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Volumn 46, Issue 13, 2007, Pages 4204-4209

pH-activated fusogenic transmembrane LV-peptides

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CELL CULTURE; HYDROPHOBICITY; PH EFFECTS; PROTEINS;

EID: 34047197811     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi602539n     Document Type: Article
Times cited : (9)

References (28)
  • 1
    • 0041428123 scopus 로고    scopus 로고
    • Membrane fusion: A structural perspective on the interplay of lipids and proteins
    • Tamm, L. K., Crane, J., and Kiessling, V. (2003) Membrane fusion: a structural perspective on the interplay of lipids and proteins, Curr. Opin. Struct. Biol. 13, 453-466.
    • (2003) Curr. Opin. Struct. Biol , vol.13 , pp. 453-466
    • Tamm, L.K.1    Crane, J.2    Kiessling, V.3
  • 2
    • 26244457213 scopus 로고    scopus 로고
    • Functions of SNAREs in intracellular membrane fusion and lipid bilayer mixing
    • Ungermann, C., and Langosch, D. (2005) Functions of SNAREs in intracellular membrane fusion and lipid bilayer mixing, J. Cell Sci. 118, 3819-3828.
    • (2005) J. Cell Sci , vol.118 , pp. 3819-3828
    • Ungermann, C.1    Langosch, D.2
  • 3
    • 33747622293 scopus 로고    scopus 로고
    • SNAREs-engines for membrane fusion
    • Jahn, R., and Scheller, R. H. (2006) SNAREs-engines for membrane fusion, Nat. Rev. Mol. Cell Biol. 7, 631-643.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 631-643
    • Jahn, R.1    Scheller, R.H.2
  • 4
    • 0034675978 scopus 로고    scopus 로고
    • Geranylgeranylated SNAREs are dominant inhibitors of membrane fusion
    • Grote, E., Baba, M., Ohsumi, Y., and Novick, P. J. (2000) Geranylgeranylated SNAREs are dominant inhibitors of membrane fusion, J. Cell Biol. 151, 453-466.
    • (2000) J. Cell Biol , vol.151 , pp. 453-466
    • Grote, E.1    Baba, M.2    Ohsumi, Y.3    Novick, P.J.4
  • 5
    • 0037449809 scopus 로고    scopus 로고
    • The transmembrane domain of Vam3 affects the composition of cis- and trans-SNARE complexes to promote homotypic vacuole fusion
    • Rohde, J., Dietrich, L., Langosch, D., and Ungermann, C. (2003) The transmembrane domain of Vam3 affects the composition of cis- and trans-SNARE complexes to promote homotypic vacuole fusion, J. Biol. Chem. 278, 1656-1662.
    • (2003) J. Biol. Chem , vol.278 , pp. 1656-1662
    • Rohde, J.1    Dietrich, L.2    Langosch, D.3    Ungermann, C.4
  • 8
    • 0033017030 scopus 로고    scopus 로고
    • Amino acid sequence requirements of the transmembrane and cytoplasmic domains of influenza virus hemagglutinin for viable membrane fusion
    • Melikyan, G. B., Lin, S., Roth, M. G., and Cohen, F. S. (1999) Amino acid sequence requirements of the transmembrane and cytoplasmic domains of influenza virus hemagglutinin for viable membrane fusion, Mol. Biol. Cell 10, 1821-1836.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1821-1836
    • Melikyan, G.B.1    Lin, S.2    Roth, M.G.3    Cohen, F.S.4
  • 9
    • 0034676041 scopus 로고    scopus 로고
    • The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transition
    • Armstrong, R. T., Kushnir, A. S., and White, J. M. (2000) The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transition, J. Cell Biol. 151, 425-437.
    • (2000) J. Cell Biol , vol.151 , pp. 425-437
    • Armstrong, R.T.1    Kushnir, A.S.2    White, J.M.3
  • 10
    • 0032584146 scopus 로고    scopus 로고
    • The transmembrane domain in viral fusion: Essential role for a conserved glycine residue in vesicular stomatitis virus G protein
    • Cleverley, D. Z., and Lenard, J. (1998) The transmembrane domain in viral fusion: essential role for a conserved glycine residue in vesicular stomatitis virus G protein, Proc. Natl. Acad. Sci. U.S.A. 95, 3425-3430.
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 3425-3430
    • Cleverley, D.Z.1    Lenard, J.2
  • 11
    • 33751342912 scopus 로고    scopus 로고
    • Self-interaction of a SNARE transmembrane domain promotes the hemifusion-to-fusion transition
    • Hofmann, M. W., Peplowska, K., Rohde, J., Poschner, B. C., Ungermann, C., and Langosch, D. (2006) Self-interaction of a SNARE transmembrane domain promotes the hemifusion-to-fusion transition, J. Mol. Biol. 364, 1048-1060.
