메뉴 건너뛰기




Volumn 27, Issue , 2011, Pages 25-56

Membrane protein insertion at the endoplasmic reticulum

Author keywords

Protein translocation; Targeting

Indexed keywords

MEMBRANE PROTEIN; TRANSLOCON;

EID: 80054041334     PISSN: 10810706     EISSN: 15308995     Source Type: Book Series    
DOI: 10.1146/annurev-cellbio-092910-154125     Document Type: Article
Times cited : (227)

References (182)
  • 1
    • 34250183921 scopus 로고    scopus 로고
    • Post-translational integration of tail-anchored proteins is facilitated by defined molecular chaperones
    • DOI 10.1242/jcs.002410
    • Abell BM, Rabu C, Leznicki P, Young JC, High S. 2007. Post-translational integration of tail-anchored proteins is facilitated by defined molecular chaperones. J. Cell Sci. 120:1743-51 (Pubitemid 46930412)
    • (2007) Journal of Cell Science , vol.120 , Issue.10 , pp. 1743-1751
    • Abell, B.M.1    Rabu, C.2    Leznicki, P.3    Young, J.C.4    High, S.5
  • 2
    • 2542452829 scopus 로고    scopus 로고
    • Cotranslational membrane protein biogenesis at the endoplasmic reticulum
    • DOI 10.1074/jbc.R400002200
    • Alder NN, Johnson AE. 2004. Cotranslational membrane protein biogenesis at the endoplasmic reticulum. J. Biol. Chem. 279:22787-90 (Pubitemid 38685576)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.22 , pp. 22787-22790
    • Alder, N.N.1    Johnson, A.E.2
  • 3
    • 0020288333 scopus 로고
    • Signal recognition protein is required for the integration of acetylcholine receptor δ subunit, a transmembrane glycoprotein, into the endoplasmic reticulum membrane
    • DOI 10.1083/jcb.93.2.501
    • Anderson DJ, Walter P, Blobel G. 1982. Signal recognition protein is required for the integration of acetylcholine receptor delta subunit, a transmembrane glycoprotein, into the endoplasmic reticulum membrane. J. Cell Biol. 93:501-6 (Pubitemid 12014139)
    • (1982) Journal of Cell Biology , vol.93 , Issue.2 , pp. 501-506
    • Anderson, D.J.1    Walter, P.2    Blobel, G.3
  • 4
    • 0020484234 scopus 로고
    • Structural prediction of membrane-bound proteins
    • Argos P, Rao JK M, Hargrave PA. 1982. Structural prediction of membrane-bound proteins. Eur. J. Biochem. 128:565-75
    • (1982) Eur. J. Biochem. , vol.128 , pp. 565-575
    • Argos, P.1    Rao, J.K.M.2    Hargrave, P.A.3
  • 5
    • 78650546283 scopus 로고    scopus 로고
    • Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5. 5-A resolution
    • Armache J-P, Jarasch A, Anger AM, Villa E, Becker T, et al. 2010. Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5. 5-A resolution. Proc. Natl. Acad. Sci. USA 107:19748-53
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 19748-19753
    • Armache, J.-P.1    Jarasch, A.2    Anger, A.M.3    Villa, E.4    Becker, T.5
  • 6
    • 33748901612 scopus 로고    scopus 로고
    • The conserved ATPase Get3/Arr4 modulates the activity of membrane-associated proteins in Saccharomyces cerevisiae
    • DOI 10.1534/genetics.106.058362
    • Auld KL, Hitchcock AL, Doherty HK, Frietze S, Huang LS, Silver PA. 2006. The conserved ATPase Get3/Arr4 modulates the activity of membrane-associated proteins in Saccharomyces cerevisiae. Genetics 174:215-27 (Pubitemid 44427667)
    • (2006) Genetics , vol.174 , Issue.1 , pp. 215-227
    • Auld, K.L.1    Hitchcock, A.L.2    Doherty, H.K.3    Frietze, S.4    Huang, L.S.5    Silver, P.A.6
  • 8
    • 0031473345 scopus 로고    scopus 로고
    • Alignment of conduits for the nascent polypeptide chain in the ribosome- Sec61 complex
    • DOI 10.1126/science.278.5346.2123
    • Beckmann R, Bubeck D, Grassucci R, Penczek P, Verschoor A, et al. 1997. Alignment of conduits for the nascent polypeptide chain in the ribosome-Sec61 complex. Science 278:2123-26 (Pubitemid 28028322)
    • (1997) Science , vol.278 , Issue.5346 , pp. 2123-2126
    • Beckmann, R.1    Bubeck, D.2    Grassucci, R.3    Penczek, P.4    Verschoor, A.5    Blobel, G.6    Frank, J.7
  • 9
    • 0035798359 scopus 로고    scopus 로고
    • Architecture of the protein-conducting channel associated with the translating 80S ribosome
    • DOI 10.1016/S0092-8674(01)00541-4
    • Beckmann R, Spahn CM T, Eswar N, Helmers J, Penczek PA, et al. 2001. Architecture of the proteinconducting channel associated with the translating 80S ribosome. Cell 107:361-72 (Pubitemid 33049979)
    • (2001) Cell , vol.107 , Issue.3 , pp. 361-372
    • Beckmann, R.1    Spahn, C.M.T.2    Eswar, N.3    Helmers, J.4    Penczek, P.A.5    Sali, A.6    Frank, J.7    Blobel, G.8
  • 10
    • 0037424360 scopus 로고    scopus 로고
    • Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae
    • DOI 10.1074/jbc.M212725200
    • Beilharz T, Egan B, Silver PA, Hofmann K, Lithgow T. 2003. Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae. J. Biol. Chem. 278:8219-23 (Pubitemid 36800565)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.10 , pp. 8219-8223
    • Beilharz, T.1    Egan, B.2    Silver, P.A.3    Hofmann, K.4    Lithgow, T.5
  • 12
    • 60849096653 scopus 로고    scopus 로고
    • A signal-anchor sequence stimulates signal recognition particle binding to ribosomes from inside the exit tunnel
    • Berndt U, Oellerer S, Zhang Y, Johnson AE, Rospert S. 2009. A signal-anchor sequence stimulates signal recognition particle binding to ribosomes from inside the exit tunnel. Proc. Natl. Acad. Sci. USA 106:1398-403
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 1398-403
    • Berndt, U.1    Oellerer, S.2    Zhang, Y.3    Johnson, A.E.4    Rospert, S.5
  • 13
    • 0018987976 scopus 로고
    • Intracellular protein topogenesis
    • Blobel G. 1980. Intracellular protein topogenesis. Proc. Natl. Acad. Sci. USA 77:1496-500
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1496-500
    • Blobel, G.1
  • 15
    • 79851511792 scopus 로고    scopus 로고
    • Targeting pathways of C-tail-anchored proteins
    • BorgeseN, Fasana E. 2010. Targeting pathways of C-tail-anchored proteins. Biochim. Biophys. Acta 1808:937-48
    • (2010) Biochim. Biophys. Acta , vol.1808 , pp. 937-948
    • Borgesen Fasana, E.1
  • 16
    • 75849130606 scopus 로고    scopus 로고
    • Structural insights into tail-anchored protein binding and membrane insertion by Get3
    • Bozkurt G, Stjepanovic G, Vilardi F, Amlacher S, Wild K, et al. 2009. Structural insights into tail-anchored protein binding and membrane insertion by Get3. Proc. Natl. Acad. Sci. USA 106:21131-36
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 21131-21136
    • Bozkurt, G.1    Stjepanovic, G.2    Vilardi, F.3    Amlacher, S.4    Wild, K.5
  • 17
    • 77951296574 scopus 로고    scopus 로고
    • The structure of Get4 reveals an α-solenoid fold adapted for multiple interactions in tail-anchored protein biogenesis
    • Bozkurt G, Wild K, Amlacher S, Hurt E, Dobberstein B, Sinning I. 2010. The structure of Get4 reveals an α-solenoid fold adapted for multiple interactions in tail-anchored protein biogenesis. FEBS Lett. 584:1509-14
    • (2010) FEBS Lett. , Issue.584 , pp. 1509-1514
    • Bozkurt, G.1    Wild, K.2    Amlacher, S.3    Hurt, E.4    Dobberstein, B.5    Sinning, I.6
  • 18
    • 33845307248 scopus 로고    scopus 로고
    • Unassisted translocation of large polypeptide domains across phospholipid bilayers
    • DOI 10.1083/jcb.200608101
    • Brambillasca S, Yabal M, Makarow M, BorgeseN. 2006. Unassisted translocation of large polypeptide domains across phospholipid bilayers. J. Cell Biol. 175:767-77 (Pubitemid 44878509)
    • (2006) Journal of Cell Biology , vol.175 , Issue.5 , pp. 767-777
    • Brambillasca, S.1    Yabal, M.2    Makarow, M.3    Borgese, N.4
  • 19
    • 23044492259 scopus 로고    scopus 로고
    • Transmembrane topogenesis of a tail-anchored protein is modulated by membrane lipid composition
    • DOI 10.1038/sj.emboj.7600730
    • Brambillasca S, Yabal M, Soffientini P, Stefanovic S, Makarow M, et al. 2005. Transmembrane topogenesis of a tail-anchored protein is modulated by membrane lipid composition. EMBO J. 24:2533-42 (Pubitemid 41076310)
    • (2005) EMBO Journal , vol.24 , Issue.14 , pp. 2533-2542
    • Brambillasca, S.1    Yabal, M.2    Soffientini, P.3    Stefanovic, S.4    Makarow, M.5    Hegde, R.S.6    Borgese, N.7
  • 20
    • 18544380083 scopus 로고    scopus 로고
    • Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY
    • DOI 10.1083/jcb.200412019
    • Cannon KS, Or E, Clemons WM, Shibata Y, Rapoport TA. 2005. Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY. J. Cell Biol. 169:219-25 (Pubitemid 40656559)
    • (2005) Journal of Cell Biology , vol.169 , Issue.2 , pp. 219-225
