메뉴 건너뛰기




Volumn 179, Issue 5, 2007, Pages 965-980

Adenovirus RIDα regulates endosome maturation by mimicking GTP-Rab7

Author keywords

[No Author keywords available]

Indexed keywords

ADENOVIRUS RECEPTOR INTERNALIZATION AND DEGRADATION ALPHA PROTEIN; BINDING PROTEIN; CELL MEMBRANE PROTEIN; CELL PROTEIN; COPPER ION; EPIDERMAL GROWTH FACTOR RECEPTOR; FAS ANTIGEN; HISTIDINE; OXYSTEROL BINDING PROTEIN RELATED PROTEIN 1L; RAB7 INTERACTING LYSOSOMAL PROTEIN; RAB7 PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN; CARRIER PROTEIN; COPPER; FAS PROTEIN, HUMAN; OSBPL1A PROTEIN, HUMAN; RAB PROTEIN; RILP PROTEIN, HUMAN; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

EID: 36849002409     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200702187     Document Type: Article
Times cited : (24)

References (69)
  • 1
    • 0034914206 scopus 로고    scopus 로고
    • A molecular chaperone complex at the lysosomal membrane is required for protein translocation
    • Agarraberes, F.A., and J.F. Dice. 2001. A molecular chaperone complex at the lysosomal membrane is required for protein translocation. J. Cell Sci. 114:2491-2499.
    • (2001) J. Cell Sci , vol.114 , pp. 2491-2499
    • Agarraberes, F.A.1    Dice, J.F.2
  • 3
    • 0016679756 scopus 로고
    • Regulation of the activity of the low density lipoprotein receptor in human fibroblasts
    • Brown, M.S., and J.L. Goldstein. 1975. Regulation of the activity of the low density lipoprotein receptor in human fibroblasts. Cell. 6:307-316.
    • (1975) Cell , vol.6 , pp. 307-316
    • Brown, M.S.1    Goldstein, J.L.2
  • 5
    • 0026744303 scopus 로고
    • The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway
    • Bucci, C., R.G. Parton, I.H. Mather, H. Stunnenberg, K. Simons, B. Hoflack, and M. Zerial. 1992. The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway. Cell. 70:715-728.
    • (1992) Cell , vol.70 , pp. 715-728
    • Bucci, C.1    Parton, R.G.2    Mather, I.H.3    Stunnenberg, H.4    Simons, K.5    Hoflack, B.6    Zerial, M.7
  • 7
    • 0035865135 scopus 로고    scopus 로고
    • Rab-interacting lysosomal protein (RILP): The Rab7 effector required for transport to lysosomes
    • Cantalupo, G., P. Alifano, V. Roberti, C.B. Bruni, and C. Bucci. 2001. Rab-interacting lysosomal protein (RILP): the Rab7 effector required for transport to lysosomes. EMBO J. 20:683-693.
    • (2001) EMBO J , vol.20 , pp. 683-693
    • Cantalupo, G.1    Alifano, P.2    Roberti, V.3    Bruni, C.B.4    Bucci, C.5
  • 8
    • 0024557043 scopus 로고
    • Epidermal growth factor receptor is down-regulated by a 10,400 MW protein encoded by the E3 region of adenovirus
    • Carlin, C.R., A.E. Tollefson, H.A. Brady, B.L. Hoffman, and W.S. Wold. 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
  • 9
    • 33644869303 scopus 로고    scopus 로고
    • rab7 activity affects epidermal growth factor: Epidermal growth factor receptor degradation by regulating endocytic trafficking from the late endosome
    • Ceresa, B.P., and S.J. Bahr. 2006. rab7 activity affects epidermal growth factor: epidermal growth factor receptor degradation by regulating endocytic trafficking from the late endosome. J. Biol. Chem. 281:1099-1106.
    • (2006) J. Biol. Chem , vol.281 , pp. 1099-1106
    • Ceresa, B.P.1    Bahr, S.J.2
  • 10
    • 27144544036 scopus 로고    scopus 로고
    • Mechanism for removal of tumor necrosis factor receptor 1 from the cell surface by the adenovirus RIDalpha/beta complex
    • Chin, Y.R., and M.S. Horwitz. 2005. Mechanism for removal of tumor necrosis factor receptor 1 from the cell surface by the adenovirus RIDalpha/beta complex. J. Virol. 79:13606-13617.
