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Volumn 9, Issue 9, 1998, Pages 2681-2697

Coupled translocation events generate topological heterogeneity at the endoplasmic reticulum membrane

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN P;

EID: 0031686961     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.9.9.2681     Document Type: Article
Times cited : (33)

References (67)
  • 1
    • 0025375425 scopus 로고
    • Sec Y, a multispanning integral membrane protein, contains a potential leader peptidase cleavage site
    • Akiyama, Y., Inada, T., Nakamura, Y., and Ito., K. (1990). Sec Y, a multispanning integral membrane protein, contains a potential leader peptidase cleavage site. J. Bacteriol. 172, 2888-2893.
    • (1990) J. Bacteriol. , vol.172 , pp. 2888-2893
    • Akiyama, Y.1    Inada, T.2    Nakamura, Y.3    Ito, K.4
  • 3
    • 0029048812 scopus 로고
    • Multidrug resistance protein (Mdr)-alkaline phosphatase hybrids in Escherichia coli suggest a major revision in the topology of the C-terminal half of Mdr
    • Beja, O., and Bibi, E. (1995). Multidrug resistance protein (Mdr)-alkaline phosphatase hybrids in Escherichia coli suggest a major revision in the topology of the C-terminal half of Mdr. J. Biol. Chem. 270, 12351-12354.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12351-12354
    • Beja, O.1    Bibi, E.2
  • 4
    • 0030064680 scopus 로고    scopus 로고
    • A two step recognition of signal sequences determines the translocation efficiency of proteins
    • Belin, D., Bost, S., Vassalli, J.-D., and Strub, K. (1996). A two step recognition of signal sequences determines the translocation efficiency of proteins. EMBO J. 15, 468-478.
    • (1996) EMBO J. , vol.15 , pp. 468-478
    • Belin, D.1    Bost, S.2    Vassalli, J.-D.3    Strub, K.4
  • 5
    • 0024461835 scopus 로고
    • Facultative polypeptide translocation allows a single mRNA to encode the secreted and cytosolic forms of plasminogen activators inhibitor 2
    • Belin, D., Wohlend, A., Schleuning, W.-D., Kruithof, E., and Vassalli, J.-D. (1989). Facultative polypeptide translocation allows a single mRNA to encode the secreted and cytosolic forms of plasminogen activators inhibitor 2. EMBO J. 8, 3287-3294.
    • (1989) EMBO J. , vol.8 , pp. 3287-3294
    • Belin, D.1    Wohlend, A.2    Schleuning, W.-D.3    Kruithof, E.4    Vassalli, J.-D.5
  • 6
    • 0018987976 scopus 로고
    • Intracellular protein topogenesis
    • Blobel, G. (1980). Intracellular protein topogenesis. Proc. Natl. Acad. Sci. USA 77, 1496-1500.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1496-1500
    • Blobel, G.1
  • 7
    • 0014770988 scopus 로고
    • Controlled proteolysis of nascent polypeptides in rat liver cell fractions. I. Localization of polypeptides within ribosomes
    • Blobel, G., and Sabatini, D. (1970). Controlled proteolysis of nascent polypeptides in rat liver cell fractions. I. Localization of polypeptides within ribosomes. J. Cell Biol. 45, 130-145.
    • (1970) J. Cell Biol. , vol.45 , pp. 130-145
    • Blobel, G.1    Sabatini, D.2
  • 8
    • 0029894267 scopus 로고    scopus 로고
    • Biogenesis of polytopic membrane proteins: Membrane segments assemble within translocation channels prior to membrane integration
    • Borel, A., and Simon, S. (1996). Biogenesis of polytopic membrane proteins: Membrane segments assemble within translocation channels prior to membrane integration. Cell 85, 379-389.
    • (1996) Cell , vol.85 , pp. 379-389
    • Borel, A.1    Simon, S.2
  • 9
    • 0026581658 scopus 로고
    • Membrane protein spanning segments as export signals
    • Calamia, J., and Manoil, C. (1992). Membrane protein spanning segments as export signals. J. Mol. Biol. 224, 539-543.