    • Cannon, K.S.1    Or, E.2    Clemons Jr., W.M.3    Shibata, Y.4    Rapoport, T.A.5
  • 21
    • 0028935007 scopus 로고
    • The translocation of negatively charged residues across the membrane is driven by the electrochemical potential: Evidence for an electrophoresis-like membrane transfer mechanism
    • Cao G, Kuhn A, Dalbey R. 1995. The translocation of negatively charged residues across the membrane is driven by the electrochemical potential: evidence for an electrophoresis-like membrane transfer mechanism. EMBO J. 14:866-75
    • (1995) EMBO J. , vol.14 , pp. 866-875
    • Cao, G.1    Kuhn, A.2    Dalbey, R.3
  • 22
    • 77951209587 scopus 로고    scopus 로고
    • Crystal structure of Get4-Get5 complex and its interactions with Sgt2, Get3, and Ydj1
    • Chang Y-W, Chuang Y-C, Ho Y-C, Cheng M-Y, Sun Y-J, et al. 2010. Crystal structure of Get4-Get5 complex and its interactions with Sgt2, Get3, and Ydj1. J. Biol. Chem. 285:9962-70
    • (2010) J. Biol. Chem. , vol.285 , pp. 9962-9970
    • Chang, Y.-W.1    Chuang, Y.-C.2    Ho, Y.-C.3    Cheng, M.-Y.4    Sun, Y.-J.5
  • 24
    • 33749518904 scopus 로고    scopus 로고
    • Slow translocon gating causes cytosolic exposure of transmembrane and lumenal domains during membrane protein integration
    • DOI 10.1038/nsmb1146, PII NSMB1146
    • Cheng Z, Gilmore R. 2006. Slow translocon gating causes cytosolic exposure of transmembrane and lumenal domains during membrane protein integration. Nat. Struct. Mol. Biol. 13:930-36 (Pubitemid 44527376)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.10 , pp. 930-936
    • Cheng, Z.1    Gilmore, R.2
  • 25
    • 0000617991 scopus 로고    scopus 로고
    • The OST4 gene of Saccharomyces cerevisiae encodes an unusually small protein required for normal levels of oligosaccharyltransferase activity
    • DOI 10.1074/jbc.271.6.3132
    • Chi JH, Roos J, Dean N. 1996. The OST4 gene of Saccharomyces cerevisiae encodes an unusually small protein required for normal levels of oligosaccharyltransferase activity. J. Biol. Chem. 271:3132-40 (Pubitemid 26055614)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.6 , pp. 3132-3140
    • Chi, J.H.1    Roos, J.2    Dean, N.3
  • 28
    • 0027985063 scopus 로고
    • Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore
    • DOI 10.1016/0092-8674(94)90424-3
    • Crowley KS, Liao S, Worrell VE, Reinhart GD, Johnson AE. 1994. Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore. Cell 78:461-71 (Pubitemid 24250810)
    • (1994) Cell , vol.78 , Issue.3 , pp. 461-471
    • Crowley, K.S.1    Liao, S.2    Worrell, V.E.3    Reinhart, G.D.4    Johnson, A.E.5
  • 29
    • 0027162564 scopus 로고
    • The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation
    • DOI 10.1016/0092-8674(93)90640-C
    • Crowley KS, Reinhart GD, Johnson AE. 1993. The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation. Cell 73:1101-15 (Pubitemid 23180485)
    • (1993) Cell , vol.73 , Issue.6 , pp. 1101-1115
    • Crowley, K.S.1    Reinhart, G.D.2    Johnson, A.E.3
  • 30
    • 0029561894 scopus 로고
    • Transmembrane orientation of signal-anchor proteins is affected by the folding state but not the size of the N-terminal domain
    • Denzer AJ, Nabholz CE, Spiess M. 1995. Transmembrane orientation of signal-anchor proteins is affected by the folding state but not the size of the N-terminal domain. EMBO J. 14:6311-7 (Pubitemid 26007317)
    • (1995) EMBO Journal , vol.14 , Issue.24 , pp. 6311-6317
    • Denzer, A.J.1    Nabholz, C.E.2    Spiess, M.3
  • 31
    • 0027457077 scopus 로고
    • A signal sequence is not required for protein export in prlA mutants of Escherichia coli
    • Derman A, Puziss J, Bassford P Jr, Beckwith J. 1993. A signal sequence is not required for protein export in prlA mutants of Escherichia coli. EMBO J. 12:879-88 (Pubitemid 23095836)
    • (1993) EMBO Journal , vol.12 , Issue.3 , pp. 879-888
    • Derman, A.I.1    Puziss, J.W.2    Bassford Jr., P.J.3    Beckwith, J.4
  • 32
    • 0023567026 scopus 로고
    • A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum
    • Deshaies RJ, Schekman R. 1987. A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum. J. Cell Biol. 105:633-45 (Pubitemid 18043827)
    • (1987) Journal of Cell Biology , vol.105 , Issue.2 , pp. 633-645
    • Deshaies, R.J.1    Schekman, R.2
  • 33
    • 0342995731 scopus 로고    scopus 로고
    • The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process
    • DOI 10.1016/S0092-8674(00)81115-0
    • Do H, Falcone D, Lin J, Andrews DW, Johnson AE. 1996. The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process. Cell 85:369-78 (Pubitemid 26160708)
    • (1996) Cell , vol.85 , Issue.3 , pp. 369-378
    • Hung, D.1    Falcone, D.2    Lin, J.3    Andrews, D.W.4    Johnson, A.E.5
  • 34
    • 34249683488 scopus 로고    scopus 로고
    • Membrane protein structure: Prediction versus reality
    • Elofsson A, von Heijne G. 2007. Membrane protein structure: prediction versus reality. Annu. Rev. Biochem. 76:125-40
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 125-140
    • Elofsson, A.1    Von Heijne, G.2
  • 35
    • 63649153519 scopus 로고    scopus 로고
    • Membrane-integration characteristics of two ABC transporters, CFTR and P-glycoprotein
    • Enquist K, Fransson M, Boekel C, Bengtsson I, Geiger K, et al. 2009. Membrane-integration characteristics of two ABC transporters, CFTR and P-glycoprotein. J. Mol. Biol. 387:1153-64
    • (2009) J. Mol. Biol. , vol.387 , pp. 1153-1164
    • Enquist, K.1    Fransson, M.2    Boekel, C.3    Bengtsson, I.4    Geiger, K.5
  • 37
    • 46749104133 scopus 로고    scopus 로고
    • Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins
    • DOI 10.1242/jcs.020321
    • Favaloro V, Spasic M, Schwappach B, Dobberstein B. 2008. Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins. J. Cell Sci. 121:1832-40 (Pubitemid 351943376)
    • (2008) Journal of Cell Science , vol.121 , Issue.11 , pp. 1832-1840
    • Favaloro, V.1    Spasic, M.2    Schwappach, B.3    Dobberstein, B.4
  • 39
    • 33646537802 scopus 로고    scopus 로고
    • Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes
    • DOI 10.1101/gad.1422006
    • Fleischer TC, Weaver CM, McAfee KJ, Jennings JL, Link AJ. 2006. Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes. Genes Dev. 20:1294-307 (Pubitemid 43727590)
    • (2006) Genes and Development , vol.20 , Issue.10 , pp. 1294-1307
    • Fleischer, T.C.1    Weaver, C.M.2    McAfee, K.J.3    Jennings, J.L.4    Link, A.J.5
  • 40
    • 0037450802 scopus 로고    scopus 로고
    • Substrate-specific function of the translocon-associated protein complex during translocation across the ER membrane
    • DOI 10.1083/jcb.200210095
    • Fons RD, Bogert BA, Hegde RS. 2003. Substrate-specific function of the translocon-associated protein complex during translocation across the ER membrane. J. Cell Biol. 160:529-39 (Pubitemid 36254391)
    • (2003) Journal of Cell Biology , vol.160 , Issue.4 , pp. 529-539
    • Fons, R.D.1    Bogert, B.A.2    Hegde, R.S.3
  • 42
    • 77953517920 scopus 로고    scopus 로고
    • Positive charges of translocating polypeptide chain retrieve an upstream marginal hydrophobic segment from the endoplasmic reticulum lumen to the translocon
    • Fujita H, Kida Y, Hagiwara M, Morimoto F, Sakaguchi M. 2010. Positive charges of translocating polypeptide chain retrieve an upstream marginal hydrophobic segment from the endoplasmic reticulum lumen to the translocon. Mol. Biol. Cell 21:2045-56
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2045-2056
    • Fujita, H.1    Kida, Y.2    Hagiwara, M.3    Morimoto, F.4    Sakaguchi, M.5
  • 43
    • 0028175016 scopus 로고
    • Topological "frustration" in multispanning E. coli inner membrane proteins
    • Gafvelin G, von Heijne G. 1994. Topological "frustration" in multispanning E. coli inner membrane proteins. Cell 77:401-12
    • (1994) Cell , vol.77 , pp. 401-412
    • Gafvelin, G.1    Von Heijne, G.2
  • 45
    • 78650410139 scopus 로고    scopus 로고
    • Integrative analysis of the Caenorhabditis elegans genome by the modENCODE Project
    • Gerstein MB, Lu ZJ, Van Nostrand EL, Cheng C, Arshinoff BI, et al. 2010. Integrative analysis of the Caenorhabditis elegans genome by the modENCODE Project. Science 330:1775-87
    • (2010) Science , vol.330 , pp. 1775-1787
    • Gerstein, M.B.1    Lu, Z.J.2    Van Nostrand, E.L.3    Cheng, C.4    Arshinoff, B.I.5
  • 46
    • 0032727707 scopus 로고    scopus 로고
