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Volumn 8, Issue 11, 2012, Pages

Exploring New Biological Functions of Amyloids: Bacteria Cell Agglutination Mediated by Host Protein Aggregation

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; EOSINOPHIL CATIONIC PROTEIN; LIPOSOME;

EID: 84870827284     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1003005     Document Type: Article
Times cited : (89)

References (57)
  • 1
    • 28044443162 scopus 로고    scopus 로고
    • Antibacterial peptides and proteins with multiple cellular targets
    • Otvos L Jr, (2005) Antibacterial peptides and proteins with multiple cellular targets. J Pept Sci 11: 697-706.
    • (2005) J Pept Sci , vol.11 , pp. 697-706
    • Otvos Jr., L.1
  • 3
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M, (2002) Antimicrobial peptides of multicellular organisms. Nature 415: 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 4
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • Hancock RE, Sahl HG, (2006) Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat Biotechnol 24: 1551-1557.
    • (2006) Nat Biotechnol , vol.24 , pp. 1551-1557
    • Hancock, R.E.1    Sahl, H.G.2
  • 5
    • 77950499848 scopus 로고    scopus 로고
    • Potential therapeutic application of host defense peptides
    • Zhang L, Falla TJ, (2010) Potential therapeutic application of host defense peptides. Methods Mol Biol 618: 303-327.
    • (2010) Methods Mol Biol , vol.618 , pp. 303-327
    • Zhang, L.1    Falla, T.J.2
  • 6
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
    • Brogden KA, (2005) Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 3: 238-250.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 7
    • 67649262183 scopus 로고    scopus 로고
    • Structure, membrane orientation, mechanism, and function of pexiganan-a highly potent antimicrobial peptide designed from magainin
    • Gottler LM, Ramamoorthy A, (2009) Structure, membrane orientation, mechanism, and function of pexiganan-a highly potent antimicrobial peptide designed from magainin. Biochim Biophys Acta 1788: 1680-1686.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1680-1686
    • Gottler, L.M.1    Ramamoorthy, A.2
  • 8
    • 70349318199 scopus 로고    scopus 로고
    • Fluorine-a new element in the design of membrane-active peptides
    • Marsh EN, Buer BC, Ramamoorthy A, (2009) Fluorine-a new element in the design of membrane-active peptides. Mol Biosyst 5: 1143-1147.
    • (2009) Mol Biosyst , vol.5 , pp. 1143-1147
    • Marsh, E.N.1    Buer, B.C.2    Ramamoorthy, A.3
  • 9
    • 67349241519 scopus 로고    scopus 로고
    • Beyond NMR spectra of antimicrobial peptides: dynamical images at atomic resolution and functional insights
    • Ramamoorthy A, (2009) Beyond NMR spectra of antimicrobial peptides: dynamical images at atomic resolution and functional insights. Solid State Nucl Magn Reson 35: 201-207.
    • (2009) Solid State Nucl Magn Reson , vol.35 , pp. 201-207
    • Ramamoorthy, A.1
  • 10
    • 78650348571 scopus 로고    scopus 로고
    • Limiting an antimicrobial peptide to the lipid-water interface enhances its bacterial membrane selectivity: a case study of MSI-367
    • Thennarasu S, Huang R, Lee DK, Yang P, Maloy L, et al. (2010) Limiting an antimicrobial peptide to the lipid-water interface enhances its bacterial membrane selectivity: a case study of MSI-367. Biochemistry 49: 10595-10605.
    • (2010) Biochemistry , vol.49 , pp. 10595-10605
    • Thennarasu, S.1    Huang, R.2    Lee, D.K.3    Yang, P.4    Maloy, L.5
  • 11
    • 84863332845 scopus 로고    scopus 로고
    • Lipopolysaccharide neutralization by antimicrobial peptides: a gambit in the innate host defense strategy
    • Pulido D, Nogues MV, Boix E, Torrent M, (2012) Lipopolysaccharide neutralization by antimicrobial peptides: a gambit in the innate host defense strategy. J Innate Immun 4: 327-336.
    • (2012) J Innate Immun , vol.4 , pp. 327-336
    • Pulido, D.1    Nogues, M.V.2    Boix, E.3    Torrent, M.4
  • 12
    • 84864561211 scopus 로고    scopus 로고
    • Discovering new in silico tools for antimicrobial Peptide prediction
    • Torrent M, Nogues MV, Boix E, (2012) Discovering new in silico tools for antimicrobial Peptide prediction. Curr Drug Targets 13: 1148-1157.
