메뉴 건너뛰기




Volumn 112, Issue 32, 2015, Pages 9872-9877

Role of ubiquitin and the HPV E6 oncoprotein in E6APmediated ubiquitination

Author keywords

Angelman syndrome; E6 oncoprotein; E6AP UBE3A; Human papillomavirus; Ubiquitin

Indexed keywords

ISOLEUCINE; LEUCINE; PROTEIN E6; RING1B PROTEIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; CYSTEINE; PEPTIDE; PROTEIN BINDING; UBE2D2 PROTEIN, HUMAN; UBE2L3 PROTEIN, HUMAN; UBE3A PROTEIN, HUMAN; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN PROTEIN LIGASE;

EID: 84938915433     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1505923112     Document Type: Article
Times cited : (45)

References (55)
  • 1
    • 33749346301 scopus 로고    scopus 로고
    • Modification of proteins by ubiquitin and ubiquitin-like proteins
    • Kerscher O, Felberbaum R, Hochstrasser M (2006) Modification of proteins by ubiquitin and ubiquitin-like proteins. Annu Rev Cell Dev Biol 22: 159-180.
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 159-180
    • Kerscher, O.1    Felberbaum, R.2    Hochstrasser, M.3
  • 2
    • 61449156563 scopus 로고    scopus 로고
    • Targeting proteins for destruction by the ubiquitin system: Implications for human pathobiology
    • Schwartz AL, Ciechanover A (2009) Targeting proteins for destruction by the ubiquitin system: Implications for human pathobiology. Annu Rev Pharmacol Toxicol 49: 73-96.
    • (2009) Annu Rev Pharmacol Toxicol , vol.49 , pp. 73-96
    • Schwartz, A.L.1    Ciechanover, A.2
  • 3
    • 84861881296 scopus 로고    scopus 로고
    • The ubiquitin system, an immense realm
    • Varshavsky A (2012) The ubiquitin system, an immense realm. Annu Rev Biochem 81: 167-176.
    • (2012) Annu Rev Biochem , vol.81 , pp. 167-176
    • Varshavsky, A.1
  • 4
    • 84922393807 scopus 로고    scopus 로고
    • Ubiquitination in disease pathogenesis and treatment
    • Popovic D, Vucic D, Dikic I (2014) Ubiquitination in disease pathogenesis and treatment. Nat Med 20(11): 1242-1253.
    • (2014) Nat Med , vol.20 , Issue.11 , pp. 1242-1253
    • Popovic, D.1    Vucic, D.2    Dikic, I.3
  • 5
    • 84858142724 scopus 로고    scopus 로고
    • HECT and RING finger families of E3 ubiquitin ligases at a glance
    • Metzger MB, Hristova VA, Weissman AM (2012) HECT and RING finger families of E3 ubiquitin ligases at a glance. J Cell Sci 125(Pt 3): 531-537.
    • (2012) J Cell Sci , vol.125 , pp. 531-537
    • Metzger, M.B.1    Hristova, V.A.2    Weissman, A.M.3
  • 6
    • 84867097867 scopus 로고    scopus 로고
    • RING-between-RINGs-keeping the safety on loaded guns
    • Dove KK, Klevit RE (2012) RING-between-RINGs-keeping the safety on loaded guns. EMBO J 31(19): 3792-3794.
    • (2012) EMBO J , vol.31 , Issue.19 , pp. 3792-3794
    • Dove, K.K.1    Klevit, R.E.2
  • 7
    • 84890136771 scopus 로고    scopus 로고
    • Mammalian HECT ubiquitin-protein ligases: Biological and pathophysiological aspects
    • Scheffner M, Kumar S (2014) Mammalian HECT ubiquitin-protein ligases: Biological and pathophysiological aspects. Biochim Biophys Acta 1843(1): 61-74.
