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Volumn 273, Issue , 2004, Pages 29-85

Immune evasion by adenovirus E3 proteins: Exploitation of intracellular trafficking pathways

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; COAT PROTEIN; MEMBRANE PROTEIN; NEF PROTEIN; VIRUS PROTEIN;

EID: 0141569454     PISSN: 0070217X     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-3-662-05599-1_2     Document Type: Review
Times cited : (77)

References (185)
  • 1
    • 0033831421 scopus 로고    scopus 로고
    • Viral mechanisms of immune evasion
    • Alcami A, Koszinowski UH (2000) Viral mechanisms of immune evasion. Immunol Today 21:447-455
    • (2000) Immunol Today , vol.21 , pp. 447-455
    • Alcami, A.1    Koszinowski, U.H.2
  • 3
    • 0031692336 scopus 로고    scopus 로고
    • The caveolae membrane system
    • Anderson RG (1998) The caveolae membrane system. Annu Rev Biochem 67:199-225
    • (1998) Annu Rev Biochem , vol.67 , pp. 199-225
    • Anderson, R.G.1
  • 4
    • 0030979789 scopus 로고    scopus 로고
    • A retention signal necessary and sufficient for Golgi localization maps to the cytoplasmic tail of a Bunyaviridae (Uukuniemi virus) membrane glycoprotein
    • Andersson AM, Melin L, Bean A, Pettersson RF (1997) A retention signal necessary and sufficient for Golgi localization maps to the cytoplasmic tail of a Bunyaviridae (Uukuniemi virus) membrane glycoprotein. J Virol 71:4717-4727
    • (1997) J Virol , vol.71 , pp. 4717-4727
    • Andersson, A.M.1    Melin, L.2    Bean, A.3    Pettersson, R.F.4
  • 5
    • 0033591357 scopus 로고    scopus 로고
    • Protein targeting to endoplasmic reticulum by dilysine signals involves direct retention in addition to retrieval
    • Andersson H, Kappeler F, Hauri HP (1999) Protein targeting to endoplasmic reticulum by dilysine signals involves direct retention in addition to retrieval. J Biol Chem 274:15080-15084
    • (1999) J Biol Chem , vol.274 , pp. 15080-15084
    • Andersson, H.1    Kappeler, F.2    Hauri, H.P.3
  • 6
    • 0023194102 scopus 로고
    • Reduced allorecognition of adenovirus-2 infected cells
    • Andersson M, McMichael A, Peterson PA (1987) Reduced allorecognition of adenovirus-2 infected cells. J Immunol 138:3960-3966
    • (1987) J Immunol , vol.138 , pp. 3960-3966
    • Andersson, M.1    McMichael, A.2    Peterson, P.A.3
  • 7
    • 0022403592 scopus 로고
    • Impaired intracellular transport of class I MHC antigens as a possible means for adenoviruses to evade immune surveillance
    • Andersson M, Pääbo S, Nilsson T, Peterson PA (1985) Impaired intracellular transport of class I MHC antigens as a possible means for adenoviruses to evade immune surveillance. Cell 43:215-222
    • (1985) Cell , vol.43 , pp. 215-222
    • Andersson, M.1    Pääbo, S.2    Nilsson, T.3    Peterson, P.A.4
  • 8
    • 0033988228 scopus 로고    scopus 로고
    • Adenovirus type 37 uses sialic acid as a cellular receptor
    • Arnberg N, Edlund K, Kidd AH, Wadell G (2000) Adenovirus type 37 uses sialic acid as a cellular receptor. J Virol 74:42-48
    • (2000) J Virol , vol.74 , pp. 42-48
    • Arnberg, N.1    Edlund, K.2    Kidd, A.H.3    Wadell, G.4
  • 9
    • 0029040014 scopus 로고
    • Efficient endosomal localization of major histocompatibility complex class II-invariant chain complexes requires multimerization of the invariant chain targeting sequence
    • Arneson LS, Miller J (1995) Efficient endosomal localization of major histocompatibility complex class II-invariant chain complexes requires multimerization of the invariant chain targeting sequence. J Cell Biol 129:1217-1228
    • (1995) J Cell Biol , vol.129 , pp. 1217-1228
    • Arneson, L.S.1    Miller, J.2
  • 10
    • 0031052040 scopus 로고    scopus 로고
    • TGN38 and its orthologues: Roles in post-TGN vesicle formation and maintenance of TGN morphology
    • Banting G, Ponnambalam S (1997) TGN38 and its orthologues: roles in post-TGN vesicle formation and maintenance of TGN morphology. Biochim Biophys Acta 1355:209-217
    • (1997) Biochim Biophys Acta , vol.1355 , pp. 209-217
    • Banting, G.1    Ponnambalam, S.2
  • 12
    • 0034189373 scopus 로고    scopus 로고
    • Traffic COPs of the early secretory pathway
    • Barlowe C (2000) Traffic COPs of the early secretory pathway. Traffic 1:371-377
    • (2000) Traffic , vol.1 , pp. 371-377
    • Barlowe, C.1
  • 13
    • 0033535617 scopus 로고    scopus 로고
    • A novel Rab6-interacting domain defines a family of Golgi-targeted coiled-coil proteins
    • Barr FA (1999) A novel Rab6-interacting domain defines a family of Golgi-targeted coiled-coil proteins. Curr Biol 9:381-384
    • (1999) Curr Biol , vol.9 , pp. 381-384
    • Barr, F.A.1
  • 14
    • 0029921413 scopus 로고    scopus 로고
    • Sequence of the immunoregulatory early region-3 and flanking sequences of adenovirus type-35
    • Basler CF, Droguett G, Horwitz MS (1996) Sequence of the immunoregulatory early region-3 and flanking sequences of adenovirus type-35. Gene 170:249-254
    • (1996) Gene , vol.170 , pp. 249-254
    • Basler, C.F.1    Droguett, G.2    Horwitz, M.S.3
  • 15
    • 0028195011 scopus 로고
    • Association of human class I MHC alleles with the adenovirus E3/19K protein
    • Beier DC, Cox JH, Vining DR, Cresswell P, Engelhard VH (1994) Association of human class I MHC alleles with the adenovirus E3/19K protein. J Immunol 152:3862-3872
    • (1994) J Immunol , vol.152 , pp. 3862-3872
    • Beier, D.C.1    Cox, J.H.2    Vining, D.R.3    Cresswell, P.4    Engelhard, V.H.5
  • 17
    • 0033136705 scopus 로고    scopus 로고
    • Cutting edge: Adenovirus E19 has two mechanisms for affecting class I MHC expression
    • Bennett EM, Bennink JR, Yewdell JW, Brodsky FM (1999) Cutting edge: adenovirus E19 has two mechanisms for affecting class I MHC expression. J Immunol 162:5049-5052
    • (1999) J Immunol , vol.162 , pp. 5049-5052
    • Bennett, E.M.1    Bennink, J.R.2    Yewdell, J.W.3    Brodsky, F.M.4
  • 19
    • 0035424543 scopus 로고    scopus 로고
    • NK cells and NKT cells in innate defense against viral infections
    • Biron CA, Brossay L (2001) NK cells and NKT cells in innate defense against viral infections. Curr Opin Immunol 13:458-464
    • (2001) Curr Opin Immunol , vol.13 , pp. 458-464
    • Biron, C.A.1    Brossay, L.2
  • 20
    • 0035954254 scopus 로고    scopus 로고
    • Membrane traffic: How do GGAs fit in with the adaptors?