    • Glycosylation can influence topogenesis of membrane proteins and reveals dynamic reorientation of nascent polypeptides within the translocon
    • Goder V, Bieri C, Spiess M. 1999. Glycosylation can influence topogenesis of membrane proteins and reveals dynamic reorientation of nascent polypeptides within the translocon. J. Cell Biol. 147:257-66
    • (1999) J. Cell Biol. , vol.147 , pp. 257-266
    • Goder, V.1    Bieri, C.2    Spiess, M.3
  • 47
    • 1542313960 scopus 로고    scopus 로고
    • Sec61p contributes to signal sequence orientation according to the positive-inside rule
    • DOI 10.1091/mbc.E03-08-0599
    • Goder V, Junne T, Spiess M. 2004. Sec61p contributes to signal sequence orientation according to the positive-inside rule. Mol. Biol. Cell 15:1470-78 (Pubitemid 38316252)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.3 , pp. 1470-1478
    • Goder, V.1    Junne, T.2    Spiess, M.3
  • 48
    • 0042313962 scopus 로고    scopus 로고
    • Molecular mechanism of signal sequence orientation in the endoplasmic reticulum
    • DOI 10.1093/emboj/cdg361
    • Goder V, Spiess M. 2003. Molecular mechanism of signal sequence orientation in the endoplasmic reticulum. EMBO J. 22:3645-53 (Pubitemid 36898341)
    • (2003) EMBO Journal , vol.22 , Issue.14 , pp. 3645-3653
    • Goder, V.1    Spiess, M.2
  • 49
    • 0026504192 scopus 로고
    • A protein of the endoplasmic reticulum involved early in polypeptide translocation
    • G̈orlich D, Hartmann E, Prehn S, Rapoport TA. 1992a. A protein of the endoplasmic reticulum involved early in polypeptide translocation. Nature 357:47-52
    • (1992) Nature , vol.357 , pp. 47-52
    • G̈orlich D, H.1
  • 50
    • 0026466143 scopus 로고
    • A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation
    • G̈orlich D, Prehn S, Hartmann E, Kalies K-U, Rapoport TA. 1992b. A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation. Cell 71:489-503
    • (1992) Cell , vol.71 , pp. 489-503
    • G̈orlich D, P.1
  • 51
    • 0027424601 scopus 로고
    • Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
    • DOI 10.1016/0092-8674(93)90483-7
    • G̈orlich D, Rapoport TA. 1993. Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell 75: 615-30 (Pubitemid 23346361)
    • (1993) Cell , vol.75 , Issue.4 , pp. 615-630
    • Gorlich, D.1    Rapoport, T.A.2
  • 52
    • 34548057250 scopus 로고    scopus 로고
    • Membrane protein structural biology - How far can the bugs take us? (Review)
    • DOI 10.1080/09687680701413882, PII 779507779
    • Granseth E, Sepp̈al̈a S, Rapp M, Daley DO, von Heijne G. 2007. Membrane protein structural biology-how far can the bugs take us? Mol. Membr. Biol. 24:329-32 (Pubitemid 47290697)
    • (2007) Molecular Membrane Biology , vol.24 , Issue.5-6 , pp. 329-332
    • Granseth, E.1    Seppala, S.2    Rapp, M.3    Daley, D.O.4    Von Heijne, G.5
  • 53
    • 70349595267 scopus 로고    scopus 로고
    • Protein targeting by the signal recognition particle
    • Grudnik P, Bange G, Sinning I. 2009. Protein targeting by the signal recognition particle. Biol. Chem. 390:775-82
    • (2009) Biol. Chem. , vol.390 , pp. 775-782
    • Grudnik, P.1    Bange, G.2    Sinning, I.3
  • 54
    • 1542319100 scopus 로고    scopus 로고
    • Structure of the signal recognition particle interacting with the elongation-arrested ribosome
    • DOI 10.1038/nature02342
    • Halic M, Becker T, Pool MR, Spahn CMT, Grassucci RA, et al. 2004. Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Nature 427:808-14 (Pubitemid 38297736)
    • (2004) Nature , vol.427 , Issue.6977 , pp. 808-814
    • Halic, M.1    Becker, T.2    Pool, M.R.3    Spahn, C.M.T.4    Grassucci, R.A.5    Frank, J.6    Beckmann, R.7
  • 55
    • 13844266603 scopus 로고    scopus 로고
    • The signal recognition particle and its interactions during protein targeting
    • DOI 10.1016/j.sbi.2005.01.013
    • Halic M, Beckmann R. 2005. The signal recognition particle and its interactions during protein targeting. Curr. Opin. Struct. Biol. 15:116-25 (Pubitemid 40249518)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.1 SPEC. ISSUE , pp. 116-125
    • Halic, M.1    Beckmann, R.2
  • 56
    • 33646442605 scopus 로고    scopus 로고
    • Signal recognition particle receptor exposes the ribosomal translocon binding site
    • Halic M, Gartmann M, Schlenker O, Mielke T, Pool MR, et al. 2006. Signal recognition particle receptor exposes the ribosomal translocon binding site. Science 312:745-47
    • (2006) Science , vol.312 , pp. 745-747
    • Halic, M.1    Gartmann, M.2    Schlenker, O.3    Mielke, T.4    Pool, M.R.5
  • 58
    • 77955049339 scopus 로고    scopus 로고
    • Quality and quantity control at the endoplasmic reticulum
    • Hegde RS, PloeghHL. 2010. Quality and quantity control at the endoplasmic reticulum. Curr. Opin. Cell Biol. 22:437-46
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 437-446
    • Hegde, R.S.1    Ploegh, H.L.2
  • 59
    • 0034697967 scopus 로고    scopus 로고
    • The Sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain
    • Heinrich SU, Mothes W, Brunner J, Rapoport TA. 2000. The Sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain. Cell 102:233-44
    • (2000) Cell , vol.102 , pp. 233-244
    • Heinrich, S.U.1    Mothes, W.2    Brunner, J.3    Rapoport, T.A.4
  • 60
    • 0042815085 scopus 로고    scopus 로고
    • Cooperation of transmembrane segments during the integration of a double-spanning protein into the ER membrane
    • DOI 10.1093/emboj/cdg346
    • Heinrich SU, Rapoport TA. 2003. Cooperation of transmembrane segments during the integration of a double-spanning protein into the ER membrane. EMBO J. 22:3654-63 (Pubitemid 36898342)
    • (2003) EMBO Journal , vol.22 , Issue.14 , pp. 3654-3663
    • Heinrich, S.U.1    Rapoport, T.A.2
  • 61
    • 56749151013 scopus 로고    scopus 로고
    • Small membrane proteins found by comparative genomics and ribosome binding site models
    • Hemm MR, Paul BJ, Schneider TD, Storz G, Rudd KE. 2008. Small membrane proteins found by comparative genomics and ribosome binding site models. Mol. Microbiol. 70:1487-501
    • (2008) Mol. Microbiol. , vol.70 , pp. 1487-501
    • Hemm, M.R.1    Paul, B.J.2    Schneider, T.D.3    Storz, G.4    Rudd, K.E.5
  • 65
    • 20044389842 scopus 로고    scopus 로고
    • Membrane insertion of a potassium-channel voltage sensor
    • DOI 10.1126/science.1109176
    • Hessa T, White SH, vonHeijne G. 2005b. Membrane insertion of a potassium-channel voltage sensor. Science 307:1427 (Pubitemid 40321932)
    • (2005) Science , vol.307 , Issue.5714 , pp. 1427
    • Hessa, T.1    White, S.H.2    Von Heijne, G.3
  • 66
    • 13544259578 scopus 로고    scopus 로고
    • Probing the environment of signal-anchor sequences during topogenesis in the endoplasmic reticulum
    • DOI 10.1021/bi047976z
    • Higy M, Gander S, Spiess M. 2005. Probing the environment of signal-anchor sequences during topogenesis in the endoplasmic reticulum. Biochemistry 44:2039-47 (Pubitemid 40223632)
    • (2005) Biochemistry , vol.44 , Issue.6 , pp. 2039-2047
    • Higy, M.1    Gander, S.2    Spiess, M.3
  • 67
    • 4944228608 scopus 로고    scopus 로고
    • Topogenesis of membrane proteins at the endoplasmic reticulum
    • DOI 10.1021/bi048368m
    • Higy M, Junne T, Spiess M. 2004. Topogenesis of membrane proteins at the endoplasmic reticulum. Biochemistry 43:12716-22 (Pubitemid 39331790)
    • (2004) Biochemistry , vol.43 , Issue.40 , pp. 12716-12722
    • Higy, M.1    Junne, T.2    Spiess, M.3
  • 68
    • 77951246542 scopus 로고    scopus 로고
    • The crystal structures of yeast Get3 suggest a mechanism for tail-anchored protein membrane insertion
    • Hu J, Li J, Qian X, Denic V, Sha B. 2009. The crystal structures of yeast Get3 suggest a mechanism for tail-anchored protein membrane insertion. PLoS ONE 4:e8061
    • (2009) PLoS ONE , vol.4
    • Hu, J.1    Li, J.2    Qian, X.3    Denic, V.4    Sha, B.5
  • 69
    • 62549134121 scopus 로고    scopus 로고
    • Genome-wide analysis in vivo of translation with nucleotide resolution using ribosome profiling
    • Ingolia NT, Ghaemmaghami S, Newman JRS, Weissman JS. 2009. Genome-wide analysis in vivo of translation with nucleotide resolution using ribosome profiling. Science 324:218-23
    • (2009) Science , vol.324 , pp. 218-223
    • Ingolia, N.T.1    Ghaemmaghami, S.2    Newman, J.R.S.3    Weissman, J.S.4
  • 71
    • 41549097803 scopus 로고    scopus 로고
    • An interaction between the SRP receptor and the translocon is critical during cotranslational protein translocation
    • DOI 10.1083/jcb.200707196
