메뉴 건너뛰기




Volumn 10, Issue 1, 2000, Pages 1-7

Head-head/tail-tail relative orientation of the pore-forming domains of the heterodimeric ABC transporter TAP

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0033971458     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(99)00257-2     Document Type: Article
Times cited : (39)

References (25)
  • 1
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins C.F. ABC transporters: from microorganisms to man. Annu Rev Cell Biol. 8:1992;67-113.
    • (1992) Annu Rev Cell Biol , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 2
    • 0025688348 scopus 로고
    • Sequences encoded in the class II region of the MHC related to the 'ABC' superfamily of transporters
    • Trowsdale J., Hanson I., Mockridge I., Beck S., Townsend A., Kelly A. Sequences encoded in the class II region of the MHC related to the 'ABC' superfamily of transporters. Nature. 348:1990;741-744.
    • (1990) Nature , vol.348 , pp. 741-744
    • Trowsdale, J.1    Hanson, I.2    Mockridge, I.3    Beck, S.4    Townsend, A.5    Kelly, A.6
  • 3
    • 0025751612 scopus 로고
    • Two putative subunits of a peptide pump encoded in the human major histocompatibility complex class II region
    • Bahram S., Arnold D., Bresnahan M., Strominger J.L., Spies T. Two putative subunits of a peptide pump encoded in the human major histocompatibility complex class II region. Proc Natl Acad Sci USA. 88:1991;10094-10098.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10094-10098
    • Bahram, S.1    Arnold, D.2    Bresnahan, M.3    Strominger, J.L.4    Spies, T.5
  • 4
    • 0026593016 scopus 로고
    • Assembly and function of the two ABC transporter proteins encoded in the human major histocompatibility complex
    • Kelly A., Powis S.H., Kerr L.-A., Mockridge I., Elliot T., Bastin J.et al. Assembly and function of the two ABC transporter proteins encoded in the human major histocompatibility complex. Nature. 355:1992;641-644.
    • (1992) Nature , vol.355 , pp. 641-644
    • Kelly, A.1    Powis, S.H.2    Kerr, L.-A.3    Mockridge, I.4    Elliot, T.5    Bastin, J.6
  • 5
    • 0026500826 scopus 로고
    • Presentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer
    • Spies T., Cerundolo V., Colonna M., Creswell P., Townsend A., DeMars R. Presentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer. Nature. 355:1992;644-646.
    • (1992) Nature , vol.355 , pp. 644-646
    • Spies, T.1    Cerundolo, V.2    Colonna, M.3    Creswell, P.4    Townsend, A.5    DeMars, R.6
  • 6
    • 0031895637 scopus 로고    scopus 로고
    • Mechanism of MHC class I-restricted antigen processing
    • Pamer E., Cresswell P. Mechanism of MHC class I-restricted antigen processing. Annu Rev Immunol. 16:1998;323-358.
    • (1998) Annu Rev Immunol , vol.16 , pp. 323-358
    • Pamer, E.1    Cresswell, P.2
  • 7
    • 0032503029 scopus 로고    scopus 로고
    • Viral strategies of immune evasion
    • Ploegh H.L. Viral strategies of immune evasion. Science. 280:1998;248-253.
    • (1998) Science , vol.280 , pp. 248-253
    • Ploegh, H.L.1
  • 8
    • 0032757721 scopus 로고    scopus 로고
    • Membrane topology and dimerization of the two subunits of the transporter associated with antigen processing reveal a three domain structure
    • Vos J.C., Spee P., Momburg F., Neefjes J. Membrane topology and dimerization of the two subunits of the transporter associated with antigen processing reveal a three domain structure. J Immunol. 163:1999;6679-6685.
    • (1999) J Immunol , vol.163 , pp. 6679-6685
    • Vos, J.C.1    Spee, P.2    Momburg, F.3    Neefjes, J.4
  • 9
    • 0027417476 scopus 로고
    • Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane
    • Nilsson I., von Heijne G. Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane. J Biol Chem. 268:1993;5798-5801.
    • (1993) J Biol Chem , vol.268 , pp. 5798-5801
    • Nilsson, I.1    Von Heijne, G.2
  • 10
    • 0029828991 scopus 로고    scopus 로고
    • Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • Wiertz E.J.H.J., Tortorella D., Bogyo M., Yu J., Mothes W., Jones T.R.et al. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature. 384:1996;432-438.
    • (1996) Nature , vol.384 , pp. 432-438
    • Wiertz, E.J.H.J.1    Tortorella, D.2    Bogyo, M.3    Yu, J.4    Mothes, W.5    Jones, T.R.6
  • 11
    • 0030789680 scopus 로고    scopus 로고
    • Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation
    • Pilon M., Schekman R., Römisch K. Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation. EMBO J. 16:1997;4540-4548.
    • (1997) EMBO J , vol.16 , pp. 4540-4548
    • Pilon, M.1    Schekman, R.2    Römisch, K.3
  • 12
    • 1842409617 scopus 로고    scopus 로고
    • Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
    • Plemper R.K., Bohmler S., Bordallo J., Sommer T., Wolf D.H. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature. 388:1997;891-895.
    • (1997) Nature , vol.388 , pp. 891-895