    • (2014) Biochim Biophys Acta , vol.1843 , Issue.1 , pp. 61-74
    • Scheffner, M.1    Kumar, S.2
  • 8
    • 0025932933 scopus 로고
    • A cellular protein mediates association of p53 with the E6 oncoprotein of human papillomavirus types 16 or 18
    • Huibregtse JM, Scheffner M, Howley PM (1991) A cellular protein mediates association of p53 with the E6 oncoprotein of human papillomavirus types 16 or 18. EMBO J 10(13): 4129-4135.
    • (1991) EMBO J , vol.10 , Issue.13 , pp. 4129-4135
    • Huibregtse, J.M.1    Scheffner, M.2    Howley, P.M.3
  • 9
    • 0027396829 scopus 로고
    • Cloning and expression of the cDNA for E6-AP, a protein that mediates the interaction of the human papillomavirus E6 oncoprotein with p53
    • Huibregtse JM, Scheffner M, Howley PM (1993) Cloning and expression of the cDNA for E6-AP, a protein that mediates the interaction of the human papillomavirus E6 oncoprotein with p53. Mol Cell Biol 13(2): 775-784.
    • (1993) Mol Cell Biol , vol.13 , Issue.2 , pp. 775-784
    • Huibregtse, J.M.1    Scheffner, M.2    Howley, P.M.3
  • 10
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • Scheffner M, Huibregtse JM, Vierstra RD, Howley PM (1993) The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 75(3): 495-505.
    • (1993) Cell , vol.75 , Issue.3 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4
  • 11
    • 54249105821 scopus 로고    scopus 로고
    • HPV E6, E6AP and cervical cancer
    • Beaudenon S, Huibregtse JM (2008) HPV E6, E6AP and cervical cancer. BMC Biochem 9(Suppl 1): S4.
    • (2008) BMC Biochem , vol.9 , pp. S4
    • Beaudenon, S.1    Huibregtse, J.M.2
  • 12
    • 0031012849 scopus 로고    scopus 로고
    • UBE3A/E6-AP mutations cause Angelman syndrome
    • Kishino T, Lalande M, Wagstaff J (1997) UBE3A/E6-AP mutations cause Angelman syndrome. Nat Genet 15(1): 70-73.
    • (1997) Nat Genet , vol.15 , Issue.1 , pp. 70-73
    • Kishino, T.1    Lalande, M.2    Wagstaff, J.3
  • 13
    • 0031031570 scopus 로고    scopus 로고
    • De novo truncating mutations in E6-AP ubiquitin-protein ligase gene (UBE3A) in Angelman syndrome
    • Matsuura T, et al. (1997) De novo truncating mutations in E6-AP ubiquitin-protein ligase gene (UBE3A) in Angelman syndrome. Nat Genet 15(1): 74-77.
    • (1997) Nat Genet , vol.15 , Issue.1 , pp. 74-77
    • Matsuura, T.1
  • 14
    • 84860197780 scopus 로고    scopus 로고
    • Molecular and clinical aspects of Angelman syndrome
    • Dagli A, Buiting K, Williams CA (2012) Molecular and clinical aspects of Angelman syndrome. Mol Syndromol 2(3-5): 100-112.
    • (2012) Mol Syndromol , vol.2 , Issue.3-5 , pp. 100-112
    • Dagli, A.1    Buiting, K.2    Williams, C.A.3
  • 15
    • 67349182343 scopus 로고    scopus 로고
    • Autism genome-wide copy number variation reveals ubiquitin and neuronal genes
    • Glessner JT, et al. (2009) Autism genome-wide copy number variation reveals ubiquitin and neuronal genes. Nature 459(7246): 569-573.
    • (2009) Nature , vol.459 , Issue.7246 , pp. 569-573
    • Glessner, J.T.1
  • 16
    • 77951206469 scopus 로고    scopus 로고
    • The comorbidity of autism with the genomic disorders of chromosome 15q11.2-q13
    • Hogart A, Wu D, LaSalle JM, Schanen NC (2010) The comorbidity of autism with the genomic disorders of chromosome 15q11.2-q13. Neurobiol Dis 38(2): 181-191.