    • Jiang Y, Cheng Z, Mandon EC, Gilmore R. 2008. An interaction between the SRP receptor and the translocon is critical during cotranslational protein translocation. J. Cell Biol. 180:1149-61 (Pubitemid 351468471)
    • (2008) Journal of Cell Biology , vol.180 , Issue.6 , pp. 1149-1161
    • Jiang, Y.1    Cheng, Z.2    Mandon, E.C.3    Gilmore, R.4
  • 72
    • 0027263346 scopus 로고
    • Positively charged amino acids placed next to a signal sequence block protein translocation more efficiently in Escherichia coli than in mammalian microsomes
    • Johansson M, Nilsson I, von Heijne G. 1993. Positively charged amino acids placed next to a signal sequence block protein translocation more efficiently in Escherichia coli than in mammalian microsomes. Mol. Gen. Genet. MGG 239:251-56 (Pubitemid 23167505)
    • (1993) Molecular and General Genetics , vol.239 , Issue.1-2 , pp. 251-256
    • Johansson, M.1    Nilsson, I.2    Von Heijne, G.3
  • 73
    • 34047151404 scopus 로고    scopus 로고
    • Improving the accuracy of transmembrane protein topology prediction using evolutionary information
    • DOI 10.1093/bioinformatics/btl677
    • Jones DT. 2007. Improving the accuracy of transmembrane protein topology prediction using evolutionary information. Bioinformatics 23:538-44 (Pubitemid 46522586)
    • (2007) Bioinformatics , vol.23 , Issue.5 , pp. 538-544
    • Jones, D.T.1
  • 74
    • 63449128473 scopus 로고    scopus 로고
    • Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum
    • Jonikas MC, Collins SR, Denic V, Oh E, Quan EM, et al. 2009. Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum. Science 323:1693-97
    • (2009) Science , vol.323 , pp. 1693-1697
    • Jonikas, M.C.1    Collins, S.R.2    Denic, V.3    Oh, E.4    Quan, E.M.5
  • 75
    • 0028337335 scopus 로고
    • Protein translocation: Common themes from bacteria to man
    • DOI 10.1016/0014-5793(94)00367-X
    • Jungnickel B, Rapoport TA, Hartmann E. 1994. Protein translocation: common themes from bacteria to man. FEBS Lett. 346:73-77 (Pubitemid 24183831)
    • (1994) FEBS Letters , vol.346 , Issue.1 , pp. 73-77
    • Jungnickel, B.1
  • 76
    • 77952378779 scopus 로고    scopus 로고
    • The hydrophobic core of the Sec61 translocon defines the hydrophobicity threshold for membrane integration
    • Junne T, Kocik L, Spiess M. 2010. The hydrophobic core of the Sec61 translocon defines the hydrophobicity threshold for membrane integration. Mol. Biol. Cell 21:1662-70
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1662-1670
    • Junne, T.1    Kocik, L.2    Spiess, M.3
  • 77
    • 33748300566 scopus 로고    scopus 로고
    • The plug domain of yeast Sec61p is important for efficient protein translocation, but is not essential for cell viability
    • DOI 10.1091/mbc.E06-03-0200
    • Junne T, Schwede T, Goder V, Spiess M. 2006. The plug domain of yeast Sec61p is important for efficient protein translocation, but is not essential for cell viability. Mol. Biol. Cell 17:4063-68 (Pubitemid 44330888)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.9 , pp. 4063-4068
    • Junne, T.1    Schwede, T.2    Goder, V.3    Spiess, M.4
  • 78
    • 36349034451 scopus 로고    scopus 로고
    • Mutations in the Sec61p channel affecting signal sequence recognition and membrane protein topology
    • DOI 10.1074/jbc.M707219200
    • Junne T, Schwede T, Goder V, Spiess M. 2007. Mutations in the Sec61p channel affecting signal sequence recognition and membrane protein topology. J. Biol. Chem. 282:33201-9 (Pubitemid 350159300)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.45 , pp. 33201-33209
    • Junne, T.1    Schwede, T.2    Goder, V.3    Spiess, M.4
  • 79
    • 35948944937 scopus 로고    scopus 로고
    • A bioinformatics approach to identifying tail-anchored proteins in the human genome
    • DOI 10.1111/j.1600-0854.2007.00661.x
    • Kalbfleisch T, Cambon A, Wattenberg BW. 2007. A bioinformatics approach to identifying tail-anchored proteins in the human genome. Traffic 8:1687-94 (Pubitemid 350066681)
    • (2007) Traffic , vol.8 , Issue.12 , pp. 1687-1694
    • Kalbfleisch, T.1    Cambon, A.2    Wattenberg, B.W.3
  • 81
    • 0033962442 scopus 로고    scopus 로고
    • A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch
    • DOI 10.1016/S0014-5793(00)01135-2, PII S0014579300011352
    • Kaye FJ, Modi S, Ivanovska I, Koonin EV, Thress K, et al. 2000. A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch. FEBS Lett. 467:348-55 (Pubitemid 30081763)
    • (2000) FEBS Letters , vol.467 , Issue.2-3 , pp. 348-355
    • Kaye, F.J.1    Modi, S.2    Ivanovska, I.3    Koonin, E.V.4    Thress, K.5    Kubo, A.6    Kornbluth, S.7    Rose, M.D.8
  • 83
    • 0032563163 scopus 로고    scopus 로고
    • Crystal structure of the signal sequence binding subunit of the signal recognition particle
    • DOI 10.1016/S0092-8674(00)81418-X
    • Keenan RJ, Freymann DM, Walter P, Stroud RM. 1998. Crystal structure of the signal sequence binding subunit of the signal recognition particle. Cell 94:181-91 (Pubitemid 28348006)
    • (1998) Cell , vol.94 , Issue.2 , pp. 181-191
    • Keenan, R.J.1    Freymann, D.M.2    Walter, P.3    Stroud, R.M.4
  • 84
    • 25144519777 scopus 로고    scopus 로고
    • Translocation of a long amino-terminal domain through ER membrane by following signal-anchor sequence
    • DOI 10.1038/sj.emboj.7600788, PII 7600788
    • Kida Y, Mihara K, Sakaguchi M. 2005. Translocation of a long amino-terminal domain through ER membrane by following signal-anchor sequence. EMBO J. 24:3202-13 (Pubitemid 41348695)
    • (2005) EMBO Journal , vol.24 , Issue.18 , pp. 3202-3213
    • Kida, Y.1    Mihara, K.2    Sakaguchi, M.3
  • 85
    • 0035798078 scopus 로고    scopus 로고
    • Amino acid residues before the hydrophobic region which are critical for membrane translocation of the N-terminal domain of synaptotagmin II
    • DOI 10.1016/S0014-5793(01)03000-9, PII S0014579301030009
    • Kida Y, Sakaguchi M, Fukuda M, Mikoshiba K, Mihara K. 2001. Amino acid residues before the hydrophobic region which are critical for membrane translocation of the N-terminal domain of synaptotagmin II. FEBS Lett. 507:341-45 (Pubitemid 33030262)
    • (2001) FEBS Letters , vol.507 , Issue.3 , pp. 341-345
    • Kida, Y.1    Sakaguchi, M.2    Fukuda, M.3    Mikoshiba, K.4    Mihara, K.5
  • 86
    • 0033601172 scopus 로고    scopus 로고
    • Identification of the endoplasmic reticulum targeting signal in vesicle-associated membrane proteins
    • Kim PK, Hollerbach C, Trimble WS, Leber B, Andrews DW. 1999. Identification of the endoplasmic reticulum targeting signal in vesicle-associated membrane proteins. J. Biol. Chem. 274:36876-82
    • (1999) J. Biol. Chem. , vol.274 , pp. 36876-36882
    • Kim, P.K.1    Hollerbach, C.2    Trimble, W.S.3    Leber, B.4    Andrews, D.W.5
  • 87
    • 0030798914 scopus 로고    scopus 로고
    • Evidence for multiple mechanisms for membrane binding and integration via carboxyl-terminal insertion sequences
    • DOI 10.1021/bi970090t
    • Kim PK, Janiak-Spens F, Trimble WS, Leber B, Andrews DW. 1997. Evidence for multiple mechanisms for membrane binding and integration via carboxyl-terminal insertion sequences. Biochemistry 36:8873-82 (Pubitemid 27342533)
    • (1997) Biochemistry , vol.36 , Issue.29 , pp. 8873-8882
    • Kim, P.K.1    Janiak-Spens, F.2    Trimble, W.S.3    Leber, B.4    Andrews, D.W.5
  • 88
    • 0028837490 scopus 로고
    • Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane
    • Kutay U, Ahnert-Hilger G, Hartmann E, Wiedenmann B, Rapoport TA. 1995. Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane. EMBO J. 14:217-23
    • (1995) EMBO J. , vol.14 , pp. 217-223
    • Kutay, U.1    Ahnert-Hilger, G.2    Hartmann, E.3    Wiedenmann, B.4    Rapoport, T.A.5
  • 89
    • 0027401769 scopus 로고
    • A class of membrane proteins with a C-terminal anchor
    • Kutay U, Hartmann E, Rapoport TA. 1993. A class of membrane proteins with a C-terminal anchor. Trends Cell Biol. 3:72-75 (Pubitemid 23072280)
    • (1993) Trends in Cell Biology , vol.3 , Issue.3 , pp. 72-75
    • Kutay, U.1    Hartmann, E.2    Rapoport, T.A.3
  • 90
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-32
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 91
    • 42949161206 scopus 로고    scopus 로고
    • SRP keeps polypeptides translocation-competent by slowing translation to match limiting ER-targeting sites
    • DOI 10.1016/j.cell.2008.02.049, PII S0092867408003991
