메뉴 건너뛰기




Volumn 6, Issue 9, 2011, Pages

A ubiquitin independent degradation pathway utilized by a Hepatitis B virus envelope protein to limit antigen presentation

Author keywords

[No Author keywords available]

Indexed keywords

HEPATITIS B VIRUS ENVELOPE PROTEIN; HEPATITIS B VIRUS M PROTEIN; LYSINE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; POLYMER; PROTEASOME; UBIQUITIN; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN; ISOPROTEIN; PEPTIDE; POLYSACCHARIDE;

EID: 80053288136     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0024477     Document Type: Article
Times cited : (12)

References (65)
  • 1
    • 34248997838 scopus 로고    scopus 로고
    • N-glycan structure dictates extension of protein folding or onset of disposal
    • Molinari M, (2007) N-glycan structure dictates extension of protein folding or onset of disposal. Nat Chem Biol 3: 313-320.
    • (2007) Nat Chem Biol , vol.3 , pp. 313-320
    • Molinari, M.1
  • 2
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: endoplasmic reticulum-associated degradation
    • Vembar SS, Brodsky JL, (2008) One step at a time: endoplasmic reticulum-associated degradation. Nat Rev Mol Cell Biol 9: 944-957.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 3
    • 68549106150 scopus 로고    scopus 로고
    • Novel ubiquitin-dependent quality control in the endoplasmic reticulum
    • Feldman M, van der Goot FG, (2009) Novel ubiquitin-dependent quality control in the endoplasmic reticulum. Trends Cell Biol 19: 357-363.
    • (2009) Trends Cell Biol , vol.19 , pp. 357-363
    • Feldman, M.1    van der Goot, F.G.2
  • 5
    • 0027295871 scopus 로고
    • Association of folding intermediates of glycoproteins with calnexin during protein maturation
    • Ou WJ, Cameron PH, Thomas DY, Bergeron JJ, (1993) Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature 364: 771-776.
    • (1993) Nature , vol.364 , pp. 771-776
    • Ou, W.J.1    Cameron, P.H.2    Thomas, D.Y.3    Bergeron, J.J.4
  • 6
    • 74849100640 scopus 로고    scopus 로고
    • Defining the ERAD connection: assembly required
    • Sifers RN, (2009) Defining the ERAD connection: assembly required. Cell Cycle 8: 4026-4027.
    • (2009) Cell Cycle , vol.8 , pp. 4026-4027
    • Sifers, R.N.1
  • 7
    • 43149096666 scopus 로고    scopus 로고
    • The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum
    • Nakatsukasa K, Brodsky JL, (2008) The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum. Traffic 9: 861-870.
    • (2008) Traffic , vol.9 , pp. 861-870
    • Nakatsukasa, K.1    Brodsky, J.L.2
  • 8
    • 0035873704 scopus 로고    scopus 로고
    • 26S proteasomes and immunoproteasomes produce mainly N-extended versions of an antigenic peptide
    • Cascio P, Hilton C, Kisselev AF, Rock KL, Goldberg AL, (2001) 26S proteasomes and immunoproteasomes produce mainly N-extended versions of an antigenic peptide. EMBO J 20: 2357-2366.
    • (2001) EMBO J , vol.20 , pp. 2357-2366
    • Cascio, P.1    Hilton, C.2    Kisselev, A.F.3    Rock, K.L.4    Goldberg, A.L.5
  • 9
    • 0035448296 scopus 로고    scopus 로고
    • Ubiquitination is essential for human cytomegalovirus US11-mediated dislocation of MHC class I molecules from the endoplasmic reticulum to the cytosol
    • Kikkert M, Hassink G, Barel M, Hirsch C, van der Wal FJ, et al. (2001) Ubiquitination is essential for human cytomegalovirus US11-mediated dislocation of MHC class I molecules from the endoplasmic reticulum to the cytosol. Biochem J 358: 369-377.
    • (2001) Biochem J , vol.358 , pp. 369-377
    • Kikkert, M.1    Hassink, G.2    Barel, M.3    Hirsch, C.4    van der Wal, F.J.5
  • 10
    • 0035167960 scopus 로고    scopus 로고
    • Polyubiquitination is required for US11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosol
    • Shamu CE, Flierman D, Ploegh HL, Rapoport TA, Chau V, (2001) Polyubiquitination is required for US11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosol. Mol Biol Cell 12: 2546-2555.
