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Volumn 46, Issue 39, 2007, Pages 11147-11157

Structural determinants of lateral gate opening in the protein translocon

Author keywords

[No Author keywords available]

Indexed keywords

CHANNEL GATING; MOLECULAR DYNAMICS SIMULATIONS; NASCENT MEMBRANE PROTEINS; PROTEIN CONDUCTING CHANNELS; PROTEIN TRANSLOCONS;

EID: 34848895197     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700835d     Document Type: Article
Times cited : (57)

References (72)
  • 4
    • 28544442609 scopus 로고    scopus 로고
    • Protein translocation across biological membranes
    • Wickner, W., and Schekman, R. (2005) Protein translocation across biological membranes, Science 310, 1452-1456.
    • (2005) Science , vol.310 , pp. 1452-1456
    • Wickner, W.1    Schekman, R.2
  • 6
    • 33745218504 scopus 로고    scopus 로고
    • Protein secretion in the Archaea: Multiple paths towards a unique cell surface
    • Albers, S.-V., Szabó, Z., and Driessen, A. J. M. (2006) Protein secretion in the Archaea: Multiple paths towards a unique cell surface, Nat. Rev. Microbiol. 4, 537-547.
    • (2006) Nat. Rev. Microbiol , vol.4 , pp. 537-547
    • Albers, S.-V.1    Szabó, Z.2    Driessen, A.J.M.3
  • 7
    • 0032488845 scopus 로고    scopus 로고
    • Protein translocation: Tunnel vision
    • Matlack, K. E. S., Mothes, W., and Rapoport, T. A. (1998) Protein translocation: Tunnel vision, Cell 92, 381-390.
    • (1998) Cell , vol.92 , pp. 381-390
    • Matlack, K.E.S.1    Mothes, W.2    Rapoport, T.A.3
  • 9
    • 18544380083 scopus 로고    scopus 로고
    • Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY
    • Cannon, K. S., Or, E., Clemons, W. M., Jr., Shibata, Y., and Rapoport, T. A. (2005) Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY, J. Cell Biol. 169, 219-225.
    • (2005) J. Cell Biol , vol.169 , pp. 219-225
    • Cannon, K.S.1    Or, E.2    Clemons Jr., W.M.3    Shibata, Y.4    Rapoport, T.A.5
  • 10
    • 33646271115 scopus 로고    scopus 로고
    • Molecular dynamics studies of the archaeal translocon
    • Gumbart, J., and Schulten, K. (2006) Molecular dynamics studies of the archaeal translocon, Biophys. J. 90, 2356-2367.
    • (2006) Biophys. J , vol.90 , pp. 2356-2367
    • Gumbart, J.1    Schulten, K.2
  • 11
    • 33748300566 scopus 로고    scopus 로고
    • ll.Junne, T., Schwede, T., Goder, V., and 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, 4063-4068.
    • ll.Junne, T., Schwede, T., Goder, V., and 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, 4063-4068.
  • 13
    • 23044510444 scopus 로고    scopus 로고
    • Transmembrane helices before, during, and after insertion
    • White, S. H., and von Heijne, G. (2005) Transmembrane helices before, during, and after insertion, Curr. Opin. Struct. Biol. 15, 378-386.
    • (2005) Curr. Opin. Struct. Biol , vol.15 , pp. 378-386
    • White, S.H.1    von Heijne, G.2
  • 15
  • 16
    • 27144549973 scopus 로고    scopus 로고
    • Sequential triage of transmembrane segments by Sec61α during biogenesis of a native multispanning membrane protein
    • Sadlish, H., Pitonzo, D., Johnson, A. E., and Skach, W. R. (2005) Sequential triage of transmembrane segments by Sec61α during biogenesis of a native multispanning membrane protein, Nat. Struct. Mol. Biol. 10, 870-878.
    • (2005) Nat. Struct. Mol. Biol , vol.10 , pp. 870-878
    • Sadlish, H.1    Pitonzo, D.2    Johnson, A.E.3    Skach, W.R.4
  • 17
    • 33746923016 scopus 로고    scopus 로고
    • Active and passive displacement of transmembrane domains both occur during opsin biogenesis at the Sec61 translocon
    • Ismail, N., Crawshaw, S. G., and High, S. (2006) Active and passive displacement of transmembrane domains both occur during opsin biogenesis at the Sec61 translocon, J. Cell Sci. 119, 2826-2836.