    • (2010) Neurobiol Dis , vol.38 , Issue.2 , pp. 181-191
    • Hogart, A.1    Wu, D.2    LaSalle, J.M.3    Schanen, N.C.4
  • 17
    • 80053626726 scopus 로고    scopus 로고
    • Increased gene dosage of Ube3a results in autism traits and decreased glutamate synaptic transmission in mice
    • Smith SE, et al. (2011) Increased gene dosage of Ube3a results in autism traits and decreased glutamate synaptic transmission in mice. Sci Transl Med 3(103): 103ra97.
    • (2011) Sci Transl Med , vol.3 , Issue.103 , pp. 103ra97
    • Smith, S.E.1
  • 18
    • 84925227935 scopus 로고    scopus 로고
    • Towards a therapy for Angelman syndrome by targeting a long non-coding RNA
    • Meng L, et al. (2015) Towards a therapy for Angelman syndrome by targeting a long non-coding RNA. Nature 518(7539): 409-412.
    • (2015) Nature , vol.518 , Issue.7539 , pp. 409-412
    • Meng, L.1
  • 19
    • 79957613292 scopus 로고    scopus 로고
    • Physical and functional interaction of the HECT ubiquitinprotein ligases E6AP and HERC2
    • Kühnle S, et al. (2011) Physical and functional interaction of the HECT ubiquitinprotein ligases E6AP and HERC2. J Biol Chem 286(22): 19410-19416.
    • (2011) J Biol Chem , vol.286 , Issue.22 , pp. 19410-19416
    • Kühnle, S.1
  • 20
    • 84873058197 scopus 로고    scopus 로고
    • Mutation of HERC2 causes developmental delay with Angelman-like features
    • Harlalka GV, et al. (2013) Mutation of HERC2 causes developmental delay with Angelman-like features. J Med Genet 50(2): 65-73.
    • (2013) J Med Genet , vol.50 , Issue.2 , pp. 65-73
    • Harlalka, G.V.1
  • 21
    • 0035839519 scopus 로고    scopus 로고
    • Distinct functional surface regions on ubiquitin
    • Sloper-Mould KE, Jemc JC, Pickart CM, Hicke L (2001) Distinct functional surface regions on ubiquitin. J Biol Chem 276(32): 30483-30489.
    • (2001) J Biol Chem , vol.276 , Issue.32 , pp. 30483-30489
    • Sloper-Mould, K.E.1    Jemc, J.C.2    Pickart, C.M.3    Hicke, L.4
  • 22
    • 72149107116 scopus 로고    scopus 로고
    • Insights into ubiquitin transfer cascades from a structure of a UbcH5B approximately ubiquitin-HECT(NEDD4L) complex
    • Kamadurai HB, et al. (2009) Insights into ubiquitin transfer cascades from a structure of a UbcH5B approximately ubiquitin-HECT(NEDD4L) complex. Mol Cell 36(6): 1095-1102.
    • (2009) Mol Cell , vol.36 , Issue.6 , pp. 1095-1102
    • Kamadurai, H.B.1
  • 23
    • 79953310074 scopus 로고    scopus 로고
    • Structure and function of a HECT domain ubiquitin-binding site
    • Kim HC, Steffen AM, Oldham ML, Chen J, Huibregtse JM (2011) Structure and function of a HECT domain ubiquitin-binding site. EMBO Rep 12(4): 334-341.
    • (2011) EMBO Rep , vol.12 , Issue.4 , pp. 334-341
    • Kim, H.C.1    Steffen, A.M.2    Oldham, M.L.3    Chen, J.4    Huibregtse, J.M.5
  • 24
    • 79953325889 scopus 로고    scopus 로고
    • Structure of the HECT: Ubiquitin complex and its role in ubiquitin chain elongation
    • Maspero E, et al. (2011) Structure of the HECT: Ubiquitin complex and its role in ubiquitin chain elongation. EMBO Rep 12(4): 342-349.