    • (2001) Mol Biol Cell , vol.12 , pp. 2546-2555
    • Shamu, C.E.1    Flierman, D.2    Ploegh, H.L.3    Rapoport, T.A.4    Chau, V.5
  • 11
    • 0036173013 scopus 로고    scopus 로고
    • Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48
    • Jarosch E, Taxis C, Volkwein C, Bordallo J, Finley D, et al. (2002) Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nat Cell Biol 4: 134-139.
    • (2002) Nat Cell Biol , vol.4 , pp. 134-139
    • Jarosch, E.1    Taxis, C.2    Volkwein, C.3    Bordallo, J.4    Finley, D.5
  • 12
    • 0033601349 scopus 로고    scopus 로고
    • The role of multiubiquitination in dislocation and degradation of the alpha subunit of the T cell antigen receptor
    • Yu H, Kopito RR, (1999) The role of multiubiquitination in dislocation and degradation of the alpha subunit of the T cell antigen receptor. J Biol Chem 274: 36852-36858.
    • (1999) J Biol Chem , vol.274 , pp. 36852-36858
    • Yu, H.1    Kopito, R.R.2
  • 13
    • 0038487228 scopus 로고    scopus 로고
    • Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
    • Ye Y, Meyer HH, Rapoport TA, (2003) Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J Cell Biol 162: 71-84.
    • (2003) J Cell Biol , vol.162 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 14
    • 0027023231 scopus 로고
    • Functions of hepatitis B surface proteins
    • Gerlich WH, Heermann KH, Lu X, (1992) Functions of hepatitis B surface proteins. Arch Virol Suppl 4 pp. 129-132.
    • (1992) Arch Virol , Issue.SUPPL. 4 , pp. 129-132
    • Gerlich, W.H.1    Heermann, K.H.2    Lu, X.3
  • 15
    • 0022993023 scopus 로고
    • Demonstration of pre-S polypeptides of hepatitis B virus in infected livers
    • Thung SN, Gerber MA, Kasambalides EJ, Gilja BK, Keh W, et al. (1986) Demonstration of pre-S polypeptides of hepatitis B virus in infected livers. Hepatology 6: 1315-1318.
    • (1986) Hepatology , vol.6 , pp. 1315-1318
    • Thung, S.N.1    Gerber, M.A.2    Kasambalides, E.J.3    Gilja, B.K.4    Keh, W.5
  • 16
    • 41749108854 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in disease pathogenesis
    • Lin JH, Walter P, Yen TS, (2008) Endoplasmic reticulum stress in disease pathogenesis. Annual review of pathology 3: 399-425.
    • (2008) Annual Review of Pathology , vol.3 , pp. 399-425
    • Lin, J.H.1    Walter, P.2    Yen, T.S.3
  • 17
    • 79751523518 scopus 로고    scopus 로고
    • Association of hepatitis B virus pre-S deletions with the development of hepatocellular carcinoma in chronic hepatitis B
    • Yeung P, Wong DK, Lai CL, Fung J, Seto WK, et al. (2011) Association of hepatitis B virus pre-S deletions with the development of hepatocellular carcinoma in chronic hepatitis B. The Journal of infectious diseases 203: 646-654.
    • (2011) The Journal of Infectious Diseases , vol.203 , pp. 646-654
    • Yeung, P.1    Wong, D.K.2    Lai, C.L.3    Fung, J.4    Seto, W.K.5
  • 18
    • 73449131849 scopus 로고    scopus 로고
    • Pre-S2 deletions of hepatitis B virus and hepatocellular carcinoma in children
    • Huang HP, Hsu HY, Chen CL, Ni YH, Wang HY, et al. (2010) Pre-S2 deletions of hepatitis B virus and hepatocellular carcinoma in children. Pediatric research 67: 90-94.
    • (2010) Pediatric Research , vol.67 , pp. 90-94
    • Huang, H.P.1    Hsu, H.Y.2    Chen, C.L.3    Ni, Y.H.4    Wang, H.Y.5
  • 19
    • 70649083901 scopus 로고    scopus 로고
    • Pre-S2 deletion mutants of hepatitis B virus could have an important role in hepatocarcinogenesis in Asian children
    • Abe K, Thung SN, Wu HC, Tran TT, Le Hoang P, et al. (2009) Pre-S2 deletion mutants of hepatitis B virus could have an important role in hepatocarcinogenesis in Asian children. Cancer science 100: 2249-2254.
