메뉴 건너뛰기




Volumn 12, Issue , 2012, Pages

Effects of partner proteins on BCA2 RING ligase activity

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; LIGASE;

EID: 84862788928     PISSN: None     EISSN: 14712407     Source Type: Journal    
DOI: 10.1186/1471-2407-12-63     Document Type: Article
Times cited : (20)

References (45)
  • 1
    • 0032516239 scopus 로고    scopus 로고
    • Down-regulation of T1A12/mac25, a novel insulin-like growth factor binding protein related gene, is associated with disease progression in breast carcinomas
    • 10.1038/sj.onc.1201772, 9627112
    • Burger AM, Zhang X, Li H, Ostrowski JL, Beatty B, Venanzoni M, Papas T, Seth A. Down-regulation of T1A12/mac25, a novel insulin-like growth factor binding protein related gene, is associated with disease progression in breast carcinomas. Oncogene 1998, 16:2459-2467. 10.1038/sj.onc.1201772, 9627112.
    • (1998) Oncogene , vol.16 , pp. 2459-2467
    • Burger, A.M.1    Zhang, X.2    Li, H.3    Ostrowski, J.L.4    Beatty, B.5    Venanzoni, M.6    Papas, T.7    Seth, A.8
  • 2
    • 28544431575 scopus 로고    scopus 로고
    • A novel RING-type ubiquitin ligase breast cancer-associated gene 2 correlates with outcome in invasive breast cancer
    • 10.1158/0008-5472.CAN-05-2103, 16288031
    • Burger AM, Gao Y, Amemiya Y, Kahn HJ, Kitching R, Yang Y, Sun P, Narod SA, Hanna WM, Seth AK. A novel RING-type ubiquitin ligase breast cancer-associated gene 2 correlates with outcome in invasive breast cancer. Cancer Res 2005, 65:10401-10412. 10.1158/0008-5472.CAN-05-2103, 16288031.
    • (2005) Cancer Res , vol.65 , pp. 10401-10412
    • Burger, A.M.1    Gao, Y.2    Amemiya, Y.3    Kahn, H.J.4    Kitching, R.5    Yang, Y.6    Sun, P.7    Narod, S.A.8    Hanna, W.M.9    Seth, A.K.10
  • 3
    • 70349240481 scopus 로고    scopus 로고
    • High resolution genome-wide analysis of chromosomal alterations in Burkitt's lymphoma
    • 10.1371/journal.pone.0007089, 2739276, 19759907
    • Toujani S, Dessen P, Ithzar N, Danglot G, Richon C, Vassetzky Y, Robert T, Lazar V, Bosq J, Da CL, et al. High resolution genome-wide analysis of chromosomal alterations in Burkitt's lymphoma. PLoS One 2009, 4:e7089. 10.1371/journal.pone.0007089, 2739276, 19759907.
    • (2009) PLoS One , vol.4
    • Toujani, S.1    Dessen, P.2    Ithzar, N.3    Danglot, G.4    Richon, C.5    Vassetzky, Y.6    Robert, T.7    Lazar, V.8    Bosq, J.9    Da, C.L.10
  • 5
    • 0345276495 scopus 로고    scopus 로고
    • Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2, by a signalosome-like subunit and its role in DNA repair
    • 10.1016/S1097-2765(03)00424-6, 14636569
    • Dong Y, Hakimi MA, Chen X, Kumaraswamy E, Cooch NS, Godwin AK, Shiekhattar R. Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2, by a signalosome-like subunit and its role in DNA repair. Mol Cell 2003, 12:1087-1099. 10.1016/S1097-2765(03)00424-6, 14636569.