    • (1992) J. Mol. Biol. , vol.224 , pp. 539-543
    • Calamia, J.1    Manoil, C.2
  • 11
    • 0022972654 scopus 로고
    • Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug resistant human cells
    • Chen, C.-J., Chin, J.E., Ueda, K., Clark, DO.P., Pastan, I., Gottesman, M.M., and Ronninson, I.B. (1986). Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug resistant human cells. Cell 47, 381-389.
    • (1986) Cell , vol.47 , pp. 381-389
    • Chen, C.-J.1    Chin, J.E.2    Ueda, K.3    Clark, D.O.P.4    Pastan, I.5    Gottesman, M.M.6    Ronninson, I.B.7
  • 12
    • 0026536874 scopus 로고
    • Pause transfer: A topogenic sequence in apolipoprotein B mediates stopping and restarting of translocation
    • Chuck, S., and Lingappa, V.R. (1992). Pause transfer: a topogenic sequence in apolipoprotein B mediates stopping and restarting of translocation. Cell 68, 9-21.
    • (1992) Cell , vol.68 , pp. 9-21
    • Chuck, S.1    Lingappa, V.R.2
  • 13
    • 0027985063 scopus 로고
    • Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore
    • Crowley, K., Liao, S., Worrell, V., Reinhart, G., and Johnson, A. (1994). Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore. Cell 78, 461-471.
    • (1994) Cell , vol.78 , pp. 461-471
    • Crowley, K.1    Liao, S.2    Worrell, V.3    Reinhart, G.4    Johnson, A.5
  • 14
    • 0027162564 scopus 로고
    • The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation
    • Crowley, K., Reinhart, G., and Johnson, A. (1993). The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation. Cell 73, 1101-1115.
    • (1993) Cell , vol.73 , pp. 1101-1115
    • Crowley, K.1    Reinhart, G.2    Johnson, A.3
  • 15
  • 16
    • 0029128068 scopus 로고
    • Membrane insertion and assembly of ductin: A polytopic channel with dual orientations
    • Dunlop, J., Jones, P., and Finbow, M. (1995). Membrane insertion and assembly of ductin: a polytopic channel with dual orientations. EMBO J. 14, 3609-3616.
    • (1995) EMBO J. , vol.14 , pp. 3609-3616
    • Dunlop, J.1    Jones, P.2    Finbow, M.3
  • 17
    • 0028064967 scopus 로고
    • SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion
    • Economou, A., and Wickner, W. (1994). SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion. Cell 78, 835-843.
    • (1994) Cell , vol.78 , pp. 835-843
    • Economou, A.1    Wickner, W.2
  • 18
    • 0022510143 scopus 로고
    • Identifying non-polar transmembrane helices in amino acid sequences of membrane proteins
    • Engelman, D., Steitz, T., and Goldman, A. (1986). Identifying non-polar transmembrane helices in amino acid sequences of membrane proteins. Annu. Rev. Biophys. Biophys. Chem. 15, 321-353.
    • (1986) Annu. Rev. Biophys. Biophys. Chem. , vol.15 , pp. 321-353
    • Engelman, D.1    Steitz, T.2    Goldman, A.3
  • 19
    • 0028242424 scopus 로고
    • Evidence that the 16 kDa proteolipid (subunit c) of the vacuolar H(+)-ATPase and ductin from gap junctions are the same polypeptide in Drosophila and Manduca: Molecular cloning of the Vha16k gene from Drosophila
    • Finbow, M., Goodwin, S., Meagher, L., Lane, N., Keen, J., Findlay, J., and Kaiser, K. (1994). Evidence that the 16 kDa proteolipid (subunit c) of the vacuolar H(+)-ATPase and ductin from gap junctions are the same polypeptide in Drosophila and Manduca: molecular cloning of the Vha16k gene from Drosophila. J. Cell Sci. 107, 1817-1824.