    • (2009) Cancer Science , vol.100 , pp. 2249-2254
    • Abe, K.1    Thung, S.N.2    Wu, H.C.3    Tran, T.T.4    Le Hoang, P.5
  • 20
    • 56349099754 scopus 로고    scopus 로고
    • Hepatitis B virus pre-S deletion mutations are a risk factor for hepatocellular carcinoma: a matched nested case-control study
    • Fang ZL, Sabin CA, Dong BQ, Wei SC, Chen QY, et al. (2008) Hepatitis B virus pre-S deletion mutations are a risk factor for hepatocellular carcinoma: a matched nested case-control study. J Gen Virol 89: 2882-2890.
    • (2008) J Gen Virol , vol.89 , pp. 2882-2890
    • Fang, Z.L.1    Sabin, C.A.2    Dong, B.Q.3    Wei, S.C.4    Chen, Q.Y.5
  • 21
    • 33745593035 scopus 로고    scopus 로고
    • Hepatitis B virus pre-S mutants, endoplasmic reticulum stress and hepatocarcinogenesis
    • Wang HC, Huang W, Lai MD, Su IJ, (2006) Hepatitis B virus pre-S mutants, endoplasmic reticulum stress and hepatocarcinogenesis. Cancer Sci 97: 683-688.
    • (2006) Cancer Sci , vol.97 , pp. 683-688
    • Wang, H.C.1    Huang, W.2    Lai, M.D.3    Su, I.J.4
  • 22
    • 16244375544 scopus 로고    scopus 로고
    • Hepatitis B virus pre-S2 mutant upregulates cyclin A expression and induces nodular proliferation of hepatocytes
    • Wang HC, Chang WT, Chang WW, Wu HC, Huang W, et al. (2005) Hepatitis B virus pre-S2 mutant upregulates cyclin A expression and induces nodular proliferation of hepatocytes. Hepatology 41: 761-770.
    • (2005) Hepatology , vol.41 , pp. 761-770
    • Wang, H.C.1    Chang, W.T.2    Chang, W.W.3    Wu, H.C.4    Huang, W.5
  • 23
    • 6444242588 scopus 로고    scopus 로고
    • Pre-S mutant surface antigens in chronic hepatitis B virus infection induce oxidative stress and DNA damage
    • Hsieh YH, Su IJ, Wang HC, Chang WW, Lei HY, et al. (2004) Pre-S mutant surface antigens in chronic hepatitis B virus infection induce oxidative stress and DNA damage. Carcinogenesis 25: 2023-2032.
    • (2004) Carcinogenesis , vol.25 , pp. 2023-2032
    • Hsieh, Y.H.1    Su, I.J.2    Wang, H.C.3    Chang, W.W.4    Lei, H.Y.5
  • 24
    • 0345707640 scopus 로고    scopus 로고
    • Different types of ground glass hepatocytes in chronic hepatitis B virus infection contain specific pre-S mutants that may induce endoplasmic reticulum stress
    • Wang HC, Wu HC, Chen CF, Fausto N, Lei HY, et al. (2003) Different types of ground glass hepatocytes in chronic hepatitis B virus infection contain specific pre-S mutants that may induce endoplasmic reticulum stress. Am J Pathol 163: 2441-2449.
    • (2003) Am J Pathol , vol.163 , pp. 2441-2449
    • Wang, H.C.1    Wu, H.C.2    Chen, C.F.3    Fausto, N.4    Lei, H.Y.5
  • 25
    • 0035204472 scopus 로고    scopus 로고
    • Prevalence and significance of hepatitis B virus (HBV) pre-S mutants in serum and liver at different replicative stages of chronic HBV infection
    • Fan YF, Lu CC, Chen WC, Yao WJ, Wang HC, et al. (2001) Prevalence and significance of hepatitis B virus (HBV) pre-S mutants in serum and liver at different replicative stages of chronic HBV infection. Hepatology 33: 277-286.
    • (2001) Hepatology , vol.33 , pp. 277-286
    • Fan, Y.F.1    Lu, C.C.2    Chen, W.C.3    Yao, W.J.4    Wang, H.C.5
  • 26
    • 0027293511 scopus 로고
    • Mutational analysis of the cysteine residues in the hepatitis B virus small envelope protein
    • Mangold CM, Streeck RE, (1993) Mutational analysis of the cysteine residues in the hepatitis B virus small envelope protein. J Virol 67: 4588-4597.