    • (2005) J. Virol , vol.79 , pp. 13606-13617
    • Chin, Y.R.1    Horwitz, M.S.2
  • 11
    • 34648816169 scopus 로고    scopus 로고
    • A tyrosine-based signal plays a critical role in the targeting and function of adenovirus RID{alpha} protein
    • Cianciola, N.L., D. Crooks, A.H. Shah, and C. Carlin. 2007. A tyrosine-based signal plays a critical role in the targeting and function of adenovirus RID{alpha} protein. J. Virol. 81:10437-10450.
    • (2007) J. Virol , vol.81 , pp. 10437-10450
    • Cianciola, N.L.1    Crooks, D.2    Shah, A.H.3    Carlin, C.4
  • 12
    • 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., S.J. Kil, J.M. McCaffery, and C. Carlin. 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
  • 13
    • 0033880909 scopus 로고    scopus 로고
    • Spectrin tethers and mesh in the biosynthetic pathway
    • De Matteis, M.A., and J.S. Morrow. 2000. Spectrin tethers and mesh in the biosynthetic pathway. J. Cell Sci. 113:2331-2343.
    • (2000) J. Cell Sci , vol.113 , pp. 2331-2343
    • De Matteis, M.A.1    Morrow, J.S.2
  • 14
    • 2442673028 scopus 로고    scopus 로고
    • The proteasome alpha-subunit XAPC7 interacts specifically with Rab7 and late endosomes
    • Dong, J., W. Chen, A. Welford, and A. Wandinger-Ness. 2004. The proteasome alpha-subunit XAPC7 interacts specifically with Rab7 and late endosomes. J. Biol. Chem. 279:21334-21342.
    • (2004) J. Biol. Chem , vol.279 , pp. 21334-21342
    • Dong, J.1    Chen, W.2    Welford, A.3    Wandinger-Ness, A.4
  • 15
    • 0032544013 scopus 로고    scopus 로고
    • The adenovirus E3/10.4K-14.5K proteins down-modulate the apoptosis receptor Fas/Apo-1 by inducing its internalization
    • Elsing, A., and H.G. Burgert. 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
  • 16
    • 0029585762 scopus 로고
    • Rab 7: An important regulator of late endocytic membrane traffic
    • Feng, Y., B. Press, and A. Wandinger-Ness. 1995. Rab 7: an important regulator of late endocytic membrane traffic. J. Cell Biol. 131:1435-1452.
    • (1995) J. Cell Biol , vol.131 , pp. 1435-1452
    • Feng, Y.1    Press, B.2    Wandinger-Ness, A.3
  • 17
    • 8744245265 scopus 로고    scopus 로고
    • Inhibition of tumor necrosis factor (TNF) signal transduction by the adenovirus group C RID complex involves downregulation of surface levels of TNF receptor 1
    • Fessler, S.P., Y.R. Chin, and M.S. Horwitz. 2004. Inhibition of tumor necrosis factor (TNF) signal transduction by the adenovirus group C RID complex involves downregulation of surface levels of TNF receptor 1. J. Virol. 78:13113-13121.
    • (2004) J. Virol , vol.78 , pp. 13113-13121
    • Fessler, S.P.1    Chin, Y.R.2    Horwitz, M.S.3
  • 18
    • 0036838708 scopus 로고    scopus 로고
    • Prevalence and quantitation of species C adenovirus DNA in human mucosal lymphocytes
    • Garnett, C.T., D. Erdman, W. Xu, and L.R. Gooding. 2002. Prevalence and quantitation of species C adenovirus DNA in human mucosal lymphocytes. J. Virol. 76:10608-10616.
    • (2002) J. Virol , vol.76 , pp. 10608-10616
    • Garnett, C.T.1    Erdman, D.2    Xu, W.3    Gooding, L.R.4
  • 19
    • 0032671106 scopus 로고    scopus 로고
    • The life and times of adenoviruses
    • Ginsberg, H.S. 1999. The life and times of adenoviruses. Adv. Virus Res. 54:1-13.
