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Volumn 31, Issue C, 1996, Pages 425-471

Chapter 16 Assembly of proteins into membranes

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EID: 0342880541     PISSN: 01677306     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0167-7306(08)60523-2     Document Type: Chapter
Times cited : (4)

References (41)
  • 1
    • 0018987976 scopus 로고
    • Intracellular protein topogenesis
    • Blobel G. Intracellular protein topogenesis. Proc. Natl. Acad. Sci. USA 77 (1980) 1496-1500
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1496-1500
    • Blobel, G.1
  • 2
    • 0025224551 scopus 로고
    • The structure and insertion of integral proteins in membranes
    • Singer S.J. The structure and insertion of integral proteins in membranes. Annu. Rev. Cell Biol. 6 (1990) 247-296
    • (1990) Annu. Rev. Cell Biol. , vol.6 , pp. 247-296
    • Singer, S.J.1
  • 3
    • 0019464222 scopus 로고
    • The spontaneous insertion of proteins into and across membranes: the helical hairpin hypothesis
    • Engelman D.M., and Steitz T.A. The spontaneous insertion of proteins into and across membranes: the helical hairpin hypothesis. Cell 23 (1981) 411-422
    • (1981) Cell , vol.23 , pp. 411-422
    • Engelman, D.M.1    Steitz, T.A.2
  • 4
    • 0342351613 scopus 로고
    • Predicting the orientation of eucaryotic membrane-spanning proteins
    • Hartmann E., Rapoport T.A., and Lodish H.F. Predicting the orientation of eucaryotic membrane-spanning proteins. Proc. Natl. Acad. Sci. USA 86 (1989) 5786-5790
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5786-5790
    • Hartmann, E.1    Rapoport, T.A.2    Lodish, H.F.3
  • 6
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein synthesis
    • Palade G. Intracellular aspects of the process of protein synthesis. Science 169 (1975) 347-358
    • (1975) Science , vol.169 , pp. 347-358
    • Palade, G.1
  • 7
    • 0016753216 scopus 로고
    • Transfer of proteins across membranes
    • Blobel G., and Dobberstein B. Transfer of proteins across membranes. J. Cell Biol. 67 (1975) 835-851
    • (1975) J. Cell Biol. , vol.67 , pp. 835-851
    • Blobel, G.1    Dobberstein, B.2
  • 9
    • 0021332707 scopus 로고
    • Determinants for protein localization: β-lactamase signal sequence directs globin across microsomal membranes
    • Lingappa V.R., Chaidez J., Yost C.S., and Hedgpeth J. Determinants for protein localization: β-lactamase signal sequence directs globin across microsomal membranes. Proc. Natl. Acad. Sci. USA 81 (1984) 456-460
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 456-460
    • Lingappa, V.R.1    Chaidez, J.2    Yost, C.S.3    Hedgpeth, J.4
  • 10
    • 0025297583 scopus 로고
    • The signal peptide
    • von Heijne G. The signal peptide. J. Membr. Biol. 115 (1990) 195-201
    • (1990) J. Membr. Biol. , vol.115 , pp. 195-201
    • von Heijne, G.1
  • 11
    • 0028337335 scopus 로고
    • Protein translocation: common themes from bacteria to man
    • Jungnickel B., Rapoport T.A., and Hartman E. Protein translocation: common themes from bacteria to man. FEBS Lett. 346 (1994) 72-77
    • (1994) FEBS Lett. , vol.346 , pp. 72-77
    • Jungnickel, B.1    Rapoport, T.A.2    Hartman, E.3
  • 12
    • 0028142136 scopus 로고
    • Protein translocation across the ER
    • Ng D.T.W., and Walter P. Protein translocation across the ER. Curr. Opin. Cell Biol. 6 (1994) 510-516
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 510-516
    • Ng, D.T.W.1    Walter, P.2
  • 13
    • 0028170807 scopus 로고
    • Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane
    • Walter P., and Johnson A.E. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu. Rev. Cell Biol. 10 (1994) 87-119
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 87-119
    • Walter, P.1    Johnson, A.E.2
  • 14
    • 0028964746 scopus 로고
    • Signal recognition particle (SRP), a ubiquitous initiator of protein translocation
    • Lütche H. Signal recognition particle (SRP), a ubiquitous initiator of protein translocation. Eur. J. Biochem. 228 (1995) 531-550
    • (1995) Eur. J. Biochem. , vol.228 , pp. 531-550
    • Lütche, H.1
  • 15
    • 0026504192 scopus 로고
    • A protein of the endoplasmic reticulum involved early in polypeptide translocation
    • Görlich D., Hartmann E., Prehn S., and Rapoport T.A. A protein of the endoplasmic reticulum involved early in polypeptide translocation. Nature 357 (1992) 47-52
    • (1992) Nature , vol.357 , pp. 47-52
    • Görlich, D.1    Hartmann, E.2    Prehn, S.3    Rapoport, T.A.4
