메뉴 건너뛰기




Volumn 1808, Issue 10, 2011, Pages 2421-2427

Effects of positively charged arginine residues on membrane pore forming activity of Rev-NIS peptide in bacterial cells

Author keywords

Analog; Antibacterial peptide; HIV 1; Rev protein; Rev NIS

Indexed keywords

DITHIAZANINE IODIDE; FLUORESCEIN ISOTHIOCYANATE DEXTRAN; GLUTAMYLLEUCYLLEUCYLLYSYLALANYLVALYLARGINYLLEUCYLISOLEUCYLLYSINE; POLYPEPTIDE ANTIBIOTIC AGENT; REV NIS PEPTIDE; UNCLASSIFIED DRUG;

EID: 79960655427     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2011.06.024     Document Type: Article
Times cited : (13)

References (55)
  • 2
    • 19344372069 scopus 로고    scopus 로고
    • An emptying quiver: Antimicrobial drugs and resistance
    • J.T. Weber, and P. Courvalin An empting quiver: antimicrobial drugs and resistance Emerg. Infect. Dis. 11 2005 791 793 (Pubitemid 40720836)
    • (2005) Emerging Infectious Diseases , vol.11 , Issue.6 , pp. 791-793
    • Weber, J.T.1    Courvalin, P.2
  • 3
    • 27444440625 scopus 로고    scopus 로고
    • A review: Clinical significance of emergence of bacterial antimicrobial resistance in the hospital environment
    • DOI 10.1111/j.1365-2672.2005.02693.x
    • B. Cookson Clinical significance of emergence of bacterial antimicrobial resistance in the hospital environment J. Appl. Microbiol. 99 2005 989 996 (Pubitemid 41531290)
    • (2005) Journal of Applied Microbiology , vol.99 , Issue.5 , pp. 989-996
    • Cookson, B.1
  • 4
    • 5344246631 scopus 로고    scopus 로고
    • Emerging antimicrobial-resistant infection
    • K.L. Roos Emerging antimicrobial-resistant infection Arch. Neurol. 61 2004 1512 1514
    • (2004) Arch. Neurol. , vol.61 , pp. 1512-1514
    • Roos, K.L.1
  • 5
    • 33747595241 scopus 로고    scopus 로고
    • The epidemiological profile of infections with multidrug-resistant Pseudomonas aeruginosa and Acinetobacter species
    • D.L. Paterson The epidemiological profile of infections with multidrug-resistant Pseudomonas aeruginosa and Acinetobacter species Clin. Infect. Dis. 43 Suppl. 2 2006 S43 S48
    • (2006) Clin. Infect. Dis. , vol.43 , Issue.SUPPL. 2
    • Paterson, D.L.1
  • 6
    • 33745247409 scopus 로고    scopus 로고
    • Antimicrobial resistance in Gram-positive bacteria
    • L.B. Rice Antimicrobial resistance in Gram-positive bacteria Am. J. Infect. Control 34 5 Suppl. 1 2006 S11 S19
    • (2006) Am. J. Infect. Control , vol.34 , Issue.5 SUPPL. 1
    • Rice, L.B.1
  • 7
    • 0036217419 scopus 로고    scopus 로고
    • Antimicrobial resistance of foodborne pathogens
    • DOI 10.1016/S1286-4579(02)01554-X, PII S128645790201554X
    • D.G. White, S. Zhao, S. Simjee, D.D. Wagner, and P.F. McDermott Antimicrobial resistance of foodborne pathogens Microbes Infect. 4 2002 405 412 (Pubitemid 34270677)
    • (2002) Microbes and Infection , vol.4 , Issue.4 , pp. 405-412
    • White, D.G.1    Zhao, S.2    Simjee, S.3    Wagner, D.D.4    McDermott, P.F.5
  • 10
    • 33748947334 scopus 로고    scopus 로고
    • Detergent-like actions of linear amphipathic cationic antimicrobial peptides
    • DOI 10.1016/j.bbamem.2006.07.001, PII S0005273606002616
    • B. Bechinger, and K. Lohner Detergent-like actions of linear amphipathic cationic antimicrobial peptides Biochim. Biophys. Acta 1758 2006 1529 1539 (Pubitemid 44436087)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.9 , pp. 1529-1539
    • Bechinger, B.1    Lohner, K.2
  • 11
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • DOI 10.1038/415389a
    • M. Zasloff Antimicrobial peptides of multicellular organisms Nature 415 2002 389 395 (Pubitemid 34100944)