    • Black MW, Pelham HR (2001) Membrane traffic: How do GGAs fit in with the adaptors? Curr Biol 11:R460-R462
    • (2001) Curr Biol , vol.11
    • Black, M.W.1    Pelham, H.R.2
  • 21
    • 0036346242 scopus 로고    scopus 로고
    • The novel early region 3 protein E3/49K is specifically expressed by adenoviruses of subgenus D: Implications for epidemic keratokonjunctivitis and adenovirus evolution
    • Blusch J, Deryckere F, Windheim M, Ruzsics Z, Arnberg N, Adrian T, Burgert H-G (2002) The novel early region 3 protein E3/49K is specifically expressed by adenoviruses of subgenus D: Implications for epidemic keratokonjunctivitis and adenovirus evolution. Virology 296:94-106
    • (2002) Virology , vol.296 , pp. 94-106
    • Blusch, J.1    Deryckere, F.2    Windheim, M.3    Ruzsics, Z.4    Arnberg, N.5    Adrian, T.6    Burgert, H.-G.7
  • 22
    • 0029907407 scopus 로고    scopus 로고
    • Sequence requirements for the recognition of tyrosine-based endocytic signals by clathrin AP-2 complexes
    • Boll W, Ohno H, Songyang Z, Rapoport I, Cantley LC, Bonifacino JS, Kirchhausen T (1996) Sequence requirements for the recognition of tyrosine-based endocytic signals by clathrin AP-2 complexes. EMBO J 15:5789-5795
    • (1996) EMBO J , vol.15 , pp. 5789-5795
    • Boll, W.1    Ohno, H.2    Songyang, Z.3    Rapoport, I.4    Cantley, L.C.5    Bonifacino, J.S.6    Kirchhausen, T.7
  • 23
    • 0033620656 scopus 로고    scopus 로고
    • Molecular bases for the recognition of tyrosine-based sorting signals
    • Bonifacino JS, Dell-Angelica EC (1999) Molecular bases for the recognition of tyrosine-based sorting signals. J Cell Biol 145:923-926
    • (1999) J Cell Biol , vol.145 , pp. 923-926
    • Bonifacino, J.S.1    Dell-Angelica, E.C.2
  • 24
    • 0030682420 scopus 로고    scopus 로고
    • Translocation of proteins across the endoplasmic reticulum membrane
    • Brodsky JL (1998) Translocation of proteins across the endoplasmic reticulum membrane. Int Rev Cytol 178:277-328
    • (1998) Int Rev Cytol , vol.178 , pp. 277-328
    • Brodsky, J.L.1
  • 25
    • 0030880893 scopus 로고    scopus 로고
    • Expression of gp19K increases the persistence of transgene expression from an adenovirus vector in the mouse lung and liver
    • Bruder JT, Jie T, McVey DL, Kovesdi I (1997) Expression of gp19K increases the persistence of transgene expression from an adenovirus vector in the mouse lung and liver. J Virol 71:7623-7628
    • (1997) J Virol , vol.71 , pp. 7623-7628
    • Bruder, J.T.1    Jie, T.2    McVey, D.L.3    Kovesdi, I.4
  • 26
    • 0029983121 scopus 로고    scopus 로고
    • Subversion of the MHC class I antigen-presentation pathway by adenoviruses and herpes simplex viruses
    • Burgert H-G (1996) Subversion of the MHC class I antigen-presentation pathway by adenoviruses and herpes simplex viruses. Trends Microbiol 4:107-112
    • (1996) Trends Microbiol , vol.4 , pp. 107-112
    • Burgert, H.-G.1
  • 27
    • 0033834534 scopus 로고    scopus 로고
    • Immunomodulatory functions encoded by the E3 transcription unit of adenoviruses
    • Burgert H-G, Blusch JH (2000) Immunomodulatory functions encoded by the E3 transcription unit of adenoviruses. Virus Genes 21:13-25
    • (2000) Virus Genes , vol.21 , pp. 13-25
    • Burgert, H.-G.1    Blusch, J.H.2
  • 28
    • 0021972750 scopus 로고
    • An adenovirus type 2 glycoprotein blocks cell surface expression of human histocompatibility class I antigens
    • Burgert H-G, Kvist S (1985) An adenovirus type 2 glycoprotein blocks cell surface expression of human histocompatibility class I antigens. Cell 41:987-997
    • (1985) Cell , vol.41 , pp. 987-997
    • Burgert, H.-G.1    Kvist, S.2
  • 29
    • 0023377880 scopus 로고
    • The E3/19K protein of adenovirus type 2 binds to the domains of histocompatibility antigens required for CTL recognition
    • Burgert H-G, Kvist S (1987) The E3/19K protein of adenovirus type 2 binds to the domains of histocompatibility antigens required for CTL recognition. EMBO J 6:2019-2026
    • (1987) EMBO J , vol.6 , pp. 2019-2026
    • Burgert, H.-G.1    Kvist, S.2
  • 30
    • 0023154590 scopus 로고
    • "E3/19K" protein of adenovirus type 2 inhibits lysis of cytolytic T lymphocytes by blocking cell-surface expression of histocompatibility class I antigens
    • Burgert H-G, Maryanski JL, Kvist S (1987) "E3/19K" protein of adenovirus type 2 inhibits lysis of cytolytic T lymphocytes by blocking cell-surface expression of histocompatibility class I antigens. Proc Natl Acad Sci USA 84:1356-1360
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 1356-1360
    • Burgert, H.-G.1    Maryanski, J.L.2    Kvist, S.3
  • 32
    • 0033617185 scopus 로고    scopus 로고
    • A cytoplasmic sequence in human tyrosinase defines a second class of di-leucine-based sorting signals for late endosomal and lysosomal delivery
    • Calvo PA, Frank DW, Bieler BM, Berson JF, Marks MS (1999) A cytoplasmic sequence in human tyrosinase defines a second class of di-leucine-based sorting signals for late endosomal and lysosomal delivery. J Biol Chem 274:12780-12789
    • (1999) J Biol Chem , vol.274 , pp. 12780-12789
    • Calvo, P.A.1    Frank, D.W.2    Bieler, B.M.3    Berson, J.F.4    Marks, M.S.5
  • 33
    • 0024557043 scopus 로고
    • Epidermal growth factor receptor is down-regulated by a 10,400 MW protein encoded by the E3 region of adenovirus
    • Carlin CR, Tollefson AE, Brady HA, Hoffman BL, Wold WS (1989) Epidermal growth factor receptor is down-regulated by a 10,400 MW protein encoded by the E3 region of adenovirus. Cell 57:135-144
    • (1989) Cell , vol.57 , pp. 135-144
    • Carlin, C.R.1    Tollefson, A.E.2    Brady, H.A.3    Hoffman, B.L.4    Wold, W.S.5
  • 35
    • 0000864308 scopus 로고    scopus 로고
    • Systematic mutational analysis of the cation-independent mannose 6-phosphate/insulin-like growth factor II receptor cytoplasmic domain. An acidic cluster containing a key aspartate is important for function in lysosomal enzyme sorting
    • Chen HJ, Yuan J, Lobel P (1997) Systematic mutational analysis of the cation-independent mannose 6- phosphate/insulin-like growth factor II receptor cytoplasmic domain. An acidic cluster containing a key aspartate is important for function in lysosomal enzyme sorting. J Biol Chem 272:7003-7012
    • (1997) J Biol Chem , vol.272 , pp. 7003-7012
    • Chen, H.J.1    Yuan, J.2    Lobel, P.3
  • 37
    • 0025635559 scopus 로고
    • Transferrin receptor internalization sequence YXRF implicates a tight turn as the structural recognition motif for endocytosis
    • Collawn JF, Stangel M, Kuhn LA, Esekogwu V, Jing SQ, Trowbridge IS, Tainer JA (1990) Transferrin receptor internalization sequence YXRF implicates a tight turn as the structural recognition motif for endocytosis. Cell 63:1061-1072
    • (1990) Cell , vol.63 , pp. 1061-1072
    • Collawn, J.F.1    Stangel, M.2    Kuhn, L.A.3    Esekogwu, V.4    Jing, S.Q.5    Trowbridge, I.S.6    Tainer, J.A.7
  • 39
    • 0028181745 scopus 로고
    • Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
    • Cosson P, Letourneur F (1994) Coatomer interaction with di-lysine endoplasmic reticulum retention motifs. Science 263:1629-1631
    • (1994) Science , vol.263 , pp. 1629-1631
    • Cosson, P.1    Letourneur, F.2
  • 40
    • 0025836816 scopus 로고
    • Retention of adenovirus E19 glycoprotein in the endoplasmic reticulum is essential to its ability to block antigen presentation
    • Cox JH, Bennink JR, Yewdell JW (1991) Retention of adenovirus E19 glycoprotein in the endoplasmic reticulum is essential to its ability to block antigen presentation. J Exp Med 174:1629-1637
    • (1991) J Exp Med , vol.174 , pp. 1629-1637
    • Cox, J.H.1    Bennink, J.R.2    Yewdell, J.W.3
  • 41
    • 0025020492 scopus 로고
    • Antigen presentation requires transport of MHC class I molecules from the endoplasmic reticulum
    • Cox JH, Yewdell JW, Eisenlohr LC, Johnson PR, Bennink JR (1990) Antigen presentation requires transport of MHC class I molecules from the endoplasmic reticulum. Science 247:715-718
    • (1990) Science , vol.247 , pp. 715-718
    • Cox, J.H.1    Yewdell, J.W.2    Eisenlohr, L.C.3    Johnson, P.R.4    Bennink, J.R.5
  • 42
    • 0033790332 scopus 로고    scopus 로고
    • E3-13. 7 Integral membrane proteins encoded by human adenoviruses alter epidermal growth factor receptor trafficking by interacting directly with receptors in early endosomes
    • Crooks D, Kil SJ, McCaffery JM, Carlin C (2000) E3-13.7 integral membrane proteins encoded by human adenoviruses alter epidermal growth factor receptor trafficking by interacting directly with receptors in early endosomes. Mol Biol Cell 11:3559-3572
    • (2000) Mol Biol Cell , vol.11 , pp. 3559-3572
    • Crooks, D.1    Kil, S.J.2    McCaffery, J.M.3    Carlin, C.4
  • 43