    • (2006) J. Mol. Biol , vol.364 , pp. 1048-1060
    • Hofmann, M.W.1    Peplowska, K.2    Rohde, J.3    Poschner, B.C.4    Ungermann, C.5    Langosch, D.6
  • 12
    • 0035943407 scopus 로고    scopus 로고
    • Peptide mimics of SNARE transmembrane segments drive membrane fusion depending on their conformational plasticity
    • Langosch, D., Crane, J. M., Brosig, B., Hellwig, A., Tamm, L. K., and Reed, J. (2001) Peptide mimics of SNARE transmembrane segments drive membrane fusion depending on their conformational plasticity, J. Mol. Biol. 311, 709-721.
    • (2001) J. Mol. Biol , vol.311 , pp. 709-721
    • Langosch, D.1    Crane, J.M.2    Brosig, B.3    Hellwig, A.4    Tamm, L.K.5    Reed, J.6
  • 13
    • 0035943680 scopus 로고    scopus 로고
    • Peptide mimics of the vesicular stomatitis virus G-protein transmembrane segment drive membrane fusion in vitro
    • Langosch, D., Brosig, B., and Pipkorn, R. (2001) Peptide mimics of the vesicular stomatitis virus G-protein transmembrane segment drive membrane fusion in vitro, J. Biol. Chem. 276, 32016-32021.
    • (2001) J. Biol. Chem , vol.276 , pp. 32016-32021
    • Langosch, D.1    Brosig, B.2    Pipkorn, R.3
  • 14
    • 2242479303 scopus 로고    scopus 로고
    • VSV transmembrane domain (TMD) peptide promotes PEG-mediated fusion of liposomes in a conformationally sensitive fashion
    • Dennison, S. M., Greenfield, N., Lenard, J., and Lentz, B. R. (2002) VSV transmembrane domain (TMD) peptide promotes PEG-mediated fusion of liposomes in a conformationally sensitive fashion, Biochemistry 41, 14925-14934.
    • (2002) Biochemistry , vol.41 , pp. 14925-14934
    • Dennison, S.M.1    Greenfield, N.2    Lenard, J.3    Lentz, B.R.4
  • 16
    • 30144445192 scopus 로고    scopus 로고
    • Side-chain entropy effects on protein secondary structure formation
    • Chellgren, B. W., and Creamer, T. P. (2006) Side-chain entropy effects on protein secondary structure formation, Proteins 62, 411-420.
    • (2006) Proteins , vol.62 , pp. 411-420
    • Chellgren, B.W.1    Creamer, T.P.2
  • 17
    • 0019874707 scopus 로고
    • Use of resonance energy transfer to monitor membrane fusion
    • Struck, D. K., Hoekstra, D., and Pagano, R. E. (1981) Use of resonance energy transfer to monitor membrane fusion, Biochemistry 20, 4093-4099.
    • (1981) Biochemistry , vol.20 , pp. 4093-4099
    • Struck, D.K.1    Hoekstra, D.2    Pagano, R.E.3
  • 18
    • 0027198422 scopus 로고
    • Lipid mixing assays to determine fusion in liposome systems
    • Hoekstra, D., and Duzgunes, N. (1993) Lipid mixing assays to determine fusion in liposome systems, Methods Enzymol. 220, 15-32.
    • (1993) Methods Enzymol , vol.220 , pp. 15-32
    • Hoekstra, D.1    Duzgunes, N.2
  • 19
    • 0028170657 scopus 로고
    • pH titration of the histidine residues of cyclophilin and FK506 binding protein in the absence and presence of immunosuppressant ligands
    • Yu, L., and Fesik, S. W. (1994) pH titration of the histidine residues of cyclophilin and FK506 binding protein in the absence and presence of immunosuppressant ligands, Biochim. Biophys. Acta 1209, 24-32.
    • (1994) Biochim. Biophys. Acta , vol.1209 , pp. 24-32
    • Yu, L.1    Fesik, S.W.2
  • 20
    • 0028950310 scopus 로고
    • Peptide models of helical hydrophobic transmembrane segments of membrane proteins. 2. Differential scanning calorimetric and FTIR spectroscopic studies of the interaction of Ac-K2-(LA)12-K2-amide with phosphatidylcholine bilayers
    • Zhang, Y. P., Lewis, R. N., Hodges, R. S., and McElhaney, R. N. (1995) Peptide models of helical hydrophobic transmembrane segments of membrane proteins. 2. Differential scanning calorimetric and FTIR spectroscopic studies of the interaction of Ac-K2-(LA)12-K2-amide with phosphatidylcholine bilayers, Biochemistry 34, 2362-2371.
