메뉴 건너뛰기




Volumn 85, Issue 3, 1996, Pages 379-389

Biogenesis of polytopic membrane proteins: Membrane segments assemble within translocation channels prior to membrane integration

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

EID: 0029894267     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81116-2     Document Type: Article
Times cited : (120)

References (53)
  • 1
    • 0020288333 scopus 로고
    • Signal recognition protein is required for the integration of acetylcholine receptor 8 subunit, a transmembrane glycoprotein, into the endoplasmic reticulum membrane
    • Anderson, D.J., Walter, P., and Blobel, G. (1982). Signal recognition protein is required for the integration of acetylcholine receptor 8 subunit, a transmembrane glycoprotein, into the endoplasmic reticulum membrane. J. Cell Biol. 93, 501-506.
    • (1982) J. Cell Biol. , vol.93 , pp. 501-506
    • Anderson, D.J.1    Walter, P.2    Blobel, G.3
  • 2
    • 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
  • 3
    • 0016752682 scopus 로고
    • Transfer of proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components
    • Blobel, G., and Dobberstein, B. (1975). Transfer of proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components. J. Cell Biol. 67, 852-862.
    • (1975) J. Cell Biol. , vol.67 , pp. 852-862
    • Blobel, G.1    Dobberstein, B.2
  • 4
    • 0014202545 scopus 로고
    • Studies on free and membrane-bound ribosomes in rat liver. II. Interaction of ribosomes and membranes
    • Blobel, G., and Potter, V.R. (1967). Studies on free and membrane-bound ribosomes in rat liver. II. Interaction of ribosomes and membranes. J. Mol. Biol. 26, 293-301.
    • (1967) J. Mol. Biol. , vol.26 , pp. 293-301
    • Blobel, G.1    Potter, V.R.2
  • 5
    • 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, D.P., Pastan, I., Gottesman, M.M., and Roninson, 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.P.4    Pastan, I.5    Gottesman, M.M.6    Roninson, I.B.7
  • 6
    • 0027985063 scopus 로고
    • Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore
    • Crowley, K.S., Liao, S., Worrell, V.E., Reinhart, G.D., and Johnson, A.E. (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.S.1    Liao, S.2    Worrell, V.E.3    Reinhart, G.D.4    Johnson, A.E.5
  • 7
    • 0026781952 scopus 로고
    • Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive
    • Denning, G.M., Anderson, M.P., Amara, J.F., Marshall, J., Smith, A.E., and Welsh, M.J. (1992). Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive. Nature 358, 761-764.
    • (1992) Nature , vol.358 , pp. 761-764
    • Denning, G.M.1    Anderson, M.P.2    Amara, J.F.3    Marshall, J.4    Smith, A.E.5    Welsh, M.J.6
  • 8
    • 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
  • 9
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment application to endoplasmic reticulum
    • Fujiki, Y., Hubbard, A.L., Fowler, S., and Lazarow, P. (1982). Isolation of intracellular membranes by means of sodium carbonate treatment application to endoplasmic reticulum. J. Cell Biol. 93, 97-102.
    • (1982) J. Cell Biol. , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.4
  • 10
    • 0027391633 scopus 로고
    • Topology of P-glycoprotein as determined by epitope mapping of MRK-16 monoclonal antibody
    • Georges, E., Tsuruo, 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    Tsuruo, T.2    Ling, V.3
  • 11
    • 0023019651 scopus 로고
    • Homology between P-glycoprotein and a bacterial haemolysin transport protein suggests a model for multidrug resistance
    • Gerlach, J.H., Endicott, J.A., Juranka, P.F., Henderson, G., Sarangi, F., Deuchars, K.L., and Ling, V. (1986). Homology between P-glycoprotein and a bacterial haemolysin transport protein suggests a model for multidrug resistance. Nature 324, 485-489.
    • (1986) Nature , vol.324 , pp. 485-489
    • Gerlach, J.H.1    Endicott, J.A.2    Juranka, P.F.3    Henderson, G.4    Sarangi, F.5    Deuchars, K.L.6    Ling, V.7
  • 12
    • 0022129497 scopus 로고
    • Translocation of secretory proteins across the microsomal membrane occurs through an environment accessible to aqueous perturbants
    • Gilmore, R., and Blobel, G. (1985). Translocation of secretory proteins across the microsomal membrane occurs through an environment accessible to aqueous perturbants. Cell 42, 497-505.