  • 16
    • 0026466143 scopus 로고
    • A mammalian homolog of Sec61p and SecYp is associated with ribosomes and nascent polypeptides during translocation
    • Görlich D., Prehn S., Hartman E., Kalies K.-U., and Rapoport T.A. A mammalian homolog of Sec61p and SecYp is associated with ribosomes and nascent polypeptides during translocation. Cell 71 (1992) 489-503
    • (1992) Cell , vol.71 , pp. 489-503
    • Görlich, D.1    Prehn, S.2    Hartman, E.3    Kalies, K.-U.4    Rapoport, T.A.5
  • 18
    • 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. Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane. EMBO J. 13 (1994) 3973-3982
    • (1994) EMBO J. , vol.13 , pp. 3973-3982
    • Mothes, W.1    Prehn, S.2    Rapoport, T.A.3
  • 19
    • 0029073398 scopus 로고
    • Stage- and ribosome-specific alterations in nascent chain-Sec61p interactions accompany translocation across the ER membrane
    • Nicchitta C.V., Murphy E.C., Haynes R., and Shelness G.S. Stage- and ribosome-specific alterations in nascent chain-Sec61p interactions accompany translocation across the ER membrane. J. Cell Biol. 129 (1995) 957-970
    • (1995) J. Cell Biol. , vol.129 , pp. 957-970
    • Nicchitta, C.V.1    Murphy, E.C.2    Haynes, R.3    Shelness, G.S.4
  • 20
    • 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. Secretory proteins move through the endoplasmic reticulum membrane via an aqueous gated pore. Cell 78 (1994) 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
  • 21
    • 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. Binding of ribosomes to the rough endoplasmic reticulum mediated by the Sec61p complex. J. Cell Biol. 126 (1994) 925-934
    • (1994) J. Cell Biol. , vol.126 , pp. 925-934
    • Kalies, K.-U.1    Görlich, D.2    Rapoport, T.A.3
  • 22
    • 0025019704 scopus 로고
    • Assembly of translocation-competent proteoliposomes from detergent-solubilized rough microsomes
    • Nicchitta C.V., and Blobel G. Assembly of translocation-competent proteoliposomes from detergent-solubilized rough microsomes. Cell 60 (1990) 259-269
    • (1990) Cell , vol.60 , pp. 259-269
    • Nicchitta, C.V.1    Blobel, G.2
  • 23
    • 0027424601 scopus 로고
    • Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
    • Görlich D., and Rapoport T.A. Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell 75 (1993) 615-630
    • (1993) Cell , vol.75 , pp. 615-630
    • Görlich, D.1    Rapoport, T.A.2
  • 24
    • 0028955427 scopus 로고
    • The 70 carboxyl-terminal amino acids of nascent secretory proteins are protected from proteolysis by the ribosome and the protein translocation apparatus of the endoplasmic reticulum membrane
    • Matlack K.E.S., and Walter P. The 70 carboxyl-terminal amino acids of nascent secretory proteins are protected from proteolysis by the ribosome and the protein translocation apparatus of the endoplasmic reticulum membrane. J. Biol. Chem. 270 (1995) 6160-6170
    • (1995) J. Biol. Chem. , vol.270 , pp. 6160-6170
    • Matlack, K.E.S.1    Walter, P.2
  • 25
    • 0028101487 scopus 로고
    • The COOH-terminal ends of internal signal and signal-anchor sequences are positioned differently in the ER translocase
    • Nilsson I., Whitley P., and von Heijne G. The COOH-terminal ends of internal signal and signal-anchor sequences are positioned differently in the ER translocase. J. Cell Biol. 126 (1994) 1127-1132
    • (1994) J. Cell Biol. , vol.126 , pp. 1127-1132
    • Nilsson, I.1    Whitley, P.2    von Heijne, G.3
  • 26
    • 0018896724 scopus 로고
    • Two mRNAs can be produced from a single immunoglobulin μ gene by alternative RNA processing pathways
    • Early P., Rogers J., Davis M., Calame K., Band M., Wall R., and Hood L. Two mRNAs can be produced from a single immunoglobulin μ gene by alternative RNA processing pathways. Cell 20 (1980) 313-319
    • (1980) Cell , vol.20 , pp. 313-319
    • Early, P.1    Rogers, J.2    Davis, M.3    Calame, K.4    Band, M.5    Wall, R.6    Hood, L.7
  • 27
    • 0020608403 scopus 로고
    • A stop transfer sequence confers predictable orientation to a previously secreted protein in cell-free systems
    • Yost C.S., Hedgbeth J., and Lingappa V.R. A stop transfer sequence confers predictable orientation to a previously secreted protein in cell-free systems. Cell 34 (1983) 759-766
    • (1983) Cell , vol.34 , pp. 759-766
    • Yost, C.S.1    Hedgbeth, J.2    Lingappa, V.R.3
  • 28
    • 0023737896 scopus 로고
    • Evidence for the loop model of signal-sequence insertion into the ER