    • (2003) Mol Cell , vol.12 , pp. 1087-1099
    • Dong, Y.1    Hakimi, M.A.2    Chen, X.3    Kumaraswamy, E.4    Cooch, N.S.5    Godwin, A.K.6    Shiekhattar, R.7
  • 6
    • 0042206678 scopus 로고    scopus 로고
    • Cbl-mediated ubiquitinylation is required for lysosomal sorting of epidermal growth factor receptor but is dispensable for endocytosis
    • 10.1074/jbc.M304474200, 12754251
    • Duan L, Miura Y, Dimri M, Majumder B, Dodge IL, Reddi AL, Ghosh A, Fernandes N, Zhou P, Mullane-Robinson K, et al. Cbl-mediated ubiquitinylation is required for lysosomal sorting of epidermal growth factor receptor but is dispensable for endocytosis. J Biol Chem 2003, 278:28950-28960. 10.1074/jbc.M304474200, 12754251.
    • (2003) J Biol Chem , vol.278 , pp. 28950-28960
    • Duan, L.1    Miura, Y.2    Dimri, M.3    Majumder, B.4    Dodge, I.L.5    Reddi, A.L.6    Ghosh, A.7    Fernandes, N.8    Zhou, P.9    Mullane-Robinson, K.10
  • 7
    • 53349174884 scopus 로고    scopus 로고
    • Autoubiquitination of BCA2 RING E3 ligase regulates its own stability and affects cell migration
    • 10.1158/1541-7786.MCR-08-0094, 2814348, 18819927
    • Amemiya Y, Azmi P, Seth A. Autoubiquitination of BCA2 RING E3 ligase regulates its own stability and affects cell migration. Mol Cancer Res 2008, 6:1385-1396. 10.1158/1541-7786.MCR-08-0094, 2814348, 18819927.
    • (2008) Mol Cancer Res , vol.6 , pp. 1385-1396
    • Amemiya, Y.1    Azmi, P.2    Seth, A.3
  • 8
    • 24144465684 scopus 로고    scopus 로고
    • Molecular characterization of ring finger protein 11
    • 10.1158/1541-7786.MCR-04-0166, 16123141
    • Connor MK, Azmi PB, Subramaniam V, Li H, Seth A. Molecular characterization of ring finger protein 11. Mol Cancer Res 2005, 3:453-461. 10.1158/1541-7786.MCR-04-0166, 16123141.
    • (2005) Mol Cancer Res , vol.3 , pp. 453-461
    • Connor, M.K.1    Azmi, P.B.2    Subramaniam, V.3    Li, H.4    Seth, A.5
  • 9
    • 0034708458 scopus 로고    scopus 로고
    • Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53
    • 10.1074/jbc.275.12.8945, 10722742
    • Fang S, Jensen JP, Ludwig RL, Vousden KH, Weissman AM. Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53. J Biol Chem 2000, 275:8945-8951. 10.1074/jbc.275.12.8945, 10722742.
    • (2000) J Biol Chem , vol.275 , pp. 8945-8951
    • Fang, S.1    Jensen, J.P.2    Ludwig, R.L.3    Vousden, K.H.4    Weissman, A.M.5
  • 10
    • 0032933351 scopus 로고    scopus 로고
    • Siah-1 N-terminal RING domain is required for proteolysis function, and C-terminal sequences regulate oligomerization and binding to target proteins
    • 83929, 9858595
    • Hu G, Fearon ER. Siah-1 N-terminal RING domain is required for proteolysis function, and C-terminal sequences regulate oligomerization and binding to target proteins. Mol Cell Biol 1999, 19:724-732. 83929, 9858595.
    • (1999) Mol Cell Biol , vol.19 , pp. 724-732
    • Hu, G.1    Fearon, E.R.2
  • 11
    • 9744227183 scopus 로고    scopus 로고
    • Ubiquitin: structures, functions, mechanisms
    • 10.1016/j.bbamcr.2004.09.019, 15571809
    • Pickart CM, Eddins MJ. Ubiquitin: structures, functions, mechanisms. Biochim Biophys Acta 2004, 1695:55-72. 10.1016/j.bbamcr.2004.09.019, 15571809.