    • (2011) EMBO Rep , vol.12 , Issue.4 , pp. 342-349
    • Maspero, E.1
  • 25
    • 79953296212 scopus 로고    scopus 로고
    • Essential role for ubiquitinubiquitin- conjugating enzyme interaction in ubiquitin discharge from Cdc34 to substrate
    • Saha A, Lewis S, Kleiger G, Kuhlman B, Deshaies RJ (2011) Essential role for ubiquitinubiquitin- conjugating enzyme interaction in ubiquitin discharge from Cdc34 to substrate. Mol Cell 42(1): 75-83.
    • (2011) Mol Cell , vol.42 , Issue.1 , pp. 75-83
    • Saha, A.1    Lewis, S.2    Kleiger, G.3    Kuhlman, B.4    Deshaies, R.J.5
  • 26
    • 79952290609 scopus 로고    scopus 로고
    • The mechanism of linkage-specific ubiquitin chain elongation by a single-subunit E2
    • Wickliffe KE, Lorenz S, Wemmer DE, Kuriyan J, Rape M (2011) The mechanism of linkage-specific ubiquitin chain elongation by a single-subunit E2. Cell 144(5): 769-781.
    • (2011) Cell , vol.144 , Issue.5 , pp. 769-781
    • Wickliffe, K.E.1    Lorenz, S.2    Wemmer, D.E.3    Kuriyan, J.4    Rape, M.5
  • 27
    • 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, Cameron K, Huang DT (2012) BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nat Struct Mol Biol 19(9): 876-883.
    • (2012) Nat Struct Mol Biol , vol.19 , Issue.9 , pp. 876-883
    • Dou, H.1    Buetow, L.2    Sibbet, G.J.3    Cameron, K.4    Huang, D.T.5
  • 28
    • 84865781586 scopus 로고    scopus 로고
    • Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis
    • Plechanovová A, Jaffray EG, Tatham MH, Naismith JH, Hay RT (2012) Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis. Nature 489(7414): 115-120.
    • (2012) Nature , vol.489 , Issue.7414 , pp. 115-120
    • Plechanovová, A.1    Jaffray, E.G.2    Tatham, M.H.3    Naismith, J.H.4    Hay, R.T.5
  • 29
    • 84866858702 scopus 로고    scopus 로고
    • Structure of an E3: E2~Ub complex reveals an allosteric mechanism shared among RING/U-box ligases
    • Pruneda JN, et al. (2012) Structure of an E3: E2~Ub complex reveals an allosteric mechanism shared among RING/U-box ligases. Mol Cell 47(6): 933-942.
    • (2012) Mol Cell , vol.47 , Issue.6 , pp. 933-942
    • Pruneda, J.N.1
  • 30
    • 84881518558 scopus 로고    scopus 로고
    • Mechanism of ubiquitin ligation and lysine prioritization by a HECT E3
    • Kamadurai HB, et al. (2013) Mechanism of ubiquitin ligation and lysine prioritization by a HECT E3. eLife 2: E00828.
    • (2013) ELife , vol.2 , pp. e00828
    • Kamadurai, H.B.1
  • 31
    • 84878900697 scopus 로고    scopus 로고
    • Structure of a ubiquitin-loaded HECT ligase reveals the molecular basis for catalytic priming
    • Maspero E, et al. (2013) Structure of a ubiquitin-loaded HECT ligase reveals the molecular basis for catalytic priming. Nat Struct Mol Biol 20(6): 696-701.
