메뉴 건너뛰기




Volumn 51, Issue 40, 2012, Pages 7863-7872

NMR structure, localization, and vesicle fusion of chikungunya virus fusion peptide

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC CORES; AROMATIC SIDE CHAINS; ATOMIC RESOLUTION STRUCTURES; C-TERMINUS; CELL FUSION PROCESS; CHIKUNGUNYA; CLOSE PROXIMITY; ENVELOPED VIRUS; FUSION MECHANISM; FUSION PEPTIDES; FUSION PROTEINS; HOST CELLS; HYDROPHOBIC FUSION; LIPOSOME FUSION; NMR STRUCTURES; PARAMAGNETIC RELAXATION ENHANCEMENTS; PH INDEPENDENT; POLAR RESIDUES; SIDE-CHAINS; THREE-DIMENSIONAL STRUCTURE; TYPE II; VESICLE FUSION; ZWITTERIONIC LIPIDS;

EID: 84867453365     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300901f     Document Type: Article
Times cited : (15)

References (57)
  • 1
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagllutinin
    • Skehel, J. J. and Wiley, D. C. (2000) Receptor binding and membrane fusion in virus entry: the influenza hemagllutinin Annu. Rev. Biochem. 69, 531-569
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 2
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert, D. M. and Kim, P. S. (2001) Mechanisms of viral membrane fusion and its inhibition Annu. Rev. Biochem. 70, 777-810
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 3
    • 26944466459 scopus 로고    scopus 로고
    • Mechanism of membrane fusion by viral envelop proteins
    • Harrison, S. C. (2005) Mechanism of membrane fusion by viral envelop proteins Adv. Virus. Res. 64, 231-261
    • (2005) Adv. Virus. Res. , vol.64 , pp. 231-261
    • Harrison, S.C.1
  • 4
    • 31344432402 scopus 로고    scopus 로고
    • Virus membrane-fusion proteins: More than one way to make a hairpin
    • Kielian, M. and Rey, F. A. (2006) Virus membrane-fusion proteins: more than one way to make a hairpin Nat. Rev. Microbiol. 4, 67-76
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 67-76
    • Kielian, M.1    Rey, F.A.2
  • 7
    • 1842534392 scopus 로고    scopus 로고
    • How viruses enter animal cells
    • Smith, A. E. and Helenius, A. (2004) How viruses enter animal cells Science 304, 237-242
    • (2004) Science , vol.304 , pp. 237-242
    • Smith, A.E.1    Helenius, A.2
  • 8
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry cofactor: Functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor
    • Feng, Y., Broder, C. C., Kennedy, P. E., and Berger, E. A. (1996) HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor Science 272, 872-877
    • (1996) Science , vol.272 , pp. 872-877
    • Feng, Y.1    Broder, C.C.2    Kennedy, P.E.3    Berger, E.A.4
  • 9
    • 0027430672 scopus 로고
    • Paramyxovirus fusion: A hypothesis for changes
    • Lamb, R. A. (1993) Paramyxovirus fusion: a hypothesis for changes Virology 197, 1-11
    • (1993) Virology , vol.197 , pp. 1-11
    • Lamb, R.A.1
  • 11
    • 0018853517 scopus 로고
    • On the entry of semliki forest virus into BHK-21 cells
    • Helenius, A., Kartenbeck, J., Simons, K., and Fries, E. (1980) On the entry of semliki forest virus into BHK-21 cells J. Cell Biol. 84, 404-420
    • (1980) J. Cell Biol. , vol.84 , pp. 404-420
    • Helenius, A.1    Kartenbeck, J.2    Simons, K.3    Fries, E.4
  • 13
    • 0034567567 scopus 로고    scopus 로고
    • Structures and mechanisms in flavivirus fusion
    • Heinz, F. X. and Allison, S. L. (2000) Structures and mechanisms in flavivirus fusion Adv. Virus Res. 55, 231-269
    • (2000) Adv. Virus Res. , vol.55 , pp. 231-269
    • Heinz, F.X.1    Allison, S.L.2
  • 14
    • 0038487375 scopus 로고    scopus 로고
    • Fusion peptide and the mechanisms of viral fusion
    • Epand, R. M. (2003) Fusion peptide and the mechanisms of viral fusion Biochim. Biophys. Acta 1614, 116-121
    • (2003) Biochim. Biophys. Acta , vol.1614 , pp. 116-121
    • Epand, R.M.1
  • 15
    • 0037810986 scopus 로고    scopus 로고
    • Viral fusion proteins: Multiple regions contribute to membrane fusion
    • Peisajovich, S. G. and Shai, Y. (2003) Viral fusion proteins: multiple regions contribute to membrane fusion Biochim. Biophys. Acta 1614, 122-129
    • (2003) Biochim. Biophys. Acta , vol.1614 , pp. 122-129
