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Volumn 12, Issue 9, 2011, Pages 5577-5591

New user-friendly approach to obtain an Eisenberg plot and its use as a practical tool in protein sequence analysis

Author keywords

Amphitropic proteins; Eisenberg plot; Heliquest; Hydrophobic moment plot; Lipid binding regions; Protein lipid interactions; Transmembrane proteins

Indexed keywords

MEMBRANE PROTEIN; LIPID; PEPTIDE; PROTEIN; PROTEIN BINDING;

EID: 80053211934     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms12095577     Document Type: Article
Times cited : (23)

References (80)
  • 1
    • 0019934717 scopus 로고
    • The helical hydrophobic moment: A measure of the amphiphilicity of a helix
    • Eisenberg, D.; Weiss, R.M.; Terwilliger, T.C. The helical hydrophobic moment: A measure of the amphiphilicity of a helix. Nature 1982, 299, 371-374.
    • (1982) Nature , vol.299 , pp. 371-374
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger, T.C.3
  • 2
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • Eisenberg, D.; Schwarz, E.; Komaromy, M.; Wall, R. Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 1984, 15, 125-142.
    • (1984) J. Mol. Biol , vol.15 , pp. 125-142
    • Eisenberg, D.1    Schwarz, E.2    Komaromy, M.3    Wall, R.4
  • 3
    • 0000929505 scopus 로고
    • The hydrophobic moment detects periodicity in protein hydrophobicity
    • Eisenberg, D.; Weiss, R.M.; Terwilliger, T.C. The hydrophobic moment detects periodicity in protein hydrophobicity. Proc. Natl. Acad. Sci. USA 1984, 81, 140-144.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 140-144
    • Eisenberg, D.1    Weiss, R.M.2    Terwilliger, T.C.3
  • 4
    • 0021152462 scopus 로고
    • Three-dimensional structure of membrane and surface proteins
    • Eisenberg, D. Three-dimensional structure of membrane and surface proteins. Annu. Rev. Biochem. 1984, 53, 595-623.
    • (1984) Annu. Rev. Biochem , vol.53 , pp. 595-623
    • Eisenberg, D.1
  • 5
    • 0036123661 scopus 로고    scopus 로고
    • The hydrophobic moment and its use in the classification of amphiphilic structures (review)
    • Phoenix, D.A.; Harris, F. The hydrophobic moment and its use in the classification of amphiphilic structures (review). Mol. Membr. Biol. 2002, 19, 1-10.
    • (2002) Mol. Membr. Biol , vol.19 , pp. 1-10
    • Phoenix, D.A.1    Harris, F.2
  • 6
    • 51749085388 scopus 로고    scopus 로고
    • Heliquest: A web-server to screen sequences with specific α-helical properties
    • Gautier, R.; Douguet, D.; Anthonny, B.; Drin, G. Heliquest: A web-server to screen sequences with specific α-helical properties. Bioinformatics 2008, 24, 2101-2102.
    • (2008) Bioinformatics , vol.24 , pp. 2101-2102
    • Gautier, R.1    Douguet, D.2    Anthonny, B.3    Drin, G.4
  • 7
    • 33746489960 scopus 로고    scopus 로고
    • Protein-lipid interactions: Correlation of a predictive algorithm for lipid-binding sites with three-dimensional structural data
    • doi:10.1186/1742-4682-3-17
    • Scott, D.L.; Diez, G.; Goldmann, W.H. Protein-lipid interactions: Correlation of a predictive algorithm for lipid-binding sites with three-dimensional structural data. Theor. Biol. Med. Model. 2006, 3, doi:10.1186/1742-4682-3-17.
    • (2006) Theor. Biol. Med. Model , pp. 3
    • Scott, D.L.1    Diez, G.2    Goldmann, W.H.3
  • 8
    • 77949319432 scopus 로고    scopus 로고
    • An experimentally based computer search identifies unstructured membrane-binding sites in proteins: Application to class I myosins, PAKS, and CARMIL
    • Brzeska, H.; Guag, J.; Remmert, K.; Chacko, S.; Korn, E.D. An experimentally based computer search identifies unstructured membrane-binding sites in proteins: Application to class I myosins, PAKS, and CARMIL. J. Biol. Chem. 2010, 285, 5738-5747.
    • (2010) J. Biol. Chem , vol.285 , pp. 5738-5747
    • Brzeska, H.1    Guag, J.2    Remmert, K.3    Chacko, S.4    Korn, E.D.5
  • 9
    • 0027477959 scopus 로고
    • Interaction of phospholipids with proteins and peptides. New advances III
    • Cserhati, T. Interaction of phospholipids with proteins and peptides. New advances III. Int. J. Biochem. 1993, 25, 123-131.