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 55-72
    • Pickart, C.M.1    Eddins, M.J.2
  • 12
    • 34347329214 scopus 로고    scopus 로고
    • Dual E1 activation systems for ubiquitin differentially regulate E2 enzyme charging
    • 10.1038/nature05902, 17597759
    • Jin J, Li X, Gygi SP, Harper JW. Dual E1 activation systems for ubiquitin differentially regulate E2 enzyme charging. Nature 2007, 447:1135-1138. 10.1038/nature05902, 17597759.
    • (2007) Nature , vol.447 , pp. 1135-1138
    • Jin, J.1    Li, X.2    Gygi, S.P.3    Harper, J.W.4
  • 13
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction
    • Glickman MH, Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 2002, 82:373-428.
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 14
    • 0036395180 scopus 로고    scopus 로고
    • Ubiquitin-dependent proteolysis: its role in human diseases and the design of therapeutic strategies
    • 10.1016/S1096-7192(02)00146-4, 12359129
    • Sakamoto KM. Ubiquitin-dependent proteolysis: its role in human diseases and the design of therapeutic strategies. Mol Genet Metab 2002, 77:44-56. 10.1016/S1096-7192(02)00146-4, 12359129.
    • (2002) Mol Genet Metab , vol.77 , pp. 44-56
    • Sakamoto, K.M.1
  • 15
    • 80051733972 scopus 로고    scopus 로고
    • Ubiquitination of E3 ligases: self-regulation of the ubiquitin system via proteolytic and non-proteolytic mechanisms
    • 10.1038/cdd.2011.16, 21372847
    • de Bie P, Ciechanover A. Ubiquitination of E3 ligases: self-regulation of the ubiquitin system via proteolytic and non-proteolytic mechanisms. Cell Death Differ 2011, 18(9):1393-1402. 10.1038/cdd.2011.16, 21372847.
    • (2011) Cell Death Differ , vol.18 , Issue.9 , pp. 1393-1402
    • de Bie, P.1    Ciechanover, A.2
  • 16
    • 78249246032 scopus 로고    scopus 로고
    • Role of the BCA2 ubiquitin E3 ligase in hormone responsive breast cancer
    • 3004234, 21179390
    • Burger AM, Kona F, Amemiya Y, Gao Y, Bacopulos S, Seth AK. Role of the BCA2 ubiquitin E3 ligase in hormone responsive breast cancer. Open Cancer J 2010, 3:116-123. 3004234, 21179390.
    • (2010) Open Cancer J , vol.3 , pp. 116-123
    • Burger, A.M.1    Kona, F.2    Amemiya, Y.3    Gao, Y.4    Bacopulos, S.5    Seth, A.K.6
  • 17
    • 0141744731 scopus 로고    scopus 로고
    • Rabring7, a novel Rab7 target protein with a RING finger motif
    • 10.1091/mbc.E02-08-0495, 196564, 12972561
    • Mizuno K, Kitamura A, Sasaki T. Rabring7, a novel Rab7 target protein with a RING finger motif. Mol Biol Cell 2003, 14:3741-3752. 10.1091/mbc.E02-08-0495, 196564, 12972561.
    • (2003) Mol Biol Cell , vol.14 , pp. 3741-3752
    • Mizuno, K.1    Kitamura, A.2    Sasaki, T.3
  • 19
    • 63049109748 scopus 로고    scopus 로고
    • The ubiquitin receptor Rad23: at the crossroads of nucleotide excision repair and proteasomal degradation
    • Dantuma NP, Heinen C, Hoogstraten D. The ubiquitin receptor Rad23: at the crossroads of nucleotide excision repair and proteasomal degradation. DNA Repair (Amst) 2009, 8:449-460.