    • Peisajovich, S.G.1    Shai, Y.2
  • 16
    • 0038825375 scopus 로고    scopus 로고
    • Hypothesis: Spring-loaded boomerang mechanism of influenza hemagglutinin-mediated membrane fusion
    • Tamm, L. K. (2003) Hypothesis: spring-loaded boomerang mechanism of influenza hemagglutinin-mediated membrane fusion Biochim. Biophys. Acta 1614, 14-23
    • (2003) Biochim. Biophys. Acta , vol.1614 , pp. 14-23
    • Tamm, L.K.1
  • 17
    • 80051797727 scopus 로고    scopus 로고
    • Class II enveloped viruses
    • Vaney, M.-C. and Rey, F. A. (2011) Class II enveloped viruses Cell. Microbiol. 13, 1451-1459
    • (2011) Cell. Microbiol. , vol.13 , pp. 1451-1459
    • Vaney, M.-C.1    Rey, F.A.2
  • 18
    • 29144497159 scopus 로고    scopus 로고
    • Class II virus membrane fusion proteins
    • Kielian, M. (2006) Class II virus membrane fusion proteins Virology 344, 38-47
    • (2006) Virology , vol.344 , pp. 38-47
    • Kielian, M.1
  • 19
    • 33846959065 scopus 로고    scopus 로고
    • Structure of the prefusion form of the vesicular stomatitis virus glycoprotein G
    • Roche, S., Rey, F. A., Gaudin, Y., and Bressanelli, S. (2007) Structure of the prefusion form of the vesicular stomatitis virus glycoprotein G Science 315, 843-848
    • (2007) Science , vol.315 , pp. 843-848
    • Roche, S.1    Rey, F.A.2    Gaudin, Y.3    Bressanelli, S.4
  • 20
    • 0034700998 scopus 로고    scopus 로고
    • The polar region consecutive to the HIV fusion peptide participates in membrane fusion
    • Peisajovich, S. G., Epand, R. F., Pritsker, M., Shai, Y., and Epand, R. M. (2000) The polar region consecutive to the HIV fusion peptide participates in membrane fusion Biochemistry 39, 1826-1833
    • (2000) Biochemistry , vol.39 , pp. 1826-1833
    • Peisajovich, S.G.1    Epand, R.F.2    Pritsker, M.3    Shai, Y.4    Epand, R.M.5
  • 21
    • 0034718569 scopus 로고    scopus 로고
    • Sendai virus internal fusion peptide: Structural and functional characterization and a plausible mode of viral entry inhibition
    • Ghosh, J. K., Peisajovich, S. G., and Shai, Y. (2000) Sendai virus internal fusion peptide: structural and functional characterization and a plausible mode of viral entry inhibition Biochemistry 39, 11581-11592
    • (2000) Biochemistry , vol.39 , pp. 11581-11592
    • Ghosh, J.K.1    Peisajovich, S.G.2    Shai, Y.3
  • 22
    • 0034700147 scopus 로고    scopus 로고
    • A host-guest system to study structure-function relationships of membrane fusion peptides
    • Han, X. and Tamm, L. K. (2000) A host-guest system to study structure-function relationships of membrane fusion peptides Proc. Natl. Acad. Sci. U.S.A. 97, 13097-13102
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13097-13102
    • Han, X.1    Tamm, L.K.2
  • 23
    • 0028824850 scopus 로고
    • Studies of membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin
    • Steinhauer, D. A., Wharton, S. A., Skehel, J. J., and Wiley, D. C. (1995) Studies of membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin J. Virol. 69, 6643-6651
    • (1995) J. Virol. , vol.69 , pp. 6643-6651
    • Steinhauer, D.A.1    Wharton, S.A.2    Skehel, J.J.3    Wiley, D.C.4
  • 24
    • 48649092280 scopus 로고    scopus 로고
    • A second SARS-CoV S2 glycoprotein internal membrane-active peptide. Biophysical characterization and membrane interaction
    • Guillen, J., Perez-Berna, A. J., Moreno, M. R., and Villalain, J. (2008) A second SARS-CoV S2 glycoprotein internal membrane-active peptide. Biophysical characterization and membrane interaction Biochemistry 47, 8214-8224
    • (2008) Biochemistry , vol.47 , pp. 8214-8224
    • Guillen, J.1    Perez-Berna, A.J.2    Moreno, M.R.3    Villalain, J.4
  • 25
    • 12344268838 scopus 로고    scopus 로고
    • The aromatic domain of the coronavirus class i viral fusion protein induces membrane permeabilization: Putative role during viral entry
    • Sainz, B, Jr., Rausch, J. M., Gallaher, W. R., Garry, R. F., and Wimley, W. C. (2005) The aromatic domain of the coronavirus class I viral fusion protein induces membrane permeabilization: putative role during viral entry Biochemistry 44, 947-958