    • 0035341464 scopus 로고    scopus 로고
    • PACS-1 binding to adaptors is required for acidic cluster motif- mediated protein traffic
    • Crump CM, Xiang Y, Thomas L, Gu F, Austin C, Tooze SA, Thomas G (2001) PACS-1 binding to adaptors is required for acidic cluster motif- mediated protein traffic. EMBO J 20:2191-2201
    • (2001) EMBO J , vol.20 , pp. 2191-2201
    • Crump, C.M.1    Xiang, Y.2    Thomas, L.3    Gu, F.4    Austin, C.5    Tooze, S.A.6    Thomas, G.7
  • 45
    • 0032942436 scopus 로고    scopus 로고
    • To die or not to die-the quest of the TRAIL receptors
    • Degli-Esposti M (1999) To die or not to die-the quest of the TRAIL receptors. J Leukoc Biol 65:535-542
    • (1999) J Leukoc Biol , vol.65 , pp. 535-542
    • Degli-Esposti, M.1
  • 46
    • 0033007616 scopus 로고    scopus 로고
    • Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the beta 3A subunit of the AP-3 adaptor
    • Dell'Angelica EC, Shotelersuk V, Aguilar RC, Gahl WA, Bonifacino JS (1999) Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the beta 3A subunit of the AP-3 adaptor. Mol Cell 3:11-21
    • (1999) Mol Cell , vol.3 , pp. 11-21
    • Dell'Angelica, E.C.1    Shotelersuk, V.2    Aguilar, R.C.3    Gahl, W.A.4    Bonifacino, J.S.5
  • 47
    • 0029927634 scopus 로고    scopus 로고
    • Early region 3 of adenovirus type 19 (subgroup D) encodes an HLA- binding protein distinct from that of subgroups B and C
    • Deryckere F, Burgert H-G (1996) Early region 3 of adenovirus type 19 (subgroup D) encodes an HLA- binding protein distinct from that of subgroups B and C. J Virol 70:2832-2841
    • (1996) J Virol , vol.70 , pp. 2832-2841
    • Deryckere, F.1    Burgert, H.-G.2
  • 48
    • 0029961666 scopus 로고    scopus 로고
    • A di-leucine motif and an upstream serine in the interleukin-6 (IL-6) signal transducer gp130 mediate ligand-induced endocytosis and down- regulation of the IL-6 receptor
    • Dittrich E, Haft CR, Muys L, Heinrich PC, Graeve L (1996) A di-leucine motif and an upstream serine in the interleukin-6 (IL-6) signal transducer gp130 mediate ligand-induced endocytosis and down- regulation of the IL-6 receptor. J Biol Chem 271:5487-5494
    • (1996) J Biol Chem , vol.271 , pp. 5487-5494
    • Dittrich, E.1    Haft, C.R.2    Muys, L.3    Heinrich, P.C.4    Graeve, L.5
  • 49
  • 50
    • 0029125671 scopus 로고
    • Prolonged survival of pancreatic islet allografts mediated by adenovirus immunoregulatory transgenes
    • Efrat S, Fejer G, Brownlee M, Horwitz MS (1995) Prolonged survival of pancreatic islet allografts mediated by adenovirus immunoregulatory transgenes. Proc Natl Acad Sci USA 92:6947-6951
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6947-6951
    • Efrat, S.1    Fejer, G.2    Brownlee, M.3    Horwitz, M.S.4
  • 51
    • 0034996021 scopus 로고    scopus 로고
    • A single internalization signal from the dileucine family is critical for constitutive endocytosis of the type II TGF-beta receptor
    • Ehrlich M, Shmuely A, Henis YI (2001) A single internalization signal from the dileucine family is critical for constitutive endocytosis of the type II TGF-beta receptor. J Cell Sci 114:1777-1786
    • (2001) J Cell Sci , vol.114 , pp. 1777-1786
    • Ehrlich, M.1    Shmuely, A.2    Henis, Y.I.3
  • 52
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: Quality control in the secretory pathway
    • Ellgaard L, Molinari M, Helenius A (1999) Setting the standards: quality control in the secretory pathway. Science 286:1882-1888
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 53
    • 0032544013 scopus 로고    scopus 로고
    • The adenovirus E3/10.4K-145K proteins down-modulate the apoptosis receptor Fas/Apo-1 by inducing its internalization
    • Elsing A, Burgert H-G (1998) The adenovirus E3/10.4K-14.5K proteins down-modulate the apoptosis receptor Fas/Apo-1 by inducing its internalization. Proc Natl Acad Sci USA 95:10072-10077
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 10072-10077
    • Elsing, A.1    Burgert, H.-G.2
  • 54
    • 0033568213 scopus 로고    scopus 로고
    • A tyrosine-based sorting signal in the beta2 integrin cytoplasmic domain mediates its recycling to the plasma membrane and is required for ligand-supported migration
    • Fabbri M, Fumagalli L, Bossi G, Bianchi E, Bender JR, Pardi R (1999) A tyrosine-based sorting signal in the beta2 integrin cytoplasmic domain mediates its recycling to the plasma membrane and is required for ligand-supported migration. EMBO J 18:4915-4925
    • (1999) EMBO J , vol.18 , pp. 4915-4925
    • Fabbri, M.1    Fumagalli, L.2    Bossi, G.3    Bianchi, E.4    Bender, J.R.5    Pardi, R.6
  • 55
    • 0027251025 scopus 로고
    • Novel proteins associated with MHC class I antigens in cells expressing the adenovirus protein E3/19K
    • Feuerbach D, Burgert H-G (1993) Novel proteins associated with MHC class I antigens in cells expressing the adenovirus protein E3/19K. EMBO J 12:3153-3161
    • (1993) EMBO J , vol.12 , pp. 3153-3161
    • Feuerbach, D.1    Burgert, H.-G.2
  • 56
    • 0028141978 scopus 로고
    • Identification of amino acids within the MHC molecule important for the interaction with the adenovirus protein E3/19K
    • Feuerbach D, Etteldorf S, Ebenau-Jehle C, Abastado JP, Madden D, Burgert H-G (1994) Identification of amino acids within the MHC molecule important for the interaction with the adenovirus protein E3/19K. J Immunol 153:1626-1636
    • (1994) J Immunol , vol.153 , pp. 1626-1636
    • Feuerbach, D.1    Etteldorf, S.2    Ebenau-Jehle, C.3    Abastado, J.P.4    Madden, D.5    Burgert, H.-G.6
  • 57
    • 0027996952 scopus 로고
    • Identification of class I MHC regions which bind to the adenovirus E3-19K protein
    • Flomenberg P, Gutierrez E, Hogan KT (1994) Identification of class I MHC regions which bind to the adenovirus E3-19K protein. Mol Immunol 31:1277-1284
    • (1994) Mol Immunol , vol.31 , pp. 1277-1284
    • Flomenberg, P.1    Gutierrez, E.2    Hogan, K.T.3
  • 58
    • 0029793258 scopus 로고    scopus 로고
    • Human adenovirus-specific CD8+ T-cell responses are not inhibited by E3-19K in the presence of gamma interferon
    • Flomenberg P, Piaskowski V, Truitt RL, Casper JT (1996) Human adenovirus-specific CD8+ T-cell responses are not inhibited by E3-19K in the presence of gamma interferon. J Virol 70:6314-6322
    • (1996) J Virol , vol.70 , pp. 6314-6322
    • Flomenberg, P.1    Piaskowski, V.2    Truitt, R.L.3    Casper, J.T.4
  • 59
    • 0032981423 scopus 로고    scopus 로고
    • Identification of a di-leucine motif within the C terminus domain of the Menkes disease protein that mediates endocytosis from the plasma membrane
    • Francis MJ, Jones EE, Levy ER, Martin RL, Ponnambalam S, Monaco AP (1999) Identification of a di-leucine motif within the C terminus domain of the Menkes disease protein that mediates endocytosis from the plasma membrane. J Cell Sci 112:1721-1732
    • (1999) J Cell Sci , vol.112 , pp. 1721-1732
    • Francis, M.J.1    Jones, E.E.2    Levy, E.R.3    Martin, R.L.4    Ponnambalam, S.5    Monaco, A.P.6
  • 60
    • 0025165899 scopus 로고
    • The endoplasmic reticulum retention signal of the E3/19K protein of adenovirus type 2 consists of three separate amino acid segments at the carboxy terminus
    • Gabathuler R, Kvist S (1990) The endoplasmic reticulum retention signal of the E3/ 19K protein of adenovirus type 2 consists of three separate amino acid segments at the carboxy terminus. J Cell Biol 111:1803-1810
    • (1990) J Cell Biol , vol.111 , pp. 1803-1810
    • Gabathuler, R.1    Kvist, S.2
  • 62
    • 0035811033 scopus 로고    scopus 로고
    • Antigen presentation subverted: Structure of the human cytomegalovirus protein US2 bound to the class I molecule HLA-A2
    • Gewurz BE, Gaudet R, Tortorella D, Wang EW, Ploegh HL, Wiley DC (2001) Antigen presentation subverted: Structure of the human cytomegalovirus protein US2 bound to the class I molecule HLA-A2. Proc Natl Acad Sci USA 98:6794-6799
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6794-6799
    • Gewurz, B.E.1    Gaudet, R.2    Tortorella, D.3    Wang, E.W.4    Ploegh, H.L.5    Wiley, D.C.6
  • 64
    • 0032433851 scopus 로고    scopus 로고
    • The curious status of the Golgi apparatus
    • Glick BS, Malhotra V (1998) The curious status of the Golgi apparatus. Cell 95:883-889
    • (1998) Cell , vol.95 , pp. 883-889
    • Glick, B.S.1    Malhotra, V.2
  • 65
    • 0034565949 scopus 로고    scopus 로고
    • HIV-1 Nef: A critical factor in viral-induced pathogenesis
    • Greenway AL, Holloway G, McPhee DA (2000) HIV-1 Nef: a critical factor in viral-induced pathogenesis. Adv Pharmacol 48:299-343
    • (2000) Adv Pharmacol , vol.48 , pp. 299-343
    • Greenway, A.L.1    Holloway, G.2    McPhee, D.A.3
  • 66
    • 0033030397 scopus 로고    scopus 로고