    • (1999) Adv. Virus Res , vol.54 , pp. 1-13
    • Ginsberg, H.S.1
  • 20
    • 0020973547 scopus 로고
    • Receptor-mediated endocytosis of low-density lipoprotein in cultured cells
    • Goldstein, J.L., S.K. Basu, and M.S. Brown. 1983. Receptor-mediated endocytosis of low-density lipoprotein in cultured cells. Methods Enzymol. 98:241-260.
    • (1983) Methods Enzymol , vol.98 , pp. 241-260
    • Goldstein, J.L.1    Basu, S.K.2    Brown, M.S.3
  • 21
    • 0034934520 scopus 로고    scopus 로고
    • Identification of rab7 as a melanosome-associated protein involved in the intracellular transport of tyrosinase-related protein 1
    • Gomez, P.F., D. Luo, K. Hirosaki, K. Shinoda, T. Yamashita, J. Suzuki, K. Otsu, K. Ishikawa, and K. Jimbow. 2001. Identification of rab7 as a melanosome-associated protein involved in the intracellular transport of tyrosinase-related protein 1. J. Invest. Dermatol. 117:81-90.
    • (2001) J. Invest. Dermatol , vol.117 , pp. 81-90
    • Gomez, P.F.1    Luo, D.2    Hirosaki, K.3    Shinoda, K.4    Yamashita, T.5    Suzuki, J.6    Otsu, K.7    Ishikawa, K.8    Jimbow, K.9
  • 22
    • 0025019251 scopus 로고
    • Molecular mechanisms by which adenoviruses counteract antiviral immune defenses
    • Gooding, L.R., and W.S. Wold. 1990. Molecular mechanisms by which adenoviruses counteract antiviral immune defenses. Crit. Rev. Immunol. 10:53-71.
    • (1990) Crit. Rev. Immunol , vol.10 , pp. 53-71
    • Gooding, L.R.1    Wold, W.S.2
  • 23
    • 33747066132 scopus 로고    scopus 로고
    • Rabs and their effectors: Achieving specificity in membrane traffic
    • Grosshans, B.L., D. Ortiz, and P. Novick. 2006. Rabs and their effectors: achieving specificity in membrane traffic. Proc. Natl. Acad. Sci. USA. 103:11821-11827.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 11821-11827
    • Grosshans, B.L.1    Ortiz, D.2    Novick, P.3
  • 24
    • 0035490884 scopus 로고    scopus 로고
    • The endocytic pathway: A mosaic of domains
    • Gruenberg, J. 2001. The endocytic pathway: a mosaic of domains. Nat. Rev. Mol. Cell Biol. 2:721-730.
    • (2001) Nat. Rev. Mol. Cell Biol , vol.2 , pp. 721-730
    • Gruenberg, J.1
  • 25
    • 3242877218 scopus 로고    scopus 로고
    • Rab7 is required for the normal progression of the autophagic pathway in mammalian cells
    • Gutierrez, M.G., D.B. Munafo, W. Beron, and M.I. Colombo. 2004. Rab7 is required for the normal progression of the autophagic pathway in mammalian cells. J. Cell Sci. 117:2687-2697.
    • (2004) J. Cell Sci , vol.117 , pp. 2687-2697
    • Gutierrez, M.G.1    Munafo, D.B.2    Beron, W.3    Colombo, M.I.4
  • 26
    • 0346434163 scopus 로고    scopus 로고
    • Two distinct transport motifs in the adenovirus E3/10.4-14.5 proteins act in concert to down-modulate apoptosis receptors and the epidermal growth factor receptor
    • Hilgendorf, A., J. Lindberg, Z. Ruzsics, S. Honing, A. Elsing, M. Lofqvist, H. Engelmann, and H.G. Burgert. 2003. Two distinct transport motifs in the adenovirus E3/10.4-14.5 proteins act in concert to down-modulate apoptosis receptors and the epidermal growth factor receptor. J. Biol. Chem. 278:51872-51884.
    • (2003) J. Biol. Chem , vol.278 , pp. 51872-51884
    • Hilgendorf, A.1    Lindberg, J.2    Ruzsics, Z.3    Honing, S.4    Elsing, A.5    Lofqvist, M.6    Engelmann, H.7    Burgert, H.G.8
  • 27
    • 0025006949 scopus 로고
    • Retrovirus-mediated transfer of an adenovirus gene encoding an integral membrane protein is sufficient to down regulate the receptor for epidermal growth factor
    • Hoffman, B.L., A. Ullrich, W.S. Wold, and C.R. Carlin. 1990. Retrovirus-mediated transfer of an adenovirus gene encoding an integral membrane protein is sufficient to down regulate the receptor for epidermal growth factor. Mol. Cell. Biol. 10:5521-5524.