    • (1993) Int. J. Biochem , vol.25 , pp. 123-131
    • Cserhati, T.1
  • 10
    • 0030957823 scopus 로고    scopus 로고
    • Molecular basis for membrane phospholipid diversity: Why are there so many lipids
    • Dowhan, W. Molecular basis for membrane phospholipid diversity: Why are there so many lipids? Annu. Rev. Biochem. 1997, 66, 199-232.
    • (1997) Annu. Rev. Biochem , vol.66 , pp. 199-232
    • Dowhan, W.1
  • 11
    • 52449112028 scopus 로고    scopus 로고
    • Cellular membranes and lipid-binding domains as attractive targets for drug development
    • Sudhahar, C.G.; Haney, R.M.; Xue, Y.; Stahelin, R.V. Cellular membranes and lipid-binding domains as attractive targets for drug development. Curr. Drug Targets 2008, 9, 603-613.
    • (2008) Curr. Drug Targets , vol.9 , pp. 603-613
    • Sudhahar, C.G.1    Haney, R.M.2    Xue, Y.3    Stahelin, R.V.4
  • 12
    • 79955529143 scopus 로고    scopus 로고
    • The prediction of novel multiple lipid-binding regions in protein translocation motor proteins: A possible general feature
    • Keller, R.C.A. The prediction of novel multiple lipid-binding regions in protein translocation motor proteins: A possible general feature. Cell. Mol. Biol. Lett. 2011, 16, 40-54.
    • (2011) Cell. Mol. Biol. Lett , vol.16 , pp. 40-54
    • Keller, R.C.A.1
  • 13
    • 0026777830 scopus 로고
    • Deep penetration of a portion of Escherichia coli SecA protein into model membranes is promoted by anionic phospholipids and by partial unfolding
    • Ulbrandt, N.D.; London, E.L.; Oliver, D.B. Deep penetration of a portion of Escherichia coli SecA protein into model membranes is promoted by anionic phospholipids and by partial unfolding. J. Biol. Chem. 1992, 267, 15184-15192.
    • (1992) J. Biol. Chem , vol.267 , pp. 15184-15192
    • Ulbrandt, N.D.1    London, E.L.2    Oliver, D.B.3
  • 14
    • 0027484266 scopus 로고
    • Nucleotide and negatively charged lipid-dependent vesicle aggregation caused by SecA
    • Breukink, E.; Keller, R.C.A.; de Kruijff, B. Nucleotide and negatively charged lipid-dependent vesicle aggregation caused by SecA. FEBS Lett. 1993, 331, 19-24.
    • (1993) FEBS Lett , vol.331 , pp. 19-24
    • Breukink, E.1    Keller, R.C.A.2    de Kruijff, B.3
  • 15
    • 0028098766 scopus 로고
    • SecA of Escherichia coli traverses lipid bilayer of phospholipid vesicles
    • Ahn, T.; Kim, H. SecA of Escherichia coli traverses lipid bilayer of phospholipid vesicles. Biochem. Biophys. Res. Commun. 1994, 203, 326-330.
    • (1994) Biochem. Biophys. Res. Commun , vol.203 , pp. 326-330
    • Ahn, T.1    Kim, H.2
  • 16
    • 0000484499 scopus 로고
    • Hydrophobic parameters p of amino-acid side chains from the partitioning of N-acetyl-amino-acid amides
    • Fauchere, J.; Pliska, V. Hydrophobic parameters p of amino-acid side chains from the partitioning of N-acetyl-amino-acid amides. Eur. J. Med. Chem. 1983, 8, 369-375.
    • (1983) Eur. J. Med. Chem , vol.8 , pp. 369-375
    • Fauchere, J.1    Pliska, V.2
  • 17
    • 0031984072 scopus 로고    scopus 로고
    • Trojan peptides: The penetratin system for intracellular delivery
    • Derossi, D.; Chassaing, G.; Prochiantz, A. Trojan peptides: The penetratin system for intracellular delivery. Trends Cell. Biol. 1998, 8, 84-87.
    • (1998) Trends Cell. Biol , vol.8 , pp. 84-87
    • Derossi, D.1    Chassaing, G.2    Prochiantz, A.3
  • 18
    • 69249171631 scopus 로고    scopus 로고
    • Interaction of 18-residue peptides derived from amphipathic helical segments of globular proteins with model membranes
    • Sivakamasundari, C.; Nagaraj, R. Interaction of 18-residue peptides derived from amphipathic helical segments of globular proteins with model membranes. J. Biosci. 2009, 34, 239-250.
    • (2009) J. Biosci , vol.34 , pp. 239-250
    • Sivakamasundari, C.1    Nagaraj, R.2
  • 19
    • 78149268666 scopus 로고    scopus 로고
    • Disperse distribution of cationic amino acids on hydrophilic surface of helical wheel enhances antimicrobial peptide activity
    • Kim, Y.S.; Cha, H.J. Disperse distribution of cationic amino acids on hydrophilic surface of helical wheel enhances antimicrobial peptide activity. Biotechn. Bioeng. 2010, 107, 216-223.