    • Biogenesis of transport intermediates in the endocytic pathway
    • Gu F, Gruenberg J (1999) Biogenesis of transport intermediates in the endocytic pathway. FEBS Lett 452:61-66
    • (1999) FEBS Lett , vol.452 , pp. 61-66
    • Gu, F.1    Gruenberg, J.2
  • 67
    • 0034097041 scopus 로고    scopus 로고
    • CD8+ T cell effector mechanisms in resistance to infection
    • Harty JT, Tvinnereim AR, White DW (2000) CD8+ T cell effector mechanisms in resistance to infection. Annu Rev Immunol 18:275-308
    • (2000) Annu Rev Immunol , vol.18 , pp. 275-308
    • Harty, J.T.1    Tvinnereim, A.R.2    White, D.W.3
  • 69
    • 0032503232 scopus 로고    scopus 로고
    • Adenovirus death protein, a transmembrane protein encoded in the E3 region, is palmitoylated at the cytoplasmic tail
    • Hausmann J, Ortmann D, Witt E, Veit M, Seidel W (1998) Adenovirus death protein, a transmembrane protein encoded in the E3 region, is palmitoylated at the cytoplasmic tail. Virology 244:343-351
    • (1998) Virology , vol.244 , pp. 343-351
    • Hausmann, J.1    Ortmann, D.2    Witt, E.3    Veit, M.4    Seidel, W.5
  • 70
    • 0029014412 scopus 로고
    • Region E3 of subgroup B human adenoviruses encodes a 16-kilodalton membrane protein that may be a distant analog of the E3-67K protein of subgroup C adenoviruses
    • Hawkins LK, Wilson-Rawls J, Wold WS (1995) Region E3 of subgroup B human adenoviruses encodes a 16-kilodalton membrane protein that may be a distant analog of the E3-6.7K protein of subgroup C adenoviruses. J Virol 69:4292-4298
    • (1995) J Virol , vol.69 , pp. 4292-4298
    • Hawkins, L.K.1    Wilson-Rawls, J.2    Wold, W.S.3
  • 71
    • 0029130156 scopus 로고
    • The E3-20.5K membrane protein of subgroup B human adenoviruses contains O-linked and complex N-linked oligosaccharides
    • Hawkins LK, Wold WS (1995) The E3-20.5K membrane protein of subgroup B human adenoviruses contains O-linked and complex N-linked oligosaccharides. Virology 210:335-344
    • (1995) Virology , vol.210 , pp. 335-344
    • Hawkins, L.K.1    Wold, W.S.2
  • 72
    • 0033166078 scopus 로고    scopus 로고
    • Recognition of sorting signals by clathrin adaptors
    • Heilker R, Spiess M, Crottet P (1999) Recognition of sorting signals by clathrin adaptors. Bioessays 21:558-567
    • (1999) Bioessays , vol.21 , pp. 558-567
    • Heilker, R.1    Spiess, M.2    Crottet, P.3
  • 73
    • 0027328712 scopus 로고
    • Deletion mutation analysis of the adenovirus type 2 E3-gp19K protein: Identification of sequences within the endoplasmic reticulum lumenal domain that are required for class I antigen binding and protection from adenovirus-specific cytotoxic T lymphocytes
    • Hermiston TW, Tripp RA, Sparer T, Gooding LR, Wold WS (1993) Deletion mutation analysis of the adenovirus type 2 E3-gp19K protein: identification of sequences within the endoplasmic reticulum lumenal domain that are required for class I antigen binding and protection from adenovirus-specific cytotoxic T lymphocytes. J Virol 67:5289-5298
    • (1993) J Virol , vol.67 , pp. 5289-5298
    • Hermiston, T.W.1    Tripp, R.A.2    Sparer, T.3    Gooding, L.R.4    Wold, W.S.5
  • 74
    • 0033106369 scopus 로고    scopus 로고
    • Gettin' down with ubiquitin: Turning off cell-surface receptors, transporters and channels
    • Hicke L (1999) Gettin' down with ubiquitin: turning off cell-surface receptors, transporters and channels. Trends Cell Biol 9:107-112
    • (1999) Trends Cell Biol , vol.9 , pp. 107-112
    • Hicke, L.1
  • 75
    • 0034526495 scopus 로고    scopus 로고
    • Dynamin and its role in membrane fission
    • Hinshaw JE (2000) Dynamin and its role in membrane fission. Annu Rev Cell Dev Biol 16:483-519
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 483-519
    • Hinshaw, J.E.1
  • 76
    • 0028356907 scopus 로고
    • Adenovirus E3 protein causes constitutively internalized epidermal growth factor receptors to accumulate in a prelysosomal compartment, resulting in enhanced degradation
    • Hoffman P, Carlin C (1994) Adenovirus E3 protein causes constitutively internalized epidermal growth factor receptors to accumulate in a prelysosomal compartment, resulting in enhanced degradation. Mol Cell Biol 14:3695-3706
    • (1994) Mol Cell Biol , vol.14 , pp. 3695-3706
    • Hoffman, P.1    Carlin, C.2
  • 77
    • 0039109678 scopus 로고    scopus 로고
    • A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3
    • Höning S, Sandoval IV, von Figura K (1998) A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3. EMBO J 17:1304-1314
    • (1998) EMBO J , vol.17 , pp. 1304-1314
    • Höning, S.1    Sandoval, I.V.2    Von Figura, K.3
  • 78
    • 0035916010 scopus 로고    scopus 로고
    • Adenovirus immunoregulatory genes and their cellular targets
    • Horwitz MS (2001) Adenovirus immunoregulatory genes and their cellular targets. Virology 279:1-8
    • (2001) Virology , vol.279 , pp. 1-8
    • Horwitz, M.S.1
  • 79
    • 0028200044 scopus 로고
    • A di-leucine motif mediates endocytosis and basolateral sorting of macrophage IgG Fc receptors in MDCK cells
    • Hunziker W, Fumey C (1994) A di-leucine motif mediates endocytosis and basolateral sorting of macrophage IgG Fc receptors in MDCK cells. EMBO J 13:2963-2967
    • (1994) EMBO J , vol.13 , pp. 2963-2967
    • Hunziker, W.1    Fumey, C.2
  • 80
    • 0030988482 scopus 로고    scopus 로고
    • Insertion of the adenoviral E3 region into a recombinant viral vector prevents antiviral humoral and cellular immune responses and permits long-term gene expression
    • Ilan Y, Droguett G, Chowdhury NR, Li Y, Sengupta K, Thummala NR, Davidson A, Chowdhury JR, Horwitz MS (1997) Insertion of the adenoviral E3 region into a recombinant viral vector prevents antiviral humoral and cellular immune responses and permits long-term gene expression. Proc Natl Acad Sci USA 94:2587-2592
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2587-2592
    • Ilan, Y.1    Droguett, G.2    Chowdhury, N.R.3    Li, Y.4    Sengupta, K.5    Thummala, N.R.6    Davidson, A.7    Chowdhury, J.R.8    Horwitz, M.S.9
  • 81
    • 0025184422 scopus 로고
    • Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum
    • Jackson MR, Nilsson T, Peterson PA (1990) Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum. EMBO J 9:3153-3162
    • (1990) EMBO J , vol.9 , pp. 3153-3162
    • Jackson, M.R.1    Nilsson, T.2    Peterson, P.A.3
  • 82
    • 0027538121 scopus 로고
    • Retrieval of transmembrane proteins to the endoplasmic reticulum
    • Jackson MR, Nilsson T, Peterson PA (1993) Retrieval of transmembrane proteins to the endoplasmic reticulum. J Cell Biol 121:317-333
    • (1993) J Cell Biol , vol.121 , pp. 317-333
    • Jackson, M.R.1    Nilsson, T.2    Peterson, P.A.3
  • 83
    • 0030474309 scopus 로고    scopus 로고
    • Transferrin receptor containing the SDYQRL motif of TGN38 causes a reorganization of the recycling compartment but is not targeted to the TGN
    • Johnson AO, Ghosh RN, Dunn KW, Garippa R, Park J, Mayor S, Maxfield FR, McGraw TE (1996) Transferrin receptor containing the SDYQRL motif of TGN38 causes a reorganization of the recycling compartment but is not targeted to the TGN. J Cell Biol 135:1749-1762
    • (1996) J Cell Biol , vol.135 , pp. 1749-1762
    • Johnson, A.O.1    Ghosh, R.N.2    Dunn, K.W.3    Garippa, R.4    Park, J.5    Mayor, S.6    Maxfield, F.R.7    McGraw, T.E.8
  • 84
    • 0029969098 scopus 로고    scopus 로고
    • Human cytomegalovirus US3 impairs transport and maturation of major histocompatibility complex class I heavy chains
    • Jones TR, Wiertz EJ, Sun L, Fish KN, Nelson JA, Ploegh HL (1996) Human cytomegalovirus US3 impairs transport and maturation of major histocompatibility complex class I heavy chains. Proc Natl Acad Sci USA 93:11327-11333
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11327-11333
    • Jones, T.R.1    Wiertz, E.J.2    Sun, L.3    Fish, K.N.4    Nelson, J.A.5    Ploegh, H.L.6
  • 85
    • 0035147424 scopus 로고    scopus 로고
    • Multicolour imaging of post-Golgi sorting and trafficking in live cells
    • Keller P, Toomre D, Diaz E, White J, Simons K (2001) Multicolour imaging of post-Golgi sorting and trafficking in live cells. Nat Cell Biol 3:140-149
    • (2001) Nat Cell Biol , vol.3 , pp. 140-149
    • Keller, P.1    Toomre, D.2    Diaz, E.3    White, J.4    Simons, K.5
  • 86
    • 0033847398 scopus 로고    scopus 로고
    • EGF receptor residues leu(679), leu(680) mediate selective sorting of ligand-receptor complexes in early endosomal compartments
    • Kil SJ, Carlin C (2000) EGF receptor residues leu(679), leu(680) mediate selective sorting of ligand-receptor complexes in early endosomal compartments. J Cell Physiol 185:47-60
    • (2000) J Cell Physiol , vol.185 , pp. 47-60
    • Kil, S.J.1    Carlin, C.2
  • 87
    • 0000414462 scopus 로고    scopus 로고