    • (2009) DNA Repair (Amst) , vol.8 , pp. 449-460
    • Dantuma, N.P.1    Heinen, C.2    Hoogstraten, D.3
  • 20
    • 21044434194 scopus 로고    scopus 로고
    • Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer
    • 10.1074/mcp.M500021-MCP200, 15778465
    • Benzinger A, Muster N, Koch HB, Yates JR, Hermeking H. Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer. Mol Cell Proteomics 2005, 4:785-795. 10.1074/mcp.M500021-MCP200, 15778465.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 785-795
    • Benzinger, A.1    Muster, N.2    Koch, H.B.3    Yates, J.R.4    Hermeking, H.5
  • 22
    • 0034282219 scopus 로고    scopus 로고
    • The DNA repair protein rad23 is a negative regulator of multi-ubiquitin chain assembly
    • 10.1038/35023547, 10980700
    • Ortolan TG, Tongaonkar P, Lambertson D, Chen L, Schauber C, Madura K. The DNA repair protein rad23 is a negative regulator of multi-ubiquitin chain assembly. Nat Cell Biol 2000, 2:601-608. 10.1038/35023547, 10980700.
    • (2000) Nat Cell Biol , vol.2 , pp. 601-608
    • Ortolan, T.G.1    Tongaonkar, P.2    Lambertson, D.3    Chen, L.4    Schauber, C.5    Madura, K.6
  • 23
    • 0037646406 scopus 로고    scopus 로고
    • Rad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains
    • 10.1074/jbc.M212841200, 12643283
    • Raasi S, Pickart CM. Rad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains. J Biol Chem 2003, 278:8951-8959. 10.1074/jbc.M212841200, 12643283.
    • (2003) J Biol Chem , vol.278 , pp. 8951-8959
    • Raasi, S.1    Pickart, C.M.2
  • 24
    • 66249102308 scopus 로고    scopus 로고
    • Multisite protein phosphorylation-from molecular mechanisms to kinetic models
    • 10.1111/j.1742-4658.2009.07027.x, 19438722
    • Salazar C, Hofer T. Multisite protein phosphorylation-from molecular mechanisms to kinetic models. FEBS J 2009, 276:3177-3198. 10.1111/j.1742-4658.2009.07027.x, 19438722.
    • (2009) FEBS J , vol.276 , pp. 3177-3198
    • Salazar, C.1    Hofer, T.2
  • 25
    • 31344457298 scopus 로고    scopus 로고
    • UBL/UBA ubiquitin receptor proteins bind a common tetraubiquitin chain
    • 10.1016/j.jmb.2005.12.001, 16405905
    • Kang Y, Vossler RA, Diaz-Martinez LA, Winter NS, Clarke DJ, Walters KJ. UBL/UBA ubiquitin receptor proteins bind a common tetraubiquitin chain. J Mol Biol 2006, 356:1027-1035. 10.1016/j.jmb.2005.12.001, 16405905.
    • (2006) J Mol Biol , vol.356 , pp. 1027-1035
    • Kang, Y.1    Vossler, R.A.2    Diaz-Martinez, L.A.3    Winter, N.S.4    Clarke, D.J.5    Walters, K.J.6
  • 26
    • 34247349494 scopus 로고    scopus 로고
    • Defining how ubiquitin receptors hHR23a and S5a bind polyubiquitin
    • 10.1016/j.jmb.2007.03.008, 17408689
    • Kang Y, Chen X, Lary JW, Cole JL, Walters KJ. Defining how ubiquitin receptors hHR23a and S5a bind polyubiquitin. J Mol Biol 2007, 369:168-176. 10.1016/j.jmb.2007.03.008, 17408689.
    • (2007) J Mol Biol , vol.369 , pp. 168-176
    • Kang, Y.1    Chen, X.2    Lary, J.W.3    Cole, J.L.4    Walters, K.J.5
  • 27
    • 0027367944 scopus 로고
    • The Saccharomyces cerevisiae DNA repair gene RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function
    • 364847, 8246991
    • Watkins JF, Sung P, Prakash L, Prakash S. The Saccharomyces cerevisiae DNA repair gene RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function. Mol Cell Biol 1993, 13:7757-7765. 364847, 8246991.