    • (1985) Cell , vol.42 , pp. 497-505
    • Gilmore, R.1    Blobel, G.2
  • 13
    • 0026531641 scopus 로고
    • Mutants in three novel complementation groups inhibit membrane protein insertion into and soluble protein translocation across the endoplasmic reticulum membrane of Saccharomyces cerevisiae
    • Green, N., Fang, H., and Walter, P. (1992). Mutants in three novel complementation groups inhibit membrane protein insertion into and soluble protein translocation across the endoplasmic reticulum membrane of Saccharomyces cerevisiae. J. Cell Biol. 116, 597-604.
    • (1992) J. Cell Biol. , vol.116 , pp. 597-604
    • Green, N.1    Fang, H.2    Walter, P.3
  • 14
    • 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
  • 15
    • 0028198111 scopus 로고
    • How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum
    • Helenius, A. (1994). How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol. Biol. Cell 5, 253-265.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 253-265
    • Helenius, A.1
  • 16
    • 0025858671 scopus 로고
    • The identification of proteins in the proximity of signal-anchor sequences during their targeting to and insertion into the membrane of the ER
    • High, S., Görlich, D., Wiedmann, M., Rapoport, T.A., and Dobberstein, B. (1991). The identification of proteins in the proximity of signal-anchor sequences during their targeting to and insertion into the membrane of the ER. J. Cell Biol. 113, 35-44.
    • (1991) J. Cell Biol. , vol.113 , pp. 35-44
    • High, S.1    Görlich, D.2    Wiedmann, M.3    Rapoport, T.A.4    Dobberstein, B.5
  • 17
    • 0027229977 scopus 로고
    • Sec61p is adjacent to nascent type I and type II signal-anchor proteins during their membrane insertion
    • High, S., Andersen, S.S.L., Görlich, D., Hartmann, E., Prehn, S., Rapoport, T.A., and Dobberstein, B. (1993). Sec61p is adjacent to nascent type I and type II signal-anchor proteins during their membrane insertion. J. Cell Biol. 121, 743-750.
    • (1993) J. Cell Biol. , vol.121 , pp. 743-750
    • High, S.1    Andersen, S.S.L.2    Görlich, D.3    Hartmann, E.4    Prehn, S.5    Rapoport, T.A.6    Dobberstein, B.7
  • 18
    • 0027393014 scopus 로고
    • The SecA and SecY subunits of translocase are the nearest neighbors of a translocating preprotein, shielding it from phospholipids
    • Joly, J.C., and Wickner, W. (1993). The SecA and SecY subunits of translocase are the nearest neighbors of a translocating preprotein, shielding it from phospholipids. EMBO J. 12, 255-263.
    • (1993) EMBO J. , vol.12 , pp. 255-263
    • Joly, J.C.1    Wickner, W.2
  • 19
    • 0027953913 scopus 로고
    • Binding of ribosomes to the rough endoplasmic reticulum mediated by the Sec61p complex
    • Kalies, K.-U., Görlich, D., and Rapoport, T.A. (1994). Binding of ribosomes to the rough endoplasmic reticulum mediated by the Sec61p complex. J. Cell Biol. 126, 925-934.
    • (1994) J. Cell Biol. , vol.126 , pp. 925-934
    • Kalies, K.-U.1    Görlich, D.2    Rapoport, T.A.3
  • 20
    • 0013789790 scopus 로고
    • Dissociation of human co-hemoglobin by urea, guanidine hydrochloride, and other reagents
    • Kawahara, K., Kirshner, A.G., and Tanford, C. (1965). Dissociation of human co-hemoglobin by urea, guanidine hydrochloride, and other reagents. Biochemistry 4, 1203-1213.
    • (1965) Biochemistry , vol.4 , pp. 1203-1213
    • Kawahara, K.1    Kirshner, A.G.2    Tanford, C.3
  • 21
    • 0018219030 scopus 로고
    • A signal sequence for the insertion of a transmembrane glycoprotein: Similarities to the signals of secretory proteins in primary structure and function
    • Lingappa, V.R., Katz, F.N., Lodish, H.F., and Blobel, G. (1978). A signal sequence for the insertion of a transmembrane glycoprotein: similarities to the signals of secretory proteins in primary structure and function. J. Biol. Chem. 253, 8667-8670.