    • A leucine-based determinant in the epidermal growth factor receptor juxtamembrane domain is required for the efficient transport of ligand- receptor complexes to lysosomes
    • Kil SJ, Hobert M, Carlin C (1999) A leucine-based determinant in the epidermal growth factor receptor juxtamembrane domain is required for the efficient transport of ligand- receptor complexes to lysosomes. J Biol Chem 274:3141-3150
    • (1999) J Biol Chem , vol.274 , pp. 3141-3150
    • Kil, S.J.1    Hobert, M.2    Carlin, C.3
  • 88
    • 0033280324 scopus 로고    scopus 로고
    • Adaptors for clathrin-mediated traffic
    • Kirchhausen T (1999) Adaptors for clathrin-mediated traffic. Annu Rev Cell Dev Biol 15:705-732
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 705-732
    • Kirchhausen, T.1
  • 90
    • 0034572830 scopus 로고    scopus 로고
    • Three ways to make a vesicle
    • Kirchhausen T (2000b) Three ways to make a vesicle. Nat Rev Mol Cell Biol 1:187-198
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 187-198
    • Kirchhausen, T.1
  • 91
    • 0033535542 scopus 로고    scopus 로고
    • A novel Golgi-localisation domain shared by a class of coiled-coil peripheral membrane proteins
    • Kjer-Nielsen L, Teasdale RD, van Vliet C, Gleeson PA (1999) A novel Golgi-localisation domain shared by a class of coiled-coil peripheral membrane proteins. Curr Biol 9:385-388
    • (1999) Curr Biol , vol.9 , pp. 385-388
    • Kjer-Nielsen, L.1    Teasdale, R.D.2    Van Vliet, C.3    Gleeson, P.A.4
  • 92
    • 0033938963 scopus 로고    scopus 로고
    • Transport between ER and Golgi
    • Klumperman J (2000) Transport between ER and Golgi. Curr Opin Cell Biol 12:445-449
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 445-449
    • Klumperman, J.1
  • 93
  • 94
    • 0028154008 scopus 로고
    • Down-regulation of HLA antigens by the adenovirus type 2 E3/19K protein in a T-lymphoma cell line
    • Kôrner H, Burgert HG (1994) Down-regulation of HLA antigens by the adenovirus type 2 E3/19K protein in a T-lymphoma cell line. J Virol 68:1442-1448
    • (1994) J Virol , vol.68 , pp. 1442-1448
    • Kôrner, H.1    Burgert, H.G.2
  • 95
    • 0027439702 scopus 로고
    • Structurally related class I and class II receptor protein tyrosine kinases are down-regulated by the same E3 protein coded for by human group C adenoviruses
    • Kuivinen E, Hoffman BL, Hoffman PA, Carlin CR (1993) Structurally related class I and class II receptor protein tyrosine kinases are down-regulated by the same E3 protein coded for by human group C adenoviruses. J Cell Biol 120:1271-1279
    • (1993) J Cell Biol , vol.120 , pp. 1271-1279
    • Kuivinen, E.1    Hoffman, B.L.2    Hoffman, P.A.3    Carlin, C.R.4
  • 96
    • 0018256968 scopus 로고
    • Molecular association between transplantation antigens and a cell surface antigen in an adenovirus-transformed cell line
    • Kvist S, Östberg L, Persson H, Philipson L, Peterson PA (1978) Molecular association between transplantation antigens and a cell surface antigen in an adenovirus-transformed cell line. Proc Natl Acad Sci USA 75:5674-5678
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 5674-5678
    • Kvist, S.1    Östberg, L.2    Persson, H.3    Philipson, L.4    Peterson, P.A.5
  • 97
    • 0032491411 scopus 로고    scopus 로고
    • The mammalian AP-3 adaptor-like complex mediates the intracellular transport of lysosomal membrane glycoproteins
    • Le Borgne R, Alconada A, Bauer U, Hoflack B (1998) The mammalian AP-3 adaptor-like complex mediates the intracellular transport of lysosomal membrane glycoproteins. J Biol Chem 273:29451-29461
    • (1998) J Biol Chem , vol.273 , pp. 29451-29461
    • Le Borgne, R.1    Alconada, A.2    Bauer, U.3    Hoflack, B.4
  • 98
    • 0026772733 scopus 로고
    • A novel di-leucine motif and a tyrosine-based motif independently mediate lysosomal targeting and endocytosis of CD3 chains
    • Letourneur F, Klausner RD (1992) A novel di-leucine motif and a tyrosine-based motif independently mediate lysosomal targeting and endocytosis of CD3 chains. Cell 69:1143-1157
    • (1992) Cell , vol.69 , pp. 1143-1157
    • Letourneur, F.1    Klausner, R.D.2
  • 99
    • 0025289981 scopus 로고
    • The ERD2 gene determines the specificity of the luminal ER protein retention system
    • Lewis MJ, Sweet DJ, Pelham HR (1990) The ERD2 gene determines the specificity of the luminal ER protein retention system. Cell 61:1359-1363
    • (1990) Cell , vol.61 , pp. 1359-1363
    • Lewis, M.J.1    Sweet, D.J.2    Pelham, H.R.3
  • 100
    • 0034691598 scopus 로고    scopus 로고
    • Identification and characterization of a 30 K protein (Ad4E3-30 K) encoded by the E3 region of human adenovirus type 4
    • Li Y, Wold WS (2000) Identification and characterization of a 30 K protein (Ad4E3-30 K) encoded by the E3 region of human adenovirus type 4. Virology 273:127-138
    • (2000) Virology , vol.273 , pp. 127-138
    • Li, Y.1    Wold, W.S.2
  • 101
    • 0030685122 scopus 로고    scopus 로고
    • Tyrosine-dependent basolateral sorting signals are distinct from tyrosine-dependent internalization signals
    • Lin S, Naim HY, Roth MG (1997) Tyrosine-dependent basolateral sorting signals are distinct from tyrosine-dependent internalization signals. J Biol Chem 272:26300-26305
    • (1997) J Biol Chem , vol.272 , pp. 26300-26305
    • Lin, S.1    Naim, H.Y.2    Roth, M.G.3
  • 103
    • 0028113010 scopus 로고
    • The cytoplasmic tail of mouse hepatitis virus M protein is essential but not sufficient for its retention in the Golgi complex
    • Locker JK, Klumperman J, Oorschot V, Horzinek MC, Geuze HJ, Rottier PJ (1994) The cytoplasmic tail of mouse hepatitis virus M protein is essential but not sufficient for its retention in the Golgi complex. J Biol Chem 269:28263-28269
    • (1994) J Biol Chem , vol.269 , pp. 28263-28269
    • Locker, J.K.1    Klumperman, J.2    Oorschot, V.3    Horzinek, M.C.4    Geuze, H.J.5    Rottier, P.J.6
  • 104
    • 0033041588 scopus 로고    scopus 로고
    • Immune evasion by adenoviruses
    • Mahr JA, Gooding LR (1999) Immune evasion by adenoviruses. Immunol Rev 168:121-130
    • (1999) Immunol Rev , vol.168 , pp. 121-130
    • Mahr, J.A.1    Gooding, L.R.2
  • 105
    • 0030003317 scopus 로고    scopus 로고
    • Protein targeting by tyrosine- and di-leucine-based signals: Evidence for distinct saturable components
    • Marks MS, Woodruff L, Ohno H, Bonifacino JS (1996) Protein targeting by tyrosine- and di-leucine-based signals: evidence for distinct saturable components. J Cell Biol 135:341-354
    • (1996) J Cell Biol , vol.135 , pp. 341-354
    • Marks, M.S.1    Woodruff, L.2    Ohno, H.3    Bonifacino, J.S.4
  • 106
    • 0033538549 scopus 로고    scopus 로고
    • Vesicular tubular clusters between the ER and Golgi mediate concentration of soluble secretory proteins by exclusion from COPI- coated vesicles
    • Martinez-Menarguez JA, Geuze HJ, Slot JW, Klumperman J (1999) Vesicular tubular clusters between the ER and Golgi mediate concentration of soluble secretory proteins by exclusion from COPI- coated vesicles. Cell 98:81-90
    • (1999) Cell , vol.98 , pp. 81-90
    • Martinez-Menarguez, J.A.1    Geuze, H.J.2    Slot, J.W.3    Klumperman, J.4
  • 107
    • 0030022935 scopus 로고    scopus 로고
    • A casein kinase II phosphorylation site in the cytoplasmic domain of the cation -dependent mannose 6-phosphate receptor determines the high affinity interaction of the AP-1 Golgi assembly proteins with membranes
    • Mauxion F, Le Borgne R, Munier-Lehmann H, Hoflack B (1996) A casein kinase II phosphorylation site in the cytoplasmic domain of the cation -dependent mannose 6-phosphate receptor determines the high affinity interaction of the AP-1 Golgi assembly proteins with membranes. J Biol Chem 271:2171-2178
    • (1996) J Biol Chem , vol.271 , pp. 2171-2178
    • Mauxion, F.1    Le Borgne, R.2    Munier-Lehmann, H.3    Hoflack, B.4
  • 108
    • 0026802151 scopus 로고
    • The nudeotide sequence of adenovirus type 11 early 3 region: Comparison of genome type Ad11p and Ad11a
    • Mei YF, Wadell G (1992) The nudeotide sequence of adenovirus type 11 early 3 region: comparison of genome type Ad11p and Ad11a. Virology 191:125-133
    • (1992) Virology , vol.191 , pp. 125-133
    • Mei, Y.F.1    Wadell, G.2
  • 109
    • 0034614647 scopus 로고    scopus 로고
    • The road taken: Past and future foundations of membrane traffic
    • Mellman I, Warren G (2000) The road taken: past and future foundations of membrane traffic. Cell 100:99-112
    • (2000) Cell , vol.100 , pp. 99-112
    • Mellman, I.1    Warren, G.2
  • 110
    • 0034657033 scopus 로고    scopus 로고
    • mu1A-adaptin-deficient mice: Lethality, loss of AP-1 binding and rerouting of mannose 6-phosphate receptors