    • Lakkaraju AKK, Mary C, Scherrer A, Johnson AE, Strub K. 2008. SRP keeps polypeptides translocationcompetent by slowing translation to match limiting ER-targeting sites. Cell 133:440-51 (Pubitemid 351608693)
    • (2008) Cell , vol.133 , Issue.3 , pp. 440-451
    • Lakkaraju, A.K.K.1    Mary, C.2    Scherrer, A.3    Johnson, A.E.4    Strub, K.5
  • 92
    • 77954352789 scopus 로고    scopus 로고
    • Bat3 promotes the membrane integration of tail-anchored proteins
    • Leznicki P, Clancy A, Schwappach B, High S. 2010. Bat3 promotes the membrane integration of tail-anchored proteins. J. Cell Sci. 123:2170-78
    • (2010) J. Cell Sci. , vol.123 , pp. 2170-2178
    • Leznicki, P.1    Clancy, A.2    Schwappach, B.3    High, S.4
  • 93
    • 0031471055 scopus 로고    scopus 로고
    • Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration
    • DOI 10.1016/S0092-8674(00)80311-6
    • Liao S, Lin J, Do H, Johnson AE. 1997. Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration. Cell 90:31-41 (Pubitemid 28009416)
    • (1997) Cell , vol.90 , Issue.1 , pp. 31-41
    • Liao, S.1    Lin, J.2    Do, H.3    Johnson, A.E.4
  • 94
    • 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 VR, Katz FN, Lodish HF, 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. 253:8667-70 (Pubitemid 9104643)
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.24 , pp. 8667-8670
    • Lingappa, V.R.1    Katz, F.N.2    Lodish, H.F.3    Blobel, G.4
  • 95
    • 0023644552 scopus 로고
    • Signal recognition particle arrests elongation of nascent secretory and membrane proteins at multiple sites in a transient manner
    • Lipp J, Dobberstein B, Haeuptle MT. 1987. Signal recognition particle arrests elongation of nascent secretory and membrane proteins at multiple sites in a transient manner. J. Biol. Chem. 262:1680-84
    • (1987) J. Biol. Chem. , vol.262 , pp. 1680-1684
    • Lipp, J.1    Dobberstein, B.2    Haeuptle, M.T.3
  • 97
    • 57349168025 scopus 로고    scopus 로고
    • Molecular code for protein insertion in the endoplasmic reticulum membrane is similar for Nin-Cout and Nout-Cin transmembrane helices
    • Lundin C, Kim H, Nilsson I, White SH, von Heijne G. 2008. Molecular code for protein insertion in the endoplasmic reticulum membrane is similar for Nin-Cout and Nout-Cin transmembrane helices. Proc. Natl. Acad. Sci. USA 105:15702-7
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 15702-7
    • Lundin, C.1    Kim, H.2    Nilsson, I.3    White, S.H.4    Von Heijne, G.5
  • 98
    • 77956183398 scopus 로고    scopus 로고
    • A ribosome-associating factor chaperones tail-anchored membrane proteins
    • Mariappan M, Li X, Stefanovic S, Sharma A, Mateja A, et al. 2010. A ribosome-associating factor chaperones tail-anchored membrane proteins. Nature 466:1120-24
    • (2010) Nature , vol.466 , pp. 1120-1124
    • Mariappan, M.1    Li, X.2    Stefanovic, S.3    Sharma, A.4    Mateja, A.5
  • 99
    • 0029002962 scopus 로고
    • The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer
    • Martoglio B, Hofmann MW, Brunner J, Dobberstein B. 1995. The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer. Cell 81:207-14
    • (1995) Cell , vol.81 , pp. 207-214
    • Martoglio, B.1    Hofmann, M.W.2    Brunner, J.3    Dobberstein, B.4
  • 100
    • 0142058381 scopus 로고    scopus 로고
    • Post-Translational Targeting of a Tail-Anchored Green Fluorescent Protein to the Endolpasmic Reticulum
    • DOI 10.1093/jb/mvg159
    • Masaki R, Kameyama K, Yamamoto A. 2003. Post-translational targeting of a tail-anchored green fluorescent protein to the endolpasmic reticulum. J. Biochem. 134:415-26 (Pubitemid 37288340)
    • (2003) Journal of Biochemistry , vol.134 , Issue.3 , pp. 415-426
    • Masaki, R.1    Kameyama, K.2    Yamamoto, A.3
  • 101
    • 0034254190 scopus 로고    scopus 로고
    • Elongation arrest is a physiologically important function of signal recognition particle
    • Mason N, Ciufo LF, Brown JD. 2000. Elongation arrest is a physiologically important function of signal recognition particle. EMBO J. 19:4164-74 (Pubitemid 30608554)
    • (2000) EMBO Journal , vol.19 , Issue.15 , pp. 4164-4174
    • Mason, N.1    Ciufo, L.F.2    Brown, J.D.3
  • 102
    • 70349272618 scopus 로고    scopus 로고
    • The structural basis of tailanchored membrane protein recognition by Get3
    • Mateja A, Szlachcic A, Downing ME, Dobosz M, Mariappan M, et al. 2009. The structural basis of tailanchored membrane protein recognition by Get3. Nature 461:361-66
    • (2009) Nature , vol.461 , pp. 361-366
    • Mateja, A.1    Szlachcic, A.2    Downing, M.E.3    Dobosz, M.4    Mariappan, M.5
  • 103
    • 0141992130 scopus 로고    scopus 로고
    • Cotranslational protein integration into the ER membrane is mediated by the binding of nascent chains to translocon proteins
    • DOI 10.1016/S1097-2765(03)00304-6
    • McCormick PJ, Miao Y, Shao Y, Lin J, Johnson AE. 2003. Cotranslational protein integration into the ER membrane is mediated by the binding of nascent chains to translocon proteins. Mol. Cell 12:329-41 (Pubitemid 37238920)
    • (2003) Molecular Cell , vol.12 , Issue.2 , pp. 329-341
    • McCormick, P.J.1    Miao, Y.2    Shao, Y.3    Lin, J.4    Johnson, A.E.5
  • 104
    • 33750498869 scopus 로고    scopus 로고
    • Asn- and Asp-mediated interactions between transmembrane helices during translocon-mediated membrane protein assembly
    • DOI 10.1038/sj.embor.7400818, PII 7400818
    • Meindl-Beinker NM, Lundin C, Nilsson I, White SH, von Heijne G. 2006. Asn-and Asp-mediated interactions between transmembrane helices during translocon-mediated membrane protein assembly. EMBO Rep. 7:1111-16 (Pubitemid 44660566)
    • (2006) EMBO Reports , vol.7 , Issue.11 , pp. 1111-1116
    • Meindl-Beinker, N.M.1    Lundin, C.2    Nilsson, I.3    White, S.H.4    Von Heijne, G.5
  • 105
    • 0033638455 scopus 로고    scopus 로고
    • The structure of ribosomechannel complexes engaged in protein translocation
    • Ḿeńetret J-F, Neuhof A, Morgan DG, Plath K, Radermacher M, et al. 2000. The structure of ribosomechannel complexes engaged in protein translocation. Mol. Cell 6:1219-32
    • (2000) Mol. Cell , vol.6 , pp. 1219-1232
    • Ḿeńetret, J.-F.1    Neuhof, A.2    Morgan, D.G.3    Plath, K.4    Radermacher, M.5
  • 106
  • 110
    • 0027936633 scopus 로고
    • Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane
    • Mothes W, Prehn S, Rapoport TA. 1994. Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane. EMBO J. 13:3973-82 (Pubitemid 24275852)
    • (1994) EMBO Journal , vol.13 , Issue.17 , pp. 3973-3982
    • Mothes, W.1    Prehn, S.2    Rapoport, T.A.3
  • 111
    • 0030592511 scopus 로고    scopus 로고
    • Emerging understanding of translation termination
    • DOI 10.1016/S0092-8674(00)81331-8
    • Nakamura Y, Ito K, Isaksson LA. 1996. Emerging understanding of translation termination. Cell 87:147-50 (Pubitemid 26358994)
    • (1996) Cell , vol.87 , Issue.2 , pp. 147-150
    • Nakamura, Y.1    Ito, K.2    Isaksson, L.A.3
  • 113
    • 0026649409 scopus 로고
    • The translation machinery and 70 kD heat shock protein cooperate in protein synthesis
    • Nelson RJ, Ziegelhoffer T, Nicolet C, Werner-Washburne M, Craig EA. 1992. The translation machinery and 70 kD heat shock protein cooperate in protein synthesis. Cell 71:97-105
    • (1992) Cell , vol.71 , pp. 97-105
    • Nelson, R.J.1    Ziegelhoffer, T.2    Nicolet, C.3    Werner-Washburne, M.4    Craig, E.A.5
  • 114
    • 0034053280 scopus 로고    scopus 로고
    • Distant downstream sequence determinants can control N-tail translocation during protein insertion into the endoplasmic reticulum membrane
    • DOI 10.1074/jbc.275.9.6207
    • Nilsson I, Witt S, Kiefer H, Mingarro I, von Heijne G. 2000. Distant downstream sequence determinants can control N-tail translocation during protein insertion into the endoplasmic reticulum membrane. J. Biol. Chem. 275:6207-13 (Pubitemid 30129908)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.9 , pp. 6207-6213
    • Nilsson, I.1    Witt, S.2    Kiefer, H.3    Mingarro, I.4    Von Heijne, G.5
  • 115
    • 0028929094 scopus 로고
    • The Sec61 complex is essential for the insertion of proteins into the membrane of the endoplasmic reticulum
    • Oliver J, Jungnickel B, G̈orlich D, Rapoport T, High S. 1995. The Sec61 complex is essential for the insertion of proteins into the membrane of the endoplasmic reticulum. FEBS Lett. 362:126-30
    • (1995) FEBS Lett. , vol.362 , pp. 126-130
    • Oliver, J.1    Jungnickel, B.2    G̈orlich, D.3    Rapoport, T.4    High, S.5
  • 117