    • (1978) J. Biol. Chem. , vol.253 , pp. 8667-8670
    • Lingappa, V.R.1    Katz, F.N.2    Lodish, H.F.3    Blobel, G.4
  • 23
    • 0028127183 scopus 로고
    • Prolonged association of temperature-sensitive mutants of human P-glycoprotein with calnexin during biogenesis
    • Loo, T.W., and Clarke, D.M. (1994). Prolonged association of temperature-sensitive mutants of human P-glycoprotein with calnexin during biogenesis. J. Biol. Chem. 269, 28683-28689.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28683-28689
    • Loo, T.W.1    Clarke, D.M.2
  • 24
    • 0023879525 scopus 로고
    • Vesicular stomatitis virus G proteins with altered glycosylation sites display temperature-sensitive intracellular transport and are subject to aberrant intermolecular disulfide bonding
    • Machamer, C.E., and Rose, J.K. (1988). Vesicular stomatitis virus G proteins with altered glycosylation sites display temperature-sensitive intracellular transport and are subject to aberrant intermolecular disulfide bonding. J. Biol. Chem. 263, 5955-5960.
    • (1988) J. Biol. Chem. , vol.263 , pp. 5955-5960
    • Machamer, C.E.1    Rose, J.K.2
  • 25
    • 0029002962 scopus 로고
    • The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer
    • Martoglio, B., Hofmann, M.W., Brunner, J., and Dobberstein, B. (1995). The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer. Cell 81, 207-214.
    • (1995) Cell , vol.81 , pp. 207-214
    • Martoglio, B.1    Hofmann, M.W.2    Brunner, J.3    Dobberstein, B.4
  • 26
    • 0019047935 scopus 로고
    • Biogenesis of membrane-bound and secreted immunoglobulins. I. Two distinct translation products of human μ-chain, with identical N-termini and different C-termini
    • McCune, J.M., Lingappa, V.R., Fu, S.M., Blobel, G., and Kunkel, H.G. (1980). Biogenesis of membrane-bound and secreted immunoglobulins. I. Two distinct translation products of human μ-chain, with identical N-termini and different C-termini. J. Exp. Med. 152, 463-468.
    • (1980) J. Exp. Med. , vol.152 , pp. 463-468
    • McCune, J.M.1    Lingappa, V.R.2    Fu, S.M.3    Blobel, G.4    Kunkel, H.G.5
  • 27
    • 0019845153 scopus 로고
    • Biogenesis of membrane-bound and secreted immunoglobulins: Two primary translation products of the human 8 chain, differentially N-glycosylated to four discrete forms in vivo and in vitro
    • McCune, J.M., Fu, S.M., Kunkel, H.G., and Blobel, G. (1981). Biogenesis of membrane-bound and secreted immunoglobulins: two primary translation products of the human 8 chain, differentially N-glycosylated to four discrete forms in vivo and in vitro. Proc. Natl. Acad. Sci. USA 78, 5127-5131.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 5127-5131
    • McCune, J.M.1    Fu, S.M.2    Kunkel, H.G.3    Blobel, G.4
  • 28
    • 0014219393 scopus 로고
    • Ribosome-catalysed reaction of puromycin with a formylmethionine-containing oligonucleotide
    • Monro, R.E., and Marcker, K.A. (1967). Ribosome-catalysed reaction of puromycin with a formylmethionine-containing oligonucleotide. J. Mol. Biol. 25, 347-350.
    • (1967) J. Mol. Biol. , vol.25 , pp. 347-350
    • Monro, R.E.1    Marcker, K.A.2
  • 29
    • 0027936633 scopus 로고
    • Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane
    • Mothes, W., Prehn, S., and Rapoport, T.A. (1994). Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane. EMBO J. 13, 3973-3982.
    • (1994) EMBO J. , vol.13 , pp. 3973-3982
    • Mothes, W.1    Prehn, S.2    Rapoport, T.A.3
  • 30
    • 0028929094 scopus 로고
    • The Sec61 complex is essential for the insertion of proteins into the membrane of the endoplasmic reticulum
    • Oliver, J., Jungnickel, B., Görlich, D., Rapoport, T., and High, S. (1995). The Sec61 complex is essential for the insertion of proteins into the membrane of the endoplasmic reticulum. FEBS Lett. 362, 126-130.
    • (1995) FEBS Lett. , vol.362 , pp. 126-130
    • Oliver, J.1    Jungnickel, B.2    Görlich, D.3    Rapoport, T.4    High, S.5
  • 31
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein secretion
    • Palade, G.E. (1975). Intracellular aspects of the process of protein secretion. Science 189, 347-358.