    • Meyer C, Zizioli D, Lausmann S, Eskelinen EL, Hamann J, Saftig P, von Figura K, Schu P (2000) mu1A-adaptin-deficient mice: lethality, loss of AP-1 binding and rerouting of mannose 6-phosphate receptors. EMBO J 19:2193-2203
    • (2000) EMBO J , vol.19 , pp. 2193-2203
    • Meyer, C.1    Zizioli, D.2    Lausmann, S.3    Eskelinen, E.L.4    Hamann, J.5    Saftig, P.6    Von Figura, K.7    Schu, P.8
  • 111
    • 0033059994 scopus 로고    scopus 로고
    • Bi-cycling the furin pathway: From TGN localization to pathogen activation and embryogenesis
    • Molloy SS, Anderson ED, Jean F, Thomas G (1999) Bi-cycling the furin pathway: from TGN localization to pathogen activation and embryogenesis. Trends Cell Biol 9:28-35
    • (1999) Trends Cell Biol , vol.9 , pp. 28-35
    • Molloy, S.S.1    Anderson, E.D.2    Jean, F.3    Thomas, G.4
  • 112
    • 0035951401 scopus 로고    scopus 로고
    • Protein sorting upon exit from the endoplasmic reticulum
    • Muniz M, Morsomme P, Riezman H (2001) Protein sorting upon exit from the endoplasmic reticulum. Cell 104:313-320
    • (2001) Cell , vol.104 , pp. 313-320
    • Muniz, M.1    Morsomme, P.2    Riezman, H.3
  • 113
    • 0031976015 scopus 로고    scopus 로고
    • Localization of proteins to the Golgi apparatus
    • Munro S (1998) Localization of proteins to the Golgi apparatus. Trends Cell Biol 8:11-15
    • (1998) Trends Cell Biol , vol.8 , pp. 11-15
    • Munro, S.1
  • 114
    • 0033535585 scopus 로고    scopus 로고
    • The GRIP domain-a novel Golgi-targeting domain found in several coiled-coil proteins
    • Munro S, Nichols BJ (1999) The GRIP domain-a novel Golgi-targeting domain found in several coiled-coil proteins. Curr Biol 9:377-380
    • (1999) Curr Biol , vol.9 , pp. 377-380
    • Munro, S.1    Nichols, B.J.2
  • 115
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • Nagata S (1997) Apoptosis by death factor. Cell 88:355-365
    • (1997) Cell , vol.88 , pp. 355-365
    • Nagata, S.1
  • 116
    • 0034663422 scopus 로고    scopus 로고
    • Cell receptors involved in adenovirus entry
    • Nemerow GR (2000) Cell receptors involved in adenovirus entry. Virology 274:1-4
    • (2000) Virology , vol.274 , pp. 1-4
    • Nemerow, G.R.1
  • 117
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H, Engelbrecht J, Brunak S, von Heijne G (1997) Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 10:1-6
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 119
    • 0024314706 scopus 로고
    • Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum
    • Nilsson T, Jackson M, Peterson PA (1989) Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum. Cell 58:707-718
    • (1989) Cell , vol.58 , pp. 707-718
    • Nilsson, T.1    Jackson, M.2    Peterson, P.A.3
  • 120
    • 0032476017 scopus 로고    scopus 로고
    • The medium subunits of adaptor complexes recognize distinct but overlapping sets of tyrosine-based sorting signals
    • Ohno H, Aguilar RC, Yeh D, Taura D, Saito T, Bonifacino JS (1998) The medium subunits of adaptor complexes recognize distinct but overlapping sets of tyrosine-based sorting signals. J Biol Chem 273:25915-25921
    • (1998) J Biol Chem , vol.273 , pp. 25915-25921
    • Ohno, H.1    Aguilar, R.C.2    Yeh, D.3    Taura, D.4    Saito, T.5    Bonifacino, J.S.6
  • 121
    • 0029826535 scopus 로고    scopus 로고
    • Structural determinants of interaction of tyrosine-based sorting signals with the adaptor medium chains
    • Ohno H, Fournier MC, Poy G, Bonifacino JS (1996) Structural determinants of interaction of tyrosine-based sorting signals with the adaptor medium chains. J Biol Chem 271:29009-29015
    • (1996) J Biol Chem , vol.271 , pp. 29009-29015
    • Ohno, H.1    Fournier, M.C.2    Poy, G.3    Bonifacino, J.S.4
  • 122
    • 0032514874 scopus 로고    scopus 로고
    • A structural explanation for the recognition of tyrosine-based endocytotic signals
    • Owen DJ, Evans PR (1998) A structural explanation for the recognition of tyrosine-based endocytotic signals. Science 282:1327-1332
    • (1998) Science , vol.282 , pp. 1327-1332
    • Owen, D.J.1    Evans, P.R.2
  • 123
    • 0022859809 scopus 로고
    • Adenoviruses of subgenera B, C, D, and E modulate cell-surface expression of major histocompatibility complex class I antigens
    • Pääbo S, Nilsson T, Peterson PA (1986a) Adenoviruses of subgenera B, C, D, and E modulate cell-surface expression of major histocompatibility complex class I antigens. Proc Natl Acad Sci USA 83:9665-9669
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 9665-9669
    • Pääbo, S.1    Nilsson, T.2    Peterson, P.A.3
  • 124
    • 0020568902 scopus 로고
    • Association between transplantation antigens and a viral membrane protein synthesized from a mammalian expression vector
    • Päábo S, Weber F, Kämpe O, Schaffner W, Peterson PA (1983) Association between transplantation antigens and a viral membrane protein synthesized from a mammalian expression vector. Cell 33:445-453
    • (1983) Cell , vol.33 , pp. 445-453
    • Päábo, S.1    Weber, F.2    Kämpe, O.3    Schaffner, W.4    Peterson, P.A.5
  • 125
    • 0022760180 scopus 로고
    • Structural and functional dissection of an MHC class I antigen-binding adenovirus glycoprotein
    • Páäbo S, Weber F, Nilsson T, Schaffner W, Peterson PA (1986b) Structural and functional dissection of an MHC class I antigen-binding adenovirus glycoprotein. EMBO J 5:1921-1927
    • (1986) EMBO J , vol.5 , pp. 1921-1927
    • Páäbo, S.1    Weber, F.2    Nilsson, T.3    Schaffner, W.4    Peterson, P.A.5
  • 126
    • 0031895637 scopus 로고    scopus 로고
    • Mechanisms of MHC class I-restricted antigen processing
    • Pamer E, Cresswell P (1998) Mechanisms of MHC class I-restricted antigen processing. Annu Rev Immunol 16:323-358
    • (1998) Annu Rev Immunol , vol.16 , pp. 323-358
    • Pamer, E.1    Cresswell, P.2
  • 127
    • 0034664730 scopus 로고    scopus 로고
    • The debate about transport in the Golgi-two sides of the same coin?
    • Pelham HR, Rothman JE (2000) The debate about transport in the Golgi-two sides of the same coin? Cell 102:713-719
    • (2000) Cell , vol.102 , pp. 713-719
    • Pelham, H.R.1    Rothman, J.E.2
  • 128
    • 0031730641 scopus 로고    scopus 로고
    • A C-terminal di-leucine is required for localization of the Menkes protein in the trans-Golgi network
    • Petris MJ, Camakaris J, Greenough M, LaFontaine S, Mercer JF (1998) A C-terminal di-leucine is required for localization of the Menkes protein in the trans-Golgi network. Hum Mol Genet 7:2063-2071
    • (1998) Hum Mol Genet , vol.7 , pp. 2063-2071
    • Petris, M.J.1    Camakaris, J.2    Greenough, M.3    LaFontaine, S.4    Mercer, J.F.5
  • 129
    • 0033130103 scopus 로고    scopus 로고
    • Transport-vesicle targeting: Tethers before SNAREs
    • Pfeffer SR (1999) Transport-vesicle targeting: tethers before SNAREs. Nat Cell Biol 1: E17-E22
    • (1999) Nat Cell Biol , vol.1
    • Pfeffer, S.R.1
  • 130
    • 0035051976 scopus 로고    scopus 로고
    • Living in oblivion: HIV immune evasion
    • Piguet V, Trono D (2001) Living in oblivion: HIV immune evasion. Semin Immunol 13:51-57
    • (2001) Semin Immunol , vol.13 , pp. 51-57
    • Piguet, V.1    Trono, D.2
  • 131
    • 0033776709 scopus 로고    scopus 로고
    • HIV-1 Nef protein binds to the cellular protein PACS-1 to downregulate class I major histocompatibility complexes
    • Piguet V, Wan L, Borel C, Mangasarian A, Demaurex N, Thomas G, Trono D (2000) HIV-1 Nef protein binds to the cellular protein PACS-1 to downregulate class I major histocompatibility complexes. Nat Cell Biol 2:163-167
    • (2000) Nat Cell Biol , vol.2 , pp. 163-167
    • Piguet, V.1    Wan, L.2    Borel, C.3    Mangasarian, A.4    Demaurex, N.5    Thomas, G.6    Trono, D.7
  • 134
    • 0033558051 scopus 로고    scopus 로고
    • A cytomegalovirus glycoprotein re-routes MHC class I complexes to lysosomes for degradation
    • Reusch U, Muranyi W, Lucin P, Burgert H-G, Hengel H, Koszinowski UH (1999) A cytomegalovirus glycoprotein re-routes MHC class I complexes to lysosomes for degradation. EMBO J 18:1081-1091
    • (1999) EMBO J , vol.18 , pp. 1081-1091
    • Reusch, U.1    Muranyi, W.2    Lucin, P.3    Burgert, H.-G.4    Hengel, H.5    Koszinowski, U.H.6
  • 135
    • 0032524316 scopus 로고    scopus 로고
    • Molecular basis of lysosomal enzyme recognition: Three dimensional structure of the cation-dependent mannose 6-phosphate receptor
    • Roberts DL, Weix DJ, Dahms NM, Kim J-JP (1998) Molecular basis of lysosomal enzyme recognition: Three dimensional structure of the cation-dependent mannose 6-phosphate receptor. Cell 93:639-648
    • (1998) Cell , vol.93 , pp. 639-648
    • Roberts, D.L.1    Weix, D.J.2    Dahms, N.M.3    Kim, J.-J.P.4
  • 137
    • 0033179221 scopus 로고    scopus 로고
    • Glycans in post-Golgi apical targeting: Sorting signals or structural props?