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1
  • 12
    • 0027973040 scopus 로고
    • The human immunodeficiency virus type 1 Rev protein shuttles between the cytoplasm and nuclear compartments
    • K.H. Kalland, A.M. Szilvay, K.A. Brokstad, W. Saetrevik, and G. Haukenes The human immunodeficiency virus type 1 Rev protein shuttles between the cytoplasm and nuclear compartments Mol. Cell. Biol. 14 1994 7436 7444 (Pubitemid 24326409)
    • (1994) Molecular and Cellular Biology , vol.14 , Issue.11 , pp. 7436-7444
    • Kalland, K.-H.1    Szilvay, A.M.2    Brokstad, K.A.3    Saetrevik, W.4    Haukenes, G.5
  • 13
    • 0028239268 scopus 로고
    • The HIV-1 Rev trans-activator shuttles between the nucleus and the cytoplasm
    • B.E. Meyer, and M.H. Malim The HIV-1 Rev trans-activator shuttles between the nucleus and the cytoplasm Genes Dev. 8 1994 1538 1547 (Pubitemid 24218288)
    • (1994) Genes and Development , vol.8 , Issue.13 , pp. 1538-1547
    • Meyer, B.E.1    Malim, M.H.2
  • 14
    • 0027993696 scopus 로고
    • HIV-1 Rev is capable of shuttling between the nucleus and cytoplasm
    • DOI 10.1006/viro.1994.1516
    • N. Richard, S. Iacampo, and A. Cochrane HIV-1 Rev is capable of shuttling between the nucleus and cytoplasm Virology 204 1994 123 131 (Pubitemid 24305324)
    • (1994) Virology , vol.204 , Issue.1 , pp. 123-131
    • Richard, N.1    Iacampo, S.2    Cochrane, A.3
  • 15
    • 0028916872 scopus 로고
    • Nucleocytoplasmic transport of the Rev protein of human immunodeficiency virus type 1 is dependent on the activation domain of the protein
    • B. Wolff, G. Cohen, J. Hauber, D. Meshcheryakova, and C. Rabeck Nucleocytoplasmic transport of the Rev protein of human immunodeficiency virus type 1 is dependent on the activation domain of the protein Exp. Cell Res. 217 1995 31 41
    • (1995) Exp. Cell Res. , vol.217 , pp. 31-41
    • Wolff, B.1    Cohen, G.2    Hauber, J.3    Meshcheryakova, D.4    Rabeck, C.5
  • 16
    • 0032499220 scopus 로고    scopus 로고
    • A cis-acting peptide signal in human immunodeficiency virus type I Rev which inhibits nuclear entry of small proteins
    • S. Kubota, and R.J. Pomerantz A cis-acting peptide signal in human immunodeficiency virus type I Rev which inhibits nuclear entry of small proteins Oncogene 16 1998 1851 1861 (Pubitemid 28197404)
    • (1998) Oncogene , vol.16 , Issue.14 , pp. 1851-1861
    • Kubota, S.1    Pomerantz, R.J.2
  • 17
    • 67349286175 scopus 로고    scopus 로고
    • Antifungal properties of a peptide derived from the signal peptide of the HIV-1 regulatory protein, Rev
    • J. Lee, and D.G. Lee Antifungal properties of a peptide derived from the signal peptide of the HIV-1 regulatory protein, Rev FEBS Lett. 583 2009 1544 1547
    • (2009) FEBS Lett. , vol.583 , pp. 1544-1547
    • Lee, J.1    Lee, D.G.2
  • 18
    • 0022699646 scopus 로고
    • Solid phase synthesis
    • B. Merrifield Solid phase synthesis Science 232 1986 341 347 (Pubitemid 16047587)
    • (1986) Science , vol.232 , Issue.4748 , pp. 341-347
    • Merrifield, B.1
  • 19
    • 0141838723 scopus 로고    scopus 로고
    • The fluorenymethoxycarbonyl group in solid phase synthesis
    • DOI 10.1002/psc.479
    • R. Sheppard The fluorenylmethoxycarbonyl group in solid phase synthesis J. Pept. Sci. 9 2003 545 552 (Pubitemid 37184483)
    • (2003) Journal of Peptide Science , vol.9 , Issue.9 , pp. 545-552
    • Sheppard, R.1
  • 20
    • 51949114856 scopus 로고    scopus 로고
    • Structure-antimicrobial activity relationship between pleurocidin and its enantiomer
