메뉴 건너뛰기




Volumn 84, Issue 14, 2010, Pages 6995-7004

Opposing effects of a tyrosine-based sorting motif and a PDZ-binding motif regulate human T-lymphotropic virus type 1 envelope trafficking

Author keywords

[No Author keywords available]

Indexed keywords

ENVELOPE PROTEIN; GLYCOPROTEIN; PDZ PROTEIN; TYROSINE;

EID: 77953795571     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01853-09     Document Type: Article
Times cited : (13)

References (54)
  • 1
    • 0032901996 scopus 로고    scopus 로고
    • Interactions of the cytoplasmic domains of human and simian retroviral transmembrane proteins with components of the clathrin adaptor complexes modulate intracellular and cell surface expression of envelope glycoproteins
    • Berlioz-Torrent, C., B. L. Shacklett, L. Erdtmann, L. Delamarre, I. Bouchaert, P. Sonigo, M. C. Dokhelar, and R. Benarous. 1999. Interactions of the cytoplasmic domains of human and simian retroviral transmembrane proteins with components of the clathrin adaptor complexes modulate intracellular and cell surface expression of envelope glycoproteins. J. Virol. 73:1350-1361.
    • (1999) J. Virol. , vol.73 , pp. 1350-1361
    • Berlioz-Torrent, C.1    Shacklett, B.L.2    Erdtmann, L.3    Delamarre, L.4    Bouchaert, I.5    Sonigo, P.6    Dokhelar, M.C.7    Benarous, R.8
  • 2
    • 4444251676 scopus 로고    scopus 로고
    • Human Dlg protein binds to the envelope glycoproteins of human T-cell leukemia virus type 1 and regulates envelope mediated cell-cell fusion in T lymphocytes
    • Blot, V., L. Delamarre, F. Perugi, D. Pham, S. Benichou, R. Benarous, T. Hanada, A. H. Chishti, M. C. Dokhelar, and C. Pique. 2004. Human Dlg protein binds to the envelope glycoproteins of human T-cell leukemia virus type 1 and regulates envelope mediated cell-cell fusion in T lymphocytes. J. Cell Sci. 117:3983-3993.
    • (2004) J. Cell Sci. , vol.117 , pp. 3983-3993
    • Blot, V.1    Delamarre, L.2    Perugi, F.3    Pham, D.4    Benichou, S.5    Benarous, R.6    Hanada, T.7    Chishti, A.H.8    Dokhelar, M.C.9    Pique, C.10
  • 4
    • 0032546927 scopus 로고    scopus 로고
    • A membrane-proximal tyrosine-based signal mediates internalization of the HIV-1 envelope glycoprotein via interaction with the AP-2 clathrin adaptor
    • Boge, M., S. Wyss, J. S. Bonifacino, and M. Thali. 1998. A membrane-proximal tyrosine-based signal mediates internalization of the HIV-1 envelope glycoprotein via interaction with the AP-2 clathrin adaptor. J. Biol. Chem. 273:15773-15778.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15773-15778
    • Boge, M.1    Wyss, S.2    Bonifacino, J.S.3    Thali, M.4
  • 5
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino, J. S., and L. M. Traub. 2003. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 72:395-447.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 6
    • 0026522457 scopus 로고
    • A viral protease-mediated cleavage of the transmembrane glycoprotein of Mason-Pfizer monkey virus can be suppressed by mutations within the matrix protein
    • Brody, B. A., S. S. Rhee, M. A. Sommerfelt, and E. Hunter. 1992. A viral protease-mediated cleavage of the transmembrane glycoprotein of Mason-Pfizer monkey virus can be suppressed by mutations within the matrix protein. Proc. Natl. Acad. Sci. U. S. A. 89:3443-3447.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 3443-3447
    • Brody, B.A.1    Rhee, S.S.2    Sommerfelt, M.A.3    Hunter, E.4
  • 7
  • 8
    • 0022980377 scopus 로고
    • Envelope proteins of human T cell leukemia virus type I: Characterization by antisera to synthetic peptides and identification of a natural epitope
    • Copeland, T. D., W. P. Tsai, Y. D. Kim, and S. Oroszlan. 1986. Envelope proteins of human T cell leukemia virus type I: characterization by antisera to synthetic peptides and identification of a natural epitope. J. Immunol. 137:2945-2951.