    • (1994) J. Cell Sci. , vol.107 , pp. 1817-1824
    • Finbow, M.1    Goodwin, S.2    Meagher, L.3    Lane, N.4    Keen, J.5    Findlay, J.6    Kaiser, K.7
  • 20
    • 0030860899 scopus 로고    scopus 로고
    • The degradation of apolipoprotein B100 is mediated by the ubiquitin-proteasome pathway and involves heat shock protein 70
    • Fisher, E., Zhou, M., Mitchell, D., Wu, X., Omura, S., Wang, H., Goldberg, A., and Ginsberg, H. (1997). The degradation of apolipoprotein B100 is mediated by the ubiquitin-proteasome pathway and involves heat shock protein 70. J. Biol. Chem. 272, 20427-20434.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20427-20434
    • Fisher, E.1    Zhou, M.2    Mitchell, D.3    Wu, X.4    Omura, S.5    Wang, H.6    Goldberg, A.7    Ginsberg, H.8
  • 21
    • 0022358406 scopus 로고
    • Bovine opsin has more than one signal sequence
    • Friedlander, M., and Blobel, G. (1985). Bovine opsin has more than one signal sequence. Nature 318, 338-343.
    • (1985) Nature , vol.318 , pp. 338-343
    • Friedlander, M.1    Blobel, G.2
  • 22
    • 0028175016 scopus 로고
    • Topological "frustration" in multispanning E. coli inner membrane
    • Gafvelin, G., and von Heijne., G. (1994). Topological "frustration" in multispanning E. coli inner membrane. Cell 77, 401-412.
    • (1994) Cell , vol.77 , pp. 401-412
    • Gafvelin, G.1    Von Heijne, G.2
  • 23
    • 0027391633 scopus 로고
    • Topology of P-glycoprotein as determined by epitope mapping of MRK-16 monoclonal antibody
    • Georges, E., Tsuro, T., and Ling, V. (1993). Topology of P-glycoprotein as determined by epitope mapping of MRK-16 monoclonal antibody. J. Biol. Chem. 268, 1792-1798.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1792-1798
    • Georges, E.1    Tsuro, T.2    Ling, V.3
  • 24
    • 0022993652 scopus 로고
    • Mammalian multidrug resistance gene: Complete cDNA sequence indicates strong homology to bacterial transport proteins
    • Gros, P., Croop, J., and Housman, D. (1986). Mammalian multidrug resistance gene: complete cDNA sequence indicates strong homology to bacterial transport proteins. Cell 47, 371-380.
    • (1986) Cell , vol.47 , pp. 371-380
    • Gros, P.1    Croop, J.2    Housman, D.3
  • 25
    • 0032549767 scopus 로고    scopus 로고
    • Bip maintains the permeability of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation
    • Hamman, B., Hendershot, L., and Johnson, A. (1998). Bip maintains the permeability of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell 92, 747-758.
    • (1998) Cell , vol.92 , pp. 747-758
    • Hamman, B.1    Hendershot, L.2    Johnson, A.3
  • 26
    • 0023098327 scopus 로고
    • Biogenesis and transmembrane orientation of the cellular isoform of the scrapie prion protein
    • Hay, B., Barry, R., Lieberburg, I., Prusiner, S., and Lingappa, V.R. (1987a). Biogenesis and transmembrane orientation of the cellular isoform of the scrapie prion protein. Mol. Cell. Biol. 7, 914-920.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 914-920
    • Hay, B.1    Barry, R.2    Lieberburg, I.3    Prusiner, S.4    Lingappa, V.R.5
  • 27
    • 0023566948 scopus 로고
    • Evidence for a secretory form of the cellular prion protein
    • Hay, B., Prusiner, S., and Lingappa, V.R. (1987b). Evidence for a secretory form of the cellular prion protein. Biochemistry 26, 8110-8115.