    • (1975) Science , vol.189 , pp. 347-358
    • Palade, G.E.1
  • 32
    • 0014481138 scopus 로고
    • Energy of an ion crossing a low dielectric membrane: Solutions to four relevant electrostatic problems
    • Parsegian, V.A. (1969). Energy of an ion crossing a low dielectric membrane: solutions to four relevant electrostatic problems. Nature 227, 844-846.
    • (1969) Nature , vol.227 , pp. 844-846
    • Parsegian, V.A.1
  • 33
    • 0013936848 scopus 로고
    • Vectorial discharge of peptides released by puromycin from attached ribosomes
    • Redman, C.M., and Sabatini, D.D. (1966). Vectorial discharge of peptides released by puromycin from attached ribosomes. Proc. Natl. Acad. Sci. USA 56, 608-615.
    • (1966) Proc. Natl. Acad. Sci. USA , vol.56 , pp. 608-615
    • Redman, C.M.1    Sabatini, D.D.2
  • 34
    • 0014010396 scopus 로고
    • Synthesis and transfer of amylase in pigeon pancreatic microsomes
    • Redman, C.M., Siekevitz, P., and Palade, G.E. (1966). Synthesis and transfer of amylase in pigeon pancreatic microsomes. J. Biol. Chem. 241, 1150-1158.
    • (1966) J. Biol. Chem. , vol.241 , pp. 1150-1158
    • Redman, C.M.1    Siekevitz, P.2    Palade, G.E.3
  • 35
    • 0024835142 scopus 로고
    • Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast
    • Rothblatt, J.A., Deshaies, R.J., Sanders, S.L., Daum, G., and Schekman, R. (1989). Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast. J. Cell Biol. 109, 2641-2652.
    • (1989) J. Cell Biol. , vol.109 , pp. 2641-2652
    • Rothblatt, J.A.1    Deshaies, R.J.2    Sanders, S.L.3    Daum, G.4    Schekman, R.5
  • 36
    • 0023729159 scopus 로고
    • Construction of defined polytopic integral transmembrane proteins: The role of signal and stop transfer sequence permutations
    • Rothman, R.E., Andrews, D.W., Calayag, M.C., and Lingappa, V.R. (1988). Construction of defined polytopic integral transmembrane proteins: the role of signal and stop transfer sequence permutations. 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
  • 37
    • 0020042649 scopus 로고
    • Filamentous phage pre-coat is an integral membrane protein: Analysis by a new method of membrane preparation
    • Russel, M., and Model, P. (1982). Filamentous phage pre-coat is an integral membrane protein: analysis by a new method of membrane preparation. Cell 28, 177-184.
    • (1982) Cell , vol.28 , pp. 177-184
    • Russel, M.1    Model, P.2
  • 38
    • 0025854858 scopus 로고
    • A protein-conducting channel in the endoplasmic reticulum
    • Simon, S.M., and Blobel, G. (1991). A protein-conducting channel in the endoplasmic reticulum. Cell 65, 371-380.
    • (1991) Cell , vol.65 , pp. 371-380
    • Simon, S.M.1    Blobel, G.2
  • 39
    • 0026684458 scopus 로고
    • Signal peptides open protein-conducting channels in E. coli
    • Simon, S.M., and Blobel, G. (1992). Signal peptides open protein-conducting channels in E. coli. Cell 69, 677-684.
    • (1992) Cell , vol.69 , pp. 677-684
    • Simon, S.M.1    Blobel, G.2
  • 40
    • 0040038098 scopus 로고
    • Large aqueous channels in membrane vesicles derived from the rough endoplasmic reticulum of canine pancreas or the plasma membrane of Escherichia coli
    • Simon, S.M., Blobel, G., and Zimmerberg, J. (1989). Large aqueous channels in membrane vesicles derived from the rough endoplasmic reticulum of canine pancreas or the plasma membrane of Escherichia coli. Proc. Natl. Acad. Sci. USA 86, 6176-6180.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6176-6180
    • Simon, S.M.1    Blobel, G.2    Zimmerberg, J.3
  • 42
    • 0027512232 scopus 로고
    • Evidence for an alternate model of human P-glycoprotein structure and biogenesis
    • Skach, W.R., Calayag, M.C., and Lingappa, V.R. (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.R.1    Calayag, M.C.2    Lingappa, V.R.3
  • 43
    • 0014286155 scopus 로고
    • Evidence for aminoacyl-tRNA binding, peptide bond synthesis, and translocase activities in the aminoacyl transfer reaction
    • Skogerson, L., and Moldave, K. (1968). Evidence for aminoacyl-tRNA binding, peptide bond synthesis, and translocase activities in the aminoacyl transfer reaction. Arch. Biochem. Biophys. 125, 497-505.