    • (1986) J. Immunol. , vol.137 , pp. 2945-2951
    • Copeland, T.D.1    Tsai, W.P.2    Kim, Y.D.3    Oroszlan, S.4
  • 9
    • 2942558946 scopus 로고    scopus 로고
    • The tyrosine-based YXXΦ targeting motif of murine leukemia virus envelope glycoprotein affects pathogenesis
    • Danis, C., J. Deschambeault, S. Do Carmo, E. A. Cohen, E. Rassart, and G. Lemay. 2004. The tyrosine-based YXXΦ targeting motif of murine leukemia virus envelope glycoprotein affects pathogenesis. Virology 324:173-183.
    • (2004) Virology , vol.324 , pp. 173-183
    • Danis, C.1    Deschambeault, J.2    Do Carmo, S.3    Cohen, E.A.4    Rassart, E.5    Lemay, G.6
  • 10
    • 0032876560 scopus 로고    scopus 로고
    • The Y-S-L-I tyrosine-based motif in the cytoplasmic domain of the human T-cell leukemia virus type 1 envelope is essential for cell-to-cell transmission
    • Delamarre, L., C. Pique, A. R. Rosenberg, V. Blot, M. P. Grange, I. Le Blanc, and M. C. Dokhelar. 1999. The Y-S-L-I tyrosine-based motif in the cytoplasmic domain of the human T-cell leukemia virus type 1 envelope is essential for cell-to-cell transmission. J. Virol. 73:9659-9663. (Pubitemid 29487127)
    • (1999) Journal of Virology , vol.73 , Issue.11 , pp. 9659-9663
    • Delamarre, L.1    Pique, C.2    Rosenberg, A.R.3    Blot, V.4    Grange, M.-P.5    Le Blanc, I.6    Dokhear, M.-C.7
  • 13
    • 0033548575 scopus 로고    scopus 로고
    • AP-4, a novel protein complex related to clathrin adaptors
    • Dell'Angelica, E. C., C. Mullins, and J. S. Bonifacino. 1999. AP-4, a novel protein complex related to clathrin adaptors. J. Biol. Chem. 274:7278-7285.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7278-7285
    • Dell'Angelica, E.C.1    Mullins, C.2    Bonifacino, J.S.3
  • 14
    • 0034887093 scopus 로고    scopus 로고
    • Examining human T-lymphotropic virus type 1 infection and replication by cell-free infection with recombinant virus vectors
    • DOI 10.1128/JVI.75.18.8461-8468.2001
    • Derse, D., S. A. Hill, P. A. Lloyd, H. Chung, and B. A. Morse. 2001. Examining human T-lymphotropic virus type 1 infection and replication by cell-free infection with recombinant virus vectors. J. Virol. 75:8461-8468. (Pubitemid 32768950)
    • (2001) Journal of Virology , vol.75 , Issue.18 , pp. 8461-8468
    • Derse, D.1    Hill, S.A.2    Lloyd, P.A.3    Chung, H.-K.4    Morse, B.A.5
  • 15
    • 33847244948 scopus 로고    scopus 로고
    • Resistance of human T cell leukemia virus type 1 to APOBEC3G restriction is mediated by elements in nucleocapsid
    • Derse, D., S. A. Hill, G. Princler, P. Lloyd, and G. Heidecker. 2007. Resistance of human T cell leukemia virus type 1 to APOBEC3G restriction is mediated by elements in nucleocapsid. Proc. Natl. Acad. Sci. U. S. A. 104:2915-2920.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 2915-2920
    • Derse, D.1    Hill, S.A.2    Princler, G.3    Lloyd, P.4    Heidecker, G.5
  • 16
    • 0034466830 scopus 로고    scopus 로고
    • Identification of two intracellular mechanisms leading to reduced expression of oncoretrovirus envelope glycoproteins at the cell surface
    • Grange, M. P., V. Blot, L. Delamarre, I. Bouchaert, A. Rocca, A. Dautry-Varsat, and M. C. Dokhelar. 2000. Identification of two intracellular mechanisms leading to reduced expression of oncoretrovirus envelope glycoproteins at the cell surface. J. Virol. 74:11734-11743.