    • (2006) J. Cell Sci , vol.119 , pp. 2826-2836
    • Ismail, N.1    Crawshaw, S.G.2    High, S.3
  • 21
    • 0037043724 scopus 로고    scopus 로고
    • Three-dimensional structure of the bacterial protein-translocation complex SecYEG
    • Breyton, C., Haase, W., Rapoport, T. A., Kühlbrandt, W., and Collinson, I. (2002) Three-dimensional structure of the bacterial protein-translocation complex SecYEG, Nature 418, 662-665.
    • (2002) Nature , vol.418 , pp. 662-665
    • Breyton, C.1    Haase, W.2    Rapoport, T.A.3    Kühlbrandt, W.4    Collinson, I.5
  • 22
    • 0036500974 scopus 로고    scopus 로고
    • The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure
    • Bessonneau, P., Besson, V., Collinson, I., and Duong, F. (2002) The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure, EMBO J. 21, 995-1003.
    • (2002) EMBO J , vol.21 , pp. 995-1003
    • Bessonneau, P.1    Besson, V.2    Collinson, I.3    Duong, F.4
  • 23
    • 27844444793 scopus 로고    scopus 로고
    • Structure of the E. coli protein-conducting channel bound to a translating ribosome
    • Mitra, K., Schaffitzel, C., Shaikh, T., Tama, F., Jenni, S., Brooks, C. L., Ban, N., and Frank, J. (2005) Structure of the E. coli protein-conducting channel bound to a translating ribosome, Nature 438, 318-324.
    • (2005) Nature , vol.438 , pp. 318-324
    • Mitra, K.1    Schaffitzel, C.2    Shaikh, T.3    Tama, F.4    Jenni, S.5    Brooks, C.L.6    Ban, N.7    Frank, J.8
  • 26
    • 0033551435 scopus 로고    scopus 로고
    • Cysteine-directed cross-linking demonstrates that helix 3 of SecE is close to helix 2 of SecY and helix 3 of a neighboring SecE
    • Kaufmann, A., Manting, E. H., Veenendaal, A. K. J., Driessen, A. J. M., and van der Does, C. (1999) Cysteine-directed cross-linking demonstrates that helix 3 of SecE is close to helix 2 of SecY and helix 3 of a neighboring SecE, Biochemistry 38, 9115-9125.
    • (1999) Biochemistry , vol.38 , pp. 9115-9125
    • Kaufmann, A.1    Manting, E.H.2    Veenendaal, A.K.J.3    Driessen, A.J.M.4    van der Does, C.5
  • 27
    • 0035980042 scopus 로고    scopus 로고
    • Mapping the sites of interaction between SecY and SecE by cysteine scanning mutagenesis
    • Veenendaal, A. K., van der Does, C., and Driessen, A. J. (2001) Mapping the sites of interaction between SecY and SecE by cysteine scanning mutagenesis, J. Biol. Chem. 276, 32559-32566.
    • (2001) J. Biol. Chem , vol.276 , pp. 32559-32566
    • Veenendaal, A.K.1    van der Does, C.2    Driessen, A.J.3
  • 28
    • 24944458963 scopus 로고    scopus 로고
    • Atomic model of the E. coli membrane-bound protein translocation complex SecYEG
    • Bostina, M., Mohsin, B., Kühlbrandt, W., and Collinson, I. (2005) Atomic model of the E. coli membrane-bound protein translocation complex SecYEG, J. Mol. Biol. 352, 1035-1043.
    • (2005) J. Mol. Biol , vol.352 , pp. 1035-1043
    • Bostina, M.1    Mohsin, B.2    Kühlbrandt, W.3    Collinson, I.4
  • 29
    • 33646931831 scopus 로고    scopus 로고
    • A model for co-translational translocation: Ribosome-regulated nascent polypeptide translocation at the protein-conducting channel
    • Mitra, K., and Frank, J. (2006) A model for co-translational translocation: Ribosome-regulated nascent polypeptide translocation at the protein-conducting channel, FEBS Lett. 580, 3353-3360.
    • (2006) FEBS Lett , vol.580 , pp. 3353-3360
    • Mitra, K.1    Frank, J.2
  • 30
    • 33750580851 scopus 로고    scopus 로고
    • Co- and post-translational translocation through the protein-conducting channel: Analogous mechanisms at work?
    • Mitra, K., Frank, J., and Driessen, A. (2006) Co- and post-translational translocation through the protein-conducting channel: Analogous mechanisms at work? Nat. Struct. Mol. Biol. 13, 957-964.