    • (2005) Biochemistry , vol.44 , pp. 947-958
    • Sainz, Jr.B.1    Rausch, J.M.2    Gallaher, W.R.3    Garry, R.F.4    Wimley, W.C.5
  • 26
    • 34548212404 scopus 로고    scopus 로고
    • Locking the kink in the influenza hemagglutinin fusion domain structure
    • Lai, A. L. and Tamm, L. K. (2007) Locking the kink in the influenza hemagglutinin fusion domain structure J. Biol. Chem. 282, 23946-23956
    • (2007) J. Biol. Chem. , vol.282 , pp. 23946-23956
    • Lai, A.L.1    Tamm, L.K.2
  • 27
    • 0034892952 scopus 로고    scopus 로고
    • Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin
    • Han, X., Bushweller, J. H., Cafiso, D. S., and Tamm, L. K. (2001) Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin Nat. Struct. Biol. 8, 715-720
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 715-720
    • Han, X.1    Bushweller, J.H.2    Cafiso, D.S.3    Tamm, L.K.4
  • 28
    • 34547652634 scopus 로고    scopus 로고
    • Structure and plasticity of the human immunodeficiency virus gp41 fusion domain in lipid micelles and bilayers
    • Li, Y. and Tamm, L. K. (2007) Structure and plasticity of the human immunodeficiency virus gp41 fusion domain in lipid micelles and bilayers Biophys. J. 93, 876-885
    • (2007) Biophys. J. , vol.93 , pp. 876-885
    • Li, Y.1    Tamm, L.K.2
  • 29
    • 0035859948 scopus 로고    scopus 로고
    • The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles
    • Schibli, D. J., Montelaro, R. C., and Vogel, H. J. (2001) The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles Biochemistry 40, 9570-9580
    • (2001) Biochemistry , vol.40 , pp. 9570-9580
    • Schibli, D.J.1    Montelaro, R.C.2    Vogel, H.J.3
  • 30
    • 77954947285 scopus 로고    scopus 로고
    • The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface
    • Lorieau, J. L., Louis, J. M., and Bax, A. (2010) The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface Proc. Natl. Acad. Sci. U.S.A. 107, 11341-11346
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 11341-11346
    • Lorieau, J.L.1    Louis, J.M.2    Bax, A.3
  • 31
  • 32
    • 0034705463 scopus 로고    scopus 로고
    • The amino-terminal region of the fusion peptide of influenza virus hemagglutinin HA2 inserts into sodium dodecyl sulfate micelle with residues 16-18 at the aqueous boundary at acidic pH. Oligomerization and the conformational flexibility
    • Chang, D. K., Cheng, S. F., Deo, V., and Yang, S. H. (2000) The amino-terminal region of the fusion peptide of influenza virus hemagglutinin HA2 inserts into sodium dodecyl sulfate micelle with residues 16-18 at the aqueous boundary at acidic pH. Oligomerization and the conformational flexibility J. Biol. Chem. 275, 19150-19180
    • (2000) J. Biol. Chem. , vol.275 , pp. 19150-19180
    • Chang, D.K.1    Cheng, S.F.2    Deo, V.3    Yang, S.H.4
  • 33
  • 34
    • 78650317603 scopus 로고    scopus 로고
    • Major antiparallel and minor parallel β sheet populations detected in the membrane-associated human immunodeficiency virus fusion peptide
    • Schmick, S. D. and Weliky, D. P. (2010) Major antiparallel and minor parallel β sheet populations detected in the membrane-associated human immunodeficiency virus fusion peptide Biochemistry 49, 10623-10635
    • (2010) Biochemistry , vol.49 , pp. 10623-10635
    • Schmick, S.D.1    Weliky, D.P.2
  • 35
    • 70349304444 scopus 로고    scopus 로고
    • A strong correlation between fusogenicity and membrane insertion depth of the HIV fusion peptide
    • Qiang, W., Sun, Y., and Weliky, D. P. (2009) A strong correlation between fusogenicity and membrane insertion depth of the HIV fusion peptide Proc. Natl. Acad. Sci. U. S. A. 106, 15314-15319
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 15314-15319
    • Qiang, W.1    Sun, Y.2    Weliky, D.P.3
  • 36
    • 69549116106 scopus 로고    scopus 로고
    • Interaction of the dengue virus fusion peptide with membranes assessed by NMR: The essential role of the envelope protein Trp101 for membrane fusion