    • (2000) J. Virol. , vol.74 , pp. 11734-11743
    • Grange, M.P.1    Blot, V.2    Delamarre, L.3    Bouchaert, I.4    Rocca, A.5    Dautry-Varsat, A.6    Dokhelar, M.C.7
  • 17
    • 33749051206 scopus 로고    scopus 로고
    • Cargo takes control of endocytosis
    • Haucke, V. 2006. Cargo takes control of endocytosis. Cell 127:35-37.
    • (2006) Cell , vol.127 , pp. 35-37
    • Haucke, V.1
  • 18
    • 34347398956 scopus 로고    scopus 로고
    • A novel AAK1 splice variant functions at multiple steps of the endocytic pathway
    • Henderson, D. M., and S. D. Conner. 2007. A novel AAK1 splice variant functions at multiple steps of the endocytic pathway. Mol. Biol. Cell 18:2698-2706.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2698-2706
    • Henderson, D.M.1    Conner, S.D.2
  • 19
    • 0021690345 scopus 로고
    • Quantitative separation of murine leukemia virus proteins by reversed-phase high-pressure liquid chromatography reveals newly described gag and env cleavage products
    • Henderson, L. E., R. Sowder, T. D. Copeland, G. Smythers, and S. Oroszlan. 1984. Quantitative separation of murine leukemia virus proteins by reversed-phase high-pressure liquid chromatography reveals newly described gag and env cleavage products. J. Virol. 52:492-500.
    • (1984) J. Virol. , vol.52 , pp. 492-500
    • Henderson, L.E.1    Sowder, R.2    Copeland, T.D.3    Smythers, G.4    Oroszlan, S.5
  • 20
    • 0042658317 scopus 로고    scopus 로고
    • Susceptibility of human T cell leukemia virus type I to nucleoside reverse transcriptase inhibitors
    • Hill, S. A., P. A. Lloyd, S. McDonald, J. Wykoff, and D. Derse. 2003. Susceptibility of human T cell leukemia virus type I to nucleoside reverse transcriptase inhibitors. J. Infect. Dis. 188:424-427.
    • (2003) J. Infect. Dis. , vol.188 , pp. 424-427
    • Hill, S.A.1    Lloyd, P.A.2    McDonald, S.3    Wykoff, J.4    Derse, D.5
  • 23
    • 0030952367 scopus 로고    scopus 로고
    • Functional analysis of the cytoplasmic tail of moloney murine leukemia virus envelope protein
    • Januszeski, M. M., P. M. Cannon, D. Chen, Y. Rozenberg, and W. F. Anderson. 1997. Functional analysis of the cytoplasmic tail of Moloney murine leukemia virus envelope protein. J. Virol. 71:3613-3619. (Pubitemid 27172372)
    • (1997) Journal of Virology , vol.71 , Issue.5 , pp. 3613-3619
    • Januszeski, M.M.1    Cannon, P.M.2    Chen, D.3    Rozenberg, Y.4    Anderson, W.F.5
  • 24
    • 24344449035 scopus 로고    scopus 로고
    • Role of the endocytic machinery in the sorting of lysosome-associated membrane proteins
    • Janvier, K., and J. S. Bonifacino. 2005. Role of the endocytic machinery in the sorting of lysosome-associated membrane proteins. Mol. Biol. Cell 16:4231-4242.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4231-4242
    • Janvier, K.1    Bonifacino, J.S.2
  • 25
    • 68049136145 scopus 로고    scopus 로고
    • Assembly of the murine leukemia virus is directed towards sites of cell-cell contact
    • Jin, J., N. M. Sherer, G. Heidecker, D. Derse, and W. Mothes. 2009. Assembly of the murine leukemia virus is directed towards sites of cell-cell contact. PLoS Biol. 7:e1000163.
    • (2009) PLoS Biol. , vol.7
    • Jin, J.1    Sherer, N.M.2    Heidecker, G.3    Derse, D.4    Mothes, W.5
  • 26
    • 5044224260 scopus 로고    scopus 로고
    • PDZ domain proteins of synapses
    • Kim, E., and M. Sheng. 2004. PDZ domain proteins of synapses. Nat. Rev. Neurosci. 5:771-781.
    • (2004) Nat. Rev. Neurosci. , vol.5 , pp. 771-781
    • Kim, E.1    Sheng, M.2
  • 27
    • 0344420207 scopus 로고    scopus 로고
    • Sorting motifs in receptor trafficking
    • Kurten, R. C. 2003. Sorting motifs in receptor trafficking. Adv. Drug Deliv. Rev. 55:1405-1419.