    • (1987) Biochemistry , vol.26 , pp. 8110-8115
    • Hay, B.1    Prusiner, S.2    Lingappa, V.R.3
  • 28
    • 3543051499 scopus 로고    scopus 로고
    • Sequence-specific alteration of the ribosome-membrane junction exposes nascent secretory proteins to the cytosol
    • Hedge, K., and Lingappa, V. (1996). Sequence-specific alteration of the ribosome-membrane junction exposes nascent secretory proteins to the cytosol. Cell 85, 721-732.
    • (1996) Cell , vol.85 , pp. 721-732
    • Hedge, K.1    Lingappa, V.2
  • 29
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, N., Hunt, H., Horton, R., Pullen, J., and Pease, P. (1989). Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, N.1    Hunt, H.2    Horton, R.3    Pullen, J.4    Pease, P.5
  • 30
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteosome, contribute to CFTR processing
    • Jensen, T., Loo, M., Pind, S., Williams, D., Goldberg, A., and Riordan, J. (1995). Multiple proteolytic systems, including the proteosome, contribute to CFTR processing. Cell 83, 129-136.
    • (1995) Cell , vol.83 , pp. 129-136
    • Jensen, T.1    Loo, M.2    Pind, S.3    Williams, D.4    Goldberg, A.5    Riordan, J.6
  • 31
    • 0031106619 scopus 로고    scopus 로고
    • Protein translocation at the ER membrane: A complex process becomes more so
    • Johnson, A. (1997). Protein translocation at the ER membrane: a complex process becomes more so. Trends Cell Biol. 7, 90-94.
    • (1997) Trends Cell Biol. , vol.7 , pp. 90-94
    • Johnson, A.1
  • 32
    • 0029918133 scopus 로고    scopus 로고
    • Transmembrane organization of mouse P-glycoprotein determined by epitope insertion and immunofluorescence
    • Kast, C., Canfield, V., Levenson, R., and Gros, P. (1996). Transmembrane organization of mouse P-glycoprotein determined by epitope insertion and immunofluorescence. J. Biol. Chem. 271, 9240-9248.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9240-9248
    • Kast, C.1    Canfield, V.2    Levenson, R.3    Gros, P.4
  • 33
    • 0025882870 scopus 로고
    • Systematic analysis of stop-transfer sequence for microsomal membrane
    • Kuroiwa, T., Sakaguchi, M., Mihara, K., and Omura, T. (1991). Systematic analysis of stop-transfer sequence for microsomal membrane. J. Biol. Chem. 266, 9251-9255.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9251-9255
    • Kuroiwa, T.1    Sakaguchi, M.2    Mihara, K.3    Omura, T.4
  • 34
    • 0031030059 scopus 로고    scopus 로고
    • Discrete cross-linking products identified during membrane protein biosynthesis
    • Laird, V., and High, S. (1997). Discrete cross-linking products identified during membrane protein biosynthesis. J. Biol. Chem. 271, 1983-1989.
    • (1997) J. Biol. Chem. , vol.271 , pp. 1983-1989
    • Laird, V.1    High, S.2
  • 35
    • 0031471055 scopus 로고    scopus 로고
    • Both luminal and cytosolic gating of the aqueous translocon pore are regulated from inside the ribosome during membrane protein integration
    • Liao, S., Lin, J., Do, H., and Johnson, A. (1997). Both luminal and cytosolic gating of the aqueous translocon pore are regulated from inside the ribosome during membrane protein integration. Cell 90, 31-42.
    • (1997) Cell , vol.90 , pp. 31-42
    • Liao, S.1    Lin, J.2    Do, H.3    Johnson, A.4
  • 36
    • 0028900576 scopus 로고
    • A novel integration signal that is composed of two transmembrane segments is required to integrate the neorospora plasma membrane H+-ATPase into microsomes
    • Lin, J., and Addison, R. (1995). A novel integration signal that is composed of two transmembrane segments is required to integrate the neorospora plasma membrane H+-ATPase into microsomes. J. Biol. Chem. 270, 6935-6941.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6935-6941
    • Lin, J.1    Addison, R.2
  • 37
    • 0024454463 scopus 로고
    • Structural requirements for membrane assembly of proteins spanning the membrane several times
    • Lipp, J., Flint, N., Haeuptle, M.T., and Dobberstein, B. (1989). Structural requirements for membrane assembly of proteins spanning the membrane several times. J. Cell Biol. 109, 2013-2022.