    • (1993) Mol Cell Biol , vol.13 , pp. 7757-7765
    • Watkins, J.F.1    Sung, P.2    Prakash, L.3    Prakash, S.4
  • 28
    • 0033634846 scopus 로고    scopus 로고
    • Concerted dephosphorylation of the transcription factor NFAT1 induces a conformational switch that regulates transcriptional activity
    • 10.1016/S1097-2765(00)00053-8, 11030334
    • Okamura H, Aramburu J, Garcia-Rodriguez C, Viola JP, Raghavan A, Tahiliani M, Zhang X, Qin J, Hogan PG, Rao A. Concerted dephosphorylation of the transcription factor NFAT1 induces a conformational switch that regulates transcriptional activity. Mol Cell 2000, 6:539-550. 10.1016/S1097-2765(00)00053-8, 11030334.
    • (2000) Mol Cell , vol.6 , pp. 539-550
    • Okamura, H.1    Aramburu, J.2    Garcia-Rodriguez, C.3    Viola, J.P.4    Raghavan, A.5    Tahiliani, M.6    Zhang, X.7    Qin, J.8    Hogan, P.G.9    Rao, A.10
  • 29
    • 24644442164 scopus 로고    scopus 로고
    • The folding energy landscape and phosphorylation: modeling the conformational switch of the NFAT regulatory domain
    • 10.1096/fj.04-3590hyp, 16126906
    • Shen T, Zong C, Hamelberg D, McCammon JA, Wolynes PG. The folding energy landscape and phosphorylation: modeling the conformational switch of the NFAT regulatory domain. FASEB J 2005, 19:1389-1395. 10.1096/fj.04-3590hyp, 16126906.
    • (2005) FASEB J , vol.19 , pp. 1389-1395
    • Shen, T.1    Zong, C.2    Hamelberg, D.3    McCammon, J.A.4    Wolynes, P.G.5
  • 30
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signaling: navigating downstream
    • 10.1016/j.cell.2007.06.009, 2756685, 17604717
    • Manning BD, Cantley LC. AKT/PKB signaling: navigating downstream. Cell 2007, 129:1261-1274. 10.1016/j.cell.2007.06.009, 2756685, 17604717.
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 32
    • 0034725698 scopus 로고    scopus 로고
    • Association of the cyclin-dependent kinases and 14-3-3 sigma negatively regulates cell cycle progression
    • 10.1074/jbc.M905616199, 10767298
    • Laronga C, Yang HY, Neal C, Lee MH. Association of the cyclin-dependent kinases and 14-3-3 sigma negatively regulates cell cycle progression. J Biol Chem 2000, 275:23106-23112. 10.1074/jbc.M905616199, 10767298.
    • (2000) J Biol Chem , vol.275 , pp. 23106-23112
    • Laronga, C.1    Yang, H.Y.2    Neal, C.3    Lee, M.H.4
  • 33
    • 21444436802 scopus 로고    scopus 로고
    • A structural basis for 14-3-3sigma functional specificity
    • 10.1074/jbc.M500982200, 15731107
    • Wilker EW, Grant RA, Artim SC, Yaffe MB. A structural basis for 14-3-3sigma functional specificity. J Biol Chem 2005, 280:18891-18898. 10.1074/jbc.M500982200, 15731107.
    • (2005) J Biol Chem , vol.280 , pp. 18891-18898
    • Wilker, E.W.1    Grant, R.A.2    Artim, S.C.3    Yaffe, M.B.4
  • 34
    • 1642442587 scopus 로고    scopus 로고
    • Stability of homologue of Slimb F-box protein is regulated by availability of its substrate
    • 10.1074/jbc.M312301200, 14707120
    • Li Y, Gazdoiu S, Pan ZQ, Fuchs SY. Stability of homologue of Slimb F-box protein is regulated by availability of its substrate. J Biol Chem 2004, 279:11074-11080. 10.1074/jbc.M312301200, 14707120.