    • Rodriguez-Boulan E, Gonzalez A (1999) Glycans in post-Golgi apical targeting: sorting signals or structural props? Trends Cell Biol 9:291-294
    • (1999) Trends Cell Biol , vol.9 , pp. 291-294
    • Rodriguez-Boulan, E.1    Gonzalez, A.2
  • 138
    • 0033933026 scopus 로고    scopus 로고
    • Bi-directional trafficking between the trans-Golgi network and the endosomal/lysosomal system
    • Rohn WM, Rouille Y, Waguri S, Hoflack B (2000) Bi-directional trafficking between the trans-Golgi network and the endosomal/lysosomal system. J Cell Sci 113:2093-2101
    • (2000) J Cell Sci , vol.113 , pp. 2093-2101
    • Rohn, W.M.1    Rouille, Y.2    Waguri, S.3    Hoflack, B.4
  • 139
    • 0029670902 scopus 로고    scopus 로고
    • The targeting of Lamp1 to lysosomes is dependent on the spacing of its cytoplasmic tail tyrosine sorting motif relative to the membrane
    • Rohrer J, Schweizer A, Russell D, Kornfeld S (1996) The targeting of Lamp1 to lysosomes is dependent on the spacing of its cytoplasmic tail tyrosine sorting motif relative to the membrane. J Cell Biol 132:565-576
    • (1996) J Cell Biol , vol.132 , pp. 565-576
    • Rohrer, J.1    Schweizer, A.2    Russell, D.3    Kornfeld, S.4
  • 140
    • 0031855694 scopus 로고    scopus 로고
    • Efficient trafficking of TGN38 from the endosome to the trans-Golgi network requires a free hydroxyl group at position 331 in the cytosolic domain
    • Roquemore EP, Banting G (1998) Efficient trafficking of TGN38 from the endosome to the trans-Golgi network requires a free hydroxyl group at position 331 in the cytosolic domain. Mol Biol Cell 9:2125-2144
    • (1998) Mol Biol Cell , vol.9 , pp. 2125-2144
    • Roquemore, E.P.1    Banting, G.2
  • 141
    • 0034667997 scopus 로고    scopus 로고
    • Adenovirus E1A oncogene expression in tumor cells enhances killing by TNF-related apoptosis-inducing ligand
    • Routes J, Ryan S, Clase A, Miura T, Kuhl A, Potter T, Cook J (2000) Adenovirus E1A oncogene expression in tumor cells enhances killing by TNF-related apoptosis-inducing ligand. J Immunol 165:4522-4527
    • (2000) J Immunol , vol.165 , pp. 4522-4527
    • Routes, J.1    Ryan, S.2    Clase, A.3    Miura, T.4    Kuhl, A.5    Potter, T.6    Cook, J.7
  • 142
    • 0033756217 scopus 로고    scopus 로고
    • Update on adenovirus and its vectors
    • Russell WC (2000) Update on adenovirus and its vectors. J Gen Virol 81:2573-2604
    • (2000) J Gen Virol , vol.81 , pp. 2573-2604
    • Russell, W.C.1
  • 143
    • 0034704132 scopus 로고    scopus 로고
    • Distinct reading of different structural determinants modulates the dileucine-mediated transport steps of the lysosomal membrane protein LIMPII and the insulin-sensitive glucose transporter GLUT4
    • Sandoval IV, Martinez-Arca S, Valdueza J, Palacios S, Holman GD (2000) Distinct reading of different structural determinants modulates the dileucine-mediated transport steps of the lysosomal membrane protein LIMPII and the insulin-sensitive glucose transporter GLUT4. J Biol Chem 275:39874-39885
    • (2000) J Biol Chem , vol.275 , pp. 39874-39885
    • Sandoval, I.V.1    Martinez-Arca, S.2    Valdueza, J.3    Palacios, S.4    Holman, G.D.5
  • 144
    • 0027064711 scopus 로고
    • The E3-11.6K protein of adenovirus is an Asn-glycosylated integral membrane protein that localizes to the nuclear membrane
    • Scaria A, Tollefson AE, Saha SK, Wold WS (1992) The E3-11.6K protein of adenovirus is an Asn-glycosylated integral membrane protein that localizes to the nuclear membrane. Virology 191:743-753
    • (1992) Virology , vol.191 , pp. 743-753
    • Scaria, A.1    Tollefson, A.E.2    Saha, S.K.3    Wold, W.S.4
  • 145
    • 0030943737 scopus 로고    scopus 로고
    • Heterologous expression of adenovirus E3-gp19K in an Ela-deleted adenovirus vector inhibits MHC I expression in vitro, but does not prolong transgene expression in vivo
    • Schowalter DB, Tubb JC, Liu M, Wilson CB, Kay MA (1997) Heterologous expression of adenovirus E3-gp19K in an Ela-deleted adenovirus vector inhibits MHC I expression in vitro, but does not prolong transgene expression in vivo. Gene Ther 4:351-360
    • (1997) Gene Ther , vol.4 , pp. 351-360
    • Schowalter, D.B.1    Tubb, J.C.2    Liu, M.3    Wilson, C.B.4    Kay, M.A.5
  • 146
    • 0029670903 scopus 로고    scopus 로고
    • Cysteine34 of the cytoplasmic tail of the cation-dependent mannose 6- phosphate receptor is reversibly palmitoylated and required for normal trafficking and lysosomal enzyme sorting
    • Schweizer A, Kornfeld S, Rohrer J (1996) Cysteine34 of the cytoplasmic tail of the cation-dependent mannose 6- phosphate receptor is reversibly palmitoylated and required for normal trafficking and lysosomal enzyme sorting. J Cell Biol 132:577-584
    • (1996) J Cell Biol , vol.132 , pp. 577-584
    • Schweizer, A.1    Kornfeld, S.2    Rohrer, J.3
  • 147
    • 0027991237 scopus 로고
    • Conserved cysteine residues within the E3/19K protein of adenovirus type 2 are essential for binding to major histocompatibility complex antigens
    • Sester M, Burgert H-G (1994) Conserved cysteine residues within the E3/19K protein of adenovirus type 2 are essential for binding to major histocompatibility complex antigens. J Virol 68:5423-5432
    • (1994) J Virol , vol.68 , pp. 5423-5432
    • Sester, M.1    Burgert, H.-G.2
  • 148
    • 0034602996 scopus 로고    scopus 로고
    • The amyloid precursor-like protein 2 associates with the major histocompatibility complex class I molecule K(d)
    • Sester M, Feuerbach D, Frank R, Preckel T, Gutermann A, Burgert H-G (2000) The amyloid precursor-like protein 2 associates with the major histocompatibility complex class I molecule K(d). J Biol Chem 275:3645-3654
    • (2000) J Biol Chem , vol.275 , pp. 3645-3654
    • Sester, M.1    Feuerbach, D.2    Frank, R.3    Preckel, T.4    Gutermann, A.5    Burgert, H.-G.6
  • 149
    • 0000557447 scopus 로고    scopus 로고
    • B. N. Fields, D. M. Knipe and P. M. Howley (eds.), Lippincott-Raven Publishers, Philadelphia, New York
    • Shenk T (1996) In B. N. Fields, D. M. Knipe and P. M. Howley (eds.), Adenoviridae: The Viruses and Their Replication, Lippincott-Raven Publishers, Philadelphia, New York, pp. 2111-2148
    • (1996) Adenoviridae: The Viruses and Their Replication , pp. 2111-2148
    • Shenk, T.1
  • 150
    • 0030874023 scopus 로고    scopus 로고
    • The adenovirus E3-10.4K/14.5K complex mediates loss of cell surface Fas (CD95) and resistance to Fas-induced apoptosis
    • Shisler J, Yang C, Walter B, Ware CF, Gooding LR (1997) The adenovirus E3-10.4K/ 14.5K complex mediates loss of cell surface Fas (CD95) and resistance to Fas-induced apoptosis. J Virol 71:8299-8306
    • (1997) J Virol , vol.71 , pp. 8299-8306
    • Shisler, J.1    Yang, C.2    Walter, B.3    Ware, C.F.4    Gooding, L.R.5
  • 151
    • 0022884750 scopus 로고
    • Region E3 of human adenoviruses; differences between the oncogenic adenovirus-3 and the non-oncogenic adenovirus-2
    • Signäs C, Akusjarvi G, Pettersson U (1986) Region E3 of human adenoviruses; differences between the oncogenic adenovirus-3 and the non-oncogenic adenovirus-2. Gene 50:173-184
    • (1986) Gene , vol.50 , pp. 173-184
    • Signäs, C.1    Akusjarvi, G.2    Pettersson, U.3
  • 152
    • 0025224551 scopus 로고
    • The structure and insertion of integral proteins in membranes
    • Singer SJ (1990) The structure and insertion of integral proteins in membranes. Annu Rev Cell Biol 6:247-296
    • (1990) Annu Rev Cell Biol , vol.6 , pp. 247-296
    • Singer, S.J.1
  • 153
    • 0027620152 scopus 로고
    • Endocytosis of growth factor receptors
    • Sorkin A, Waters CM (1993) Endocytosis of growth factor receptors. Bioessays 15:375-382
    • (1993) Bioessays , vol.15 , pp. 375-382
    • Sorkin, A.1    Waters, C.M.2
  • 154
    • 0033061892 scopus 로고    scopus 로고
    • Clathrin, adaptors and eps15 in endosomes containing activated epidermal growth factor receptors
    • Sorkina T, Bild A, Tebar F, Sorkin A (1999) Clathrin, adaptors and eps15 in endosomes containing activated epidermal growth factor receptors. J Cell Sci 112:317-327
    • (1999) J Cell Sci , vol.112 , pp. 317-327
    • Sorkina, T.1    Bild, A.2    Tebar, F.3    Sorkin, A.4
  • 155
    • 0034517368 scopus 로고    scopus 로고
    • Selective export of MHC class I molecules from the ER after their dissociation from TAP
    • Spiliotis ET, Osorio M, Zuniga MC, Edidin M (2000) Selective export of MHC class I molecules from the ER after their dissociation from TAP. Immunity 13:841-851
    • (2000) Immunity , vol.13 , pp. 841-851
    • Spiliotis, E.T.1    Osorio, M.2    Zuniga, M.C.3    Edidin, M.4
  • 156
    • 0030983552 scopus 로고    scopus 로고
    • Serine 331 and tyrosine 333 are both involved in the interaction between the cytosolic domain of TGN38 and the mu2 subunit of the AP2 clathrin adaptor complex
    • Stephens DJ, Crump CM, Clarke AR, Banting G (1997) Serine 331 and tyrosine 333 are both involved in the interaction between the cytosolic domain of TGN38 and the mu2 subunit of the AP2 clathrin adaptor complex. J Biol Chem 272:14104-14109
    • (1997) J Biol Chem , vol.272 , pp. 14104-14109
    • Stephens, D.J.1    Crump, C.M.2    Clarke, A.R.3    Banting, G.4
  • 157
    • 0028950471 scopus 로고
    • The adenovirus E3 10.4K and 14.5K proteins, which function to prevent cytolysis by tumor necrosis factor and to down-regulate the epidermal growth factor receptor, are localized in the plasma membrane