    • (2010) Biotechn. Bioeng , vol.107 , pp. 216-223
    • Kim, Y.S.1    Cha, H.J.2
  • 20
    • 0027274908 scopus 로고
    • Identification of a second membrane-active 13-residue peptide segment in the antimicrobial protein, bovine seminalplasmin
    • Sitaram, N.; Subbalakshmi, C.; Nagaraj, R. Identification of a second membrane-active 13-residue peptide segment in the antimicrobial protein, bovine seminalplasmin. FEBS Lett. 1993, 328, 239-242.
    • (1993) FEBS Lett , vol.328 , pp. 239-242
    • Sitaram, N.1    Subbalakshmi, C.2    Nagaraj, R.3
  • 21
    • 0035937109 scopus 로고    scopus 로고
    • Characterization of Histatin 5 with respect to amphipathicity, hydrophobicity, and effects on cell and mitochondrial membrane integrity excludes a candidacidal mechanism of pore formation
    • Helmerhors, E.J.; van't Hof, W.; Breeuweri, P.; Veerman, E.C.I.; Abee, T.; Troxler, R.F.; Nieuw Amerongen, A.V.; Oppenheim, F.G. Characterization of Histatin 5 with respect to amphipathicity, hydrophobicity, and effects on cell and mitochondrial membrane integrity excludes a candidacidal mechanism of pore formation. J. Biol. Chem. 2001, 276, 5643-5649.
    • (2001) J. Biol. Chem , vol.276 , pp. 5643-5649
    • Helmerhors, E.J.1    Van't hof, W.2    Breeuweri, P.3    Veerman, E.C.I.4    Abee, T.5    Troxler, R.F.6    Amerongen, A.V.N.7    Oppenheim, F.G.8
  • 22
    • 0025770286 scopus 로고
    • Surfactant protein B. Lipid interactions of synthetic peptides representing the amino-terminal amphipathic domain
    • Bruni, R.; Taeusch, H.W.; Waring, A.J. Surfactant protein B: Lipid interactions of synthetic peptides representing the amino-terminal amphipathic domain. Proc. Natl. Acad. Sci. USA 1991, 88, 7451-7455.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7451-7455
    • Bruni, R.1    Taeusch, H.W.2    Waring, A.J.3
  • 23
    • 0034687723 scopus 로고    scopus 로고
    • High-level expression and mutagenesis of recombinant human phosphatidylcholine transfer protein using a synthetic gene: Evidence for a C-terminal membrane binding domain
    • Feng, L.; Chan, W.W.; Roderick, S.L.; Cohen, D.E. High-level expression and mutagenesis of recombinant human phosphatidylcholine transfer protein using a synthetic gene: Evidence for a C-terminal membrane binding domain. Biochemistry 2000, 39, 15399-15409.
    • (2000) Biochemistry , vol.39 , pp. 15399-15409
    • Feng, L.1    Chan, W.W.2    Roderick, S.L.3    Cohen, D.E.4
  • 24
    • 0028240076 scopus 로고
    • Primary and secondary structure of a pore-forming toxin from the sea anemone, Actinia equina L., and its association with lipid vesicles
    • Belmonte, G.; Menestrina, G.; Perderzolli, C.; Krizaj, I.; Gubensek, F.; Macek, P. Primary and secondary structure of a pore-forming toxin from the sea anemone, Actinia equina L., and its association with lipid vesicles. Biochim. Biophys. Acta 1994, 1192, 197-204.
    • (1994) Biochim. Biophys. Acta , vol.1192 , pp. 197-204
    • Belmonte, G.1    Menestrina, G.2    Perderzolli, C.3    Krizaj, I.4    Gubensek, F.5    Macek, P.6
  • 25
    • 0029866148 scopus 로고    scopus 로고
    • The 21-residue surfactant peptide (LysLeu4)4Lys(KL4) is a transmembrane α-helix with a mixed nonpolar/polar surface
    • Gustafsson, M.; Vandenbussche, G.; Cursted, T.; Ruysschaert, J.-M.; Johansson, J. The 21-residue surfactant peptide (LysLeu4)4Lys(KL4) is a transmembrane α-helix with a mixed nonpolar/polar surface. FEBS Lett. 1996, 384, 185-188.
    • (1996) FEBS Lett , vol.384 , pp. 185-188
    • Gustafsson, M.1    Vandenbussche, G.2    Cursted, T.3    Ruysschaert, J.-M.4    Johansson, J.5
  • 27
    • 0027092981 scopus 로고
    • The glycophorin A transmembrane domain dimer: Sequence-specific propensity for a right-handed supercoil of helices
    • Treutlein, H.R.; Lemmon, M.A.; Engelman, D.M.; Brunger, A.T. The glycophorin A transmembrane domain dimer: Sequence-specific propensity for a right-handed supercoil of helices. Biochemistry 1992, 31, 12726-12732.