    • Shaw A.S., Rottier P.J.M., and Rose J.K. Evidence for the loop model of signal-sequence insertion into the ER. Proc. Natl. Acad. Sci. USA 85 (1988) 7592-7596
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7592-7596
    • Shaw, A.S.1    Rottier, P.J.M.2    Rose, J.K.3
  • 29
    • 0026909328 scopus 로고
    • Mechanisms that determine the TM disposition of proteins
    • High S., and Dobberstein B. Mechanisms that determine the TM disposition of proteins. Curr. Opin. Cell Biol. 4 (1992) 581-586
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 581-586
    • High, S.1    Dobberstein, B.2
  • 30
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: the two-stage model
    • Popot J.-L., and Engelman D.M. Membrane protein folding and oligomerization: the two-stage model. Biochemistry 29 (1990) 4031-4037
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.-L.1    Engelman, D.M.2
  • 31
    • 0023729159 scopus 로고
    • Construction of defined polytopic integral TM proteins: the role of signal and stop transfer sequence permutations
    • Rothman R.E., Andrews D.W., Calayag M.C., and Lingappa V.R. Construction of defined polytopic integral TM proteins: the role of signal and stop transfer sequence permutations. J. Biol. Chem. 263 (1988) 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
  • 32
    • 0023782388 scopus 로고
    • Insertion of a multispanning membrane protein occurs sequentially and requires only one signal sequence
    • Wessels H.P., and Spiess M. Insertion of a multispanning membrane protein occurs sequentially and requires only one signal sequence. Cell 55 (1988) 61-70
    • (1988) Cell , vol.55 , pp. 61-70
    • Wessels, H.P.1    Spiess, M.2
  • 33
    • 0023663543 scopus 로고
    • Oligosaccharyl transferase: the central enzyme in the pathway of glycoprotein assembly
    • Kaplan H.A., Welpy J.K., and Lennarz W.J. Oligosaccharyl transferase: the central enzyme in the pathway of glycoprotein assembly. Biochim. Biophys. Acta 906 (1987) 161-173
    • (1987) Biochim. Biophys. Acta , vol.906 , pp. 161-173
    • Kaplan, H.A.1    Welpy, J.K.2    Lennarz, W.J.3
  • 34
    • 0026716017 scopus 로고
    • Oligosaccharyltransferase activity is associated with a protein complex composed of ribophorins I and II and a 48 kd protein
    • Kelleher D.J., Kreibic G., and Gilmore R. Oligosaccharyltransferase activity is associated with a protein complex composed of ribophorins I and II and a 48 kd protein. Cell 69 (1992) 55-65
    • (1992) Cell , vol.69 , pp. 55-65
    • Kelleher, D.J.1    Kreibic, G.2    Gilmore, R.3
  • 35
    • 0029268063 scopus 로고
    • Calnexin: a molecular chaperone with a taste for carbohydrate
    • Williams D.B. Calnexin: a molecular chaperone with a taste for carbohydrate. Biochem. Cell Biol. 73 (1995) 123-132
    • (1995) Biochem. Cell Biol. , vol.73 , pp. 123-132
    • Williams, D.B.1
  • 36
    • 0024337857 scopus 로고
    • Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteins
    • Freedman R.B. Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteins. Cell 57 (1989) 1069-1072
    • (1989) Cell , vol.57 , pp. 1069-1072
    • Freedman, R.B.1
  • 37
    • 0023838784 scopus 로고
    • Transport of secretory and membrane glycoproteins from rough ER to the Golgi
    • Lodish H.F. Transport of secretory and membrane glycoproteins from rough ER to the Golgi. J. Biol. Chem. 263 (1988) 2107-2110
    • (1988) J. Biol. Chem. , vol.263 , pp. 2107-2110
    • Lodish, H.F.1
  • 38
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman J.E. Mechanisms of intracellular protein transport. Nature 372 (1994) 55-63
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 39
    • 0027640284 scopus 로고
    • Targeting and retention of Golgi membrane proteins
    • Machamer C.E. Targeting and retention of Golgi membrane proteins. Curr. Opin. Cell Biol. 5 (1993) 606-612
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 606-612
    • Machamer, C.E.1
  • 40
    • 0023507407 scopus 로고
    • Trafficking of lysosomal enzymes
    • Kornfeld S. Trafficking of lysosomal enzymes. FASEB J. 1 (1987) 462-468
    • (1987) FASEB J. , vol.1 , pp. 462-468
    • Kornfeld, S.1
  • 41
    • 0028068273 scopus 로고
    • Mechanisms of cell polarity: sorting and transport in epithelial cells
    • Matter K., and Mellman I. Mechanisms of cell polarity: sorting and transport in epithelial cells. Curr. Opin. Cell Biol. 6 (1994) 545-554
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 545-554
    • Matter, K.1    Mellman, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.