    • J. Lee, and D.G. Lee Structure-antimicrobial activity relationship between pleurocidin and its enantiomer Exp. Mol. Med. 40 2008 370 376
    • (2008) Exp. Mol. Med. , vol.40 , pp. 370-376
    • Lee, J.1    Lee, D.G.2
  • 21
    • 33644790418 scopus 로고    scopus 로고
    • Structure-activity relationships of anti-HIV-1 peptides with disulfide linkage between d- and l-cysteine at positions i and i + 3, respectively, derived from HIV-1 gp41 C-peptide
    • M.K. Lee, H.K. Kim, T.Y. Lee, K.S. Hahm, and K.L. Kim Structure-activity relationships of anti-HIV-1 peptides with disulfide linkage between d- and l-cysteine at positions i and i + 3, respectively, derived from HIV-1 gp41 C-peptide Exp. Mol. Med. 38 2006 18 26
    • (2006) Exp. Mol. Med. , vol.38 , pp. 18-26
    • Lee, M.K.1    Kim, H.K.2    Lee, T.Y.3    Hahm, K.S.4    Kim, K.L.5
  • 22
    • 64549121168 scopus 로고    scopus 로고
    • Antibacterial and synergistic activity of isocryptomerin isolated from Selaginella tamariscina
    • J. Lee, Y. Choi, E.R. Woo, and D.G. Lee Antibacterial and synergistic activity of isocryptomerin isolated from Selaginella tamariscina J. Microbiol. Biotechnol. 19 2009 204 207
    • (2009) J. Microbiol. Biotechnol. , vol.19 , pp. 204-207
    • Lee, J.1    Choi, Y.2    Woo, E.R.3    Lee, D.G.4
  • 23
    • 33749071615 scopus 로고    scopus 로고
    • Different modes in antibiotic action of tritrpticin analogs, cathelicidin-derived Trp-rich and Pro/Arg-rich peptides
    • DOI 10.1016/j.bbamem.2006.06.007, PII S0005273606002173
    • S.T. Yang, S.Y. Shin, K.S. Hahm, and J.I. Kim Different modes in antibiotic action of tritrpticin analogs, cathelicidin-derived Trp-rich and Pro/Arg-rich peptides Biochim. Biophys. Acta 1758 2006 1580 1586 (Pubitemid 44466702)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.10 , pp. 1580-1586
    • Yang, S.-T.1    Shin, S.Y.2    Hahm, K.-S.3    Kim, J.I.4
  • 25
    • 38149030149 scopus 로고    scopus 로고
    • Amphipathic alpha-helical peptide, HP (2-20), and its analogues derived from Helicobacter pylori: Pore formation mechanism in various lipid compositions
    • S.C. Park, M.H. Kim, M.A. Hossain, S.Y. Shin, Y. Kim, L. Stella, J.D. Wade, Y. Park, and K.S. Hahm Amphipathic alpha-helical peptide, HP (2-20), and its analogues derived from Helicobacter pylori: pore formation mechanism in various lipid compositions Biochim. Biophys. Acta 1778 2008 229 241
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 229-241
    • Park, S.C.1    Kim, M.H.2    Hossain, M.A.3    Shin, S.Y.4    Kim, Y.5    Stella, L.6    Wade, J.D.7    Park, Y.8    Hahm, K.S.9
  • 26
    • 0015527253 scopus 로고
    • Bee and wasp venoms
    • E. Habermann Bee and wasp venoms Science 177 1972 314 322
    • (1972) Science , vol.177 , pp. 314-322
    • Habermann, E.1
  • 28
    • 0025217893 scopus 로고
    • The actions of melittin on membranes
    • C.E. Dempsey The actions of melittin on membranes Biochim. Biophys. Acta 1031 1990 143 161
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 143-161
    • Dempsey, C.E.1
  • 31
    • 0025852347 scopus 로고
    • Rev is necessary for translation but not cytoplasmic accumulation of HIV-1 vif, vpr, and env/vpu 2 RNAs
    • S.J. Arrigo, and I.S. Chen Rev is necessary for translation but not cytoplasmic accumulation of HIV-1 vif, vpr, and env/vpu 2 RNAs Genes Dev. 5 1991 808 819 (Pubitemid 21905998)
    • (1991) Genes and Development , vol.5 , Issue.5 , pp. 808-819
    • Arrigo, S.J.1    Chen, I.S.Y.2
  • 32
    • 0026591789 scopus 로고
    • The Rev protein of human immunodeficiency virus type 1 promotes polysomal association and translation of gag/pol and vpu/env mRNAs