    • (2004) J Biol Chem , vol.279 , pp. 11074-11080
    • Li, Y.1    Gazdoiu, S.2    Pan, Z.Q.3    Fuchs, S.Y.4
  • 35
    • 78149456945 scopus 로고    scopus 로고
    • WD40 repeat propellers define a ubiquitin-binding domain that regulates turnover of F box proteins
    • 10.1016/j.molcel.2010.10.018, 3266742, 21070969
    • Pashkova N, Gakhar L, Winistorfer SC, Yu L, Ramaswamy S, Piper RC. WD40 repeat propellers define a ubiquitin-binding domain that regulates turnover of F box proteins. Mol Cell 2010, 40:433-443. 10.1016/j.molcel.2010.10.018, 3266742, 21070969.
    • (2010) Mol Cell , vol.40 , pp. 433-443
    • Pashkova, N.1    Gakhar, L.2    Winistorfer, S.C.3    Yu, L.4    Ramaswamy, S.5    Piper, R.C.6
  • 36
    • 0035920225 scopus 로고    scopus 로고
    • Cbl-b-dependent coordinated degradation of the epidermal growth factor receptor signaling complex
    • 10.1074/jbc.M102641200, 11375397
    • Ettenberg SA, Magnifico A, Cuello M, Nau MM, Rubinstein YR, Yarden Y, Weissman AM, Lipkowitz S. Cbl-b-dependent coordinated degradation of the epidermal growth factor receptor signaling complex. J Biol Chem 2001, 276:27677-27684. 10.1074/jbc.M102641200, 11375397.
    • (2001) J Biol Chem , vol.276 , pp. 27677-27684
    • Ettenberg, S.A.1    Magnifico, A.2    Cuello, M.3    Nau, M.M.4    Rubinstein, Y.R.5    Yarden, Y.6    Weissman, A.M.7    Lipkowitz, S.8
  • 37
    • 11144244315 scopus 로고    scopus 로고
    • Regulation of stem cell factor receptor signaling by Cbl family proteins (Cbl-b/c-Cbl)
    • 10.1182/blood-2004-05-1768, 15315962
    • Zeng S, Xu Z, Lipkowitz S, Longley JB. Regulation of stem cell factor receptor signaling by Cbl family proteins (Cbl-b/c-Cbl). Blood 2005, 105:226-232. 10.1182/blood-2004-05-1768, 15315962.
    • (2005) Blood , vol.105 , pp. 226-232
    • Zeng, S.1    Xu, Z.2    Lipkowitz, S.3    Longley, J.B.4
  • 38
    • 0041816011 scopus 로고    scopus 로고
    • Ligand-induced lysosomal epidermal growth factor receptor (EGFR) degradation is preceded by proteasome-dependent EGFR de-ubiquitination
    • 10.1074/jbc.M301326200, 12829707
    • Alwan HA, van Zoelen EJ, van Leeuwen JE. Ligand-induced lysosomal epidermal growth factor receptor (EGFR) degradation is preceded by proteasome-dependent EGFR de-ubiquitination. J Biol Chem 2003, 278:35781-35790. 10.1074/jbc.M301326200, 12829707.
    • (2003) J Biol Chem , vol.278 , pp. 35781-35790
    • Alwan, H.A.1    van Zoelen, E.J.2    van Leeuwen, J.E.3
  • 39
    • 0041765751 scopus 로고    scopus 로고
    • Bortezomib (velcade) for multiple myeloma
    • Bortezomib (velcade) for multiple myeloma. Med Lett Drugs Ther 2003, 45:57-58.
    • (2003) Med Lett Drugs Ther , vol.45 , pp. 57-58
  • 40
    • 0038649638 scopus 로고    scopus 로고
    • The proteasome-an emerging therapeutic target in cancer
    • 10.1056/NEJMp030092, 12826633
    • Mitchell BS. The proteasome-an emerging therapeutic target in cancer. N Engl J Med 2003, 348:2597-2598. 10.1056/NEJMp030092, 12826633.