    • (2013) Nat Struct Mol Biol , vol.20 , Issue.6 , pp. 696-701
    • Maspero, E.1
  • 32
    • 66449125689 scopus 로고    scopus 로고
    • Regulation of the RSP5 ubiquitin ligase by an intrinsic ubiquitin-binding site
    • French ME, Kretzmann BR, Hicke L (2009) Regulation of the RSP5 ubiquitin ligase by an intrinsic ubiquitin-binding site. J Biol Chem 284(18): 12071-12079.
    • (2009) J Biol Chem , vol.284 , Issue.18 , pp. 12071-12079
    • French, M.E.1    Kretzmann, B.R.2    Hicke, L.3
  • 33
    • 77949888615 scopus 로고    scopus 로고
    • The ubiquitin binding region of the Smurf HECT domain facilitates polyubiquitylation and binding of ubiquitylated substrates
    • Ogunjimi AA, et al. (2010) The ubiquitin binding region of the Smurf HECT domain facilitates polyubiquitylation and binding of ubiquitylated substrates. J Biol Chem 285(9): 6308-6315.
    • (2010) J Biol Chem , vol.285 , Issue.9 , pp. 6308-6315
    • Ogunjimi, A.A.1
  • 34
    • 77951075391 scopus 로고    scopus 로고
    • Regulation of the polycomb protein Ring1B by selfubiquitination or by E6-AP may have implications to the pathogenesis of Angelman syndrome
    • Zaaroor-Regev D, et al. (2010) Regulation of the polycomb protein Ring1B by selfubiquitination or by E6-AP may have implications to the pathogenesis of Angelman syndrome. Proc Natl Acad Sci USA 107(15): 6788-6793.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.15 , pp. 6788-6793
    • Zaaroor-Regev, D.1
  • 35
    • 0033548432 scopus 로고    scopus 로고
    • Identification of determinants in E2 ubiquitin-conjugating enzymes required for hect E3 ubiquitin-protein ligase interaction
    • Nuber U, Scheffner M (1999) Identification of determinants in E2 ubiquitin-conjugating enzymes required for hect E3 ubiquitin-protein ligase interaction. J Biol Chem 274(11): 7576-7582.
    • (1999) J Biol Chem , vol.274 , Issue.11 , pp. 7576-7582
    • Nuber, U.1    Scheffner, M.2
  • 36
    • 77449105964 scopus 로고    scopus 로고
    • Kinetics of the transfer of ubiquitin from UbcH7 to E6AP
    • Purbeck C, Eletr ZM, Kuhlman B (2010) Kinetics of the transfer of ubiquitin from UbcH7 to E6AP. Biochemistry 49(7): 1361-1363.
    • (2010) Biochemistry , vol.49 , Issue.7 , pp. 1361-1363
    • Purbeck, C.1    Eletr, Z.M.2    Kuhlman, B.3
  • 37
    • 0028898424 scopus 로고
    • Protein ubiquitination involving an E1- E2-E3 enzyme ubiquitin thioester cascade
    • Scheffner M, Nuber U, Huibregtse JM (1995) Protein ubiquitination involving an E1- E2-E3 enzyme ubiquitin thioester cascade. Nature 373(6509): 81-83.
    • (1995) Nature , vol.373 , Issue.6509 , pp. 81-83
    • Scheffner, M.1    Nuber, U.2    Huibregtse, J.M.3
  • 38
    • 79957949190 scopus 로고    scopus 로고
    • UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids
    • Wenzel DM, Lissounov A, Brzovic PS, Klevit RE (2011) UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 474(7349): 105-108.
    • (2011) Nature , vol.474 , Issue.7349 , pp. 105-108
    • Wenzel, D.M.1    Lissounov, A.2    Brzovic, P.S.3    Klevit, R.E.4
  • 39
    • 0141753130 scopus 로고    scopus 로고
    • A conserved catalytic residue in the ubiquitin-conjugating enzyme family
    • Wu PY, et al. (2003) A conserved catalytic residue in the ubiquitin-conjugating enzyme family. EMBO J 22(19): 5241-5250.