    • (1993) J Virol , vol.67 , pp. 4588-4597
    • Mangold, C.M.1    Streeck, R.E.2
  • 27
    • 0348049829 scopus 로고    scopus 로고
    • Retrograde transport of toxins across the endoplasmic reticulum membrane
    • Lord JM, Deeks E, Marsden CJ, Moore K, Pateman C, et al. (2003) Retrograde transport of toxins across the endoplasmic reticulum membrane. Biochem Soc Trans 31: 1260-1262.
    • (2003) Biochem Soc Trans , vol.31 , pp. 1260-1262
    • Lord, J.M.1    Deeks, E.2    Marsden, C.J.3    Moore, K.4    Pateman, C.5
  • 28
    • 33750220958 scopus 로고    scopus 로고
    • Retrotranslocation of a viral A/B toxin from the yeast endoplasmic reticulum is independent of ubiquitination and ERAD
    • Heiligenstein S, Eisfeld K, Sendzik T, Jimenez-Becker N, Breinig F, et al. (2006) Retrotranslocation of a viral A/B toxin from the yeast endoplasmic reticulum is independent of ubiquitination and ERAD. EMBO J 25: 4717-4727.
    • (2006) EMBO J , vol.25 , pp. 4717-4727
    • Heiligenstein, S.1    Eisfeld, K.2    Sendzik, T.3    Jimenez-Becker, N.4    Breinig, F.5
  • 29
    • 4644318292 scopus 로고    scopus 로고
    • A complex between peptide:N-glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteins
    • Katiyar S, Li G, Lennarz WJ, (2004) A complex between peptide:N-glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteins. Proc Natl Acad Sci U S A 101: 13774-13779.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 13774-13779
    • Katiyar, S.1    Li, G.2    Lennarz, W.J.3
  • 31
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye Y, Meyer HH, Rapoport TA, (2001) The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414: 652-656.
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 32
    • 23044460010 scopus 로고    scopus 로고
    • Role of p97 AAA-ATPase in the retrotranslocation of the cholera toxin A1 chain, a non-ubiquitinated substrate
    • Kothe M, Ye Y, Wagner JS, De Luca HE, Kern E, et al. (2005) Role of p97 AAA-ATPase in the retrotranslocation of the cholera toxin A1 chain, a non-ubiquitinated substrate. J Biol Chem 280: 28127-28132.
    • (2005) J Biol Chem , vol.280 , pp. 28127-28132
    • Kothe, M.1    Ye, Y.2    Wagner, J.S.3    De Luca, H.E.4    Kern, E.5
  • 33
    • 0031023756 scopus 로고    scopus 로고
    • Reduced ubiquitin-dependent degradation of c-Jun after phosphorylation by MAP kinases
    • Musti AM, Treier M, Bohmann D, (1997) Reduced ubiquitin-dependent degradation of c-Jun after phosphorylation by MAP kinases. Science 275: 400-402.
    • (1997) Science , vol.275 , pp. 400-402
    • Musti, A.M.1    Treier, M.2    Bohmann, D.3
  • 34
    • 77949295782 scopus 로고    scopus 로고
    • Lectin-like ERAD players in ER and cytosol
    • Yoshida Y, Tanaka K, (2010) Lectin-like ERAD players in ER and cytosol. Biochim Biophys Acta 1800 pp. 172-180.
    • (2010) Biochim Biophys Acta 1800 , pp. 172-180
    • Yoshida, Y.1    Tanaka, K.2
  • 35
    • 40249088336 scopus 로고    scopus 로고
    • OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
    • Christianson JC, Shaler TA, Tyler RE, Kopito RR, (2008) OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat Cell Biol 10: 272-282.
    • (2008) Nat Cell Biol , vol.10 , pp. 272-282
    • Christianson, J.C.1    Shaler, T.A.2    Tyler, R.E.3    Kopito, R.R.4
  • 36
    • 2542501657 scopus 로고    scopus 로고
    • Ubiquitin ligases and the immune response
    • Liu YC, (2004) Ubiquitin ligases and the immune response. Annu Rev Immunol 22: 81-127.