    • (1992) Biochemistry , vol.31 , pp. 12726-12732
    • Treutlein, H.R.1    Lemmon, M.A.2    Engelman, D.M.3    Brunger, A.T.4
  • 28
    • 0034711760 scopus 로고    scopus 로고
    • Secondary structure, orientation, oligomerization and lipid interactions of the transmembrane domain of Influenza Hemagglutinin
    • Tatulian, S.A.; Tamm, L.K. Secondary structure, orientation, oligomerization and lipid interactions of the transmembrane domain of Influenza Hemagglutinin. Biochemistry 2000, 39, 496-507.
    • (2000) Biochemistry , vol.39 , pp. 496-507
    • Tatulian, S.A.1    Tamm, L.K.2
  • 29
    • 0036071621 scopus 로고    scopus 로고
    • A.structure for the trimeric MHC class II-associated invariant chain transmembrane domain
    • Kukol, A.; Torres, J.; Arkin, I.T. A structure for the trimeric MHC class II-associated invariant chain transmembrane domain. J. Mol. Biol. 2002, 320, 1109-1117.
    • (2002) J. Mol. Biol , vol.320 , pp. 1109-1117
    • Kukol, A.1    Torres, J.2    Arkin, I.T.3
  • 31
    • 0026573926 scopus 로고
    • Anionic phospholipids are essential for α-helix formation of the signal peptide of prePhoE upon interaction with phospholipid vesicles
    • Keller, R.C.A.; Killian, J.A.; de Kruijff, B. Anionic phospholipids are essential for α-helix formation of the signal peptide of prePhoE upon interaction with phospholipid vesicles. Biochemistry 1992, 31, 1672-1677.
    • (1992) Biochemistry , vol.31 , pp. 1672-1677
    • Keller, R.C.A.1    Killian, J.A.2    de Kruijff, B.3
  • 32
    • 0027993450 scopus 로고
    • Effect of charged residue substitutions on the thermodynamics of signal peptide-lipid interactions for the Escherichia coli LamB signal sequence
    • Jones, J.D.; Gierasch, L.M. Effect of charged residue substitutions on the thermodynamics of signal peptide-lipid interactions for the Escherichia coli LamB signal sequence. Biophys. J. 1994, 67, 1546-1561.
    • (1994) Biophys. J , vol.67 , pp. 1546-1561
    • Jones, J.D.1    Gierasch, L.M.2
  • 33
    • 0027180807 scopus 로고
    • Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments
    • Rizo, J.; Blanco, F.J.; Kobe, B.; Bruch, M.D.; Gierasch, L.M. Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments. Biochemistry 1993, 32, 4881-4894.
    • (1993) Biochemistry , vol.32 , pp. 4881-4894
    • Rizo, J.1    Blanco, F.J.2    Kobe, B.3    Bruch, M.D.4    Gierasch, L.M.5
  • 34
    • 0348162681 scopus 로고    scopus 로고
    • Effect of membrane phospholipid composition and charge of the signal peptide of Escherichia coli alkaline phosphatase on efficiency of its secretion
    • Golovastov, V.V.; Nesmeyanova, M.A. Effect of membrane phospholipid composition and charge of the signal peptide of Escherichia coli alkaline phosphatase on efficiency of its secretion. Biochemistry (Mosc) 2003, 68, 1089-1096.
    • (2003) Biochemistry (Mosc) , vol.68 , pp. 1089-1096
    • Golovastov, V.V.1    Nesmeyanova, M.A.2
  • 38
    • 0036436859 scopus 로고    scopus 로고
    • Domain V of m-calpain shows the potential to form an oblique-orientated α-helix, which may modulate the enzyme's activity via interactions with anionic lipid
    • Brandenburg, K.; Harris, F.; Dennison, S.; Seydel1, U.; Phoenix, D. Domain V of m-calpain shows the potential to form an oblique-orientated α-helix, which may modulate the enzyme's activity via interactions with anionic lipid. Eur. J. Biochem. 2002, 269, 5414-5422.
    • (2002) Eur. J. Biochem , vol.269 , pp. 5414-5422
    • Brandenburg, K.1    Harris, F.2    Dennison, S.3    Seydel, U.4    Phoenix, D.5
  • 39
    • 33746695401 scopus 로고    scopus 로고
    • Investigations into the ability of an oblique alpha-helical template to provide the basis for design of an antimicrobial anionic amphiphilic peptide
    • Dennison, S.R.; Morto, L.H.; Brandenburg, K.; Harris, F.; Phoenix, D.A. Investigations into the ability of an oblique alpha-helical template to provide the basis for design of an antimicrobial anionic amphiphilic peptide. FEBS J. 2006, 273, 3792-3803.