    • (2012) Curr Drug Targets , vol.13 , pp. 1148-1157
    • Torrent, M.1    Nogues, M.V.2    Boix, E.3
  • 13
    • 77958085274 scopus 로고    scopus 로고
    • Describing the mechanism of antimicrobial peptide action with the interfacial activity model
    • Wimley WC, (2010) Describing the mechanism of antimicrobial peptide action with the interfacial activity model. ACS Chem Biol 5: 905-917.
    • (2010) ACS Chem Biol , vol.5 , pp. 905-917
    • Wimley, W.C.1
  • 14
    • 80051785173 scopus 로고    scopus 로고
    • The expanding scope of antimicrobial peptide structures and their modes of action
    • Nguyen LT, Haney EF, Vogel HJ, (2011) The expanding scope of antimicrobial peptide structures and their modes of action. Trends Biotechnol 29: 464-472.
    • (2011) Trends Biotechnol , vol.29 , pp. 464-472
    • Nguyen, L.T.1    Haney, E.F.2    Vogel, H.J.3
  • 15
    • 77955312210 scopus 로고    scopus 로고
    • Amyloidogenic protein-membrane interactions: mechanistic insight from model systems
    • Butterfield SM, Lashuel HA, (2010) Amyloidogenic protein-membrane interactions: mechanistic insight from model systems. Angew Chem Int Ed Engl 49: 5628-5654.
    • (2010) Angew Chem Int Ed Engl , vol.49 , pp. 5628-5654
    • Butterfield, S.M.1    Lashuel, H.A.2
  • 16
    • 67649274356 scopus 로고    scopus 로고
    • Binding of amphipathic alpha-helical antimicrobial peptides to lipid membranes: lessons from temporins B and L
    • Mahalka AK, Kinnunen PK, (2009) Binding of amphipathic alpha-helical antimicrobial peptides to lipid membranes: lessons from temporins B and L. Biochim Biophys Acta. 1788: 1600-1609.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1600-1609
    • Mahalka, A.K.1    Kinnunen, P.K.2
  • 18
    • 34548494605 scopus 로고    scopus 로고
    • Membrane fragmentation by an amyloidogenic fragment of human Islet Amyloid Polypeptide detected by solid-state NMR spectroscopy of membrane nanotubes
    • Brender JR, Durr UH, Heyl D, Budarapu MB, Ramamoorthy A, (2007) Membrane fragmentation by an amyloidogenic fragment of human Islet Amyloid Polypeptide detected by solid-state NMR spectroscopy of membrane nanotubes. Biochim Biophys Acta 1768: 2026-2029.
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 2026-2029
    • Brender, J.R.1    Durr, U.H.2    Heyl, D.3    Budarapu, M.B.4    Ramamoorthy, A.5
  • 19
    • 71749109209 scopus 로고    scopus 로고
    • Helical conformation of the SEVI precursor peptide PAP248-286, a dramatic enhancer of HIV infectivity, promotes lipid aggregation and fusion
    • Brender JR, Hartman K, Gottler LM, Cavitt ME, Youngstrom DW, et al. (2009) Helical conformation of the SEVI precursor peptide PAP248-286, a dramatic enhancer of HIV infectivity, promotes lipid aggregation and fusion. Biophys J 97: 2474-2483.
    • (2009) Biophys J , vol.97 , pp. 2474-2483
    • Brender, J.R.1    Hartman, K.2    Gottler, L.M.3    Cavitt, M.E.4    Youngstrom, D.W.5
  • 20
    • 57049086457 scopus 로고    scopus 로고
    • A single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicity
    • Brender JR, Hartman K, Reid KR, Kennedy RT, Ramamoorthy A, (2008) A single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicity. Biochemistry 47: 12680-12688.
    • (2008) Biochemistry , vol.47 , pp. 12680-12688
    • Brender, J.R.1    Hartman, K.2    Reid, K.R.3    Kennedy, R.T.4    Ramamoorthy, A.5
  • 21
    • 43949107500 scopus 로고    scopus 로고
    • Amyloid fiber formation and membrane disruption are separate processes localized in two distinct regions of IAPP, the type-2-diabetes-related peptide
    • Brender JR, Lee EL, Cavitt MA, Gafni A, Steel DG, et al. (2008) Amyloid fiber formation and membrane disruption are separate processes localized in two distinct regions of IAPP, the type-2-diabetes-related peptide. J Am Chem Soc 130: 6424-6429.