    • Melo, M. N., Sousa, F. J., Carneiro, F. A., Castanho, M. A., Valente, A. P., Almeida, F. C., Da-Poian, A. T., and Mohana-Borges, R. (2009) Interaction of the dengue virus fusion peptide with membranes assessed by NMR: the essential role of the envelope protein Trp101 for membrane fusion J. Mol. Biol. 392, 736-746
    • (2009) J. Mol. Biol. , vol.392 , pp. 736-746
    • Melo, M.N.1    Sousa, F.J.2    Carneiro, F.A.3    Castanho, M.A.4    Valente, A.P.5    Almeida, F.C.6    Da-Poian, A.T.7    Mohana-Borges, R.8
  • 38
    • 77953552629 scopus 로고    scopus 로고
    • Biology and pathogenesis of chikungunya virus
    • Schwartz, O. and Albert, M. L. (2010) Biology and pathogenesis of chikungunya virus Nat. Rev. Microbiol. 8, 491-500
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 491-500
    • Schwartz, O.1    Albert, M.L.2
  • 40
    • 0028088152 scopus 로고
    • The alphaviruses: Gene expression, replication and evolution
    • Strauss, J. H. and Strauss, E. G. (1994) The alphaviruses: gene expression, replication and evolution Microbiol. Rev. 58, 491-562
    • (1994) Microbiol. Rev. , vol.58 , pp. 491-562
    • Strauss, J.H.1    Strauss, E.G.2
  • 41
    • 0024455501 scopus 로고
    • The heterodimeric association between the membrane proteins of semliki forest virus changes its sensitivity to low pH during virus maturation
    • Wahlberg, J. M., Boere, W. A., and Garoff, H. (1989) The heterodimeric association between the membrane proteins of semliki forest virus changes its sensitivity to low pH during virus maturation J. Virol. 63, 4991-4997
    • (1989) J. Virol. , vol.63 , pp. 4991-4997
    • Wahlberg, J.M.1    Boere, W.A.2    Garoff, H.3
  • 42
    • 0022273625 scopus 로고
    • PH-induced alterations in the fusogenic spike protein of semliki forest virus
    • Kielian, M. and Helenius, A. (1985) pH-induced alterations in the fusogenic spike protein of semliki forest virus J. Cell Biol. 101, 2284-2291
    • (1985) J. Cell Biol. , vol.101 , pp. 2284-2291
    • Kielian, M.1    Helenius, A.2
  • 43
    • 0026495818 scopus 로고
    • Membrane fusion of Semliki Forest virus involves homotrimers of the fusion protein
    • Wahlberg, J. M., Bron, R., Wilschut, J., and Garoff, H. (1992) Membrane fusion of Semliki Forest virus involves homotrimers of the fusion protein J. Virol. 66, 7309-7318
    • (1992) J. Virol. , vol.66 , pp. 7309-7318
    • Wahlberg, J.M.1    Bron, R.2    Wilschut, J.3    Garoff, H.4
  • 44
    • 0035815282 scopus 로고    scopus 로고
    • The fusion glycoprotein shell of semliki forest virus: An icosahedral assembly primed for fusogenic activation at endosomal pH
    • Lescar, J., Roussel, A., Wien, M. W., Navaza, J., Fuller, S. D., Wengler, G., Wengler, G., and Rey, F. A. (2001) The fusion glycoprotein shell of semliki forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH Cell 105, 137-148
    • (2001) Cell , vol.105 , pp. 137-148
    • Lescar, J.1    Roussel, A.2    Wien, M.W.3    Navaza, J.4    Fuller, S.D.5    Wengler, G.6    Wengler, G.7    Rey, F.A.8
  • 45
    • 1642540249 scopus 로고    scopus 로고
    • Conformational change and protein-protein interactions of the fusion protein of semliki forest virus
    • Gibbons, D. L., Vaney, M. C., Roussel, A., Vigouroux, A., Reilly, B., Lepault, J., Kielian, M., and Rey, F. A. (2004) Conformational change and protein-protein interactions of the fusion protein of semliki forest virus Nature 427, 320-325
    • (2004) Nature , vol.427 , pp. 320-325
    • Gibbons, D.L.1    Vaney, M.C.2    Roussel, A.3    Vigouroux, A.4    Reilly, B.5    Lepault, J.6    Kielian, M.7    Rey, F.A.8
  • 47
    • 78649891889 scopus 로고    scopus 로고
    • Structural changes of envelope proteins during alphavirus fusion
    • Li, L., Jose, J., Xiang, Y., Kuhn, R. J., and Rossmann, M. G. (2010) Structural changes of envelope proteins during alphavirus fusion Nature 468, 705-708
    • (2010) Nature , vol.468 , pp. 705-708
    • Li, L.1    Jose, J.2    Xiang, Y.3    Kuhn, R.J.4    Rossmann, M.G.5
  • 48
    • 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
  • 49