    • (2006) FEBS J , vol.273 , pp. 3792-3803
    • Dennison, S.R.1    Morto, L.H.2    Brandenburg, K.3    Harris, F.4    Phoenix, D.A.5
  • 40
    • 0040952847 scopus 로고    scopus 로고
    • Oblique membrane insertion of viral fusion peptide probed by neutron diffraction
    • Bradshaw, J.P.; Darkes, M.J.M.; Harroun, T.A.; Katsaras, J.; Epand, R.M. Oblique membrane insertion of viral fusion peptide probed by neutron diffraction. Biochemistry 2000, 39, 6581-6585.
    • (2000) Biochemistry , vol.39 , pp. 6581-6585
    • Bradshaw, J.P.1    Darkes, M.J.M.2    Harroun, T.A.3    Katsaras, J.4    Epand, R.M.5
  • 41
    • 0037113127 scopus 로고    scopus 로고
    • Role of praline, cysteine and a disulphide bridge in the structure and activity of the anti-microbial peptide gaegurin 5
    • Park, S.-H.; Kim, H.-E.; Kim, C.-M; Yun, H.-J.; Choi, E.-C.; Lee, B.-J. Role of praline, cysteine and a disulphide bridge in the structure and activity of the anti-microbial peptide gaegurin 5. Biochem. J. 2002, 368, 171-182.
    • (2002) Biochem. J , vol.368 , pp. 171-182
    • Park, S.-H.1    Kim, H.-E.2    Kim, C.-M.3    Yun, H.-J.4    Choi, E.-C.5    Lee, B.-J.6
  • 42
    • 18744393069 scopus 로고    scopus 로고
    • Investigations into the mechanisms used by the C-terminal anchors of Escherichia coli penicillin-binding proteins 4, 5, 6 and 6b for membrane interaction
    • Harris, F.; Brandenburg, K.; Seydel, U.; Phoenix, D. Investigations into the mechanisms used by the C-terminal anchors of Escherichia coli penicillin-binding proteins 4, 5, 6 and 6b for membrane interaction. Eur. J. Biochem. 2002, 269, 5821-5829.
    • (2002) Eur. J. Biochem , vol.269 , pp. 5821-5829
    • Harris, F.1    Brandenburg, K.2    Seydel, U.3    Phoenix, D.4
  • 43
    • 0026653453 scopus 로고
    • Binding of substance P to monolayers and vesicles made of phosphatidylcholine and/or phosphatidylserine
    • Duplaa, H.; Convert, O.; Sautereau, A.M.; Tocanne, J.F.; Chassaing, G. Binding of substance P to monolayers and vesicles made of phosphatidylcholine and/or phosphatidylserine. Biochim. Biophys. Acta 1992, 1107, 12-22.
    • (1992) Biochim. Biophys. Acta , vol.1107 , pp. 12-22
    • Duplaa, H.1    Convert, O.2    Sautereau, A.M.3    Tocanne, J.F.4    Chassaing, G.5
  • 44
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • Derossi, D.; Joliot, A.H.; Chassaing, G.; Prochiantz, A. The third helix of the Antennapedia homeodomain translocates through biological membranes. J. Biol. Chem. 1994, 269, 10444-10450.
    • (1994) J. Biol. Chem , vol.269 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 45
    • 0033794501 scopus 로고    scopus 로고
    • Polyarginine enters cells more efficiently than other polycationic homopolymers
    • Mitchell, D.J.; Kim, D.T.; Steinman, L.; Fathman, C.G.; Rothbard, J.B. Polyarginine enters cells more efficiently than other polycationic homopolymers. J. Pept. Res. 2000, 56, 318-325.
    • (2000) J. Pept. Res , vol.56 , pp. 318-325
    • Mitchell, D.J.1    Kim, D.T.2    Steinman, L.3    Fathman, C.G.4    Rothbard, J.B.5
  • 46
    • 59849092098 scopus 로고    scopus 로고
    • Mechanism of antibacterial action of Dermaseptin B2: Interplay between helix-hinge-helix structure and membrane curvature strain
    • Galanth, C.; Abbassi, F.; Lequin, O.; Ayala-Sanmartin, J.; Ladram, A.; Nicolas, P.; Amiche, M. Mechanism of antibacterial action of Dermaseptin B2: Interplay between helix-hinge-helix structure and membrane curvature strain. Biochemistry 2009, 48, 313-327.
    • (2009) Biochemistry , vol.48 , pp. 313-327
    • Galanth, C.1    Abbassi, F.2    Lequin, O.3    Ayala-Sanmartin, J.4    Ladram, A.5    Nicolas, P.6    Amiche, M.7
  • 48
    • 49349084439 scopus 로고    scopus 로고
    • SecA, the motor of the secretion machine, binds diverse partners on one interactive surface
    • Cooper, D.B.; Smith, V.F.; Crane, J.M.; Roth, H.C.; Lilly, A.A.; Randall, L.L. SecA, the motor of the secretion machine, binds diverse partners on one interactive surface. J. Mol. Biol. 2008, 382, 74-87.