    • (1989) J. Cell Biol. , vol.109 , pp. 2013-2022
    • Lipp, J.1    Flint, N.2    Haeuptle, M.T.3    Dobberstein, B.4
  • 38
    • 0028928984 scopus 로고
    • Membrane topology of a cysteine-less mutant of human P-glycoprotein
    • Loo, T., and Clarke, D. (1995). Membrane topology of a cysteine-less mutant of human P-glycoprotein. J. Biol. Chem. 270, 843-848.
    • (1995) J. Biol. Chem. , vol.270 , pp. 843-848
    • Loo, T.1    Clarke, D.2
  • 39
    • 0025239839 scopus 로고
    • Unusual topogenic sequence directs prion protein biogenesis
    • Lopez, C.D., Yost, C.S., Prusiner, S.B., Myers, R.M., and Lingappa, V.R. (1990). Unusual topogenic sequence directs prion protein biogenesis. Science 248, 226-229.
    • (1990) Science , vol.248 , pp. 226-229
    • Lopez, C.D.1    Yost, C.S.2    Prusiner, S.B.3    Myers, R.M.4    Lingappa, V.R.5
  • 40
    • 0031983038 scopus 로고    scopus 로고
    • Co-and posttranslational mechanisms direct CFTR N-terminus transmembrane assembly
    • Lu, Y., Xiong, X., Bragin, A., Kamani, K., and Skach, W. (1997). Co-and posttranslational mechanisms direct CFTR N-terminus transmembrane assembly. J. Biol. Chem. 273, 568-576.
    • (1997) J. Biol. Chem. , vol.273 , pp. 568-576
    • Lu, Y.1    Xiong, X.2    Bragin, A.3    Kamani, K.4    Skach, W.5
  • 41
    • 0029112669 scopus 로고
    • Membrane disposition of the M5-M6 hairpin of the Na, K-ATPase a-subunit is ligand dependent
    • Lutsenko, S., Anderko, R., and Kaplan, J. (1995). Membrane disposition of the M5-M6 hairpin of the Na, K-ATPase a-subunit is ligand dependent. Proc. Natl. Acad. Sci USA 92, 7936-7940.
    • (1995) Proc. Natl. Acad. Sci USA , vol.92 , pp. 7936-7940
    • Lutsenko, S.1    Anderko, R.2    Kaplan, J.3
  • 42
    • 0022878780 scopus 로고
    • A stop transfer sequence recognizes receptors for nascent chain translocation across the endoplasmic reticulum membrane
    • Mize, N.K., Andrews, D.W., and Lingappa, V.R. (1986). A stop transfer sequence recognizes receptors for nascent chain translocation across the endoplasmic reticulum membrane. Cell 47, 711-719.
    • (1986) Cell , vol.47 , pp. 711-719
    • Mize, N.K.1    Andrews, D.W.2    Lingappa, V.R.3
  • 43
    • 0030825974 scopus 로고    scopus 로고
    • Molecular mechanism of membrane protein integration into the endoplasmic reticulum
    • Mothes, W., Heinrich, S., Graf, R., Nilsson, I., von Heijne, G., Brunner, J., and Rapoport, T. (1997). Molecular mechanism of membrane protein integration into the endoplasmic reticulum. Cell 89, 523-533.