    • (2004) Annu Rev Immunol , vol.22 , pp. 81-127
    • Liu, Y.C.1
  • 38
    • 79951825002 scopus 로고    scopus 로고
    • Selective role of ubiquitin in MHC class I antigen presentation
    • Huang L, Marvin JM, Tatsis N, Eisenlohr LC, (2011) Selective role of ubiquitin in MHC class I antigen presentation. J Immunol 186: 1904-1908.
    • (2011) J Immunol , vol.186 , pp. 1904-1908
    • Huang, L.1    Marvin, J.M.2    Tatsis, N.3    Eisenlohr, L.C.4
  • 39
    • 0029120173 scopus 로고
    • Rate of antigen degradation by the ubiquitin-proteasome pathway influences MHC class I presentation
    • Grant EP, Michalek MT, Goldberg AL, Rock KL, (1995) Rate of antigen degradation by the ubiquitin-proteasome pathway influences MHC class I presentation. J Immunol 155: 3750-3758.
    • (1995) J Immunol , vol.155 , pp. 3750-3758
    • Grant, E.P.1    Michalek, M.T.2    Goldberg, A.L.3    Rock, K.L.4
  • 40
    • 77249090175 scopus 로고    scopus 로고
    • Antigen processing and presentation
    • Mellman I, Cresswell P, (2010) Antigen processing and presentation. Curr Opin Immunol 22: 78-80.
    • (2010) Curr Opin Immunol , vol.22 , pp. 78-80
    • Mellman, I.1    Cresswell, P.2
  • 41
    • 14044270751 scopus 로고    scopus 로고
    • The impact of misfolding versus targeted degradation on the efficiency of the MHC class I-restricted antigen processing
    • Golovina TN, Morrison SE, Eisenlohr LC, (2005) The impact of misfolding versus targeted degradation on the efficiency of the MHC class I-restricted antigen processing. J Immunol 174: 2763-2769.
    • (2005) J Immunol , vol.174 , pp. 2763-2769
    • Golovina, T.N.1    Morrison, S.E.2    Eisenlohr, L.C.3
  • 42
    • 0026639652 scopus 로고
    • Detection of rare antigen-presenting cells by the lacZ T-cell activation assay suggests an expression cloning strategy for T-cell antigens
    • Karttunen J, Sanderson S, Shastri N, (1992) Detection of rare antigen-presenting cells by the lacZ T-cell activation assay suggests an expression cloning strategy for T-cell antigens. Proc Natl Acad Sci U S A 89: 6020-6024.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 6020-6024
    • Karttunen, J.1    Sanderson, S.2    Shastri, N.3
  • 43
    • 0025806781 scopus 로고
    • Measurement of ligand-induced activation in single viable T cells using the lacZ reporter gene
    • Karttunen J, Shastri N, (1991) Measurement of ligand-induced activation in single viable T cells using the lacZ reporter gene. Proc Natl Acad Sci U S A 88: 3972-3976.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 3972-3976
    • Karttunen, J.1    Shastri, N.2
  • 44
    • 34250194001 scopus 로고    scopus 로고
    • The role of the downstream signal sequences in the maturation of the HBV middle surface glycoprotein: development of a novel therapeutic vaccine candidate
    • Liu Y, Simsek E, Norton P, Sinnathamby G, Philip R, et al. (2007) The role of the downstream signal sequences in the maturation of the HBV middle surface glycoprotein: development of a novel therapeutic vaccine candidate. Virology 365: 10-19.
    • (2007) Virology , vol.365 , pp. 10-19
    • Liu, Y.1    Simsek, E.2    Norton, P.3    Sinnathamby, G.4    Philip, R.5
  • 45
    • 77957939988 scopus 로고    scopus 로고
    • Glucosidase inhibition enhances presentation of de-N-glycosylated hepatitis B virus epitopes by major histocompatibility complex class I in vitro and in woodchucks
    • Norton PA, Menne S, Sinnathamby G, Betesh L, Cote PJ, et al. (2010) Glucosidase inhibition enhances presentation of de-N-glycosylated hepatitis B virus epitopes by major histocompatibility complex class I in vitro and in woodchucks. Hepatology 52: 1242-1250.