    • (2008) J. Mol. Biol , vol.382 , pp. 74-87
    • Cooper, D.B.1    Smith, V.F.2    Crane, J.M.3    Roth, H.C.4    Lilly, A.A.5    Randall, L.L.6
  • 49
    • 40649093985 scopus 로고    scopus 로고
    • A Cleavable N-terminal membrane anchor is involved in membrane binding of the Escherichia coli SRP receptor
    • Weiche, B.; Bürk, J.; Angelini, S.; Schiltz, E.; Thumfart, J.-O.; Koch, H.-G. A cleavable N-terminal membrane anchor is involved in membrane binding of the Escherichia coli SRP receptor. J. Mol. Biol. 2008, 28, 761-773.
    • (2008) J. Mol. Biol , vol.28 , pp. 761-773
    • Weiche, B.1    Bürk, J.2    Angelini, S.3    Schiltz, E.4    Thumfart, J.-O.5    Koch, H.-G.6
  • 50
    • 36148937889 scopus 로고    scopus 로고
    • Escherichia coli signal recognition particle receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix
    • Parlitz, R.; Eitan, A.; Stjepanovic, G.; Bahari, L.; Bange, G.; Bibi, E.; Sinning, I. Escherichia coli signal recognition particle receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix. J. Biol. Chem. 2007, 44, 32176-32321.
    • (2007) J. Biol. Chem , vol.44 , pp. 32176-32321
    • Parlitz, R.1    Eitan, A.2    Stjepanovic, G.3    Bahari, L.4    Bange, G.5    Bibi, E.6    Sinning, I.7
  • 51
    • 0024447757 scopus 로고
    • Specificity of the interaction of amino-and carboxy-terminal fragments of the mitochondrial precursor protein apocytochrome c with negatively charged phospholipids
    • Jordi, W.; de Kruijff, B.; Marsh, D. Specificity of the interaction of amino-and carboxy-terminal fragments of the mitochondrial precursor protein apocytochrome c with negatively charged phospholipids. A spin-label electron spin resonance study. Biochemistry 1989, 28, 8998-9005.
    • (1989) A spin-label electron spin resonance study Biochemistry , vol.28 , pp. 8998-9005
    • Jordi, W.1    de Kruijff, B.2    Marsh, D.3
  • 52
    • 0037180562 scopus 로고    scopus 로고
    • Membrane localization of MinD is mediated by a C-terminal motif that is conserved across eubacteria, archaea, and chloroplasts
    • Szeto, T.H.; Rowland, S.L.; Rothfield, L.I.; King, G.F. Membrane localization of MinD is mediated by a C-terminal motif that is conserved across eubacteria, archaea, and chloroplasts. Proc. Natl. Acad. Sci. USA 2002, 99, 15693-15698.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 15693-15698
    • Szeto, T.H.1    Rowland, S.L.2    Rothfield, L.I.3    King, G.F.4
  • 53
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of α-Synuclein secondary structure upon binding to synthetic membranes
    • Davidson, W.S.; Jonas, A.; Clayton, D.F.; George, J.M. Stabilization of α-Synuclein secondary structure upon binding to synthetic membranes. J. Biol. Chem. 1998, 273, 9443-9449.
    • (1998) J. Biol. Chem , vol.273 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 54
    • 33847140438 scopus 로고    scopus 로고
    • Plant dehydrins-Tissue location, structure and function
    • Rorat, T. Plant dehydrins-Tissue location, structure and function. Cell. Mol Biol. Lett. 2006, 11, 536-556.
    • (2006) Cell. Mol Biol. Lett , vol.11 , pp. 536-556
    • Rorat, T.1
  • 55
    • 0043238695 scopus 로고    scopus 로고
    • The membrane bound N-terminal domain of human adenosine diphosphate ribosylation factor-1 (ARF1)
    • Davies, S.M.A.; Harroun, T.A.; Hauß, T.; Kelly, S.M.; Bradshaw, J.P. The membrane bound N-terminal domain of human adenosine diphosphate ribosylation factor-1 (ARF1). FEBS Lett. 2003, 548, 119-124.
    • (2003) FEBS Lett , vol.548 , pp. 119-124
    • Davies, S.M.A.1    Harroun, T.A.2    Hauß, T.3    Kelly, S.M.4    Bradshaw, J.P.5
  • 57
    • 78751564282 scopus 로고    scopus 로고
    • Characterization of a Binding Site for Anionic Phospholipids on KCNQ1
    • Thomas, A.M.; Harmer, S.C.; Khambra, T.; Tinker, A. Characterization of a Binding Site for Anionic Phospholipids on KCNQ1. J. Biol. Chem. 2011, 286, 2088-2100.