    • (1990) Mol. Cell. Biol , vol.10 , pp. 5521-5524
    • Hoffman, B.L.1    Ullrich, A.2    Wold, W.S.3    Carlin, C.R.4
  • 28
    • 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., and C. Carlin. 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
  • 29
    • 0026513815 scopus 로고
    • Evidence for intracellular down-regulation of the epidermal growth factor (EGF) receptor during adenovirus infection by an EGF-independent mechanism
    • Hoffman, P., P. Rajakumar, B. Hoffman, R. Heuertz, W.S. Wold, and C.R. Carlin. 1992a. Evidence for intracellular down-regulation of the epidermal growth factor (EGF) receptor during adenovirus infection by an EGF-independent mechanism. J. Virol. 66:197-203.
    • (1992) J. Virol , vol.66 , pp. 197-203
    • Hoffman, P.1    Rajakumar, P.2    Hoffman, B.3    Heuertz, R.4    Wold, W.S.5    Carlin, C.R.6
  • 30
    • 0026717609 scopus 로고
    • Characterization of the adenovirus E3 protein that down-regulates the epidermal growth factor receptor. Evidence for intermolecular disulfide bonding and plasma membrane localization
    • Hoffman, P., M.B. Yaffe, B.L. Hoffman, S. Yei, W.S. Wold, and C. Carlin. 1992b. Characterization of the adenovirus E3 protein that down-regulates the epidermal growth factor receptor. Evidence for intermolecular disulfide bonding and plasma membrane localization. J. Biol. Chem. 267:13480-13487.
    • (1992) J. Biol. Chem , vol.267 , pp. 13480-13487
    • Hoffman, P.1    Yaffe, M.B.2    Hoffman, B.L.3    Yei, S.4    Wold, W.S.5    Carlin, C.6
  • 32
    • 0022558433 scopus 로고
    • Group C adenovirus DNA sequences in human lymphoid cells
    • Horvath, J., L. Palkonyay, and J. Weber. 1986. Group C adenovirus DNA sequences in human lymphoid cells. J. Virol. 59:189-192.
    • (1986) J. Virol , vol.59 , pp. 189-192
    • Horvath, J.1    Palkonyay, L.2    Weber, J.3
  • 33
    • 4644289537 scopus 로고    scopus 로고
    • Function of adenovirus E3 proteins and their interactions with immunoregulatory cell proteins
    • Horwitz, M.S. 2004. Function of adenovirus E3 proteins and their interactions with immunoregulatory cell proteins. J. Gene Med. 6:S172-S183.
    • (2004) J. Gene Med , vol.6
    • Horwitz, M.S.1
  • 34
    • 0035885867 scopus 로고    scopus 로고
    • A family of 12 human genes containing oxysterol-binding domains
    • Jaworski, C.J., E. Moreira, A. Li, R. Lee, and I.R. Rodriguez. 2001. A family of 12 human genes containing oxysterol-binding domains. Genomics. 78:185-196.
    • (2001) Genomics , vol.78 , pp. 185-196
    • Jaworski, C.J.1    Moreira, E.2    Li, A.3    Lee, R.4    Rodriguez, I.R.5
  • 35
    • 22244478077 scopus 로고    scopus 로고
    • Structure and physiologic function of the low-density lipoprotein receptor
    • Jeon, H., and S.C. Blacklow. 2005. Structure and physiologic function of the low-density lipoprotein receptor. Annu. Rev. Biochem. 74:535-562.
