메뉴 건너뛰기




Volumn 31, Issue 4, 2006, Pages 192-196

Has the code for protein translocation been broken?

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CARRIER PROTEIN; MEMBRANE PROTEIN; TRANSLOCON;

EID: 33645984562     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2006.02.002     Document Type: Article
Times cited : (18)

References (27)
  • 1
    • 27844485836 scopus 로고    scopus 로고
    • protein translocation by the Sec61/SecY channel
    • Osborne A.R., et al. protein translocation by the Sec61/SecY channel. Annu. Rev. Cell Dev. Biol. 21 (2005) 529-550
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 529-550
    • Osborne, A.R.1
  • 2
    • 13444274461 scopus 로고    scopus 로고
    • Cell biology: border crossing
    • Bowie J.U. Cell biology: border crossing. Nature 433 (2005) 367-369
    • (2005) Nature , vol.433 , pp. 367-369
    • Bowie, J.U.1
  • 3
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: physical principles
    • White S.H., and Wimley W.C. Membrane protein folding and stability: physical principles. Annu. Rev. Biophys. Biomol. Struct. 28 (1999) 319-365
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 4
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., and Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157 (1982) 105-132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 5
    • 35448950945 scopus 로고    scopus 로고
    • Kessel, A. and Ben-Tal, N. (2002) Free energy determinants of peptide association with lipid bilayers. In Current topics in membranes (Vol. 52) (Simon, S. and McIntosh, T., eds), pp. 205-253, Academic Press
  • 6
    • 0022510143 scopus 로고
    • Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins
    • Engelman D.M., et al. Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins. Annu. Rev. Biophys. Biophys. Chem. 15 (1986) 321-353
    • (1986) Annu. Rev. Biophys. Biophys. Chem. , vol.15 , pp. 321-353
    • Engelman, D.M.1
  • 7
    • 0022539429 scopus 로고
    • Hydrophobicity and amphiphilicity in protein structure
    • Eisenberg D., et al. Hydrophobicity and amphiphilicity in protein structure. J. Cell. Biochem. 31 (1986) 11-17
    • (1986) J. Cell. Biochem. , vol.31 , pp. 11-17
    • Eisenberg, D.1
  • 8
    • 0026716643 scopus 로고
    • Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule
    • von Heijne G. Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule. J. Mol. Biol. 225 (1992) 487-494
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-494
    • von Heijne, G.1
  • 9
    • 0036893269 scopus 로고    scopus 로고
    • Transmembrane helix predictions revisited
    • Chen C.P., et al. Transmembrane helix predictions revisited. Protein Sci. 11 (2002) 2774-2791
    • (2002) Protein Sci. , vol.11 , pp. 2774-2791
    • Chen, C.P.1
  • 10
    • 13444262028 scopus 로고    scopus 로고
    • Recognition of transmembrane helices by the endoplasmic reticulum translocon
    • Hessa T., et al. Recognition of transmembrane helices by the endoplasmic reticulum translocon. Nature 433 (2005) 377-381
    • (2005) Nature , vol.433 , pp. 377-381
    • Hessa, T.1
  • 11
    • 0033167996 scopus 로고    scopus 로고
    • Are membrane proteins 'inside-out' proteins?
    • Stevens T.J., and Arkin I.T. Are membrane proteins 'inside-out' proteins?. Proteins 36 (1999) 135-143
    • (1999) Proteins , vol.36 , pp. 135-143
    • Stevens, T.J.1    Arkin, I.T.2
  • 12
    • 0036382758 scopus 로고    scopus 로고
    • A novel scoring function for predicting the conformations of tightly packed pairs of transmembrane α-helices
    • Fleishman S.J., and Ben-Tal N. A novel scoring function for predicting the conformations of tightly packed pairs of transmembrane α-helices. J. Mol. Biol. 321 (2002) 363-378
    • (2002) J. Mol. Biol. , vol.321 , pp. 363-378
    • Fleishman, S.J.1    Ben-Tal, N.2
  • 13
    • 0344687314 scopus 로고    scopus 로고
    • Side-chain contributions to membrane protein structure and stability
    • Faham S., et al. Side-chain contributions to membrane protein structure and stability. J. Mol. Biol. 335 (2004) 297-305
    • (2004) J. Mol. Biol. , vol.335 , pp. 297-305
    • Faham, S.1
  • 14
    • 0042931286 scopus 로고    scopus 로고