    • (1997) Cell , vol.89 , pp. 523-533
    • Mothes, W.1    Heinrich, S.2    Graf, R.3    Nilsson, I.4    Von Heijne, G.5    Brunner, J.6    Rapoport, T.7
  • 44
    • 0028363370 scopus 로고
    • Translocational pausing is a common step in the biosynthesis of unconventional integral membrane and secretory proteins
    • Nakahara, D., Lingappa, V., and Chuck, S. (1994). Translocational pausing is a common step in the biosynthesis of unconventional integral membrane and secretory proteins. J. Biol. Chem. 269, 7617-7622.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7617-7622
    • Nakahara, D.1    Lingappa, V.2    Chuck, S.3
  • 45
    • 0029997381 scopus 로고    scopus 로고
    • Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation
    • Nishiyama, K., Suzuki, T., and Tokuda, H. (1996). Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation. Cell 85, 71-82.
    • (1996) Cell , vol.85 , pp. 71-82
    • Nishiyama, K.1    Suzuki, T.2    Tokuda, H.3
  • 46
    • 0025970881 scopus 로고
    • Topology of eukaryotic type II membrane proteins: Importance of N-terminal positively charged residues flanking the hydrophobic domain
    • Parks, G., and Lamb, R. (1991). Topology of eukaryotic type II membrane proteins: importance of N-terminal positively charged residues flanking the hydrophobic domain. Cell 64, 777-787.
    • (1991) Cell , vol.64 , pp. 777-787
    • Parks, G.1    Lamb, R.2
  • 47
    • 0024473093 scopus 로고
    • Transposition of domains between the M2 and HN viral membrane proteins results in polypeptides which can adopt more than one membrane orientation
    • Parks, G.D., Hull, D., and Lamb, R.A. (1989). Transposition of domains between the M2 and HN viral membrane proteins results in polypeptides which can adopt more than one membrane orientation. J. Cell Biol. 109, 2023-2032.
    • (1989) J. Cell Biol. , vol.109 , pp. 2023-2032
    • Parks, G.D.1    Hull, D.2    Lamb, R.A.3
  • 48
    • 0029036714 scopus 로고
    • Isolation of antigenic mimics of MDR1-P-glycoprotein by phage-displayed peptide libraries
    • Poloni, F., Romagnoli, G., Cianfriglia, M., and Felici, F. (1995). Isolation of antigenic mimics of MDR1-P-glycoprotein by phage-displayed peptide libraries. Int. J. Cancer 61, 727-731.
    • (1995) Int. J. Cancer , vol.61 , pp. 727-731
    • Poloni, F.1    Romagnoli, G.2    Cianfriglia, M.3    Felici, F.4
  • 49
    • 0030222331 scopus 로고    scopus 로고
    • Approaching the mechanism of protein transport across the ER membrane
    • Rapoport, T., Rolls, M., and Jungnickel, B. (1996). Approaching the mechanism of protein transport across the ER membrane. Curr. Opin. Cell Biol. 8, 499-504.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 499-504
    • Rapoport, T.1    Rolls, M.2    Jungnickel, B.3
  • 50
    • 0002369324 scopus 로고
    • Intrinsic membrane protein structure: Principles and predictions
    • ed. P. Yeagle, Boca Raton, FL: CRC Press
    • Reithmeier, R., and Deber, C. (1992). Intrinsic membrane protein structure: principles and predictions. In: The Structure of Biological Membranes, ed. P. Yeagle, Boca Raton, FL: CRC Press, 337-393.
    • (1992) The Structure of Biological Membranes , pp. 337-393
    • Reithmeier, R.1    Deber, C.2
  • 51
    • 0023729159 scopus 로고
    • Construction of defined polytopic integral transmembrane proteins
    • Rothman, R.E., Andrews, D.W., Calayag, M.C., and Lingappa, V.R. (1988). Construction of defined polytopic integral transmembrane proteins. J. Biol. Chem. 263, 10470-10480.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10470-10480
    • Rothman, R.E.1    Andrews, D.W.2    Calayag, M.C.3    Lingappa, V.R.4
  • 53
    • 0023806486 scopus 로고
    • Deletion of the amino-terminal domain of asialoglycoprotein receptor H1 allows cleavage of the internal signal sequence
    • Schmid, S.R., and Spiess, M. (1988). Deletion of the amino-terminal domain of asialoglycoprotein receptor H1 allows cleavage of the internal signal sequence. J. Biol. Chem. 163, 16886-16891.
