family is a candidate for the partner of myosin V
    • Ohkawa N, Kokura K, Matsu-Ura T, Obinata T, Konishi Y, et al. 2001. Molecular cloning and characterization of neural activity-related RING finger protein (NARF): a new member of the RBCC family is a candidate for the partner of myosin V. J Neurochem 78:75-87.
    • (2001) J Neurochem , vol.78 , pp. 75-87
    • Ohkawa, N.1    Kokura, K.2    Matsu-Ura, T.3    Obinata, T.4    Konishi, Y.5
  • 88
    • 0033538519 scopus 로고    scopus 로고
    • Cloning and characterization of a novel RING finger protein that interacts with class V myosins
    • El-Husseini AE, Vincent SR. 1999. Cloning and characterization of a novel RING finger protein that interacts with class V myosins. J Biol Chem 274:19771-19777.
    • (1999) J Biol Chem , vol.274 , pp. 19771-19777
    • El-Husseini, A.E.1    Vincent, S.R.2
  • 89
    • 0037205413 scopus 로고    scopus 로고
    • GNIP, a novel protein that binds and activates glycogenin, the self-glucosylating initiator of glycogen biosynthesis
    • Skurat AV, Dietrich AD, Zhai L, Roach PJ. 2002. GNIP, a novel protein that binds and activates glycogenin, the self-glucosylating initiator of glycogen biosynthesis. J Biol Chem 277:19331-19338.
    • (2002) J Biol Chem , vol.277 , pp. 19331-19338
    • Skurat, A.V.1    Dietrich, A.D.2    Zhai, L.3    Roach, P.J.4
  • 90
    • 0032961415 scopus 로고    scopus 로고
    • HERF1, a novel hematopoiesis-specific RING finger protein, is required for terminal differentiation of erythroid cells
    • Harada H, Harada Y, O'Brien DP, Rice DS, Naeve CW, et al. 1999. HERF1, a novel hematopoiesis-specific RING finger protein, is required for terminal differentiation of erythroid cells. Mol Cell Biol 19:3808-3815.
    • (1999) Mol Cell Biol , vol.19 , pp. 3808-3815
    • Harada, H.1    Harada, Y.2    O'Brien, D.P.3    Rice, D.S.4    Naeve, C.W.5
  • 91
    • 0242331288 scopus 로고    scopus 로고
    • Pub, a novel PU.1. binding protein, regulates the transcriptional activity of PU.1
    • Hirose S, Nishizumi H, Sakano H. 2003. Pub, a novel PU.1. binding protein, regulates the transcriptional activity of PU.1. Biochem Biophys Res Commun 311:351-360.
    • (2003) Biochem Biophys Res Commun , vol.311 , pp. 351-360
    • Hirose, S.1    Nishizumi, H.2    Sakano, H.3
  • 92
    • 0037036406 scopus 로고    scopus 로고
    • The estrogen-responsive B box protein: A novel regulator of keratinocyte differentiation
    • Beer HD, Munding C, Dubois N, Mamie C, Hohl D, et al. 2002. The estrogen-responsive B box protein: a novel regulator of keratinocyte differentiation. J Biol Chem 277:20740-20749.
    • (2002) J Biol Chem , vol.277 , pp. 20740-20749
    • Beer, H.D.1    Munding, C.2    Dubois, N.3    Mamie, C.4    Hohl, D.5
  • 93
    • 0037349294 scopus 로고    scopus 로고
    • Targeted disruption of pyrin, the FMF protein, causes heightened sensitivity to endotoxin and a defect in macrophage apoptosis
    • Chae JJ, Komarow HD, Cheng J, Wood G, Raben N, et al. 2003. Targeted disruption of pyrin, the FMF protein, causes heightened sensitivity to endotoxin and a defect in macrophage apoptosis. Mol Cell 11:591-604.
    • (2003) Mol Cell , vol.11 , pp. 591-604
    • Chae, J.J.1    Komarow, H.D.2    Cheng, J.3    Wood, G.4    Raben, N.5
  • 94
    • 0346665753 scopus 로고    scopus 로고
    • SS-A/Ro52, an autoantigen involved in CD28-mediated IL-2 production
    • Ishii T, Ohnuma K, Murakami A, Takasawa N, Yamochi T, et al. 2003. SS-A/Ro52, an autoantigen involved in CD28-mediated IL-2 production. J Immunol 170:3653-3661.
    • (2003) J Immunol , vol.170 , pp. 3653-3661
    • Ishii, T.1    Ohnuma, K.2    Murakami, A.3    Takasawa, N.4    Yamochi, T.5
  • 96
    • 0033915781 scopus 로고    scopus 로고
    • Mice lacking the transcriptional corepressor TIF1beta are defective in early postimplantation development
    • Gammas F, Mark M, Dolle P, Dierich A, Chambon P, et al. 2000. Mice lacking the transcriptional corepressor TIF1beta are defective in early postimplantation development. Development 127:2955-2963.