    • (2003) Adv. Drug Deliv. Rev. , vol.55 , pp. 1405-1419
    • Kurten, R.C.1
  • 28
    • 47049126218 scopus 로고    scopus 로고
    • Intersubunit disulfide isomerization controls membrane fusion of human T-cell leukemia virus Env
    • DOI 10.1128/JVI.00448-08
    • Li, K., S. Zhang, M. Kronqvist, M. Wallin, M. Ekstrom, D. Derse, and H. Garoff. 2008. Intersubunit disulfide isomerization controls membrane fusion of human T-cell leukemia virus Env. J. Virol. 82:7135-7143. (Pubitemid 351977731)
    • (2008) Journal of Virology , vol.82 , Issue.14 , pp. 7135-7143
    • Li, K.1    Zhang, S.2    Kronqvist, M.3    Wallin, M.4    Ekstrom, M.5    Derse, D.6    Garoff, H.7
  • 29
    • 0030991945 scopus 로고    scopus 로고
    • Two distinct oncornaviruses harbor an intracytoplasmic tyrosine-based basolateral targeting signal in their viral envelope glycoprotein
    • Lodge, R., L. Delamarre, J. P. Lalonde, J. Alvarado, D. A. Sanders, M. C. Dokhelar, E. A. Cohen, and G. Lemay. 1997. Two distinct oncornaviruses harbor an intracytoplasmic tyrosine-based basolateral targeting signal in their viral envelope glycoprotein. J. Virol. 71:5696-5702. (Pubitemid 27258257)
    • (1997) Journal of Virology , vol.71 , Issue.7 , pp. 5696-5702
    • Lodge, R.1    Delamarre, L.2    Lalonde, J.-P.3    Alvarado, J.4    Sanders, D.A.5    Dokhelar, M.-C.6    Cohen, E.A.7    Lemay, G.8
  • 31
    • 25444495686 scopus 로고    scopus 로고
    • HTLV-1 tropism and envelope receptor
    • Manel, N., J. L. Battini, N. Taylor, and M. Sitbon. 2005. HTLV-1 tropism and envelope receptor. Oncogene 24:6016-6025.
    • (2005) Oncogene , vol.24 , pp. 6016-6025
    • Manel, N.1    Battini, J.L.2    Taylor, N.3    Sitbon, M.4
  • 32
    • 77649242985 scopus 로고    scopus 로고
    • Quantitative comparison of HTLV-1 and HIV-1 cell-to-cell infection with new replication dependent vectors
    • Mazurov, D., A. Ilinskaya, G. Heidecker, P. Lloyd, and D. Derse. 2010. Quantitative comparison of HTLV-1 and HIV-1 cell-to-cell infection with new replication dependent vectors. PLoS Pathog. 6:e1000788.
    • (2010) PLoS Pathog. , vol.6
    • Mazurov, D.1    Ilinskaya, A.2    Heidecker, G.3    Lloyd, P.4    Derse, D.5
  • 33
    • 1342289622 scopus 로고    scopus 로고
    • Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network
    • Nakatsu, F., and H. Ohno. 2003. Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network. Cell Struct. Funct. 28:419-429.
    • (2003) Cell Struct. Funct. , vol.28 , pp. 419-429
    • Nakatsu, F.1    Ohno, H.2
  • 34
    • 0037076273 scopus 로고    scopus 로고
    • The delta subunit of AP-3 is required for efficient transport of VSV-G from the trans-Golgi network to the cell surface
    • Nishimura, N., H. Plutner, K. Hahn, and W. E. Balch. 2002. The delta subunit of AP-3 is required for efficient transport of VSV-G from the trans-Golgi network to the cell surface. Proc. Natl. Acad. Sci. U. S. A. 99:6755-6760.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 6755-6760
    • Nishimura, N.1    Plutner, H.2    Hahn, K.3    Balch, W.E.4
  • 35
    • 0028842364 scopus 로고
    • Inositol hexakisphosphate binds to clathrin assembly protein 3 (AP-3/AP180) and inhibits clathrin cage assembly in vitro
    • Norris, F. A., E. Ungewickell, and P. W. Majerus. 1995. Inositol hexakisphosphate binds to clathrin assembly protein 3 (AP-3/AP180) and inhibits clathrin cage assembly in vitro. J. Biol. Chem. 270:214-217.