    • (1995) Biochemistry , vol.34 , pp. 2362-2371
    • Zhang, Y.P.1    Lewis, R.N.2    Hodges, R.S.3    McElhaney, R.N.4
  • 21
    • 0036708458 scopus 로고    scopus 로고
    • Geometry and intrinsic tilt of a tryptophan-anchored transmembrane alpha-helix determined by (2)H NMR
    • van der Wel, P. C., Strandberg, E., Killian, J. A., and Koeppe, R. E., II. (2002) Geometry and intrinsic tilt of a tryptophan-anchored transmembrane alpha-helix determined by (2)H NMR, Biophys. J. 83, 1479-1488.
    • (2002) Biophys. J , vol.83 , pp. 1479-1488
    • van der Wel, P.C.1    Strandberg, E.2    Killian, J.A.3    Koeppe II, R.E.4
  • 22
    • 0042316723 scopus 로고    scopus 로고
    • Bilayer mixing, fusion, and lysis following the interaction of populations of cationic and anionic phospholipid bilayer vesicles
    • Pantazatos, D. P., Pantazatos, S. P., and MacDonald, R. C. (2003) Bilayer mixing, fusion, and lysis following the interaction of populations of cationic and anionic phospholipid bilayer vesicles, J. Membr. Biol. 194, 129-139.
    • (2003) J. Membr. Biol , vol.194 , pp. 129-139
    • Pantazatos, D.P.1    Pantazatos, S.P.2    MacDonald, R.C.3
  • 23
    • 0034284386 scopus 로고    scopus 로고
    • How proteins adapt to a membrane-water interface
    • Killian, J. A., and von Heijne, G. (2000) How proteins adapt to a membrane-water interface, Trends Biochem. Sci. 25, 429-434.
    • (2000) Trends Biochem. Sci , vol.25 , pp. 429-434
    • Killian, J.A.1    von Heijne, G.2
  • 24
    • 0242659352 scopus 로고    scopus 로고
    • Protein-lipid interactions studied with designed transmembrane peptides: Role of hydrophobic matching and interfacial anchoring
    • de Planque, M. R., and Killian, J. A. (2003) Protein-lipid interactions studied with designed transmembrane peptides: role of hydrophobic matching and interfacial anchoring, Mol. Membr. Biol. 20, 271-284.
    • (2003) Mol. Membr. Biol , vol.20 , pp. 271-284
    • de Planque, M.R.1    Killian, J.A.2
  • 25
    • 28444450878 scopus 로고    scopus 로고
    • Lipid-protein interactions in double-layered two-dimensional AQP0 crystals
    • Gonen, T., Cheng, Y., Sliz, P., Hiroaki, Y., Fujiyoshi, Y., Harrison, S. C., and Walz, T. (2005) Lipid-protein interactions in double-layered two-dimensional AQP0 crystals, Nature 438, 633-638.
    • (2005) Nature , vol.438 , pp. 633-638
    • Gonen, T.1    Cheng, Y.2    Sliz, P.3    Hiroaki, Y.4    Fujiyoshi, Y.5    Harrison, S.C.6    Walz, T.7
  • 26
    • 0036555163 scopus 로고    scopus 로고
    • Biophysical aspects of using liposomes as delivery vehicles
    • Ulrich, A. S. (2002) Biophysical aspects of using liposomes as delivery vehicles, Biosci. Rep. 22, 129-150.
    • (2002) Biosci. Rep , vol.22 , pp. 129-150
    • Ulrich, A.S.1
  • 27
    • 0037980258 scopus 로고    scopus 로고
    • Enhancing drug function
    • Hubbell, J. A. (2003) Enhancing drug function, Science 300, 595-596.
    • (2003) Science , vol.300 , pp. 595-596
    • Hubbell, J.A.1
  • 28
    • 33947201703 scopus 로고    scopus 로고
    • An automated application for deconvolution of circular dichroism spectra of small peptides
    • in press
    • Poschner, B. C., Reed, J., Langosch, D., and Hofmann, M. W. (2007) An automated application for deconvolution of circular dichroism spectra of small peptides, Anal. Biochem., in press.
    • (2007) Anal. Biochem
    • Poschner, B.C.1    Reed, J.2    Langosch, D.3    Hofmann, M.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.