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 957-964
    • Mitra, K.1    Frank, J.2    Driessen, A.3
  • 33
    • 0041784950 scopus 로고    scopus 로고
    • MacKerell, A. D., Jr., Bashford, D., Bellott, M., Dunbrack, R. L., Jr., Evanseck, J., Field, M. J., Fischer, S., Gao, J., Guo, H., Ha, S., Joseph, D., Kuchnir, L., Kuczera, K., Lau, F. T. K., Mattos, C., Michnick, S., Ngo, T., Nguyen, D. T., Prodhom, B., Reiher, I. W. E., Roux, B., Schlenkrich, M., Smith, J., Stote, R., Straub, J., Watanabe, M., Wiorkiewicz-Kuczera, J., Yin, D., and Karplus, M. (1998) All-atom empirical potential for molecular modeling and dynamics studies of proteins, J. Phys. Chem. B 102, 3586-3616.
    • MacKerell, A. D., Jr., Bashford, D., Bellott, M., Dunbrack, R. L., Jr., Evanseck, J., Field, M. J., Fischer, S., Gao, J., Guo, H., Ha, S., Joseph, D., Kuchnir, L., Kuczera, K., Lau, F. T. K., Mattos, C., Michnick, S., Ngo, T., Nguyen, D. T., Prodhom, B., Reiher, I. W. E., Roux, B., Schlenkrich, M., Smith, J., Stote, R., Straub, J., Watanabe, M., Wiorkiewicz-Kuczera, J., Yin, D., and Karplus, M. (1998) All-atom empirical potential for molecular modeling and dynamics studies of proteins, J. Phys. Chem. B 102, 3586-3616.
  • 34
    • 1642485164 scopus 로고    scopus 로고
    • Coarse grained model for semiquantitative lipid simulations
    • Marrink, S. J., de Vries, A. H., and Mark, A. E. (2004) Coarse grained model for semiquantitative lipid simulations, J. Phys. Chem. B 108, 750-760.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 750-760
    • Marrink, S.J.1    de Vries, A.H.2    Mark, A.E.3
  • 35
    • 33644893631 scopus 로고    scopus 로고
    • Coarse grained protein-lipid model with application to lipoprotein particles
    • Shih, A. Y., Arkhipov, A., Freddolino, P. L., and Schulten, K. (2006) Coarse grained protein-lipid model with application to lipoprotein particles, J. Phys. Chem. B 110, 3674-3684.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 3674-3684
    • Shih, A.Y.1    Arkhipov, A.2    Freddolino, P.L.3    Schulten, K.4
  • 36
    • 33847193915 scopus 로고    scopus 로고
    • Assembly of lipoprotein particles revealed by coarse-grained molecular dynamics simulations
    • Shih, A. Y., Freddolino, P. L., Arkhipov, A., and Schulten, K. (2007) Assembly of lipoprotein particles revealed by coarse-grained molecular dynamics simulations, J. Struct. Biol. 157, 579-592.
    • (2007) J. Struct. Biol , vol.157 , pp. 579-592
    • Shih, A.Y.1    Freddolino, P.L.2    Arkhipov, A.3    Schulten, K.4
  • 37
    • 0030987036 scopus 로고    scopus 로고
    • Molecular dynamics study of unbinding of the avidin-biotin complex
    • Izrailev, S., Stepaniants, S., Baisera, M., Oono, Y., and Schulten, K. (1997) Molecular dynamics study of unbinding of the avidin-biotin complex, Biophys. J. 72, 1568-1581.
    • (1997) Biophys. J , vol.72 , pp. 1568-1581
    • Izrailev, S.1    Stepaniants, S.2    Baisera, M.3    Oono, Y.4    Schulten, K.5
  • 38
    • 0035312645 scopus 로고    scopus 로고
    • Steered molecular dynamics and mechanical functions of proteins
    • Isralewitz, B., Gao, M., and Schulten, K. (2001) Steered molecular dynamics and mechanical functions of proteins, Curr. Opin. Struct. Biol. 11, 224-230.
    • (2001) Curr. Opin. Struct. Biol , vol.11 , pp. 224-230
    • Isralewitz, B.1    Gao, M.2    Schulten, K.3
  • 39
    • 33750337536 scopus 로고    scopus 로고
    • How the headpiece hinge angle is opened: New insights into the dynamics of integrin activation
    • Puklin-Faucher, E., Gao, M., Schulten, K., and Vogel, V. (2006) How the headpiece hinge angle is opened: New insights into the dynamics of integrin activation, J. Cell Biol. 175, 349-360.