    • (1995) J. Biol. Chem. , vol.270 , pp. 214-217
    • Norris, F.A.1    Ungewickell, E.2    Majerus, P.W.3
  • 36
    • 0012927828 scopus 로고    scopus 로고
    • PDZ domain proteins: Plug and play!
    • Nourry, C., S. G. Grant, and J. P. Borg. 2003. PDZ domain proteins: plug and play! Sci. STKE 2003:RE7.
    • (2003) Sci. STKE , vol.2003
    • Nourry, C.1    Grant, S.G.2    Borg, J.P.3
  • 37
    • 0032476017 scopus 로고    scopus 로고
    • The medium subunits of adaptor complexes recognize distinct but overlapping sets of tyrosine-based sorting signals
    • Ohno, H., R. C. Aguilar, D. Yeh, D. Taura, T. Saito, and J. S. Bonifacino. 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
  • 38
    • 0035810915 scopus 로고    scopus 로고
    • Phosphorylation of threonine 156 of the mu2 subunit of the AP2 complex is essential for endocytosis in vitro and in vivo
    • Olusanya, O., P. D. Andrews, J. R. Swedlow, and E. Smythe. 2001. Phosphorylation of threonine 156 of the mu2 subunit of the AP2 complex is essential for endocytosis in vitro and in vivo. Curr. Biol. 11:896-900.
    • (2001) Curr. Biol. , vol.11 , pp. 896-900
    • Olusanya, O.1    Andrews, P.D.2    Swedlow, J.R.3    Smythe, E.4
  • 39
    • 69149083700 scopus 로고    scopus 로고
    • Functional roles of short sequence motifs in the endocytosis of membrane receptors
    • Pandey, K. N. 2009. Functional roles of short sequence motifs in the endocytosis of membrane receptors. Front. Biosci. 14:5339-5360.
    • (2009) Front. Biosci. , vol.14 , pp. 5339-5360
    • Pandey, K.N.1
  • 40
    • 0034715523 scopus 로고    scopus 로고
    • Interaction of CD82 tetraspanin proteins with HTLV-1 envelope glycoproteins inhibits cell-to-cell fusion and virus transmission
    • Pique, C., C. Lagaudriere-Gesbert, L. Delamarre, A. R. Rosenberg, H. Conjeaud, and M. C. Dokhelar. 2000. Interaction of CD82 tetraspanin proteins with HTLV-1 envelope glycoproteins inhibits cell-to-cell fusion and virus transmission. Virology 276:455-465.
    • (2000) Virology , vol.276 , pp. 455-465
    • Pique, C.1    Lagaudriere-Gesbert, C.2    Delamarre, L.3    Rosenberg, A.R.4    Conjeaud, H.5    Dokhelar, M.C.6
  • 41
    • 33749079184 scopus 로고    scopus 로고
    • Cargo regulates clathrin-coated pit dynamics
    • Puthenveedu, M. A., and M. von Zastrow. 2006. Cargo regulates clathrin-coated pit dynamics. Cell 127:113-124.
    • (2006) Cell , vol.127 , pp. 113-124
    • Puthenveedu, M.A.1    Von Zastrow, M.2
  • 42
    • 0028047579 scopus 로고
    • Function of the cytoplasmic domain of a retroviral transmembrane protein: P15E-p2E cleavage activates the membrane fusion capability of the murine leukemia virus Env protein
    • Rein, A., J. Mirro, J. G. Haynes, S. M. Ernst, and K. Nagashima. 1994. Function of the cytoplasmic domain of a retroviral transmembrane protein: p15E-p2E cleavage activates the membrane fusion capability of the murine leukemia virus Env protein. J. Virol. 68:1773-1781. (Pubitemid 24065746)
    • (1994) Journal of Virology , vol.68 , Issue.3 , pp. 1773-1781
    • Rein, A.1    Mirro, J.2    Haynes, J.G.3    Ernst, S.M.4    Nagashima, K.5
  • 43
    • 0025378990 scopus 로고
    • Intracellular processing and immunogenicity of the envelope proteins of human T-cell leukemia virus type I that are expressed from recombinant vaccinia viruses
    • Seki, M., H. Sashiyama, M. Hayami, and H. Shida. 1990. Intracellular processing and immunogenicity of the envelope proteins of human T-cell leukemia virus type I that are expressed from recombinant vaccinia viruses. Virus Genes 3:235-249.