    • D.M. D'Agostino, B.K. Felber, J.E. Harrison, and G.N. Pavlakis The Rev protein of human immunodeficiency virus type 1 promotes polysomal association and translation of gag/pol and vpu/env mRNAs Mol. Cell. Biol. 12 1992 1375 1386
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1375-1386
    • D'Agostino, D.M.1    Felber, B.K.2    Harrison, J.E.3    Pavlakis, G.N.4
  • 33
    • 0027981916 scopus 로고
    • Evidence that HIV-1 Rev directly promotes the nuclear export of unspliced RNA
    • U. Fischer, S. Meyer, M. Teufel, C. Heckel, R. Lührmann, and G. Rautmann Evidence that HIV-1 Rev directly promotes the nuclear export of unspliced RNA EMBO J. 13 1994 4105 4112 (Pubitemid 24275867)
    • (1994) EMBO Journal , vol.13 , Issue.17 , pp. 4105-4112
    • Fischer, U.1    Meyer, S.2    Teufel, M.3    Heckel, C.4    Luhrmann, R.5    Rautmann, G.6
  • 34
    • 0024518918 scopus 로고
    • The HIV-1 rev trans-activator acts through a structured target sequence to activate nuclear export of unspliced viral mRNA
    • DOI 10.1038/338254a0
    • M.H. Malim, J. Hauber, S.Y. Le, J.V. Maizel, and B.R. Cullen The HIV-1 rev trans-activator acts through a structured target sequence to activate nuclear export of unspliced viral mRNA Nature 338 1989 254 257 (Pubitemid 19086926)
    • (1989) Nature , vol.338 , Issue.6212 , pp. 254-257
    • Malim, M.H.1    Hauber, J.2    Le, S.-Y.3    Maizel, J.V.4    Cullen, B.R.5
  • 35
    • 0025882673 scopus 로고
    • Human immunodeficiency virus type 1 regulator of virion expression, rev, forms nucleoprotein filaments after binding to a purine-rich "bubble" located within the rev-responsive region of viral mRNAs
    • S. Heaphy, J.T. Finch, M.J. Gait, J. Karn, and M. Singh Human immunodeficiency virus type 1 regulator of virion expression, rev, forms nucleoprotein filaments after binding to a purine-rich "bubble" located within the rev-responsive region of viral mRNAs Proc. Natl. Acad. Sci. U.S.A. 88 1991 7366 7370 (Pubitemid 21915152)
    • (1991) Proceedings of the National Academy of Sciences of the United States of America , vol.88 , Issue.16 , pp. 7366-7370
    • Heaphy, S.1    Finch, J.T.2    Gait, M.J.3    Karn, J.4    Singh, M.5
  • 36
    • 0025818452 scopus 로고
    • HIV-1 structural gene expression requires the binding of multiple rev monomers to the viral RRE: Implications for HIV-1 latency
    • M.H. Malim, and B.R. Cullen HIV-1 structural gene expression requires the binding of multiple Rev monomers to the viral RRE: implications for HIV-1 latency Cell 65 1991 241 248 (Pubitemid 121006055)
    • (1991) Cell , vol.65 , Issue.2 , pp. 241-248
    • Malim, M.H.1    Cullen, B.R.2
  • 37
    • 0024310483 scopus 로고
    • Sequence-specific RNA binding by the HIV-1 Rev protein
    • DOI 10.1038/342714a0
    • M.L. Zapp, and M.R. Green Sequence-specific RNA binding by the HIV-1 Rev protein Nature 342 1989 714 716 (Pubitemid 20001594)
    • (1989) Nature , vol.342 , Issue.6250 , pp. 714-716
    • Zapp, M.L.1    Green, M.R.2
  • 38
    • 0024325692 scopus 로고
    • Functional similarity of HIV-I rev and HTLV-I rex proteins: Identification of a new nucleolar-targeting signal in rev protein
    • DOI 10.1016/0006-291X(89)90767-5
    • S. Kubota, H. Siomi, T. Satoh, S. Endo, M. Maki, and M. Hatanaka Functional similarity of HIV-I rev and HTLV-I rex proteins: identification of a new nucleolar-targeting signal in rev protein Biochem. Biophys. Res. Commun. 162 1989 963 970 (Pubitemid 19214678)
    • (1989) Biochemical and Biophysical Research Communications , vol.162 , Issue.3 , pp. 963-970