    • Sequence motifs, polar interactions and conformational changes in helical membrane proteins
    • Curran A.R., and Engelman D.M. Sequence motifs, polar interactions and conformational changes in helical membrane proteins. Curr. Opin. Struct. Biol. 13 (2003) 412-417
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 412-417
    • Curran, A.R.1    Engelman, D.M.2
  • 15
    • 0024976405 scopus 로고
    • Neu receptor dimerization
    • Sternberg M.J., and Gullick W.J. Neu receptor dimerization. Nature 339 (1989) 587
    • (1989) Nature , vol.339 , pp. 587
    • Sternberg, M.J.1    Gullick, W.J.2
  • 16
    • 20044389842 scopus 로고    scopus 로고
    • Membrane insertion of a potassium-channel voltage sensor
    • Hessa T., et al. Membrane insertion of a potassium-channel voltage sensor. Science 307 (2005) 1427
    • (2005) Science , vol.307 , pp. 1427
    • Hessa, T.1
  • 17
    • 0019410055 scopus 로고
    • Leader peptidase is found in both the inner and outer membranes of Escherichia coli
    • Zwizinski C., et al. Leader peptidase is found in both the inner and outer membranes of Escherichia coli. J. Biol. Chem. 256 (1981) 3593-3597
    • (1981) J. Biol. Chem. , vol.256 , pp. 3593-3597
    • Zwizinski, C.1
  • 18
    • 0037435021 scopus 로고    scopus 로고
    • + channel
    • + channel. Nature 422 (2003) 180-185
    • (2003) Nature , vol.422 , pp. 180-185
    • Ruta, V.1
  • 19
    • 0026594721 scopus 로고
    • The size of gating charge in wild-type and mutant Shaker potassium channels
    • Schoppa N.E., et al. The size of gating charge in wild-type and mutant Shaker potassium channels. Science 255 (1992) 1712-1715
    • (1992) Science , vol.255 , pp. 1712-1715
    • Schoppa, N.E.1
  • 20
    • 0038442831 scopus 로고    scopus 로고
    • A charged view of voltage-gated ion channels
    • Miller C. A charged view of voltage-gated ion channels. Nat. Struct. Biol. 10 (2003) 422-424
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 422-424
    • Miller, C.1
  • 21
    • 0038076054 scopus 로고    scopus 로고
    • + channel
    • + channel. Nature 423 (2003) 33-41
    • (2003) Nature , vol.423 , pp. 33-41
    • Jiang, Y.1
  • 22
    • 27244444569 scopus 로고    scopus 로고
    • Interface connections of a transmembrane voltage sensor
    • Freites J.A., et al. Interface connections of a transmembrane voltage sensor. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 15059-15064
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 15059-15064
    • Freites, J.A.1
  • 23
    • 0027362726 scopus 로고
    • A molecular model for lipid-protein interaction in membranes: the role of hydrophobic mismatch
    • Fattal D.R., and Ben-Shaul A. A molecular model for lipid-protein interaction in membranes: the role of hydrophobic mismatch. Biophys. J. 65 (1993) 1795-1809
    • (1993) Biophys. J. , vol.65 , pp. 1795-1809
    • Fattal, D.R.1    Ben-Shaul, A.2
  • 24
    • 0033635131 scopus 로고    scopus 로고
    • Understanding peptide interactions with the lipid bilayer: a guide to membrane protein engineering
    • Bechinger B. Understanding peptide interactions with the lipid bilayer: a guide to membrane protein engineering. Curr. Opin. Chem. Biol. 4 (2000) 639-644
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 639-644
    • Bechinger, B.1
  • 25
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • Long S.B., et al. Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science 309 (2005) 897-903
    • (2005) Science , vol.309 , pp. 897-903
    • Long, S.B.1
  • 26
    • 13844297577 scopus 로고    scopus 로고
    • Imaging protein molecules using FRET and FLIM microscopy
    • Wallrabe H., and Periasamy A. Imaging protein molecules using FRET and FLIM microscopy. Curr. Opin. Biotechnol. 16 (2005) 19-27
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 19-27
    • Wallrabe, H.1    Periasamy, A.2
  • 27
    • 23044510444 scopus 로고    scopus 로고
    • Transmembrane helices before, during, and after insertion
    • White S.H., and von Heijne G. Transmembrane helices before, during, and after insertion. Curr. Opin. Struct. Biol. 15 (2005) 378-386
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 378-386
    • White, S.H.1    von Heijne, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.