    • (2006) J. Cell Biol , vol.175 , pp. 349-360
    • Puklin-Faucher, E.1    Gao, M.2    Schulten, K.3    Vogel, V.4
  • 40
    • 33749442647 scopus 로고    scopus 로고
    • MultiSeq: Unifying sequence and structure data for evolutionary analysis
    • Roberts, E., Eargle, J., Wright, D., and Luthey-Schulten, Z. (2006) MultiSeq: Unifying sequence and structure data for evolutionary analysis, BMC Bioinformatics 7, 382.
    • (2006) BMC Bioinformatics , vol.7 , pp. 382
    • Roberts, E.1    Eargle, J.2    Wright, D.3    Luthey-Schulten, Z.4
  • 45
    • 0344736695 scopus 로고    scopus 로고
    • Structure and functional significance of mechanically unfolded fibronectin type III1 intermediates
    • Gao, M., Craig, D., Lequin, O., Campbell, I. D., Vogel, V., and Schulten, K. (2003) Structure and functional significance of mechanically unfolded fibronectin type III1 intermediates, Proc. Natl. Acad. Sci. U.S.A. 100, 14784-14789.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 14784-14789
    • Gao, M.1    Craig, D.2    Lequin, O.3    Campbell, I.D.4    Vogel, V.5    Schulten, K.6
  • 46
    • 17044401714 scopus 로고    scopus 로고
    • In search of the hair-cell gating spring: Elastic properties of ankyrin and Cadherin repeats
    • Sotomayor, M., Corey, D. P., and Schulten, K. (2005) In search of the hair-cell gating spring: Elastic properties of ankyrin and Cadherin repeats, Structure 13, 669-682.
    • (2005) Structure , vol.13 , pp. 669-682
    • Sotomayor, M.1    Corey, D.P.2    Schulten, K.3
  • 48
    • 33645770767 scopus 로고    scopus 로고
    • Stepwise unfolding of ankyrin repeats in a single protein revealed by atomic force microscopy
    • Li, L., Wetzel, S., Pluckthun, A., and Fernandez, J. M. (2006) Stepwise unfolding of ankyrin repeats in a single protein revealed by atomic force microscopy, Biophys. J. 90, L30-L32.
    • (2006) Biophys. J , vol.90
    • Li, L.1    Wetzel, S.2    Pluckthun, A.3    Fernandez, J.M.4
  • 49
    • 34249930159 scopus 로고    scopus 로고
    • Single-molecule experiments in vitro and in silico
    • Sotomayor, M., and Schulten, K. (2007) Single-molecule experiments in vitro and in silico, Science 316, 1144-1148.
    • (2007) Science , vol.316 , pp. 1144-1148
    • Sotomayor, M.1    Schulten, K.2
  • 50
    • 33646191829 scopus 로고    scopus 로고
    • Size, motion, and function of the SecY translocon revealed by molecular dynamics simulations with virtual probes
    • Tian, P., and Andricioaei, I. (2006) Size, motion, and function of the SecY translocon revealed by molecular dynamics simulations with virtual probes, Biophys. J. 90, 2718-2730.
    • (2006) Biophys. J , vol.90 , pp. 2718-2730
    • Tian, P.1    Andricioaei, I.2
  • 51
    • 33751074442 scopus 로고    scopus 로고
    • Simulations of a protein translocation pore: SecY
    • Haider, S., Hall, B. A., and Sansom, M. S. P. (2006) Simulations of a protein translocation pore: SecY, Biochemistry 45, 13018-13024.
    • (2006) Biochemistry , vol.45 , pp. 13018-13024
    • Haider, S.1    Hall, B.A.2    Sansom, M.S.P.3
  • 52
    • 0030883755 scopus 로고    scopus 로고
    • Protein domain movements: Detection of rigid domains and visualization of hinges in comparisons of atomic coordinates
    • Wriggers, W., and Schulten, K. (1997) Protein domain movements: Detection of rigid domains and visualization of hinges in comparisons of atomic coordinates, Proteins: Struct., Funct., Genet. 29, 1-14.
    • (1997) Proteins: Struct., Funct., Genet , vol.29 , pp. 1-14
    • Wriggers, W.1    Schulten, K.2
  • 53
    • 0030888546 scopus 로고    scopus 로고
    • Model-free methods of analyzing domain motions in proteins from simulation: A comparison of normal mode analysis and molecular dynamics simulation of lysozyme
    • Hayward, S., Kitao, A., and Berendsen, H. J. C. (1997) Model-free methods of analyzing domain motions in proteins from simulation: A comparison of normal mode analysis and molecular dynamics simulation of lysozyme, Proteins: Struct, Funct., Genet. 27, 425-437.