    • (2010) Hepatology , vol.52 , pp. 1242-1250
    • Norton, P.A.1    Menne, S.2    Sinnathamby, G.3    Betesh, L.4    Cote, P.J.5
  • 46
    • 33748670056 scopus 로고    scopus 로고
    • Inhibition by woodchuck hepatitis virus of class I major histocompatibility complex presentation on hepatocytes is mediated by virus envelope pre-S2 protein and can be reversed by treatment with gamma interferon
    • Wang J, Michalak TI, (2006) Inhibition by woodchuck hepatitis virus of class I major histocompatibility complex presentation on hepatocytes is mediated by virus envelope pre-S2 protein and can be reversed by treatment with gamma interferon. J Virol 80: 8541-8553.
    • (2006) J Virol , vol.80 , pp. 8541-8553
    • Wang, J.1    Michalak, T.I.2
  • 48
    • 0025980689 scopus 로고
    • Morphogenetic and regulatory effects of mutations in the envelope proteins of an avian hepadnavirus
    • Summers J, Smith PM, Huang MJ, Yu MS, (1991) Morphogenetic and regulatory effects of mutations in the envelope proteins of an avian hepadnavirus. J Virol 65: 1310-1317.
    • (1991) J Virol , vol.65 , pp. 1310-1317
    • Summers, J.1    Smith, P.M.2    Huang, M.J.3    Yu, M.S.4
  • 49
    • 0028334395 scopus 로고
    • Coordinate regulation of replication and virus assembly by the large envelope protein of an avian hepadnavirus
    • Lenhoff RJ, Summers J, (1994) Coordinate regulation of replication and virus assembly by the large envelope protein of an avian hepadnavirus. J Virol 68: 4565-4571.
    • (1994) J Virol , vol.68 , pp. 4565-4571
    • Lenhoff, R.J.1    Summers, J.2
  • 51
    • 34247585533 scopus 로고    scopus 로고
    • Rethinking peptide supply to MHC class I molecules
    • Eisenlohr LC, Huang L, Golovina TN, (2007) Rethinking peptide supply to MHC class I molecules. Nat Rev Immunol 7: 403-410.
    • (2007) Nat Rev Immunol , vol.7 , pp. 403-410
    • Eisenlohr, L.C.1    Huang, L.2    Golovina, T.N.3
  • 52
    • 0034967925 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and proteasome inhibitors
    • Myung J, Kim KB, Crews CM, (2001) The ubiquitin-proteasome pathway and proteasome inhibitors. Med Res Rev 21: 245-273.
    • (2001) Med Res Rev , vol.21 , pp. 245-273
    • Myung, J.1    Kim, K.B.2    Crews, C.M.3
  • 53
    • 58149517677 scopus 로고    scopus 로고
    • Ubiquitin-independent degradation of hepatitis C virus F protein
    • Yuksek K, Chen WL, Chien D, Ou JH, (2009) Ubiquitin-independent degradation of hepatitis C virus F protein. J Virol 83: 612-621.
    • (2009) J Virol , vol.83 , pp. 612-621
    • Yuksek, K.1    Chen, W.L.2    Chien, D.3    Ou, J.H.4
  • 54
    • 78650253267 scopus 로고    scopus 로고
    • Ubiquitylation of an ERAD substrate occurs on multiple types of amino acids
    • Shimizu Y, Okuda-Shimizu Y, Hendershot LM, (2010) Ubiquitylation of an ERAD substrate occurs on multiple types of amino acids. Molecular cell 40: 917-926.
    • (2010) Molecular Cell , vol.40 , pp. 917-926
    • Shimizu, Y.1    Okuda-Shimizu, Y.2    Hendershot, L.M.3
  • 55
    • 3142566639 scopus 로고    scopus 로고
    • Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system
    • Verma R, Oania R, Graumann J, Deshaies RJ, (2004) Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system. Cell 118: 99-110.
    • (2004) Cell , vol.118 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 56
    • 4344560565 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator degradation depends on the lectins Htm1p/EDEM and the Cdc48 protein complex in yeast
    • Gnann A, Riordan JR, Wolf DH, (2004) Cystic fibrosis transmembrane conductance regulator degradation depends on the lectins Htm1p/EDEM and the Cdc48 protein complex in yeast. Mol Biol Cell 15: 4125-4135.
    • (2004) Mol Biol Cell , vol.15 , pp. 4125-4135
    • Gnann, A.1    Riordan, J.R.2    Wolf, D.H.3
  • 57
    • 0030817978 scopus 로고    scopus 로고
    • Cytosolic degradation of T-cell receptor alpha chains by the proteasome
    • Yu H, Kaung G, Kobayashi S, Kopito RR, (1997) Cytosolic degradation of T-cell receptor alpha chains by the proteasome. J Biol Chem 272: 20800-20804.