    • Kubota, S.1    Siomi, H.2    Satoh, T.3    Endo, S.4    Maki, M.5    Hatanaka, M.6
  • 39
    • 0029130169 scopus 로고
    • The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs
    • U. Fischer, J. Huber, W.C. Boelens, I.W. Mattaj, and R. Lührmann The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs Cell 82 1995 475 483
    • (1995) Cell , vol.82 , pp. 475-483
    • Fischer, U.1    Huber, J.2    Boelens, W.C.3    Mattaj, I.W.4    Lührmann, R.5
  • 40
    • 0028845313 scopus 로고
    • A nuclear export signal in hnRNP A1: A signal-mediated, temperature-dependent nuclear protein export pathway
    • W.M. Michael, M. Choi, and G. Dreyfuss A nuclear export signal in hnRNP A1: a signal-mediated, temperature-dependent nuclear protein export pathway Cell 83 1995 415 422
    • (1995) Cell , vol.83 , pp. 415-422
    • Michael, W.M.1    Choi, M.2    Dreyfuss, G.3
  • 41
    • 0029130168 scopus 로고
    • Identification of a signal for rapid export of proteins from the nucleus
    • W. Wen, J.L. Meinkoth, R.Y. Tsien, and S.S. Taylor Identification of a signal for rapid export of proteins from the nucleus Cell 82 1995 463 473
    • (1995) Cell , vol.82 , pp. 463-473
    • Wen, W.1    Meinkoth, J.L.2    Tsien, R.Y.3    Taylor, S.S.4
  • 42
    • 0030581089 scopus 로고    scopus 로고
    • The intestinal peptide carrier: A potential transport system for small peptide derived drugs
    • DOI 10.1016/0169-409X(95)00129-U
    • E. Walter, T. Kissel, and G.L. Amidon The intestinal peptide carrier: a potential transport system for small peptide derived drugs Adv. Drug Deliv. Rev. 20 1996 33 58 (Pubitemid 26281251)
    • (1996) Advanced Drug Delivery Reviews , vol.20 , Issue.1 , pp. 33-58
    • Walter, E.1    Kissel, T.2    Amidon, G.L.3
  • 43
    • 0001166311 scopus 로고
    • Transmembrane transport of small peptides
    • D.M. Matthews, and J.W. Payne Transmembrane transport of small peptides Curr. Top. Membr. 14 1980 331 425
    • (1980) Curr. Top. Membr. , vol.14 , pp. 331-425
    • Matthews, D.M.1    Payne, J.W.2
  • 44
    • 0032717887 scopus 로고    scopus 로고
    • The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy
    • B. Bechinger The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy Biochim. Biophys. Acta 1462 1999 157 183
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 157-183
    • Bechinger, B.1
  • 45
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Y. Shai Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides Biochim. Biophys. Acta 1462 1999 55 70
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 46
    • 0027978980 scopus 로고
    • Antibacterial peptides and mitochondrial presequences affect mitochondrial coupling, respiration and protein import
    • DOI 10.1111/j.1432-1033.1994.tb19081.x
    • M. Hugosson, D. Andreu, H.G. Boman, and E. Glaser Antibacterial peptides and mitochondrial presequences affect mitochondrial coupling, respiration and protein import Eur. J. Biochem. 223 1994 1027 1033 (Pubitemid 24263188)
    • (1994) European Journal of Biochemistry , vol.223 , Issue.3 , pp. 1027-1033
    • Hugosson, M.1    Andreu, D.2    Boman, H.G.3    Glaser, E.4
  • 48
    • 0030886178 scopus 로고    scopus 로고
    • The concentration-dependent membrane activity of cecropin A
    • DOI 10.1021/bi9630826
    • L. Silvestro, K. Gupta, J.N. Weiser, and P.H. Axelsen The concentration-dependent membrane activity of cecropin A Biochemistry 36 1997 11452 11460 (Pubitemid 27408628)
    • (1997) Biochemistry , vol.36 , Issue.38 , pp. 11452-11460
    • Silvestro, L.1    Gupta, K.2    Weiser, J.N.3    Axelsen, P.H.4
  • 49