    • (1997) Proteins: Struct, Funct., Genet , vol.27 , pp. 425-437
    • Hayward, S.1    Kitao, A.2    Berendsen, H.J.C.3
  • 54
  • 55
    • 33644644163 scopus 로고    scopus 로고
    • Insertion and assembly of membrane proteins via simulation
    • Bond, P. J., and Sansom, M. S. P. (2006) Insertion and assembly of membrane proteins via simulation, J. Am. Chem. Soc. 128, 2697-2704.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 2697-2704
    • Bond, P.J.1    Sansom, M.S.P.2
  • 56
    • 33847242278 scopus 로고    scopus 로고
    • Coarse-grained molecular dynamics simulations of membrane proteins and peptides
    • Bond, P. J., Holyoake, J., Ivetac, A., Khalid, S., and Sansom, M. (2007) Coarse-grained molecular dynamics simulations of membrane proteins and peptides, J. Struct. Biol. 157, 593-605.
    • (2007) J. Struct. Biol , vol.157 , pp. 593-605
    • Bond, P.J.1    Holyoake, J.2    Ivetac, A.3    Khalid, S.4    Sansom, M.5
  • 57
    • 33847258823 scopus 로고    scopus 로고
    • Bilayer deformation by the Kv channel voltage sensor domain revealed by self-assembly simulations
    • Bond, P. J., and Sansom, M. (2007) Bilayer deformation by the Kv channel voltage sensor domain revealed by self-assembly simulations, Proc. Natl. Acad. Sci. U.S.A. 104, 2631-2636.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 2631-2636
    • Bond, P.J.1    Sansom, M.2
  • 58
    • 0025732834 scopus 로고
    • One of three transmembrane stretches is sufficient for the functioning of the SecE protein, a membrane component of the E. coli secretion machinery
    • Schatz, P. J., Bieker, K. L., Ottemann, K. M., Silhavy, T. J., and Beckwith, J. (1991) One of three transmembrane stretches is sufficient for the functioning of the SecE protein, a membrane component of the E. coli secretion machinery, EMBO J. 10, 1749-1757.
    • (1991) EMBO J , vol.10 , pp. 1749-1757
    • Schatz, P.J.1    Bieker, K.L.2    Ottemann, K.M.3    Silhavy, T.J.4    Beckwith, J.5
  • 59
    • 0026688434 scopus 로고
    • The carboxyl-terminal region of SecE interacts with SecY and is functional in the reconstitution of protein translocation activity in Escherichia coli
    • Nishiyama, K., Mizushima, S., and Tokuda, H. (1992) The carboxyl-terminal region of SecE interacts with SecY and is functional in the reconstitution of protein translocation activity in Escherichia coli, J. Biol. Chem. 267, 7170-7176.
    • (1992) J. Biol. Chem , vol.267 , pp. 7170-7176
    • Nishiyama, K.1    Mizushima, S.2    Tokuda, H.3
  • 60
    • 0028334912 scopus 로고
    • Residues essential for the function of SecE, a membrane component of the Escherichia coli secretion apparatus, are located in a conserved cytoplasmic region
    • Murphy, C. K., and Beckwith, J. (1994) Residues essential for the function of SecE, a membrane component of the Escherichia coli secretion apparatus, are located in a conserved cytoplasmic region, Proc. Natl. Acad. Sci. U.S.A. 91, 2557-2561.
    • (1994) Proc. Natl. Acad. Sci. U.S.A , vol.91 , pp. 2557-2561
    • Murphy, C.K.1    Beckwith, J.2
  • 61
    • 0037361759 scopus 로고    scopus 로고
    • Interfering mutations provide in vivo evidence that Escherichia coli SecE functions in multimeric states
    • Matsuo, E., Mori, H., and Ito, K. (2003) Interfering mutations provide in vivo evidence that Escherichia coli SecE functions in multimeric states, Mol. Gen. Genomics 268, 808-815.
    • (2003) Mol. Gen. Genomics , vol.268 , pp. 808-815
    • Matsuo, E.1    Mori, H.2    Ito, K.3
  • 62
    • 0029989855 scopus 로고    scopus 로고
    • FtsH (Hf1B) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins
    • Akiyama, Y., Kihara, A., Tokuda, H., and Ito, K. (1996) FtsH (Hf1B) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins, J. Biol. Chem. 271, 31196-31201.