    • (2005) Annu. Rev. Biochem , vol.74 , pp. 535-562
    • Jeon, H.1    Blacklow, S.C.2
  • 36
    • 0037342401 scopus 로고    scopus 로고
    • The two variants of oxysterol binding protein-related protein-1 display different tissue expression patterns, have different intracellular localization, and are functionally distinct
    • Johansson, M., V. Bocher, M. Lehto, G. Chinetti, E. Kuismanen, C. Ehnholm, B. Staels, and V.M. Olkkonen. 2003. The two variants of oxysterol binding protein-related protein-1 display different tissue expression patterns, have different intracellular localization, and are functionally distinct. Mol. Biol. Cell. 14:903-915.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 903-915
    • Johansson, M.1    Bocher, V.2    Lehto, M.3    Chinetti, G.4    Kuismanen, E.5    Ehnholm, C.6    Staels, B.7    Olkkonen, V.M.8
  • 37
    • 28644446115 scopus 로고    scopus 로고
    • The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments
    • Johansson, M., M. Lehto, K. Tanhuanpaa, T.L. Cover, and V.M. Olkkonen. 2005. The oxysterol-binding protein homologue ORP1L interacts with Rab7 and alters functional properties of late endocytic compartments. Mol. Biol. Cell. 16:5480-5492.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5480-5492
    • Johansson, M.1    Lehto, M.2    Tanhuanpaa, K.3    Cover, T.L.4    Olkkonen, V.M.5
  • 38
    • 33847003020 scopus 로고    scopus 로고
    • Activation of endosomal dynein motors by stepwise assembly of Rab7-RILP-p150Glued, ORP1L, and the receptor βlll spectrin
    • Johansson, M., N. Rocha, W. Zwart, I. Jordens, L. Janssen, C. Kuijl, V.M. Olkkonen, and J. Neefjes. 2007. Activation of endosomal dynein motors by stepwise assembly of Rab7-RILP-p150Glued, ORP1L, and the receptor βlll spectrin. J. Cell Biol. 176:459-471.
    • (2007) J. Cell Biol , vol.176 , pp. 459-471
    • Johansson, M.1    Rocha, N.2    Zwart, W.3    Jordens, I.4    Janssen, L.5    Kuijl, C.6    Olkkonen, V.M.7    Neefjes, J.8
  • 40
    • 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, S.J., M. Hobert, and C. Carlin. 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
  • 41
    • 0036231646 scopus 로고    scopus 로고
    • Characterization of Ad5 E3-14.7K, an adenoviral inhibitor of apoptosis: Structure, oligomeric state, and metal binding
    • Kim, H.J., and M.P. Foster. 2002. Characterization of Ad5 E3-14.7K, an adenoviral inhibitor of apoptosis: structure, oligomeric state, and metal binding. Protein Sci. 11:1117-1128.
    • (2002) Protein Sci , vol.11 , pp. 1117-1128
    • Kim, H.J.1    Foster, M.P.2
  • 42
    • 0027439702 scopus 로고
    • Structurally related class I and class II receptor protein tyrosine kinases are downregulated by the same E3 protein coded for by human group C adenoviruses
    • Kuivinen, E., B.L. Hoffman, P.A. Hoffman, and C.R. Carlin. 1993. Structurally related class I and class II receptor protein tyrosine kinases are downregulated 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
  • 44
    • 0028238387 scopus 로고
    • Structural features of the GTP-binding defective Rab5 mutants required for their inhibitory activity on endocytosis
    • Li, G., M.A. Barbieri, M.I. Colombo, and P.D. Stahl. 1994. Structural features of the GTP-binding defective Rab5 mutants required for their inhibitory activity on endocytosis. J. Biol. Chem. 269:14631-14635.
    • (1994) J. Biol. Chem , vol.269 , pp. 14631-14635
    • Li, G.1    Barbieri, M.A.2    Colombo, M.I.3    Stahl, P.D.4
  • 45
    • 7644230912 scopus 로고    scopus 로고
    • Adenovirus E3-6.7K protein is required in conjunction with the E3-RID protein complex for the internalization and degradation of TRAIL receptor 2
    • Lichtenstein, D.L., K. Doronin, K. Toth, M. Kuppuswamy, W.S. Wold, and A.E. Tollefson. 2004a. Adenovirus E3-6.7K protein is required in conjunction with the E3-RID protein complex for the internalization and degradation of TRAIL receptor 2. J. Virol. 78:12297-12307.