    • (2000) Development , vol.127 , pp. 2955-2963
    • Gammas, F.1    Mark, M.2    Dolle, P.3    Dierich, A.4    Chambon, P.5
  • 98
    • 0242497873 scopus 로고    scopus 로고
    • Haprin, a novel haploid germ cell-specific RING finger protein involved in the acrosome reaction
    • Kitamura K, Tanaka H, Nishimune Y. 2003. Haprin, a novel haploid germ cell-specific RING finger protein involved in the acrosome reaction. J Biol Chem 278:44417-44423.
    • (2003) J Biol Chem , vol.278 , pp. 44417-44423
    • Kitamura, K.1    Tanaka, H.2    Nishimune, Y.3
  • 99
    • 4444301523 scopus 로고    scopus 로고
    • TRIM45, a novel human RBCC/TRIM protein, inhibits transcriptional activities of EIK-1 and AP-1
    • Wang Y, Li Y, Qi X, Yuan W, Ai J, et al. 2004. TRIM45, a novel human RBCC/TRIM protein, inhibits transcriptional activities of EIK-1 and AP-1. Biochem Biophys Res Commun 323:9-16.
    • (2004) Biochem Biophys Res Commun , vol.323 , pp. 9-16
    • Wang, Y.1    Li, Y.2    Qi, X.3    Yuan, W.4    Ai, J.5
  • 100
    • 0041703139 scopus 로고    scopus 로고
    • Forced expression of RNF36 induces cell apoptosis
    • Shyu HW, Hsu SH, Hsieh-Li HM, Li H. 2003. Forced expression of RNF36 induces cell apoptosis. Exp Cell Res 287:301-313.
    • (2003) Exp Cell Res , vol.287 , pp. 301-313
    • Shyu, H.W.1    Hsu, S.H.2    Hsieh-Li, H.M.3    Li, H.4
  • 101
    • 0034698695 scopus 로고    scopus 로고
    • Regulation of microtubule dynamics and myogenic differentiation by MURF, a striated muscle RING-finger protein
    • Spencer JA, Eliazer S, Ilaria RL Jr, Richardson JA, Olson EN. 2000. Regulation of microtubule dynamics and myogenic differentiation by MURF, a striated muscle RING-finger protein. J Cell Biol 150:771-784.
    • (2000) J Cell Biol , vol.150 , pp. 771-784
    • Spencer, J.A.1    Eliazer, S.2    Ilaria Jr., R.L.3    Richardson, J.A.4    Olson, E.N.5
  • 102
    • 0031260192 scopus 로고    scopus 로고
    • xnf7 functions in dorsal-ventral patterning of the Xenopus embryo
    • El-Hodiri HM, Shou W, Etkin LD. 1997. xnf7 functions in dorsal-ventral patterning of the Xenopus embryo. Dev Biol 190:1-17.
    • (1997) Dev Biol , vol.190 , pp. 1-17
    • El-Hodiri, H.M.1    Shou, W.2    Etkin, L.D.3
  • 103
    • 0033634943 scopus 로고    scopus 로고
    • The lin-41 RBCC gene acts in the C. elegans heterochronic pathway between the let-7 regulatory RNA and the LIN-29 transcription factor
    • Slack FJ, Basson M, Liu Z, Ambras V, Horvitz HR, et al. 2000. The lin-41 RBCC gene acts in the C. elegans heterochronic pathway between the let-7 regulatory RNA and the LIN-29 transcription factor. Mol Cell 5:659-669.
    • (2000) Mol Cell , vol.5 , pp. 659-669
    • Slack, F.J.1    Basson, M.2    Liu, Z.3    Ambras, V.4    Horvitz, H.R.5
  • 104
    • 0032559797 scopus 로고    scopus 로고
    • ncl-1 is required for the regulation of cell size and ribosomal RNA synthesis in Caenorhabditis elegans
    • Frank DJ, Roth MB. 1998. ncl-1 is required for the regulation of cell size and ribosomal RNA synthesis in Caenorhabditis elegans. J Cell Biol 140:1321-1329.
    • (1998) J Cell Biol , vol.140 , pp. 1321-1329
    • Frank, D.J.1    Roth, M.B.2
  • 105
    • 0034601366 scopus 로고    scopus 로고
    • Mutations in the beta-propeller domain of the Drosophila brain tumor (brat) protein induce neoplasm in the larval brain
    • Arama E, Dickman D, Kimchie Z, Shearn A, Lev Z. 2000. Mutations in the beta-propeller domain of the Drosophila brain tumor (brat) protein induce neoplasm in the larval brain. Oncogene 19:3706-3716.
    • (2000) Oncogene , vol.19 , pp. 3706-3716
    • Arama, E.1    Dickman, D.2    Kimchie, Z.3    Shearn, A.4    Lev, Z.5
  • 106
    • 0035868645 scopus 로고    scopus 로고
    • Drosophila Brain Tumor is a translational repressor
    • Sonoda J, Wharton RP. 2001. Drosophila Brain Tumor is a translational repressor. Genes Dev 15:762-773.
    • (2001) Genes Dev , vol.15 , pp. 762-773
    • Sonoda, J.1    Wharton, R.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.