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Guntert, P., Mumenthaler, C., and Wuthrich, K. (1997) Torsion angle dynamics for NMR structure calculation with the new program DYANA J. Mol. Biol. 273, 283-298
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 50
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R. A., Rullmannn, J. A., MacArthur, M. W., Kaptein, R., and Thornton, J. M. (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR J. Biomol. NMR 8, 477-486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 51
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley, W. C. and White, S. H. (1996) Experimentally determined hydrophobicity scale for proteins at membrane interfaces Nat. Struct. Biol. 3, 842-848
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 52
    • 0037881905 scopus 로고    scopus 로고
    • Interfacial anchor properties of tryptophan residues in transmembrane peptides can dominate over hydrophobic matching effects in peptide-lipid interactions
    • de Planque, M. R., Bonev, B. B., Demmers, J. A., Greathouse, D. V., Koeppe, R. E., Separovic, F., Watts, A., and Killian, J. A. (2003) Interfacial anchor properties of tryptophan residues in transmembrane peptides can dominate over hydrophobic matching effects in peptide-lipid interactions Biochemistry 42, 5341-5348
    • (2003) Biochemistry , vol.42 , pp. 5341-5348
    • De Planque, M.R.1    Bonev, B.B.2    Demmers, J.A.3    Greathouse, D.V.4    Koeppe, R.E.5    Separovic, F.6    Watts, A.7    Killian, J.A.8
  • 53
    • 69249155615 scopus 로고    scopus 로고
    • The role of solution NMR in the structure determinations of VDAC-1 and other membrane proteins
    • Hiller, S. and Wagner, G. (2009) The role of solution NMR in the structure determinations of VDAC-1 and other membrane proteins Curr. Opin. Struct. Biol. 19, 396-401
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 396-401
    • Hiller, S.1    Wagner, G.2
  • 54
    • 0035443197 scopus 로고    scopus 로고
    • Biophysical approaches to membrane protein structure determination
    • Arora, A. and Tamm, L. K. (2001) Biophysical approaches to membrane protein structure determination Curr. Opin. Struct. Biol. 11, 540-547
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 540-547
    • Arora, A.1    Tamm, L.K.2
  • 55
    • 16344378243 scopus 로고    scopus 로고
    • Mapping the interaction surface of a membrane protein: Unveiling the conformational switch of phospholamban in calcium pump regulation
    • Zamoon, J., Nitu, F., Karim, C., Thomas, D. D., and Veglia, G. (2005) Mapping the interaction surface of a membrane protein: unveiling the conformational switch of phospholamban in calcium pump regulation Proc. Natl. Acad. Sci. U. S. A. 102, 4747-4752
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 4747-4752
    • Zamoon, J.1    Nitu, F.2    Karim, C.3    Thomas, D.D.4    Veglia, G.5
  • 56
    • 0030067073 scopus 로고    scopus 로고
    • Surface location and orientation of lantibiotic nisin bound to membrane-mimicking micelles of dodecylphosphocholine and of sodium dodecylsulphate
    • Van-den-Hooven, H., Spronk, C., Van-de-Kamp, M., Konings, R., Hilbers, C. W., and Van-de-ven, F. (1996) Surface location and orientation of lantibiotic nisin bound to membrane-mimicking micelles of dodecylphosphocholine and of sodium dodecylsulphate Eur. J. Biochem. 235, 394-403
    • (1996) Eur. J. Biochem. , vol.235 , pp. 394-403
    • Van-Den-Hooven, H.1    Spronk, C.2    Van-De-Kamp, M.3    Konings, R.4    Hilbers, C.W.5    Van-De-Ven, F.6
  • 57
    • 3242655534 scopus 로고    scopus 로고
    • Membrane protein-lipid interactions in mixed micelles studied by NMR spectroscopy with the use of paramagnetic reagents
    • Hilty, C., Wider, G., Fernandez, C., and Wüthrich, K. (2004) Membrane protein-lipid interactions in mixed micelles studied by NMR spectroscopy with the use of paramagnetic reagents ChemBioChem 5, 467-473
    • (2004) ChemBioChem , vol.5 , pp. 467-473
    • Hilty, C.1    Wider, G.2    Fernandez, C.3    Wüthrich, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.