    • (2004) J. Virol , vol.78 , pp. 12297-12307
    • Lichtenstein, D.L.1    Doronin, K.2    Toth, K.3    Kuppuswamy, M.4    Wold, W.S.5    Tollefson, A.E.6
  • 47
    • 33744922690 scopus 로고    scopus 로고
    • Copper-dependent interaction of dynactin subunit p62 with the N terminus of ATP7B but not ATP7A
    • Lim, C.M., M.A. Cater, J.F. Mercer, and S. La Fontaine. 2006. Copper-dependent interaction of dynactin subunit p62 with the N terminus of ATP7B but not ATP7A. J. Biol. Chem. 281:14006-14014.
    • (2006) J. Biol. Chem , vol.281 , pp. 14006-14014
    • Lim, C.M.1    Cater, M.A.2    Mercer, J.F.3    La Fontaine, S.4
  • 48
    • 0038306878 scopus 로고    scopus 로고
    • Blockade of the EGF receptor induces a deranged chemokine expression in keratinocytes leading to enhanced skin inflammation
    • Mascia, F., V. Mariani, G. Girolomoni, and S. Pastore. 2003. Blockade of the EGF receptor induces a deranged chemokine expression in keratinocytes leading to enhanced skin inflammation. Am. J. Pathol. 163:303-312.
    • (2003) Am. J. Pathol , vol.163 , pp. 303-312
    • Mascia, F.1    Mariani, V.2    Girolomoni, G.3    Pastore, S.4
  • 49
    • 0036776319 scopus 로고    scopus 로고
    • The adenovirus E3 RID complex protects some cultured human T and B lymphocytes from Fas-induced apoptosis
    • McNees, A.L., C.T. Garnett, and L.R. Gooding. 2002. The adenovirus E3 RID complex protects some cultured human T and B lymphocytes from Fas-induced apoptosis. J. Virol. 76:9716-9723.
    • (2002) J. Virol , vol.76 , pp. 9716-9723
    • McNees, A.L.1    Garnett, C.T.2    Gooding, L.R.3
  • 50
    • 0141744731 scopus 로고    scopus 로고
    • Rabring7, a novel Rab7 target protein with a RING finger motif
    • Mizuno, K., A. Kitamura, and T. Sasaki. 2003. Rabring7, a novel Rab7 target protein with a RING finger motif. Mol. Biol. Cell. 14:3741-3752.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3741-3752
    • Mizuno, K.1    Kitamura, A.2    Sasaki, T.3
  • 52
    • 33748989856 scopus 로고    scopus 로고
    • Higher order Rab programming in phagolysosome biogenesis
    • Roberts, E.A., J. Chua, G.B. Kyei, and V. Deretic. 2006. Higher order Rab programming in phagolysosome biogenesis. J. Cell Biol. 174:923-929.
    • (2006) J. Cell Biol , vol.174 , pp. 923-929
    • Roberts, E.A.1    Chua, J.2    Kyei, G.B.3    Deretic, V.4
  • 53
    • 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., C. Yang, B. Walter, C.F. Ware, and L.R. Gooding. 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
  • 54
    • 0345547405 scopus 로고    scopus 로고
    • Evaluation of the metal binding properties of a histidine-rich fusogenic peptide by electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry
    • Sinz, A., A.J. Jin, and O. Zschornig. 2003. Evaluation of the metal binding properties of a histidine-rich fusogenic peptide by electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry. J. Mass Spectrom. 38:1150-1159.
    • (2003) J. Mass Spectrom , vol.38 , pp. 1150-1159
    • Sinz, A.1    Jin, A.J.2    Zschornig, O.3
  • 57
    • 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, A.R., A.E. Tollefson, P. Krajcsi, S.P. Yei, and W.S. Wold. 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
  • 58
    • 0025266516 scopus 로고
    • A 14,500 MW protein is coded by region E3 of group C human adenoviruses
    • Tollefson, A.E., P. Krajcsi, M.H. Pursley, L.R. Gooding, and W.S. Wold. 1990. A 14,500 MW protein is coded by region E3 of group C human adenoviruses. Virology. 175:19-29.