    • 0037092503 scopus 로고    scopus 로고
    • Integral membrane protein biosynthesis: Why topology is hard to predict
    • Ott CM, Lingappa VR. 2002. Integral membrane protein biosynthesis: why topology is hard to predict. J. Cell Sci. 115:2003-9 (Pubitemid 34746367)
    • (2002) Journal of Cell Science , vol.115 , Issue.10 , pp. 2003-2009
    • Ott, C.M.1    Lingappa, V.R.2
  • 118
    • 78651477794 scopus 로고    scopus 로고
    • Hph1 and Hph2 are novel components of the Sec63/Sec62 posttranslational translocation complex that aid in vacuolar proton ATPase biogenesis
    • Pina FJ, O'Donnell AF, Pagant S, Piao HL, Miller JP, et al. 2011. Hph1 and Hph2 are novel components of the Sec63/Sec62 posttranslational translocation complex that aid in vacuolar proton ATPase biogenesis. Eukaryot. Cell 10:63-71
    • (2011) Eukaryot. Cell , vol.10 , pp. 63-71
    • Pina, F.J.1    O'Donnell, A.F.2    Pagant, S.3    Piao, H.L.4    Miller, J.P.5
  • 119
    • 0346099350 scopus 로고    scopus 로고
    • Interactions between sec complex and prepro-α-factor during posttranslational protein transport into the endoplasmic reticulum
    • DOI 10.1091/mbc.E03-06-0390
    • Plath K, Wilkinson BM, Stirling CJ, Rapoport TA. 2004. Interactions between Sec complex and prepro-α-factor during posttranslational protein transport into the endoplasmic reticulum. Mol. Biol. Cell 15:1-10 (Pubitemid 38044938)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.1 , pp. 1-10
    • Plath, K.1    Wilkinson, B.M.2    Stirling, C.J.3    Rapoport, T.A.4
  • 120
    • 66349109602 scopus 로고    scopus 로고
    • A trans-membrane segment inside the ribosome exit tunnel triggers RAMP4 recruitment to the Sec61p translocase
    • Pool MR. 2009. A trans-membrane segment inside the ribosome exit tunnel triggers RAMP4 recruitment to the Sec61p translocase. J. Cell Biol. 185:889-902
    • (2009) J. Cell Biol. , vol.185 , pp. 889-902
    • Pool, M.R.1
  • 121
    • 0025605808 scopus 로고
    • An E. coli ribonucleoprotein containing 4.5S RNA resembles mammalian signal recognition particle
    • Poritz MA, Bernstein HD, Strub K, Zopf D, Wilhelm H, Walter P. 1990. An E. coli ribonucleoprotein containing 4. 5S RNA resembles mammalian signal recognition particle. Science 250:1111-17 (Pubitemid 120031815)
    • (1990) Science , vol.250 , Issue.4984 , pp. 1111-1117
    • Poritz, M.A.1    Bernstein, H.D.2    Strub, K.3    Zopf, D.4    Wilhelm, H.5    Walter, P.6
  • 122
    • 0034678632 scopus 로고    scopus 로고
    • Evolutionarily conserved binding of ribosomes to the translocation channel via the large ribosomal RNA
    • Prinz A, Behrens C, Rapoport TA, Hartmann E, Kalies K-U. 2000. Evolutionarily conserved binding of ribosomes to the translocation channel via the large ribosomal RNA. EMBO J. 19:1900-6 (Pubitemid 30204400)
    • (2000) EMBO Journal , vol.19 , Issue.8 , pp. 1900-1906
    • Prinz, A.1    Behrens, C.2    Rapoport, T.A.3    Hartmann, E.4    Kalies, K.-U.5
  • 124
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • DOI 10.1038/nature06384, PII NATURE06384
    • Rapoport TA. 2007. Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes. Nature 450:663-69 (Pubitemid 350207698)
    • (2007) Nature , vol.450 , Issue.7170 , pp. 663-669
    • Rapoport, T.A.1
  • 125
    • 4644356464 scopus 로고    scopus 로고
    • Membrane-protein integration and the role of the translocation channel
    • DOI 10.1016/j.tcb.2004.09.002, PII S096289240400234X
    • Rapoport TA, Goder V, Heinrich SU, Matlack KES. 2004. Membrane-protein integration and the role of the translocation channel. Trends Cell Biol. 14:568-75 (Pubitemid 39296619)
    • (2004) Trends in Cell Biology , vol.14 , Issue.10 , pp. 568-575
    • Rapoport, T.A.1    Goder, V.2    Heinrich, S.U.3    Matlack, K.E.S.4
  • 126
    • 0024835142 scopus 로고
    • Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast
    • DOI 10.1083/jcb.109.6.2641
    • Rothblatt JA, Deshaies RJ, Sanders SL, Daum G, Schekman R. 1989. Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast. J. Cell Biol. 109:2641-52 (Pubitemid 20011893)
    • (1989) Journal of Cell Biology , vol.109 , Issue.6 , pp. 2641-2652
    • Rothblatt, J.A.1    Deshaies, R.J.2    Sanders, S.L.3    Daum, G.4    Schekman, R.5
  • 127
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • DOI 10.1038/372055a0
    • Rothman JE. 1994. Mechanisms of intracellular protein transport. Nature 372:55-63 (Pubitemid 24339484)
    • (1994) Nature , vol.372 , Issue.6501 , pp. 55-63
    • Rothman, J.E.1
  • 128
    • 78650331647 scopus 로고    scopus 로고
    • Identification of functional elements and regulatory circuits by Drosophila modENCODE
    • Roy S, Ernst J, Kharchenko PV, Kheradpour P, Negre N, et al. 2010. Identification of functional elements and regulatory circuits by Drosophila modENCODE. Science 330:1787-97
    • (2010) Science , vol.330 , pp. 1787-1797
    • Roy, S.1    Ernst, J.2    Kharchenko, P.V.3    Kheradpour, P.4    Negre, N.5
  • 129
    • 27144549973 scopus 로고    scopus 로고
    • Sequential triage of transmembrane segments by Sec61α during biogenesis of a native multispanning membrane protein
    • DOI 10.1038/nsmb994, PII N994
    • SadlishH, Pitonzo D, Johnson AE, SkachWR. 2005. Sequential triage of transmembrane segments by Sec61-α during biogenesis of a native multispanning membrane protein. Nat. Struct. Mol. Biol. 12:870-78 (Pubitemid 41486710)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.10 , pp. 870-878
    • Sadlish, H.1    Pitonzo, D.2    Johnson, A.E.3    Skach, W.R.4
  • 130
    • 0032566739 scopus 로고    scopus 로고
    • Testing the charge difference hypothesis for the assembly of a eucaryotic multispanning membrane protein
    • DOI 10.1074/jbc.273.39.25203
    • Sato M, Hresko R, Mueckler M. 1998. Testing the charge difference hypothesis for the assembly of a eukaryotic multispanning membrane protein. J. Biol. Chem. 273:25203-8 (Pubitemid 28443282)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.39 , pp. 25203-25208
    • Sato, M.1    Hresko, R.2    Mueckler, M.3
  • 131
    • 0025310666 scopus 로고
    • Identification of a ribosome receptor in the rough endoplasmic reticulum
    • Savitz AJ, Meyer DI. 1990. Identification of a ribosome receptor in the rough endoplasmic reticulum. Nature 346:540-44
    • (1990) Nature , vol.346 , pp. 540-544
    • Savitz, A.J.1    Meyer, D.I.2
  • 133
    • 49549086224 scopus 로고    scopus 로고
    • The GET complex mediates insertion of tail-anchored proteins into the ER membrane
    • Schuldiner M, Metz J, Schmid V, Denic V, Rakwalska M, et al. 2008. The GET complex mediates insertion of tail-anchored proteins into the ER membrane. Cell 134:634-45
    • (2008) Cell , vol.134 , pp. 634-645
    • Schuldiner, M.1    Metz, J.2    Schmid, V.3    Denic, V.4    Rakwalska, M.5
  • 135
    • 77954299061 scopus 로고    scopus 로고
    • A comprehensive comparison of transmembrane domains reveals organelle-specific properties
    • Sharpe HJ, Stevens TJ, Munro S. 2010. A comprehensive comparison of transmembrane domains reveals organelle-specific properties. Cell 142:158-69
    • (2010) Cell , vol.142 , pp. 158-169
    • Sharpe, H.J.1    Stevens, T.J.2    Munro, S.3
  • 136
    • 0037412034 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Arr4p is involved in metal and heat tolerance
    • DOI 10.1023/A:1022504311669
    • Shen J, Hsu C-M, Kang B-K, Rosen BP, Bhattacharjee H. 2003. The Saccharomyces cerevisiae Arr4p is involved in metal and heat tolerance. BioMetals 16:369-78 (Pubitemid 36356767)
    • (2003) BioMetals , vol.16 , Issue.3 , pp. 369-378
    • Shen, J.1    Hsu, C.-M.2    Kang, B.-K.3    Rosen, B.P.4    Bhattacharjee, H.5
  • 137
    • 0025854858 scopus 로고
    • A protein-conducting channel in the endoplasmic reticulum
    • Simon SM, Blobel G. 1991. A protein-conducting channel in the endoplasmic reticulum. Cell 65:371-80 (Pubitemid 121002047)
    • (1991) Cell , vol.65 , Issue.3 , pp. 371-380
    • Simon, S.M.1    Blobel, G.2
  • 138
    • 0027264995 scopus 로고
    • Predicting the topology of eukaryotic membrane proteins
    • DOI 10.1111/j.1432-1033.1993.tb17885.x
    • Sipos L, von Heijne G. 1993. Predicting the topology of eukaryotic membrane proteins. Eur. J. Biochem. 213:1333-40 (Pubitemid 23152245)
    • (1993) European Journal of Biochemistry , vol.213 , Issue.3 , pp. 1333-1340
    • Sipos, L.1    Von Heijne, G.2
  • 139
    • 66849131417 scopus 로고    scopus 로고
    • Cellular mechanisms of membrane protein folding
    • Skach WR. 2009. Cellular mechanisms of membrane protein folding. Nat. Struct. Mol. Biol. 16:606-12