    • (1968) Arch. Biochem. Biophys. , vol.125 , pp. 497-505
    • Skogerson, L.1    Moldave, K.2
  • 44
    • 0015882579 scopus 로고
    • Selective solubilization of proteins from red blood cell membranes by protein perturbants
    • Steck, T.L., and Yu, J. (1973). Selective solubilization of proteins from red blood cell membranes by protein perturbants. J. Supramol. Struct. 1, 220-232.
    • (1973) J. Supramol. Struct. , vol.1 , pp. 220-232
    • Steck, T.L.1    Yu, J.2
  • 45
    • 0027058051 scopus 로고
    • Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum
    • Stirling, C.J., Rothblatt, J., Hosobuchi, M., Deshaies, R., and Schekman, R. (1992). Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum. Mol. Biol. Cell 3, 129-142.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 129-142
    • Stirling, C.J.1    Rothblatt, J.2    Hosobuchi, M.3    Deshaies, R.4    Schekman, R.5
  • 46
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford, C. (1968). Protein denaturation. Adv. Prot. Chem. 23, 121-282.
    • (1968) Adv. Prot. Chem. , vol.23 , pp. 121-282
    • Tanford, C.1
  • 47
    • 0014718113 scopus 로고
    • Protein denaturation. C. Theoretical models for the mechanism of denaturation
    • Tanford, C. (1970). Protein denaturation. C. Theoretical models for the mechanism of denaturation. Adv. Prot. Chem. 24, 1-95.
    • (1970) Adv. Prot. Chem. , vol.24 , pp. 1-95
    • Tanford, C.1
  • 48
    • 0026061020 scopus 로고
    • A nascent membrane protein is located adjacent to ER membrane proteins throughout its integration and translation
    • Thrift, R.N., Andrews, D.W., Walter, P., and Johnson, A.E. (1991). A nascent membrane protein is located adjacent to ER membrane proteins throughout its integration and translation. J. Cell Biol. 112, 809-821.
    • (1991) J. Cell Biol. , vol.112 , pp. 809-821
    • Thrift, R.N.1    Andrews, D.W.2    Walter, P.3    Johnson, A.E.4
  • 49
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak interactions with water: How do solvents affect these processes?
    • Timasheff, S.N. (1993). The control of protein stability and association by weak interactions with water: how do solvents affect these processes? Annu. Rev. Biophy. Biomol. Struct. 22, 67-97.
    • (1993) Annu. Rev. Biophy. Biomol. Struct. , vol.22 , pp. 67-97
    • Timasheff, S.N.1
  • 50
    • 0002445013 scopus 로고
    • The puromycin reaction and its relation to protein synthesis
    • Traut, R.R., and Monro, R.E. (1964). The puromycin reaction and its relation to protein synthesis. J. Mol. Biol. 10, 63-72.
    • (1964) J. Mol. Biol. , vol.10 , pp. 63-72
    • Traut, R.R.1    Monro, R.E.2
  • 51
    • 0023676242 scopus 로고
    • Topogenic signals in internal membrane proteins
    • Von Heijne, G., and Gavel, Y. (1988). Topogenic signals in internal membrane proteins. Eur. J. Biochem. 174, 671-678.
    • (1988) Eur. J. Biochem. , vol.174 , pp. 671-678
    • Von Heijne, G.1    Gavel, Y.2
  • 52
    • 0020994721 scopus 로고
    • Preparation of microsomal membranes for cotranslational protein translocation
    • Walter, P., and Blobel, G. (1983). Preparation of microsomal membranes for cotranslational protein translocation. Meth. Enzymol. 96, 84-93.
    • (1983) Meth. Enzymol. , vol.96 , pp. 84-93
    • Walter, P.1    Blobel, G.2
  • 53
    • 0027284115 scopus 로고
    • Membrane topology of the N-terminal half of the hamster P-glycoprotein molecule
    • Zhang, J.-T., Duthie, M., and Ling, V. (1993). Membrane topology of the N-terminal half of the hamster P-glycoprotein molecule. J. Biol. Chem. 268, 15101-15110.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15101-15110
    • Zhang, J.-T.1    Duthie, M.2    Ling, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.