    • (2008) J Am Chem Soc , vol.130 , pp. 6424-6429
    • Brender, J.R.1    Lee, E.L.2    Cavitt, M.A.3    Gafni, A.4    Steel, D.G.5
  • 22
    • 71749117350 scopus 로고    scopus 로고
    • NMR structure in a membrane environment reveals putative amyloidogenic regions of the SEVI precursor peptide PAP(248-286
    • Nanga RP, Brender JR, Vivekanandan S, Popovych N, Ramamoorthy A, (2009) NMR structure in a membrane environment reveals putative amyloidogenic regions of the SEVI precursor peptide PAP(248-286). J Am Chem Soc 131: 17972-17979.
    • (2009) J Am Chem Soc , vol.131 , pp. 17972-17979
    • Nanga, R.P.1    Brender, J.R.2    Vivekanandan, S.3    Popovych, N.4    Ramamoorthy, A.5
  • 23
    • 67650533782 scopus 로고    scopus 로고
    • Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy
    • Nanga RP, Brender JR, Xu J, Hartman K, Subramanian V, et al. (2009) Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy. J Am Chem Soc 131: 8252-8261.
    • (2009) J Am Chem Soc , vol.131 , pp. 8252-8261
    • Nanga, R.P.1    Brender, J.R.2    Xu, J.3    Hartman, K.4    Subramanian, V.5
  • 24
    • 84858973650 scopus 로고    scopus 로고
    • Site specific interaction of the polyphenol EGCG with the SEVI amyloid precursor peptide PAP(248-286
    • Popovych N, Brender JR, Soong R, Vivekanandan S, Hartman K, et al. (2012) Site specific interaction of the polyphenol EGCG with the SEVI amyloid precursor peptide PAP(248-286). J Phys Chem B 116: 3650-3658.
    • (2012) J Phys Chem B , vol.116 , pp. 3650-3658
    • Popovych, N.1    Brender, J.R.2    Soong, R.3    Vivekanandan, S.4    Hartman, K.5
  • 25
    • 13844308071 scopus 로고    scopus 로고
    • Membrane interactions of host-defense peptides studied in model systems
    • Jelinek R, Kolusheva S, (2005) Membrane interactions of host-defense peptides studied in model systems. Curr Protein Pept Sci 6: 103-114.
    • (2005) Curr Protein Pept Sci , vol.6 , pp. 103-114
    • Jelinek, R.1    Kolusheva, S.2
  • 26
    • 62949097134 scopus 로고    scopus 로고
    • Structure and mechanism of beta-hairpin antimicrobial peptides in lipid bilayers from solid-state NMR spectroscopy
    • Tang M, Hong M, (2009) Structure and mechanism of beta-hairpin antimicrobial peptides in lipid bilayers from solid-state NMR spectroscopy. Mol Biosyst 5: 317-322.
    • (2009) Mol Biosyst , vol.5 , pp. 317-322
    • Tang, M.1    Hong, M.2
  • 27
    • 80155128846 scopus 로고    scopus 로고
    • The generation of antimicrobial peptide activity: a trade-off between charge and aggregation?
    • Torrent M, Valle J, Nogues MV, Boix E, Andreu D, (2011) The generation of antimicrobial peptide activity: a trade-off between charge and aggregation? Angew Chem Int Ed Engl 50: 10686-10689.
    • (2011) Angew Chem Int Ed Engl , vol.50 , pp. 10686-10689
    • Torrent, M.1    Valle, J.2    Nogues, M.V.3    Boix, E.4    Andreu, D.5
  • 28
    • 77955578891 scopus 로고    scopus 로고
    • Eosinophil cationic protein aggregation: identification of an N-terminus amyloid prone region
    • Torrent M, Odorizzi F, Nogues MV, Boix E, (2010) Eosinophil cationic protein aggregation: identification of an N-terminus amyloid prone region. Biomacromolecules 11: 1983-1990.
    • (2010) Biomacromolecules , vol.11 , pp. 1983-1990
    • Torrent, M.1    Odorizzi, F.2    Nogues, M.V.3    Boix, E.4
  • 29
    • 79959651424 scopus 로고    scopus 로고
    • Antimicrobial protegrin-1 forms amyloid-like fibrils with rapid kinetics suggesting a functional link
    • Jang H, Arce FT, Mustata M, Ramachandran S, Capone R, et al. (2011) Antimicrobial protegrin-1 forms amyloid-like fibrils with rapid kinetics suggesting a functional link. Biophys J 100: 1775-1783.