    • Stewart AR, Tollefson AE, Krajcsi P, Yei SP, Wold WS (1995) The adenovirus E3 10.4K and 14.5K proteins, which function to prevent cytolysis by tumor necrosis factor and to down-regulate the epidermal growth factor receptor, are localized in the plasma membrane. J Virol 69:172-181
    • (1995) J Virol , vol.69 , pp. 172-181
    • Stewart, A.R.1    Tollefson, A.E.2    Krajcsi, P.3    Yei, S.P.4    Wold, W.S.5
  • 158
    • 0035830849 scopus 로고    scopus 로고
    • Multiple C-terminal motifs of the 46-kDa mannose 6-phosphate receptor tail contribute to efficient binding of medium chains of AP-2 and AP-3
    • Storch S, Braulke T (2001) Multiple C-terminal motifs of the 46-kDa mannose 6-phosphate receptor tail contribute to efficient binding of medium chains of AP-2 and AP-3. J Biol Chem 276:4298-4303
    • (2001) J Biol Chem , vol.276 , pp. 4298-4303
    • Storch, S.1    Braulke, T.2
  • 159
    • 0033593811 scopus 로고    scopus 로고
    • Microtubule-dependent plus-and minus end-directed motilities are competing processes for nuclear targeting of adenovirus
    • Suomalainen M, Nakano MY, Keller S, Boucke K, Stidwill RP, Greber UF (1999) Microtubule-dependent plus- and minus end-directed motilities are competing processes for nuclear targeting of adenovirus. J Cell Biol 144:657-672
    • (1999) J Cell Biol , vol.144 , pp. 657-672
    • Suomalainen, M.1    Nakano, M.Y.2    Keller, S.3    Boucke, K.4    Stidwill, R.P.5    Greber, U.F.6
  • 160
    • 0029778556 scopus 로고    scopus 로고
    • Signal-mediated sorting of membrane proteins between the endoplasmic reticulum and the golgi apparatus
    • Teasdale RD, Jackson MR (1996) Signal-mediated sorting of membrane proteins between the endoplasmic reticulum and the golgi apparatus. Annu Rev Cell Dev Biol 12:27-54
    • (1996) Annu Rev Cell Dev Biol , vol.12 , pp. 27-54
    • Teasdale, R.D.1    Jackson, M.R.2
  • 163
    • 0030003101 scopus 로고    scopus 로고
    • The E3-11.6-kDa adenovirus death protein (ADP) is required for efficient cell death: Characterization of cells infected with adp mutants
    • Tollefson AE, Ryerse JS, Scaria A, Hermiston TW, Wold WS (1996a) The E3-11.6-kDa adenovirus death protein (ADP) is required for efficient cell death: characterization of cells infected with adp mutants. Virology 220:152-162
    • (1996) Virology , vol.220 , pp. 152-162
    • Tollefson, A.E.1    Ryerse, J.S.2    Scaria, A.3    Hermiston, T.W.4    Wold, W.S.5
  • 164
    • 0029872241 scopus 로고    scopus 로고
    • The adenovirus death protein (E3-11.6K) is required at very late stages of infection for efficient cell lysis and release of adenovirus from infected cells
    • Tollefson AE, Scaria A, Hermiston TW, Ryerse JS, Wold LJ, Wold WS (1996b) The adenovirus death protein (E3-11.6K) is required at very late stages of infection for efficient cell lysis and release of adenovirus from infected cells. J Virol 70:2296-2306
    • (1996) J Virol , vol.70 , pp. 2296-2306
    • Tollefson, A.E.1    Scaria, A.2    Hermiston, T.W.3    Ryerse, J.S.4    Wold, L.J.5    Wold, W.S.6
  • 165
    • 0026610807 scopus 로고
    • The 11,600-MW protein encoded by region E3 of adenovirus is expressed early but is greatly amplified at late stages of infection
    • Tollefson AE, Scaria A, Saha SK, Wold WS (1992) The 11,600-MW protein encoded by region E3 of adenovirus is expressed early but is greatly amplified at late stages of infection. J Virol 66:3633-3642
    • (1992) J Virol , vol.66 , pp. 3633-3642
    • Tollefson, A.E.1    Scaria, A.2    Saha, S.K.3    Wold, W.S.4
  • 166
    • 0025941874 scopus 로고
    • The 10,400- and 14,500-dalton proteins encoded by region E3 of adenovirus form a complex and function together to down-regulate the epidermal growth factor receptor
    • Tollefson AE, Stewart AR, Yei SP, Saha SK, Wold WS (1991) The 10,400- and 14,500-dalton proteins encoded by region E3 of adenovirus form a complex and function together to down-regulate the epidermal growth factor receptor. J Virol 65:3095-3105
    • (1991) J Virol , vol.65 , pp. 3095-3105
    • Tollefson, A.E.1    Stewart, A.R.2    Yei, S.P.3    Saha, S.K.4    Wold, W.S.5
  • 168
    • 0030915715 scopus 로고    scopus 로고
    • HCAR and MCAR: The human and mouse cellular receptors for subgroup C adenoviruses and group B coxsackieviruses
    • Tomko RP, Xu R, Philipson L (1997) HCAR and MCAR: the human and mouse cellular receptors for subgroup C adenoviruses and group B coxsackieviruses. Proc Natl Acad Sci USA 94:3352-3356
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3352-3356
    • Tomko, R.P.1    Xu, R.2    Philipson, L.3
  • 170
    • 0034104585 scopus 로고    scopus 로고
    • Proapoptotic functions of cytotoxic lymphocyte granule constituents in vitro and in vivo
    • Trapani JA, Davis J, Sutton VR, Smyth MJ (2000) Proapoptotic functions of cytotoxic lymphocyte granule constituents in vitro and in vivo. Curr Opin Immunol 12:323-329
    • (2000) Curr Opin Immunol , vol.12 , pp. 323-329
    • Trapani, J.A.1    Davis, J.2    Sutton, V.R.3    Smyth, M.J.4
  • 171
    • 0030816038 scopus 로고    scopus 로고
    • The trans-Golgi network: A late secretory sorting station
    • Traub LM, Kornfeld S (1997) The trans-Golgi network: a late secretory sorting station. Curr Opin Cell Biol 9:527-533
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 527-533
    • Traub, L.M.1    Kornfeld, S.2
  • 172
    • 0030955355 scopus 로고    scopus 로고
    • Expression of adenoviral E3 transgenes in beta cells prevents autoimmune diabetes
    • von Herrath MG, Efrat S, Oldstone MB, Horwitz MS (1997) Expression of adenoviral E3 transgenes in beta cells prevents autoimmune diabetes. Proc Natl Acad Sci USA 94:9808-9813
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9808-9813
    • Von Herrath, M.G.1    Efrat, S.2    Oldstone, M.B.3    Horwitz, M.S.4
  • 173
    • 0028839910 scopus 로고
    • An acidic sequence within the cytoplasmic domain of furin functions as a determinant of trans-Golgi network localization and internalization from the cell surface
    • Voorhees P, Deignan E, van Donselaar E, Humphrey J, Marks MS, Peters PJ, Bonifacino JS (1995) An acidic sequence within the cytoplasmic domain of furin functions as a determinant of trans-Golgi network localization and internalization from the cell surface. EMBO J 14:4961-4975
    • (1995) EMBO J , vol.14 , pp. 4961-4975
    • Voorhees, P.1    Deignan, E.2    Van Donselaar, E.3    Humphrey, J.4    Marks, M.S.5    Peters, P.J.6    Bonifacino, J.S.7
  • 174
    • 0031755441 scopus 로고    scopus 로고
    • Regulation of apoptosis by adenovirus E1A and E1B oncogenes
    • White E (1998) Regulation of apoptosis by adenovirus E1A and E1B oncogenes. Semin Virol 505-513
    • (1998) Semin Virol , pp. 505-513
    • White, E.1
  • 175
    • 0028290486 scopus 로고
    • Global statistics of protein sequences: Implications for the origin, evolution, and prediction of structure
    • White SH (1994) Global statistics of protein sequences: implications for the origin, evolution, and prediction of structure. Annu Rev Biophys Biomol Struct 23:407-439
    • (1994) Annu Rev Biophys Biomol Struct , vol.23 , pp. 407-439
    • White, S.H.1
  • 177
    • 0027219116 scopus 로고
    • The E3-6.7K protein of adenovirus is an Asn-linked integral membrane glycoprotein localized in the endoplasmic reticulum
    • Wilson-Rawls J, Wold WS (1993) The E3-6.7K protein of adenovirus is an Asn-linked integral membrane glycoprotein localized in the endoplasmic reticulum. Virology 195:6-15
    • (1993) Virology , vol.195 , pp. 6-15
    • Wilson-Rawls, J.1    Wold, W.S.2
  • 178
    • 0036139834 scopus 로고    scopus 로고
    • Characterization of E3/49K, a novel highly glycosylated E3 protein of the epidemic keratokonjunctivitis causing adenovirus 19a
    • Windheim M, Burgert H-G (2002) Characterization of E3/49K, a novel highly glycosylated E3 protein of the epidemic keratokonjunctivitis causing adenovirus 19a. J Virol 76:75-76
    • (2002) J Virol , vol.76 , pp. 75-76
    • Windheim, M.1    Burgert, H.-G.2
  • 181
    • 0033280323 scopus 로고    scopus 로고
    • Mechanisms of viral interference with MHC class I antigen processing and presentation
    • Yewdell JW, Bennink JR (1999) Mechanisms of viral interference with MHC class I antigen processing and presentation. Annu Rev Cell Dev Biol 15:579-606
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 579-606
    • Yewdell, J.W.1    Bennink, J.R.2
  • 183
    • 0035257013 scopus 로고    scopus 로고
    • Rab proteins as membrane organizers
    • Zerial M, McBride H (2001) Rab proteins as membrane organizers. Nat Rev Mol Cell Biol 2:107-117
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 107-117
    • Zerial, M.1    McBride, H.2
  • 184
    • 0035369692 scopus 로고    scopus 로고
    • Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6- phosphate receptor
    • Zhu Y, Doray B, Poussu A, Lehto VP, Kornfeld S (2001) Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6- phosphate receptor. Science 292:1716-1718
    • (2001) Science , vol.292 , pp. 1716-1718
    • Zhu, Y.1    Doray, B.2    Poussu, A.3    Lehto, V.P.4    Kornfeld, S.5
  • 185
    • 0030049561 scopus 로고    scopus 로고
    • Degradation of mutant influenza virus hemagglutinins is influenced by cytoplasmic sequences independent of internalization signals
    • Zwart DE, Brewer CB, Lazarovits J, Henis YI, Roth MG (1996) Degradation of mutant influenza virus hemagglutinins is influenced by cytoplasmic sequences independent of internalization signals. J Biol Chem 271:907-917
    • (1996) J Biol Chem , vol.271 , pp. 907-917
    • Zwart, D.E.1    Brewer, C.B.2    Lazarovits, J.3    Henis, Y.I.4    Roth, M.G.5


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