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 606-612
    • Skach, W.R.1
  • 140
    • 0027519416 scopus 로고
    • Amino-terminal assembly of human P-glycoprotein at the endoplasmic reticulum is directed by cooperative actions of two internal sequences
    • Skach WR, Lingappa VR. 1993. Amino-terminal assembly of human P-glycoprotein at the endoplasmic reticulum is directed by cooperative actions of two internal sequences. J. Biol. Chem. 268:23552-61 (Pubitemid 23328085)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.31 , pp. 23552-23561
    • Skach, W.R.1    Lingappa, V.R.2
  • 141
    • 0034602866 scopus 로고    scopus 로고
    • Role of Sec61α in the regulated transfer of the ribosome-nascent chain complex from the signal recognition particle to the translocation channel
    • Song W, Raden D, Mandon EC, Gilmore R. 2000. Role of Sec61αin the regulated transfer of the ribosomenascent chain complex from the signal recognition particle to the translocation channel. Cell 100:333-43 (Pubitemid 30353089)
    • (2000) Cell , vol.100 , Issue.3 , pp. 333-343
    • Song, W.1    Raden, D.2    Mandon, E.C.3    Gilmore, R.4
  • 142
    • 0036786921 scopus 로고    scopus 로고
    • Tail-anchored protein insertion into yeast ER requires a novel posttranslational mechanism which is independent of the SEC machinery
    • Steel GJ, Brownsword J, Stirling CJ. 2002. Tail-anchored protein insertion into yeast ER requires a novel posttranslational mechanism which is independent of the SEC machinery. Biochemistry 41:11914-20
    • (2002) Biochemistry , vol.41 , pp. 11914-11920
    • Steel, G.J.1    Brownsword, J.2    Stirling, C.J.3
  • 143
    • 33947218544 scopus 로고    scopus 로고
    • Identification of a Targeting Factor for Posttranslational Membrane Protein Insertion into the ER
    • DOI 10.1016/j.cell.2007.01.036, PII S009286740700195X
    • Stefanovic S, Hegde RS. 2007. Identification of a targeting factor for posttranslational membrane protein insertion into the ER. Cell 128:1147-59 (Pubitemid 46427870)
    • (2007) Cell , vol.128 , Issue.6 , pp. 1147-1159
    • Stefanovic, S.1    Hegde, R.S.2
  • 144
    • 0027058051 scopus 로고
    • Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum
    • Stirling CJ, Rothblatt J, Hosobuchi M, Deshaies R, SchekmanR. 1992. Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum. Mol. Biol. Cell 3:129-42 (Pubitemid 23084545)
    • (1992) Molecular Biology of the Cell , vol.3 , Issue.2 , pp. 129-142
    • Stirling, C.J.1    Rothblatt, J.2    Hosobuchi, M.3    Deshaies, R.4    Schekman, R.5
  • 146
    • 0035282773 scopus 로고    scopus 로고
    • Reversible inhibition of Hsp70 chaperone function by Scythe and Reaper
    • DOI 10.1093/emboj/20.5.1033
    • Thress K, Song J, Morimoto RI, Kornbluth S. 2001. Reversible inhibition of Hsp70 chaperone function by Scythe and Reaper. EMBO J. 20:1033-41 (Pubitemid 32186794)
    • (2001) EMBO Journal , vol.20 , Issue.5 , pp. 1033-1041
    • Thress, K.1    Song, J.2    Morimoto, R.I.3    Kornbluth, S.4
  • 147
    • 0036223875 scopus 로고    scopus 로고
    • Yeast genes controlling responses to topogenic signals in a model transmembrane protein
    • DOI 10.1091/mbc.01-10-0488
    • Tipper DJ, Harley CA. 2002. Yeast genes controlling responses to topogenic signals in a model transmembrane protein. Mol. Biol. Cell 13:1158-74 (Pubitemid 34309613)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.4 , pp. 1158-1174
    • Tipper, D.J.1    Harley, C.A.2
  • 148
    • 54049151196 scopus 로고    scopus 로고
    • Conformational transition of Sec machinery inferred from bacterial SecYE structures
    • Tsukazaki T, Mori H, Fukai S, Ishitani R, Mori T, et al. 2008. Conformational transition of Sec machinery inferred from bacterial SecYE structures. Nature 455:988-91
    • (2008) Nature , vol.455 , pp. 988-991
    • Tsukazaki, T.1    Mori, H.2    Fukai, S.3    Ishitani, R.4    Mori, T.5
  • 150
    • 16344390562 scopus 로고    scopus 로고
    • Properties of integral membrane protein structures: Derivation of an implicit membrane potential
    • DOI 10.1002/prot.20334
    • Ulmschneider MB, Sansom MSP, Di Nola A. 2005. Properties of integral membrane protein structures: derivation of an implicit membrane potential. Proteins: Struct. Funct. Bioinforma. 59:252-65 (Pubitemid 40471564)
    • (2005) Proteins: Structure, Function and Genetics , vol.59 , Issue.2 , pp. 252-265
    • Ulmschneider, M.B.1    Sansom, M.S.P.2    Di Nola, A.3
  • 151
    • 0036777494 scopus 로고    scopus 로고
    • Intramembrane proteolysis controls diverse signalling pathways throughout evolution
    • DOI 10.1016/S0959-437X(02)00334-9
    • Urban S, Freeman M. 2002. Intramembrane proteolysis controls diverse signaling pathways throughout evolution. Curr. Opin. Genet. Dev. 12:512-18 (Pubitemid 35013532)
    • (2002) Current Opinion in Genetics and Development , vol.12 , Issue.5 , pp. 512-518
    • Urban, S.1    Freeman, M.2
  • 153
    • 0030791975 scopus 로고    scopus 로고
    • Anionic phospholipids are determinants of membrane protein topology
    • DOI 10.1093/emboj/16.14.4261
    • van Klompenburg W, Nilsson I, von Heijne G, de Kruijff B. 1997. Anionic phospholipids are determinants of membrane protein topology. EMBO J. 16:4261-66 (Pubitemid 27298178)
    • (1997) EMBO Journal , vol.16 , Issue.14 , pp. 4261-4266
    • Van Klompenburg, W.1    Nilsson, I.2    Von Heijne, G.3    De Kruijff, B.4
  • 154
    • 79953137111 scopus 로고    scopus 로고
    • WRB is the receptor for TRC40/Asna1-mediated insertion of tail-anchored proteins into the ER membrane
    • Vilardi F, Lorenz H, Dobberstein B. 2011. WRB is the receptor for TRC40/Asna1-mediated insertion of tail-anchored proteins into the ER membrane. J. Cell Sci. 124:1301-7
    • (2011) J. Cell Sci. , vol.124 , pp. 1301-7
    • Vilardi, F.1    Lorenz, H.2    Dobberstein, B.3
  • 155
    • 0029951178 scopus 로고    scopus 로고
    • Signal sequence-dependent function of the TRAM protein during early phases of protein transport across the endoplasmic reticulum membrane
    • DOI 10.1083/jcb.134.1.25
    • Voigt S, Jungnickel B, Hartmann E, Rapoport TA. 1996. Signal sequence-dependent function of the TRAM protein during early phases of protein transport across the endoplasmic reticulum membrane. J. Cell Biol. 134:25-35 (Pubitemid 26231518)
    • (1996) Journal of Cell Biology , vol.134 , Issue.1 , pp. 25-35
    • Voigt, S.1    Jungnickel, B.2    Hartmann, E.3    Rapoport, T.A.4
  • 156
    • 0023036920 scopus 로고
    • Net N-C charge imbalance may be important for signal sequence function in bacteria
    • DOI 10.1016/0022-2836(86)90365-7
    • von Heijne G. 1986a. Net N-C charge imbalance may be important for signal sequence function in bacteria. J. Mol. Biol. 192:287-90 (Pubitemid 17203057)
    • (1986) Journal of Molecular Biology , vol.192 , Issue.2 , pp. 287-290
    • Von Heijne, G.1
  • 157
    • 0000651660 scopus 로고
    • The distribution of positively charged residues in bacterial inner membrane proteins correlates with the transmembrane topology
    • von Heijne G. 1986b. The distribution of positively charged residues in bacterial inner membrane proteins correlates with the transmembrane topology. EMBO J. 5:3021-27
    • (1986) EMBO J. , vol.5 , pp. 3021-3027
    • Von Heijne, G.1
  • 158
    • 0024442722 scopus 로고
    • Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues
    • DOI 10.1038/341456a0
    • vonHeijne G. 1989. Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues. Nature 341:456-58 (Pubitemid 19241917)
    • (1989) Nature , vol.341 , Issue.6241 , pp. 456-458
    • Von Heijne, G.1
  • 159
    • 0030919649 scopus 로고    scopus 로고
    • Multiple determinants direct the orientation of signal-anchor proteins: The topogenic role of the hydrophobic signal domain
    • DOI 10.1083/jcb.137.3.555
    • Wahlberg JM, Spiess M. 1997. Multiple determinants direct the orientation of signal-anchor proteins: the topogenic role of the hydrophobic signal domain. J. Cell Biol. 137:555-62 (Pubitemid 27200660)
    • (1997) Journal of Cell Biology , vol.137 , Issue.3 , pp. 555-562
    • Wahlberg, J.M.1    Spiess, M.2
  • 160
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin E, von Heijne G. 1998. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci. 7:1029-38 (Pubitemid 28216544)
    • (1998) Protein Science , vol.7 , Issue.4 , pp. 1029-1038
    • Wallin, E.1    Von Heijne, G.2
  • 161
    • 0028834958 scopus 로고
    • Properties of N-terminal tails in G-protein coupled receptors: A statistical study