    • (1988) J. Biol. Chem. , vol.163 , pp. 16886-16891
    • Schmid, S.R.1    Spiess, M.2
  • 54
    • 0029069427 scopus 로고
    • Distinct biogenesis mechanisms for water channels MIWC and CHIP28 at the endoplasmic reticulum
    • Shi, L.-B., Skach, W., Ma, T., and Verkman, A. (1995). Distinct biogenesis mechanisms for water channels MIWC and CHIP28 at the endoplasmic reticulum. Biochemistry 34, 8250-8256.
    • (1995) Biochemistry , vol.34 , pp. 8250-8256
    • Shi, L.-B.1    Skach, W.2    Ma, T.3    Verkman, A.4
  • 55
    • 0027512232 scopus 로고
    • Evidence for an alternate model of human P-glycoprotein structure and biogenesis
    • Skach, W., Calayag, M.C., and Lingappa, V. (1993). Evidence for an alternate model of human P-glycoprotein structure and biogenesis. J Biol. Chem. 268, 6903-6908.
    • (1993) J Biol. Chem. , vol.268 , pp. 6903-6908
    • Skach, W.1    Calayag, M.C.2    Lingappa, V.3
  • 56
    • 0027519416 scopus 로고
    • Amino terminus assembly of human P-glycoprotein at the endoplasmic reticulum is directed by cooperative actions of two internal sequences
    • Skach, W., and Lingappa, V. (1993). Amino terminus assembly of human P-glycoprotein at the endoplasmic reticulum is directed by cooperative actions of two internal sequences. J. Biol. Chem. 268, 23552-23561.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23552-23561
    • Skach, W.1    Lingappa, V.2
  • 57
    • 0028343114 scopus 로고
    • Transmembrane orientation and topogenesis of the 3rd and 4th membrane-spanning regions of human P-glycoprotein (MDR1)
    • Skach, W., and Lingappa, V. (1994). Transmembrane orientation and topogenesis of the 3rd and 4th membrane-spanning regions of human P-glycoprotein (MDR1). Cancer Res. 54, 3202-3209.
    • (1994) Cancer Res. , vol.54 , pp. 3202-3209
    • Skach, W.1    Lingappa, V.2
  • 58
    • 0028318283 scopus 로고
    • Biogenesis and transmembrane topology of the CHIP28 water channel in the endoplasmic reticulum
    • Skach, W., Shi, L.-B., Calayag, M.C., Frigeri, A., Lingappa, V., and Verkman, A. (1994). Biogenesis and transmembrane topology of the CHIP28 water channel in the endoplasmic reticulum. J. Cell Biol. 125, 803-815.
    • (1994) J. Cell Biol. , vol.125 , pp. 803-815
    • Skach, W.1    Shi, L.-B.2    Calayag, M.C.3    Frigeri, A.4    Lingappa, V.5    Verkman, A.6
  • 59
    • 0028100898 scopus 로고
    • Identification of a translocated protein segment in a voltage-dependent channel
    • Slatin, S., Qui, X.-Q., Jakes, K., and Finkelstein, A. (1994). Identification of a translocated protein segment in a voltage-dependent channel. Nature 371, 158-161.
    • (1994) Nature , vol.371 , pp. 158-161
    • Slatin, S.1    Qui, X.-Q.2    Jakes, K.3    Finkelstein, A.4
  • 60
    • 0023782388 scopus 로고
    • Insertion of a multispanning membrane protein occurs sequentially and requires only one signal sequence
    • Wessels, H., and Spiess, M. (1988). Insertion of a multispanning membrane protein occurs sequentially and requires only one signal sequence. Cell 55, 61-70.