    • (1990) Virus Genes , vol.3 , pp. 235-249
    • Seki, M.1    Sashiyama, H.2    Hayami, M.3    Shida, H.4
  • 44
    • 0034916230 scopus 로고    scopus 로고
    • PDZ domains and the organization of supramolecular complexes
    • Sheng, M., and C. Sala. 2001. PDZ domains and the organization of supramolecular complexes. Annu. Rev. Neurosci. 24:1-29.
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 1-29
    • Sheng, M.1    Sala, C.2
  • 45
    • 0037404525 scopus 로고    scopus 로고
    • A tyrosine motif in the cytoplasmic domain of Mason-Pfizer monkey virus is essential for the incorporation of glycoprotein into virions
    • DOI 10.1128/JVI.77.9.5192-5200.2003
    • Song, C., S. R. Dubay, and E. Hunter. 2003. A tyrosine motif in the cytoplasmic domain of Mason-Pfizer monkey virus is essential for the incorporation of glycoprotein into virions. J. Virol. 77:5192-5200. (Pubitemid 36460933)
    • (2003) Journal of Virology , vol.77 , Issue.9 , pp. 5192-5200
    • Song, C.1    Dubay, S.R.2    Hunter, E.3
  • 47
    • 69249135065 scopus 로고    scopus 로고
    • Tickets to ride: Selecting cargo for clathrin-regulated internalization
    • Traub, L. M. 2009. Tickets to ride: selecting cargo for clathrin-regulated internalization. Nat. Rev. Mol. Cell Biol. 10:583-596.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 583-596
    • Traub, L.M.1
  • 48
    • 0028956745 scopus 로고
    • Different domains of the AP-1 adaptor complex are required for Golgi membrane binding and clathrin recruitment
    • Traub, L. M., S. Kornfeld, and E. Ungewickell. 1995. Different domains of the AP-1 adaptor complex are required for Golgi membrane binding and clathrin recruitment. J. Biol. Chem. 270:4933-4942.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4933-4942
    • Traub, L.M.1    Kornfeld, S.2    Ungewickell, E.3
  • 49
    • 17844398478 scopus 로고    scopus 로고
    • Internal PDZ ligands: Novel endocytic recycling motifs for G protein-coupled receptors
    • Trejo, J. 2005. Internal PDZ ligands: novel endocytic recycling motifs for G protein-coupled receptors. Mol. Pharmacol. 67:1388-1390.
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1388-1390
    • Trejo, J.1
  • 50
    • 0037503653 scopus 로고    scopus 로고
    • PDZ domains - Glue and guide
    • van Ham, M., and W. Hendriks. 2003. PDZ domains - glue and guide. Mol. Biol. Rep. 30:69-82.
    • (2003) Mol. Biol. Rep. , vol.30 , pp. 69-82
    • Van Ham, M.1    Hendriks, W.2
  • 51
    • 0842307062 scopus 로고    scopus 로고
    • Isomerization of the intersubunit disulphide-bond in Env controls retrovirus fusion
    • DOI 10.1038/sj.emboj.7600012
    • Wallin, M., M. Ekstrom, and H. Garoff. 2004. Isomerization of the intersubunit disulphide-bond in Env controls retrovirus fusion. EMBO J. 23:54-65. (Pubitemid 38165747)
    • (2004) EMBO Journal , vol.23 , Issue.1 , pp. 54-65
    • Wallin, M.1    Ekstrom, M.2    Garoff, H.3
  • 52
    • 34247383616 scopus 로고    scopus 로고
    • Clathrin-dependent mechanisms of G protein-coupled receptor endocytosis
    • DOI 10.1111/j.1600-0854.2007.00551.x
    • Wolfe, B. L., and J. Trejo. 2007. Clathrin-dependent mechanisms of G protein-coupled receptor endocytosis. Traffic 8:462-470. (Pubitemid 46638559)
    • (2007) Traffic , vol.8 , Issue.5 , pp. 462-470
    • Wolfe, B.L.1    Trejo, J.2
  • 53
    • 20444480611 scopus 로고    scopus 로고
    • PDZ domains and the politics of polarity in lymphocytes
    • Xavier, R., and B. Seed. 2005. PDZ domains and the politics of polarity in lymphocytes. Immunity 22:655-656.
    • (2005) Immunity , vol.22 , pp. 655-656
    • Xavier, R.1    Seed, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.