    • (2011) Biophys J , vol.100 , pp. 1775-1783
    • Jang, H.1    Arce, F.T.2    Mustata, M.3    Ramachandran, S.4    Capone, R.5
  • 30
    • 77949830350 scopus 로고    scopus 로고
    • The Alzheimer's disease-associated amyloid beta-protein is an antimicrobial peptide
    • Soscia SJ, Kirby JE, Washicosky KJ, Tucker SM, Ingelsson M, et al. (2010) The Alzheimer's disease-associated amyloid beta-protein is an antimicrobial peptide. PLoS One 5: e9505.
    • (2010) PLoS One , vol.5
    • Soscia, S.J.1    Kirby, J.E.2    Washicosky, K.J.3    Tucker, S.M.4    Ingelsson, M.5
  • 31
    • 84860914111 scopus 로고    scopus 로고
    • Aberrant action of amyloidogenic host defense peptides: a new paradigm to investigate neurodegenerative disorders?
    • Harris F, Dennison SR, Phoenix DA, (2012) Aberrant action of amyloidogenic host defense peptides: a new paradigm to investigate neurodegenerative disorders? FASEB J 26: 1776-1781.
    • (2012) FASEB J , vol.26 , pp. 1776-1781
    • Harris, F.1    Dennison, S.R.2    Phoenix, D.A.3
  • 32
    • 79951801514 scopus 로고    scopus 로고
    • Connecting peptide physicochemical and antimicrobial properties by a rational prediction model
    • Torrent M, Andreu D, Nogues VM, Boix E, (2011) Connecting peptide physicochemical and antimicrobial properties by a rational prediction model. PLoS One 6: e16968.
    • (2011) PLoS One , vol.6
    • Torrent, M.1    Andreu, D.2    Nogues, V.M.3    Boix, E.4
  • 33
    • 55949094578 scopus 로고    scopus 로고
    • Design of bacteria-agglutinating peptides derived from parotid secretory protein, a member of the bactericidal/permeability increasing-like protein family
    • Gorr SU, Sotsky JB, Shelar AP, Demuth DR, (2008) Design of bacteria-agglutinating peptides derived from parotid secretory protein, a member of the bactericidal/permeability increasing-like protein family. Peptides 29: 2118-2127.
    • (2008) Peptides , vol.29 , pp. 2118-2127
    • Gorr, S.U.1    Sotsky, J.B.2    Shelar, A.P.3    Demuth, D.R.4
  • 34
    • 2642515362 scopus 로고    scopus 로고
    • Salivary proteins: protective and diagnostic value in cariology?
    • Van Nieuw Amerongen A, Bolscher JG, Veerman EC, (2004) Salivary proteins: protective and diagnostic value in cariology? Caries Res 38: 247-253.
    • (2004) Caries Res , vol.38 , pp. 247-253
    • van Nieuw Amerongen, A.1    Bolscher, J.G.2    Veerman, E.C.3
  • 35
    • 84860198236 scopus 로고    scopus 로고
    • Antimicrobial Action and Cell Agglutination by Eosinophil Cationic Protein Is Modulated by the Cell Wall Lipopolysaccharide Structure
    • Pulido D, Moussaoui M, Andreu D, Nogues MV, Torrent M, et al. (2012) Antimicrobial Action and Cell Agglutination by Eosinophil Cationic Protein Is Modulated by the Cell Wall Lipopolysaccharide Structure. Antimicrob Agents Chemother 56: 2378-2385.
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 2378-2385
    • Pulido, D.1    Moussaoui, M.2    Andreu, D.3    Nogues, M.V.4    Torrent, M.5
  • 37
    • 0032865118 scopus 로고    scopus 로고
    • Eosinophil cationic protein (ECP): molecular and biological properties and the use of ECP as a marker of eosinophil activation in disease
    • Venge P, Bystrom J, Carlson M, Hakansson L, Karawacjzyk M, et al. (1999) Eosinophil cationic protein (ECP): molecular and biological properties and the use of ECP as a marker of eosinophil activation in disease. Clin Exp Allergy 29: 1172-1186.
    • (1999) Clin Exp Allergy , vol.29 , pp. 1172-1186
    • Venge, P.1    Bystrom, J.2    Carlson, M.3    Hakansson, L.4    Karawacjzyk, M.5
  • 38
    • 84862259963 scopus 로고    scopus 로고
    • Structural determinants of the eosinophil cationic protein antimicrobial activity
    • Boix E, Salazar VA, Torrent M, Pulido D, Nogues MV, et al. (2012) Structural determinants of the eosinophil cationic protein antimicrobial activity. Biol Chem 393: 801-815.