    • (2003) EMBO J , vol.22 , Issue.19 , pp. 5241-5250
    • Wu, P.Y.1
  • 40
    • 0027169680 scopus 로고
    • Localization of the E6-AP regions that direct human papillomavirus E6 binding, association with p53, and ubiquitination of associated proteins
    • Huibregtse JM, Scheffner M, Howley PM (1993) Localization of the E6-AP regions that direct human papillomavirus E6 binding, association with p53, and ubiquitination of associated proteins. Mol Cell Biol 13(8): 4918-4927.
    • (1993) Mol Cell Biol , vol.13 , Issue.8 , pp. 4918-4927
    • Huibregtse, J.M.1    Scheffner, M.2    Howley, P.M.3
  • 41
    • 70349243073 scopus 로고    scopus 로고
    • The stability of the human papillomavirus E6 oncoprotein is E6AP dependent
    • Tomaic V, Pim D, Banks L (2009) The stability of the human papillomavirus E6 oncoprotein is E6AP dependent. Virology 393(1): 7-10.
    • (2009) Virology , vol.393 , Issue.1 , pp. 7-10
    • Tomaic, V.1    Pim, D.2    Banks, L.3
  • 42
    • 0033603339 scopus 로고    scopus 로고
    • Identification of HHR23A as a substrate for E6- associated protein-mediated ubiquitination
    • Kumar S, Talis AL, Howley PM (1999) Identification of HHR23A as a substrate for E6- associated protein-mediated ubiquitination. J Biol Chem 274(26): 18785-18792.
    • (1999) J Biol Chem , vol.274 , Issue.26 , pp. 18785-18792
    • Kumar, S.1    Talis, A.L.2    Howley, P.M.3
  • 43
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair A, Finley D, Varshavsky A (1986) In vivo half-life of a protein is a function of its amino-terminal residue. Science 234(4773): 179-186.
    • (1986) Science , vol.234 , Issue.4773 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 44
    • 28944437762 scopus 로고    scopus 로고
    • Ubiquitin fusion technique and related methods
    • Varshavsky A (2005) Ubiquitin fusion technique and related methods. Methods Enzymol 399: 777-799.
    • (2005) Methods Enzymol , vol.399 , pp. 777-799
    • Varshavsky, A.1
  • 45
    • 84878464396 scopus 로고    scopus 로고
    • Role of the ubiquitin ligase E6AP/UBE3A in controlling levels of the synaptic protein Arc
    • Kühnle S, Mothes B, Matentzoglu K, Scheffner M (2013) Role of the ubiquitin ligase E6AP/UBE3A in controlling levels of the synaptic protein Arc. Proc Natl Acad Sci USA 110(22): 8888-8893.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.22 , pp. 8888-8893
    • Kühnle, S.1    Mothes, B.2    Matentzoglu, K.3    Scheffner, M.4
  • 46
    • 29244447753 scopus 로고    scopus 로고
    • Different HECT domain ubiquitin ligases employ distinct mechanisms of polyubiquitin chain synthesis
    • Wang M, Pickart CM (2005) Different HECT domain ubiquitin ligases employ distinct mechanisms of polyubiquitin chain synthesis. EMBO J 24(24): 4324-4333.
    • (2005) EMBO J , vol.24 , Issue.24 , pp. 4324-4333
    • Wang, M.1    Pickart, C.M.2
  • 47
    • 0032525905 scopus 로고    scopus 로고
    • The ubiquitin-protein ligase E6-associated protein (E6-AP) serves as its own substrate
    • Nuber U, Schwarz SE, Scheffner M (1998) The ubiquitin-protein ligase E6-associated protein (E6-AP) serves as its own substrate. Eur J Biochem 254(3): 643-649.