    • (1996) J. Biol. Chem , vol.271 , pp. 31196-31201
    • Akiyama, Y.1    Kihara, A.2    Tokuda, H.3    Ito, K.4
  • 63
    • 0034293329 scopus 로고    scopus 로고
    • Role of the non-essential region encompassing the N-terminal two transmembrane stretches of Escherichia coli SecE
    • Nishiyama, K., Suzuki, H., and Tokuda, H. (2000) Role of the non-essential region encompassing the N-terminal two transmembrane stretches of Escherichia coli SecE, Biosci., Biotechnol., Biochem. 64, 2121-2127.
    • (2000) Biosci., Biotechnol., Biochem , vol.64 , pp. 2121-2127
    • Nishiyama, K.1    Suzuki, H.2    Tokuda, H.3
  • 64
    • 0029810616 scopus 로고    scopus 로고
    • In vivo analyses of interactions between SecE and SecY, core components of the Escherichia coli protein translocation machinery
    • Pohlschröder, M., Murphy, C., and Beckwith, J. (1996) In vivo analyses of interactions between SecE and SecY, core components of the Escherichia coli protein translocation machinery, J. Biol. Chem. 271, 19908-19914.
    • (1996) J. Biol. Chem , vol.271 , pp. 19908-19914
    • Pohlschröder, M.1    Murphy, C.2    Beckwith, J.3
  • 65
    • 0032719682 scopus 로고    scopus 로고
    • Preprotein translocation by a hybrid translocase composed of Escherichia coli and Bacillus subtilis subunits
    • Swaving, J., van Wely, K. H. M., and Driessen, A. J. M. (1999) Preprotein translocation by a hybrid translocase composed of Escherichia coli and Bacillus subtilis subunits, J. Bacteriol. 181, 7021-7027.
    • (1999) J. Bacteriol , vol.181 , pp. 7021-7027
    • Swaving, J.1    van Wely, K.H.M.2    Driessen, A.J.M.3
  • 66
    • 27144525002 scopus 로고    scopus 로고
    • Investigating the SecY plug movement at the SecYEG translocation channel
    • Tarn, P. C. K., Maillard, A. P., Chan, K. K. Y., and Duong, F. (2005) Investigating the SecY plug movement at the SecYEG translocation channel, EMBO J. 24, 3380-3388.
    • (2005) EMBO J , vol.24 , pp. 3380-3388
    • Tarn, P.C.K.1    Maillard, A.P.2    Chan, K.K.Y.3    Duong, F.4
  • 67
    • 0032544614 scopus 로고    scopus 로고
    • Signal sequence recognition in posttranslational protein transport across the yeast ER membrane
    • Plath, K., Mothes, W., Wilkinson, B. M., Stirling, C. J., and Rapoport, T. A. (1998) Signal sequence recognition in posttranslational protein transport across the yeast ER membrane, Cell 94, 795-807.
    • (1998) Cell , vol.94 , pp. 795-807
    • Plath, K.1    Mothes, W.2    Wilkinson, B.M.3    Stirling, C.J.4    Rapoport, T.A.5
  • 68
    • 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
  • 69
    • 0034697967 scopus 로고    scopus 로고
    • The Sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain
    • Heinrich, S. U., Mothes, W., Brunner, J., and Rapoport, T. A. (2000) The Sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain, Cell 102, 233-244.
    • (2000) Cell , vol.102 , pp. 233-244
    • Heinrich, S.U.1    Mothes, W.2    Brunner, J.3    Rapoport, T.A.4
  • 70
    • 13544259578 scopus 로고    scopus 로고
    • Probing the environment of signal-anchor sequences during topogenesis in the endoplasmic reticulum
    • Higy, M., Gander, S., and Spiess, M. (2005) Probing the environment of signal-anchor sequences during topogenesis in the endoplasmic reticulum, Biochemistry 44, 2039-2047.
    • (2005) Biochemistry , vol.44 , pp. 2039-2047
    • Higy, M.1    Gander, S.2    Spiess, M.3
  • 71
    • 34247580102 scopus 로고    scopus 로고
    • Membrane protein integration: The biology-physics nexus
    • White, S. H. (2007) Membrane protein integration: The biology-physics nexus, J. Gen. Physiol. 129, 363-369.
    • (2007) J. Gen. Physiol , vol.129 , pp. 363-369
    • White, S.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.