    • (1988) Cell , vol.55 , pp. 61-70
    • Wessels, H.1    Spiess, M.2
  • 61
    • 0029817931 scopus 로고    scopus 로고
    • Determination of the transmembrane topology of yeast Sec61p, an essential component of the endoplasmic reticulum translocation complex
    • Wilkinson, B., Critchley, A., and Stirling, C. (1996). Determination of the transmembrane topology of yeast Sec61p, an essential component of the endoplasmic reticulum translocation complex. J. Biol. Chem. 271, 25590-25597.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25590-25597
    • Wilkinson, B.1    Critchley, A.2    Stirling, C.3
  • 62
    • 0023124557 scopus 로고
    • Plasminogen activator-specific inhibitors produced by human monocytes/macrophoges
    • Wohlwend, A., Belin, D., and Vassalli, J.-D. (1987). Plasminogen activator-specific inhibitors produced by human monocytes/macrophoges. J. Exp. Med. 165, 320-339.
    • (1987) J. Exp. Med. , vol.165 , pp. 320-339
    • Wohlwend, A.1    Belin, D.2    Vassalli, J.-D.3
  • 63
    • 0030931382 scopus 로고    scopus 로고
    • Structural cues involved in ER degradation of G85E and G91R mutant CFTR
    • Xiong, X., Bragin, A., Widdicombe, J., Cohn, J., and Skach, W. (1997). Structural cues involved in ER degradation of G85E and G91R mutant CFTR. J. Clin. Invest. 100, 1079-1088.
    • (1997) J. Clin. Invest. , vol.100 , pp. 1079-1088
    • Xiong, X.1    Bragin, A.2    Widdicombe, J.3    Cohn, J.4    Skach, W.5
  • 64
    • 0024441318 scopus 로고
    • Cytoplasmic orientation and two-domain structure of the multidrug transporter, P-glycoprotein, demonstrated with sequence-specific antibodies
    • Yoshimura, A., Kuwazuru, Y., Sumizawa, T., Ichikawa, M., Ikeda, S., Uda, T., and Akitama, S. (1989). Cytoplasmic orientation and two-domain structure of the multidrug transporter, P-glycoprotein, demonstrated with sequence-specific antibodies. J. Biol. Chem. 264, 16282-16291.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16282-16291
    • Yoshimura, A.1    Kuwazuru, Y.2    Sumizawa, T.3    Ichikawa, M.4    Ikeda, S.5    Uda, T.6    Akitama, S.7
  • 65
    • 0025120245 scopus 로고
    • Non-hydrophobic extracytoplasmic determinant of stop transfer in the prion protein
    • Yost, C.S., Lopez, C.D., Prusiner, S.B., Meyers, R.M., and Lingappa, V.R. (1990). Non-hydrophobic extracytoplasmic determinant of stop transfer in the prion protein. Nature 343, 669-672.
    • (1990) Nature , vol.343 , pp. 669-672
    • Yost, C.S.1    Lopez, C.D.2    Prusiner, S.B.3    Meyers, R.M.4    Lingappa, V.R.5
  • 66
    • 0025951859 scopus 로고
    • Study of membrane orientation and glycosylated extracellular loops of mouse P-glycoprotein by in vitro translation
    • Zhang, J.-T., and Ling, V. (1991). Study of membrane orientation and glycosylated extracellular loops of mouse P-glycoprotein by in vitro translation. J. Biol. Chem. 266, 18224-18232.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18224-18232
    • Zhang, J.-T.1    Ling, V.2
  • 67
    • 0029744137 scopus 로고    scopus 로고
    • Topological folding and proteolysis profile of P-glycoprotein in membranes of multidrug-resistant cells: Implication for drug transport mechanisms
    • Zhang, M., Wang, G., Shapiro, A., and Zhang, J.-T. (1996). Topological folding and proteolysis profile of P-glycoprotein in membranes of multidrug-resistant cells: implication for drug transport mechanisms. Biochemistry 35, 9728-9736.
    • (1996) Biochemistry , vol.35 , pp. 9728-9736
    • Zhang, M.1    Wang, G.2    Shapiro, A.3    Zhang, J.-T.4


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