    • (2011) J. Biol. Chem , vol.286 , pp. 2088-2100
    • Thomas, A.M.1    Harmer, S.C.2    Khambra, T.3    Tinker, A.4
  • 58
    • 0033609293 scopus 로고    scopus 로고
    • Fragments from Actin Binding Protein (ABP-280; Filamin) insert into reconstituted lipid layers
    • Goldmann, W.H.; Teodoridis, J.M.; Sharma, C.P.; Hu, B.; Isenberg, G. Fragments from Actin Binding Protein (ABP-280; Filamin) insert into reconstituted lipid layers. Biochem. Biophys. Res. Commun. 1999, 259, 108-112.
    • (1999) Biochem. Biophys. Res. Commun , vol.259 , pp. 108-112
    • Goldmann, W.H.1    Teodoridis, J.M.2    Sharma, C.P.3    Hu, B.4    Isenberg, G.5
  • 59
    • 0028177259 scopus 로고
    • Application to the de novo design of ideally amphipathic Leu, Lys peptides with haemolytic activity higher than that of melittin
    • Cornut, I.; Büttner, K.; Dasseux, J.-L.; Dufourcq, J. Application to the de novo design of ideally amphipathic Leu, Lys peptides with haemolytic activity higher than that of melittin. FEBS Lett. 1994, 349, 29-33.
    • (1994) FEBS Lett , vol.349 , pp. 29-33
    • Cornut, I.1    Büttner, K.2    Dasseux, J.-L.3    Dufourcq, J.4
  • 60
    • 0025323708 scopus 로고
    • The distribution of physical, chemical and conformational properties in signal and nascent peptides
    • Prabhakaran, M. The distribution of physical, chemical and conformational properties in signal and nascent peptides. Biochem. J. 1990, 269, 691-696.
    • (1990) Biochem. J , vol.269 , pp. 691-696
    • Prabhakaran, M.1
  • 61
    • 0022731676 scopus 로고
    • Mitochondrial targeting sequences may form amphiphilic helices
    • von Heijne, G. Mitochondrial targeting sequences may form amphiphilic helices. EMBO J. 1986, 5, 1335-13342.
    • (1986) EMBO J , vol.5 , pp. 1335-13342
    • von Heijne, G.1
  • 62
    • 0021511573 scopus 로고
    • Analysis of the distribution of charged residues in the N-terminal region of signal sequences: Implications for protein export in prokaryotic and eukaryotic cells
    • von Heijne, G. Analysis of the distribution of charged residues in the N-terminal region of signal sequences: Implications for protein export in prokaryotic and eukaryotic cells. EMBO J. 1984, 3, 2315-2318.
    • (1984) EMBO J , vol.3 , pp. 2315-2318
    • von Heijne, G.1
  • 63
    • 0024571667 scopus 로고
    • Species-specific variation in signal peptide design Implications for secretion in foreign hosts
    • von Heijne, G.; Abrahmsen, L. Species-specific variation in signal peptide design. Implications for secretion in foreign hosts. FEBS Lett. 1989, 244, 439-446.
    • (1989) FEBS Lett , vol.244 , pp. 439-446
    • von Heijne, G.1    Abrahmsen, L.2
  • 64
    • 11244352103 scopus 로고    scopus 로고
    • Are oblique orientated α-Helices used by antimicrobial peptides for membrane invasion?
    • Dennison, S.R.; Harris, F.; Phoenix, D.A. Are oblique orientated α-Helices used by antimicrobial peptides for membrane invasion? Prot. Pept. Lett. 2005, 12, 27-29.
    • (2005) Prot. Pept. Lett , vol.12 , pp. 27-29
    • Dennison, S.R.1    Harris, F.2    Phoenix, D.A.3
  • 65
    • 0025142363 scopus 로고
    • Initial steps in protein membrane insertion Bacteriophage M13 procoat protein binds to the membrane surface by electrostatic interaction
    • Gallusser, A.; Kuhn, A. Initial steps in protein membrane insertion. Bacteriophage M13 procoat protein binds to the membrane surface by electrostatic interaction. EMBO J. 1990, 9, 2723-2729.
    • (1990) EMBO J , vol.9 , pp. 2723-2729
    • Gallusser, A.1    Kuhn, A.2
  • 66
    • 34147182082 scopus 로고    scopus 로고
    • Cysteine residues in the transmembrane regions of M13 Procoat protein suggest that oligomeric coat Proteins assemble onto phage progeny
    • Nagler, C.; Nagler, G.; Kuhn, A. Cysteine residues in the transmembrane regions of M13 Procoat protein suggest that oligomeric coat Proteins assemble onto phage progeny. J. Bacteriol. 2007, 189, 2897-2905.