    • (2003) N Engl J Med , vol.348 , pp. 2597-2598
    • Mitchell, B.S.1
  • 41
    • 0033392493 scopus 로고    scopus 로고
    • Ubiquitin ligase activity and tyrosine phosphorylation underlie suppression of growth factor signaling by c-Cbl/Sli-1
    • 10.1016/S1097-2765(00)80231-2, 10635327
    • Levkowitz G, Waterman H, Ettenberg SA, Katz M, Tsygankov AY, Alroy I, Lavi S, Iwai K, Reiss Y, Ciechanover A, et al. Ubiquitin ligase activity and tyrosine phosphorylation underlie suppression of growth factor signaling by c-Cbl/Sli-1. Mol Cell 1999, 4:1029-1040. 10.1016/S1097-2765(00)80231-2, 10635327.
    • (1999) Mol Cell , vol.4 , pp. 1029-1040
    • Levkowitz, G.1    Waterman, H.2    Ettenberg, S.A.3    Katz, M.4    Tsygankov, A.Y.5    Alroy, I.6    Lavi, S.7    Iwai, K.8    Reiss, Y.9    Ciechanover, A.10
  • 42
    • 33751515474 scopus 로고    scopus 로고
    • The polycomb protein Ring1B generates self atypical mixed ubiquitin chains required for its in vitro histone H2A ligase activity
    • 10.1016/j.molcel.2006.10.022, 17157253
    • Ben-Saadon R, Zaaroor D, Ziv T, Ciechanover A. The polycomb protein Ring1B generates self atypical mixed ubiquitin chains required for its in vitro histone H2A ligase activity. Mol Cell 2006, 24:701-711. 10.1016/j.molcel.2006.10.022, 17157253.
    • (2006) Mol Cell , vol.24 , pp. 701-711
    • Ben-Saadon, R.1    Zaaroor, D.2    Ziv, T.3    Ciechanover, A.4
  • 43
    • 29144487990 scopus 로고    scopus 로고
    • Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing
    • 10.1016/j.molcel.2005.12.002, 16359901
    • Cao R, Tsukada Y, Zhang Y. Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing. Mol Cell 2005, 20:845-854. 10.1016/j.molcel.2005.12.002, 16359901.
    • (2005) Mol Cell , vol.20 , pp. 845-854
    • Cao, R.1    Tsukada, Y.2    Zhang, Y.3
  • 44
    • 4644352805 scopus 로고    scopus 로고
    • A RING finger ubiquitin ligase is protected from autocatalyzed ubiquitination and degradation by binding to ubiquitin-specific protease USP7
    • 10.1074/jbc.M402885200, 15247261
    • Canning M, Boutell C, Parkinson J, Everett RD. A RING finger ubiquitin ligase is protected from autocatalyzed ubiquitination and degradation by binding to ubiquitin-specific protease USP7. J Biol Chem 2004, 279:38160-38168. 10.1074/jbc.M402885200, 15247261.
    • (2004) J Biol Chem , vol.279 , pp. 38160-38168
    • Canning, M.1    Boutell, C.2    Parkinson, J.3    Everett, R.D.4
  • 45
    • 0041335560 scopus 로고    scopus 로고
    • Ubiquitination of the Epstein-Barr virus-encoded latent membrane protein 1 depends on the integrity of the TRAF binding site
    • 10.1038/sj.onc.1206497, 12944909
    • Rothenberger S, Burns K, Rousseaux M, Tschopp J, Bron C. Ubiquitination of the Epstein-Barr virus-encoded latent membrane protein 1 depends on the integrity of the TRAF binding site. Oncogene 2003, 22:5614-5618. 10.1038/sj.onc.1206497, 12944909.
    • (2003) Oncogene , vol.22 , pp. 5614-5618
    • Rothenberger, S.1    Burns, K.2    Rousseaux, M.3    Tschopp, J.4    Bron, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.