    • Wallin E, von Heijne G. 1995. Properties of N-terminal tails in G-protein coupled receptors: a statistical study. Protein Eng. 8:693-98
    • (1995) Protein Eng. , vol.8 , pp. 693-698
    • Wallin, E.1    Von Heijne, G.2
  • 162
    • 0019822645 scopus 로고
    • Translocation of proteins across the endoplasmic reticulum. III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes
    • Walter P, Blobel G. 1981. Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes. J. Cell Biol. 91:557-61 (Pubitemid 12215644)
    • (1981) Journal of Cell Biology , vol.91 , Issue.2 , pp. 557-561
    • Walter, P.1    Blobel, G.2
  • 163
    • 77957376226 scopus 로고    scopus 로고
    • A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum
    • Wang F, Brown EC, Mak G, Zhuang J, Denic V. 2010. A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum. Mol. Cell 40:159-71
    • (2010) Mol. Cell , vol.40 , pp. 159-171
    • Wang, F.1    Brown, E.C.2    Mak, G.3    Zhuang, J.4    Denic, V.5
  • 164
    • 5444259691 scopus 로고    scopus 로고
    • Demonstration of a specific Escherichia coli SecY - Signal peptide interaction
    • DOI 10.1021/bi049485k
    • Wang L, Miller A, Rusch SL, Kendall DA. 2004. Demonstration of a specific Escherichia coli SecY-signal peptide interaction. Biochemistry 43:13185-92 (Pubitemid 39362787)
    • (2004) Biochemistry , vol.43 , Issue.41 , pp. 13185-13192
    • Wang, L.1    Miller, A.2    Rusch, S.L.3    Kendall, D.A.4
  • 165
    • 0035102443 scopus 로고    scopus 로고
    • Targeting of C-terminal (tail)-anchored proteins: Understanding how cytoplasmic activities are anchored to intracellular membranes
    • DOI 10.1034/j.1600-0854.2001.20108.x
    • Wattenberg B, Lithgow T. 2001. Targeting of C-terminal (tail)-anchored proteins: understanding how cytoplasmic activities are anchored to intracellular membranes. Traffic 2:66-71 (Pubitemid 32219858)
    • (2001) Traffic , vol.2 , Issue.1 , pp. 66-71
    • Wattenberg, B.1    Lithgow, T.2
  • 166
    • 0026450976 scopus 로고
    • Sarcolipin, the "proteolipid" of skeletal muscle sarcoplasmic reticulum, is a unique, amphipathic, 31-residue peptide
    • Wawrzynow A, Theibert JL, Murphy C, Jona I, Martonosi A, Collins JH. 1992. Sarcolipin, the "proteolipid" of skeletal muscle sarcoplasmic reticulum, is a unique, amphipathic, 31-residue peptide. Arch. Biochem. Biophys. 298:620-23
    • (1992) Arch. Biochem. Biophys. , vol.298 , pp. 620-623
    • Wawrzynow, A.1    Theibert, J.L.2    Murphy, C.3    Jona, I.4    Martonosi, A.5    Collins, J.H.6
  • 167
    • 0023782388 scopus 로고
    • Insertion of a multispanning membrane protein occurs sequentially and requires only one signal sequence
    • Wessels HP, 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.P.1    Spiess, M.2
  • 168
    • 48249095616 scopus 로고    scopus 로고
    • How translocons select transmembrane helices
    • White SH, von Heijne G. 2008. How translocons select transmembrane helices. Annu. Rev. Biophys. 37:23-42
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 23-42
    • White, S.H.1    Von Heijne, G.2
  • 170
    • 28544442609 scopus 로고    scopus 로고
    • Protein translocation across biological membranes
    • DOI 10.1126/science.1113752
    • Wickner W, Schekman R. 2005. Protein translocation across biological membranes. Science 310:1452-56 (Pubitemid 41746334)
    • (2005) Science , vol.310 , Issue.5753 , pp. 1452-1456
    • Wickner, W.1    Schekman, R.2
  • 171
    • 0022375406 scopus 로고
    • Multiple mechanisms of protein insertion into and across membranes
    • Wickner WT, Lodish HF. 1985. Multiple mechanisms of protein insertion into and across membranes. Science 230:400-7 (Pubitemid 16192554)
    • (1985) Science , vol.230 , Issue.4724 , pp. 400-407
    • Wickner, W.T.1    Lodish, H.F.2
  • 173
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • DOI 10.1038/nsb1096-842
    • Wimley WC, White SH. 1996. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3:842-48 (Pubitemid 26330634)
    • (1996) Nature Structural Biology , vol.3 , Issue.10 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 174
    • 0034681908 scopus 로고    scopus 로고
    • Designing transmembrane α-helices that insert spontaneously
    • DOI 10.1021/bi992746j
    • Wimley WC, White SH. 2000. Designing transmembrane α-helices that insert spontaneously. Biochemistry 39:4432-42 (Pubitemid 30212660)
    • (2000) Biochemistry , vol.39 , Issue.15 , pp. 4432-4442
    • Wimley, W.C.1    White, S.H.2
  • 175
    • 33745934813 scopus 로고    scopus 로고
    • Human SGT interacts with Bag-6/Bat-3/Scythe and cells with reduced levels of either protein display persistence of few misaligned chromosomes and mitotic arrest
    • Winnefeld M, Grewenig A, Schn̈olzer M, Spring H, Knoch TA, et al. Human SGT interacts with Bag-6/Bat-3/Scythe and cells with reduced levels of either protein display persistence of few misaligned chromosomes and mitotic arrest. Exp. Cell Res. 312:2500-14
    • Exp. Cell Res. , vol.312 , pp. 2500-2514
    • Winnefeld, M.1    Grewenig, A.2    Schn̈olzer, M.3    Spring, H.4    Knoch, T.A.5
  • 176
    • 1542358892 scopus 로고    scopus 로고
    • Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins
    • DOI 10.1016/S0092-8674(04)00169-2, PII S0092867404001692
    • Woolhead CA, McCormick PJ, Johnson AE. 2004. Nascent membrane and secretory proteins differ in FRETdetected folding far inside the ribosome and in their exposure to ribosomal proteins. Cell 116:725-36 (Pubitemid 38326730)
    • (2004) Cell , vol.116 , Issue.5 , pp. 725-736
    • Woolhead, C.A.1    McCormick, P.J.2    Johnson, A.E.3
  • 177
    • 0037474291 scopus 로고    scopus 로고
    • Translocation of the C terminus of a tail-anchored protein across the endoplasmic reticulum membrane in yeast mutants defective in signal peptide-driven translocation
    • DOI 10.1074/jbc.M210253200
    • Yabal M, Brambillasca S, Soffientini P, Pedrazzini E, Borgese N, Makarow M. 2003. Translocation of the C terminus of a tail-anchored protein across the endoplasmic reticulum membrane in yeast mutants defective in signal peptide-driven translocation. J. Biol. Chem. 278:3489-96 (Pubitemid 36801266)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.5 , pp. 3489-3496
    • Yabal, M.1    Brambillasca, S.2    Soffientini, P.3    Pedrazzini, E.4    Borgese, N.5    Makarow, M.6
  • 178
  • 179
    • 79955399910 scopus 로고    scopus 로고
    • A sugar chain at a specific position in the nascent polypeptide chain induces forward movement during translocation through the translocon
    • Yamagishi M, Fujita H, Morimoto F, Kida Y, Sakaguchi M. 2011. A sugar chain at a specific position in the nascent polypeptide chain induces forward movement during translocation through the translocon. J. Biochem. 149:591-600
    • (2011) J. Biochem. , vol.149 , pp. 591-600
    • Yamagishi, M.1    Fujita, H.2    Morimoto, F.3    Kida, Y.4    Sakaguchi, M.5
  • 180
    • 0033552594 scopus 로고    scopus 로고
    • Stress-associated endoplasmic reticulum protein 1 (SERP1)/ribosome- associated membrane protein 4 (RAMP4) stabilizes membrane proteins during stress and facilitates subsequent glycosylation
    • DOI 10.1083/jcb.147.6.1195
    • Yamaguchi A, Hori O, Stern DM, Hartmann E, Ogawa S, Tohyama M. 1999. Stress-associated endoplasmic reticulum protein 1 (Serp1)/ribosome-associated membrane protein 4 (Ramp4) stabilizes membrane proteins during stress and facilitates subsequent glycosylation. J. Cell Biol. 147:1195-204 (Pubitemid 30012806)
    • (1999) Journal of Cell Biology , vol.147 , Issue.6 , pp. 1195-1204
    • Yamaguchi, A.1    Hori, O.2    Stern, D.M.3    Hartmann, E.4    Ogawa, S.5    Tohyama, M.6
  • 181
    • 79551629027 scopus 로고    scopus 로고
    • Translational pausing ensures membrane targeting and cytoplasmic splicing of XBP1u mRNA
    • Yanagitani K, Kimata Y, Kadokura H, Kohno K. 2011. Translational pausing ensures membrane targeting and cytoplasmic splicing of XBP1u mRNA. Science 331:586-89
    • (2011) Science , vol.331 , pp. 586-589
    • Yanagitani, K.1    Kimata, Y.2    Kadokura, H.3    Kohno, K.4
  • 182
    • 54049111011 scopus 로고    scopus 로고
    • Structure of a complex of the ATPase SecA and the proteintranslocation channel
    • Zimmer J, Nam Y, Rapoport TA. 2008. Structure of a complex of the ATPase SecA and the proteintranslocation channel. Nature 455:936-43
    • (2008) Nature , vol.455 , pp. 936-943
    • Zimmer, J.1    Nam, Y.2    Rapoport, T.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.