    • 0020025608 scopus 로고
    • Kinetics and mechanism of hemolysis induced by melittin and by a synthetic melittin analogue
    • W.F. DeGrado, G.F. Musso, M. Lieber, E.T. Kaiser, and F.J. Kézdy Kinetics and mechanism of hemolysis induced by melittin and by a synthetic melittin analogue Biophys. J. 37 1982 329 338 (Pubitemid 12150026)
    • (1982) Biophysical Journal , vol.37 , Issue.1 , pp. 329-338
    • DeGrado, W.F.1    Musso, G.F.2    Lieber, M.3
  • 50
    • 0016188814 scopus 로고
    • Studies on the mechanism by which cyanine dyes measure membrane potential in red blood cells and phosphatidylcholine vesicles
    • P.J. Sims, A.S. Waggoner, C.H. Wang, and J.F. Hoffman Studies on the mechanism by which cyanine dyes measure membrane potential in red blood cells and phosphatidylcholine vesicles Biochemistry 13 1974 3315 3330
    • (1974) Biochemistry , vol.13 , pp. 3315-3330
    • Sims, P.J.1    Waggoner, A.S.2    Wang, C.H.3    Hoffman, J.F.4
  • 51
    • 0034424412 scopus 로고    scopus 로고
    • Interactions of bacterial cationic peptide antibiotics with outer and cytoplasmic membranes of Pseudomonas aeruginosa
    • DOI 10.1128/AAC.44.12.3317-3321.2000
    • L. Zhang, P. Dhillon, H. Yan, S. Farmer, and R.E. Hancock Interactions of bacterial cationic peptide antibiotics with outer and cytoplasmic membranes of Pseudomonas aeruginosa Antimicrob. Agents Chemother. 44 2000 3317 3321 (Pubitemid 33014325)
    • (2000) Antimicrobial Agents and Chemotherapy , vol.44 , Issue.12 , pp. 3317-3321
    • Zhang, L.1    Dhillon, P.2    Yan, H.3    Farmer, S.4    Hancock, R.E.W.5
  • 52
    • 14644412812 scopus 로고    scopus 로고
    • Phosphatidylethanolamine domains and localization of phospholipid synthases in Bacillus subtilis membranes
    • DOI 10.1128/JB.187.6.2163-2174.2005
    • A. Nishibori, J. Kusaka, H. Hara, M. Umeda, and K. Matsumoto Phosphatidylethanolamine domains and localization of phospholipid synthases in Bacillus subtilis membranes J. Bacteriol. 187 2005 2163 2174 (Pubitemid 40316247)
    • (2005) Journal of Bacteriology , vol.187 , Issue.6 , pp. 2163-2174
    • Nishibori, A.1    Kusaka, J.2    Hara, H.3    Umeda, M.4    Matsumoto, K.5
  • 53
    • 0035735521 scopus 로고    scopus 로고
    • Membrane lipid control of cytokinesis
    • DOI 10.1247/csf.26.659
    • K. Emoto, and M. Umeda Membrane lipid control of cytokinesis Cell Struct. Funct. 26 2001 659 665 (Pubitemid 34464434)
    • (2001) Cell Structure and Function , vol.26 , Issue.6 , pp. 659-665
    • Emoto, K.1    Umeda, M.2
  • 54
    • 0029765758 scopus 로고    scopus 로고
    • Release of lipid vesicle contents by an antibacterial cecropin A- melittin hybrid peptide
    • DOI 10.1021/bi953058c
    • J.M. Mancheño, M. Oñaderra, A. Martínez del Pozo, P. Díaz-Achirica, D. Andreu, L. Rivas, and J.G. Gavilanes Release of lipid vesicle contents by an antibacterial cecropin A-melittin hybrid peptide Biochemistry 35 1996 9892 9899 (Pubitemid 26303004)
    • (1996) Biochemistry , vol.35 , Issue.30 , pp. 9892-9899
    • Mancheno, J.M.1    Onaderra, M.2    Del Pozo, A.M.3    Diaz-Achirica, P.4    Andreu, D.5    Rivas, L.6    Gavilanes, J.G.7
  • 55
    • 0030049701 scopus 로고    scopus 로고
    • Pore formation induced by the peptide melittin in different lipid vesicle membranes
    • DOI 10.1016/0301-4622(95)00087-9
    • S. Rex Pore formation induced by the peptide melittin in different lipid vesicle membranes Biophys. Chem. 58 1996 75 85 (Pubitemid 26046709)
    • (1996) Biophysical Chemistry , vol.58 , Issue.1-2 , pp. 75-85
    • Rex, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.