    • Plemper, R.K.1    Bohmler, S.2    Bordallo, J.3    Sommer, T.4    Wolf, D.H.5
  • 13
    • 0030782178 scopus 로고    scopus 로고
    • Membrane protein biogenesis: Regulated complexity at the endoplasmic reticulum
    • Hegde R.S., Lingappa V.R. Membrane protein biogenesis: regulated complexity at the endoplasmic reticulum. Cell. 91:1997;575-582.
    • (1997) Cell , vol.91 , pp. 575-582
    • Hegde, R.S.1    Lingappa, V.R.2
  • 16
  • 17
    • 0020491932 scopus 로고
    • Size dependence of the translational diffusion of large integral membrane proteins in liquid-crystalline phase lipid bilayers. A study using fluorescence recovery after photobleaching
    • Vaz W.L.C., Criado M., Madeira V.M.C., Schoellmann G., Jovin T.M. Size dependence of the translational diffusion of large integral membrane proteins in liquid-crystalline phase lipid bilayers. A study using fluorescence recovery after photobleaching. Biochemistry. 21:1982;5608-5612.
    • (1982) Biochemistry , vol.21 , pp. 5608-5612
    • Vaz, W.L.C.1    Criado, M.2    Madeira, V.M.C.3    Schoellmann, G.4    Jovin, T.M.5
  • 18
    • 0022444873 scopus 로고
    • Large deletions in the cytoplasmic kinase domain of the epidermal growth factor receptor do not affect its lateral mobility
    • Livneh E., Benveniste M., Prywes R., Felder S., Kam Z., Schlessinger J. Large deletions in the cytoplasmic kinase domain of the epidermal growth factor receptor do not affect its lateral mobility. J Cell Biol. 103:1982;327-331.
    • (1982) J Cell Biol , vol.103 , pp. 327-331
    • Livneh, E.1    Benveniste, M.2    Prywes, R.3    Felder, S.4    Kam, Z.5    Schlessinger, J.6
  • 19
    • 0029909604 scopus 로고    scopus 로고
    • Inhibition of oxidative cross-linking between engineered cysteine residues at positions 332 in predicted transmembrane segments (TM) 6 and 975 in predicted TM12 of human P-glycoprotein by drug substrates
    • Loo T.W., Clarke D.M. Inhibition of oxidative cross-linking between engineered cysteine residues at positions 332 in predicted transmembrane segments (TM) 6 and 975 in predicted TM12 of human P-glycoprotein by drug substrates. J Biol Chem. 271:1996;27482-27487.
    • (1996) J Biol Chem , vol.271 , pp. 27482-27487
    • Loo, T.W.1    Clarke, D.M.2
  • 20
    • 0030334864 scopus 로고    scopus 로고
    • Membrane proteins which exhibit multiple topological orientations
    • Levy D. Membrane proteins which exhibit multiple topological orientations. Essays Biochem. 31:1996;49-60.
    • (1996) Essays Biochem , vol.31 , pp. 49-60
    • Levy, D.1
  • 21
    • 0032113448 scopus 로고    scopus 로고
    • Regulation of protein topology by trans-acting factors at the endoplasmic reticulum
    • Hegde R.S., Voigt S., Lingappa V.R. Regulation of protein topology by trans-acting factors at the endoplasmic reticulum. Mol Cell. 2:1998;85-91.
    • (1998) Mol Cell , vol.2 , pp. 85-91
    • Hegde, R.S.1    Voigt, S.2    Lingappa, V.R.3
  • 22
    • 0026644816 scopus 로고
    • Bidirectional movement of a nascent polypeptide across microsomal membranes reveals requirements for vectorial translocation of proteins
    • Ooi C.E., Weiss J. Bidirectional movement of a nascent polypeptide across microsomal membranes reveals requirements for vectorial translocation of proteins. Cell. 71:1992;87-96.
    • (1992) Cell , vol.71 , pp. 87-96
    • Ooi, C.E.1    Weiss, J.2
  • 23
    • 0028110959 scopus 로고
    • Functional expression and purification of the ABC transporter complex associated with antigen processing (TAP) in insect cells
    • Meyer T.M., van Endert P.M., Uebel S., Ehring B., Tampé R. Functional expression and purification of the ABC transporter complex associated with antigen processing (TAP) in insect cells. FEBS Lett. 351:1994;443-447.
    • (1994) FEBS Lett , vol.351 , pp. 443-447
    • Meyer, T.M.1    Van Endert, P.M.2    Uebel, S.3    Ehring, B.4    Tampé, R.5
  • 24
    • 0030667856 scopus 로고    scopus 로고
    • Major histocompatibility complex class I molecules interact with both subunits of the transporter associated with antigen processing, TAP1 and TAP2
    • Powis S.J. Major histocompatibility complex class I molecules interact with both subunits of the transporter associated with antigen processing, TAP1 and TAP2. Eur J Immunol. 27:1997;2744-2747.
    • (1997) Eur J Immunol , vol.27 , pp. 2744-2747
    • Powis, S.J.1
  • 25
    • 0030971840 scopus 로고    scopus 로고
    • Structure of the multidrug resistance P-glycoprotein to 2.5 nm resolution determined by electron microscopy and image analysis
    • Rosenberg M.F., Callaghan R., Ford R.C., Higgins C.F. Structure of the multidrug resistance P-glycoprotein to 2.5 nm resolution determined by electron microscopy and image analysis. J Biol Chem. 272:1997;10685-10694.
    • (1997) J Biol Chem , vol.272 , pp. 10685-10694
    • Rosenberg, M.F.1    Callaghan, R.2    Ford, R.C.3    Higgins, C.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.