    • (1990) Virology , vol.175 , pp. 19-29
    • Tollefson, A.E.1    Krajcsi, P.2    Pursley, M.H.3    Gooding, L.R.4    Wold, W.S.5
  • 59
    • 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, A.E., A.R. Stewart, S.P. Yei, S.K. Saha, and W.S. Wold. 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
  • 62
    • 0032479148 scopus 로고    scopus 로고
    • Membrane fusion is induced by a distinct peptide sequence of the sea urchin fertilization protein bindin
    • Ulrich, A.S., M. Otter, C.G. Glabe, and D. Hoekstra. 1998. Membrane fusion is induced by a distinct peptide sequence of the sea urchin fertilization protein bindin. J. Biol. Chem. 273:16748-16755.
    • (1998) J. Biol. Chem , vol.273 , pp. 16748-16755
    • Ulrich, A.S.1    Otter, M.2    Glabe, C.G.3    Hoekstra, D.4
  • 63
    • 0032504228 scopus 로고    scopus 로고
    • A membrane setting for the sorting motifs present in the adenovirus E3-13.7 protein which down-regulates the epidermal growth factor receptor
    • Vinogradova, O., C. Carlin, F.D. Sonnichsen, and C.R. Sanders II. 1998. A membrane setting for the sorting motifs present in the adenovirus E3-13.7 protein which down-regulates the epidermal growth factor receptor. J. Biol. Chem. 273:17343-17350.
    • (1998) J. Biol. Chem , vol.273 , pp. 17343-17350
    • Vinogradova, O.1    Carlin, C.2    Sonnichsen, F.D.3    Sanders II, C.R.4
  • 65
    • 33749470098 scopus 로고    scopus 로고
    • RILP interacts with VPS22 and VPS36 of ESCRT-II and regulates their membrane recruitment
    • Wang, T., and W. Hong. 2006. RILP interacts with VPS22 and VPS36 of ESCRT-II and regulates their membrane recruitment. Biochem. Biophys. Res. Commun. 350:413-423.
    • (2006) Biochem. Biophys. Res. Commun , vol.350 , pp. 413-423
    • Wang, T.1    Hong, W.2
  • 66
    • 0742270613 scopus 로고    scopus 로고
    • A unique region of RILP distinguishes it from its related proteins in its regulation of lysosomal morphology and interaction with Rab7 and Rab34
    • Wang, T., K.K. Wong, and W. Hong. 2004. A unique region of RILP distinguishes it from its related proteins in its regulation of lysosomal morphology and interaction with Rab7 and Rab34. Mol. Biol. Cell. 15:815-826.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 815-826
    • Wang, T.1    Wong, K.K.2    Hong, W.3
  • 67
    • 18444381428 scopus 로고    scopus 로고
    • Structural basis for recruitment of RILP by small GTPase Rab7
    • Wu, M., T. Wang, E. Loh, W. Hong, and H. Song. 2005. Structural basis for recruitment of RILP by small GTPase Rab7. EMBO J. 24:1491-1501.
    • (2005) EMBO J , vol.24 , pp. 1491-1501
    • Wu, M.1    Wang, T.2    Loh, E.3    Hong, W.4    Song, H.5
  • 68
    • 33746899628 scopus 로고    scopus 로고
    • Association with HSP90 inhibits Cbl-mediated down-regulation of mutant epidermal growth factor receptors
    • Yang, S., S. Qu, M. Perez-Tores, A. Sawai, N. Rosen, D.B. Solit, and C.L. Arteaga. 2006. Association with HSP90 inhibits Cbl-mediated down-regulation of mutant epidermal growth factor receptors. Cancer Res. 66:6990-6997.
    • (2006) Cancer Res , vol.66 , pp. 6990-6997
    • Yang, S.1    Qu, S.2    Perez-Tores, M.3    Sawai, A.4    Rosen, N.5    Solit, D.B.6    Arteaga, C.L.7
  • 69
    • 0142028855 scopus 로고    scopus 로고
    • Distinct domains in the adenovirus E3 RIDalpha protein are required for degradation of Fas and the epidermal growth factor receptor
    • Zanardi, T.A., S. Yei, D.L. Lichtenstein, A.E. Tollefson, and W.S. Wold. 2003. Distinct domains in the adenovirus E3 RIDalpha protein are required for degradation of Fas and the epidermal growth factor receptor. J. Virol. 77:11685-11696.
    • (2003) J. Virol , vol.77 , pp. 11685-11696
    • Zanardi, T.A.1    Yei, S.2    Lichtenstein, D.L.3    Tollefson, A.E.4    Wold, W.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.