    • (1998) Eur J Biochem , vol.254 , Issue.3 , pp. 643-649
    • Nuber, U.1    Schwarz, S.E.2    Scheffner, M.3
  • 48
    • 0033919402 scopus 로고    scopus 로고
    • Human papillomavirus type 16 E6 induces self-ubiquitination of the E6AP ubiquitin-protein ligase
    • Kao WH, Beaudenon SL, Talis AL, Huibregtse JM, Howley PM (2000) Human papillomavirus type 16 E6 induces self-ubiquitination of the E6AP ubiquitin-protein ligase. J Virol 74(14): 6408-6417.
    • (2000) J Virol , vol.74 , Issue.14 , pp. 6408-6417
    • Kao, W.H.1    Beaudenon, S.L.2    Talis, A.L.3    Huibregtse, J.M.4    Howley, P.M.5
  • 49
    • 84891957449 scopus 로고    scopus 로고
    • The active form of E6-associated protein (E6AP)/UBE3A ubiquitin ligase is an oligomer
    • Ronchi VP, Klein JM, Edwards DJ, Haas AL (2014) The active form of E6-associated protein (E6AP)/UBE3A ubiquitin ligase is an oligomer. J Biol Chem 289(2): 1033-1048.
    • (2014) J Biol Chem , vol.289 , Issue.2 , pp. 1033-1048
    • Ronchi, V.P.1    Klein, J.M.2    Edwards, D.J.3    Haas, A.L.4
  • 50
    • 33846956466 scopus 로고    scopus 로고
    • The role of the ubiquitin ligase E6-AP in human papillomavirus E6-mediated degradation of PDZ domain-containing proteins
    • Kuballa P, Matentzoglu K, ScheffnerM(2007) The role of the ubiquitin ligase E6-AP in human papillomavirus E6-mediated degradation of PDZ domain-containing proteins. J Biol Chem 282(1): 65-71.
    • (2007) J Biol Chem , vol.282 , Issue.1 , pp. 65-71
    • Kuballa, P.1    Matentzoglu, K.2    Scheffner, M.3
  • 51
    • 80052259674 scopus 로고    scopus 로고
    • A spectrophotometric assay for conjugation of ubiquitin and ubiquitin-like proteins
    • Berndsen CE, Wolberger C (2011) A spectrophotometric assay for conjugation of ubiquitin and ubiquitin-like proteins. Anal Biochem 418(1): 102-110.
    • (2011) Anal Biochem , vol.418 , Issue.1 , pp. 102-110
    • Berndsen, C.E.1    Wolberger, C.2
  • 52
    • 0031569842 scopus 로고    scopus 로고
    • The human E6-AP gene (UBE3A) encodes three potential protein isoforms generated by differential splicing
    • Yamamoto Y, Huibregtse JM, Howley PM (1997) The human E6-AP gene (UBE3A) encodes three potential protein isoforms generated by differential splicing. Genomics 41(2): 263-266.
    • (1997) Genomics , vol.41 , Issue.2 , pp. 263-266
    • Yamamoto, Y.1    Huibregtse, J.M.2    Howley, P.M.3
  • 54
    • 21644448222 scopus 로고    scopus 로고
    • Growth suppression induced by downregulation of E6- AP expression in human papillomavirus-positive cancer cell lines depends on p53
    • Hengstermann A, et al. (2005) Growth suppression induced by downregulation of E6- AP expression in human papillomavirus-positive cancer cell lines depends on p53. J Virol 79(14): 9296-9300.
    • (2005) J Virol , vol.79 , Issue.14 , pp. 9296-9300
    • Hengstermann, A.1
  • 55
    • 0032741446 scopus 로고    scopus 로고
    • Structure of an E6AP-UbcH7 complex: Insights into ubiquitination by the E2-E3 enzyme cascade
    • Huang L, et al. (1999) Structure of an E6AP-UbcH7 complex: Insights into ubiquitination by the E2-E3 enzyme cascade. Science 286(5443): 1321-1326.
    • (1999) Science , vol.286 , Issue.5443 , pp. 1321-1326
    • Huang, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.