    • (1997) J Biol Chem , vol.272 , pp. 20800-20804
    • Yu, H.1    Kaung, G.2    Kobayashi, S.3    Kopito, R.R.4
  • 58
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • Lilley BN, Ploegh HL, (2004) A membrane protein required for dislocation of misfolded proteins from the ER. Nature 429: 834-840.
    • (2004) Nature , vol.429 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 59
    • 33846008398 scopus 로고    scopus 로고
    • Derlin-1 promotes the efficient degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) and CFTR folding mutants
    • Sun F, Zhang R, Gong X, Geng X, Drain PF, et al. (2006) Derlin-1 promotes the efficient degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) and CFTR folding mutants. J Biol Chem 281: 36856-36863.
    • (2006) J Biol Chem , vol.281 , pp. 36856-36863
    • Sun, F.1    Zhang, R.2    Gong, X.3    Geng, X.4    Drain, P.F.5
  • 60
    • 2442629457 scopus 로고    scopus 로고
    • Calnexin, calreticulin, and ERp57: teammates in glycoprotein folding
    • Ellgaard L, Frickel EM, (2003) Calnexin, calreticulin, and ERp57: teammates in glycoprotein folding. Cell Biochem Biophys 39: 223-247.
    • (2003) Cell Biochem Biophys , vol.39 , pp. 223-247
    • Ellgaard, L.1    Frickel, E.M.2
  • 61
    • 0037470410 scopus 로고    scopus 로고
    • Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle
    • Molinari M, Calanca V, Galli C, Lucca P, Paganetti P, (2003) Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle. Science 299: 1397-1400.
    • (2003) Science , vol.299 , pp. 1397-1400
    • Molinari, M.1    Calanca, V.2    Galli, C.3    Lucca, P.4    Paganetti, P.5
  • 62
    • 0031970586 scopus 로고    scopus 로고
    • Cloning and characterization of three isoforms of OS-9 cDNA and expression of the OS-9 gene in various human tumor cell lines
    • Kimura Y, Nakazawa M, Yamada M, (1998) Cloning and characterization of three isoforms of OS-9 cDNA and expression of the OS-9 gene in various human tumor cell lines. J Biochem 123: 876-882.
    • (1998) J Biochem , vol.123 , pp. 876-882
    • Kimura, Y.1    Nakazawa, M.2    Yamada, M.3
  • 63
    • 0017710978 scopus 로고
    • Characteristics of a human cell line transformed by DNA from human adenovirus type 5
    • Graham FL, Smiley J, Russell WC, Nairn R, (1977) Characteristics of a human cell line transformed by DNA from human adenovirus type 5. The Journal of general virology 36: 59-74.
    • (1977) The Journal of General Virology , vol.36 , pp. 59-74
    • Graham, F.L.1    Smiley, J.2    Russell, W.C.3    Nairn, R.4
  • 64
    • 58549087715 scopus 로고    scopus 로고
    • Inhibition of cellular alpha-glucosidases results in increased presentation of hepatitis B virus glycoprotein-derived peptides by MHC class I
    • Simsek E, Sinnathamby G, Block TM, Liu Y, Philip R, et al. (2009) Inhibition of cellular alpha-glucosidases results in increased presentation of hepatitis B virus glycoprotein-derived peptides by MHC class I. Virology 384: 12-15.
    • (2009) Virology , vol.384 , pp. 12-15
    • Simsek, E.1    Sinnathamby, G.2    Block, T.M.3    Liu, Y.4    Philip, R.5
  • 65
    • 70349673721 scopus 로고    scopus 로고
    • Priming and activation of human ovarian and breast cancer-specific CD8+ T cells by polyvalent Listeria monocytogenes-based vaccines
    • Sinnathamby G, Lauer P, Zerfass J, Hanson B, Karabudak A, et al. (2009) Priming and activation of human ovarian and breast cancer-specific CD8+ T cells by polyvalent Listeria monocytogenes-based vaccines. J Immunother 32: 856-869.
    • (2009) J Immunother , vol.32 , pp. 856-869
    • Sinnathamby, G.1    Lauer, P.2    Zerfass, J.3    Hanson, B.4    Karabudak, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.