    • (2007) J. Bacteriol , vol.189 , pp. 2897-2905
    • Nagler, C.1    Nagler, G.2    Kuhn, A.3
  • 67
    • 79959585289 scopus 로고    scopus 로고
    • The cytosolic domain of Fis1 binds and reversibly clusters lipid vesicles
    • doi:10.1371/journal.pone.0021384
    • Wells, R.C.; Hill, R.B. The cytosolic domain of Fis1 binds and reversibly clusters lipid vesicles. PLoS One 2011, 6 doi:10.1371/journal.pone.0021384
    • (2011) PLoS One , pp. 6
    • Wells, R.C.1    Hill, R.B.2
  • 68
    • 0041325083 scopus 로고    scopus 로고
    • Protein-protein, protein-RNA and protein-lipid interactions of signal-recognition particle components in the hyperthermoacidophilic archaeon
    • Moll, R.G. Protein-protein, protein-RNA and protein-lipid interactions of signal-recognition particle components in the hyperthermoacidophilic archaeon Acidianus ambivalens. Biochem. J. 2003, 374, 247-254.
    • (2003) Acidianus Ambivalens. Biochem. J , vol.374 , pp. 247-254
    • Moll, R.G.1
  • 69
    • 70450221916 scopus 로고    scopus 로고
    • Stability and structure of the membrane protein transporter Ffh is modulated by substrates and lipids
    • Reinau, M.E.; Otzen D.E. Stability and structure of the membrane protein transporter Ffh is modulated by substrates and lipids. Arch. Biochem. Biophys. 2009, 492, 48-53.
    • (2009) Arch. Biochem. Biophys , vol.492 , pp. 48-53
    • Reinau, M.E.1    Otzen, D.E.2
  • 71
    • 0029595442 scopus 로고
    • SOPMA: Significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments
    • Geourjon, C.; Deleage, G. SOPMA: Significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments. Comput. Appl. Biosci. 1995, 11, 681-684.
    • (1995) Comput. Appl Biosci , vol.11 , pp. 681-684
    • Geourjon, C.1    Deleage, G.2
  • 72
    • 0028128453 scopus 로고
    • Signal peptides: Exquisitely designed transport promoters
    • Izard, J.W.; Kendall, D.A. Signal peptides: Exquisitely designed transport promoters. Mol. Microbiol. 1994, 13, 765-773.
    • (1994) Mol Microbiol , vol.13 , pp. 765-773
    • Izard, J.W.1    Kendall, D.A.2
  • 73
    • 33947393032 scopus 로고    scopus 로고
    • Antimicrobial peptides: An overview of a promising class of therapeutics
    • Giuliani, A.; Pirri, G.; Nicolette, S.F. Antimicrobial peptides: An overview of a promising class of therapeutics. Cent. Eur. J. Biol. 2007, 2, 1-33.
    • (2007) Cent. Eur. J. Biol , vol.2 , pp. 1-33
    • Giuliani, A.1    Pirri, G.2    Nicolette, S.F.3
  • 75
    • 0023977693 scopus 로고
    • Amphitropic proteins: A new class of membrane proteins
    • Burn, P. Amphitropic proteins: A new class of membrane proteins. Trends Biochem. Sci. 1988, 13, 79-83.
    • (1988) Trends Biochem. Sci , vol.13 , pp. 79-83
    • Burn, P.1
  • 76
    • 0032872786 scopus 로고    scopus 로고
    • Amphitropic proteins: Regulation by reversible membrane interactions (review)
    • Johnson, J.E.; Cornell, R.B. Amphitropic proteins: Regulation by reversible membrane interactions (review). Mol. Membr. Biol. 1999, 16, 217-235.
    • (1999) Mol. Membr. Biol , vol.16 , pp. 217-235
    • Johnson, J.E.1    Cornell, R.B.2
  • 77
    • 70349501375 scopus 로고    scopus 로고
    • Linking new paradigms in protein chemistry to reversible membrane-protein interactions
    • Halskau, Ø.; Muga, A.; Martínez, A. Linking new paradigms in protein chemistry to reversible membrane-protein interactions. Curr. Prot. Pept. Sci. 2009, 10, 339-359.
    • (2009) Curr. Prot. Pept. Sci , vol.10 , pp. 339-359
    • Halskau, Ø.1    Muga, A.2    Martínez, A.3
  • 78
    • 0028917958 scopus 로고
    • SecA restricts in a nucleotide-dependent manner acyl chain mobility up to the center of a phospholipid bilayer
    • Keller, R.C.A.; Snel, M.M.E.; de Kruijff, B.; Marsh, D. SecA restricts in a nucleotide-dependent manner acyl chain mobility up to the center of a phospholipid bilayer. FEBS Lett. 1995, 358, 251-254.
    • (1995) FEBS Lett , vol.358 , pp. 251-254
    • Keller, R.C.A.1    Snel, M.M.E.2    de Kruijff, B.3    Marsh, D.4


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