    • (2012) Biol Chem , vol.393 , pp. 801-815
    • Boix, E.1    Salazar, V.A.2    Torrent, M.3    Pulido, D.4    Nogues, M.V.5
  • 39
    • 77949586101 scopus 로고    scopus 로고
    • Comparison of human RNase 3 and RNase 7 bactericidal action at the Gram-negative and Gram-positive bacterial cell wall
    • Torrent M, Badia M, Moussaoui M, Sanchez D, Nogues MV, et al. (2010) Comparison of human RNase 3 and RNase 7 bactericidal action at the Gram-negative and Gram-positive bacterial cell wall. FEBS J 277: 1713-1725.
    • (2010) FEBS J , vol.277 , pp. 1713-1725
    • Torrent, M.1    Badia, M.2    Moussaoui, M.3    Sanchez, D.4    Nogues, M.V.5
  • 40
    • 38549179303 scopus 로고    scopus 로고
    • The cytotoxicity of eosinophil cationic protein/ribonuclease 3 on eukaryotic cell lines takes place through its aggregation on the cell membrane
    • Navarro S, Aleu J, Jimenez M, Boix E, Cuchillo CM, et al. (2008) The cytotoxicity of eosinophil cationic protein/ribonuclease 3 on eukaryotic cell lines takes place through its aggregation on the cell membrane. Cell Mol Life Sci 65: 324-337.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 324-337
    • Navarro, S.1    Aleu, J.2    Jimenez, M.3    Boix, E.4    Cuchillo, C.M.5
  • 41
    • 40849124076 scopus 로고    scopus 로고
    • Eosinophil cationic protein high-affinity binding to bacteria-wall lipopolysaccharides and peptidoglycans
    • Torrent M, Navarro S, Moussaoui M, Nogues MV, Boix E, (2008) Eosinophil cationic protein high-affinity binding to bacteria-wall lipopolysaccharides and peptidoglycans. Biochemistry 47: 3544-3555.
    • (2008) Biochemistry , vol.47 , pp. 3544-3555
    • Torrent, M.1    Navarro, S.2    Moussaoui, M.3    Nogues, M.V.4    Boix, E.5
  • 42
    • 79960648548 scopus 로고    scopus 로고
    • Refining the eosinophil cationic protein antibacterial pharmacophore by rational structure minimization
    • Torrent M, Pulido D, de la Torre BG, Garcia-Mayoral MF, Nogues MV, et al. (2011) Refining the eosinophil cationic protein antibacterial pharmacophore by rational structure minimization. J Med Chem 54: 5237-5244.
    • (2011) J Med Chem , vol.54 , pp. 5237-5244
    • Torrent, M.1    Pulido, D.2    de la Torre, B.G.3    Garcia-Mayoral, M.F.4    Nogues, M.V.5
  • 43
    • 78651308063 scopus 로고    scopus 로고
    • Mapping the eosinophil cationic protein antimicrobial activity by chemical and enzymatic cleavage
    • Sanchez D, Moussaoui M, Carreras E, Torrent M, Nogues V, et al. (2011) Mapping the eosinophil cationic protein antimicrobial activity by chemical and enzymatic cleavage. Biochimie 93: 331-338.
    • (2011) Biochimie , vol.93 , pp. 331-338
    • Sanchez, D.1    Moussaoui, M.2    Carreras, E.3    Torrent, M.4    Nogues, V.5
  • 44
    • 84855164403 scopus 로고    scopus 로고
    • AMPA: an automated web server for prediction of protein antimicrobial regions
    • Torrent M, Di Tommaso P, Pulido D, Nogues MV, Notredame C, et al. (2012) AMPA: an automated web server for prediction of protein antimicrobial regions. Bioinformatics 28: 130-131.
    • (2012) Bioinformatics , vol.28 , pp. 130-131
    • Torrent, M.1    Di Tommaso, P.2    Pulido, D.3    Nogues, M.V.4    Notredame, C.5
  • 45
    • 71049173766 scopus 로고    scopus 로고
    • A theoretical approach to spot active regions in antimicrobial proteins
    • Torrent M, Nogues VM, Boix E, (2009) A theoretical approach to spot active regions in antimicrobial proteins. BMC Bioinformatics 10: 373.
    • (2009) BMC Bioinformatics , vol.10 , pp. 373
    • Torrent, M.1    Nogues, V.M.2    Boix, E.3
  • 46
    • 69249227505 scopus 로고    scopus 로고
    • Bactericidal and membrane disruption activities of the eosinophil cationic protein are largely retained in an N-terminal fragment
    • Torrent M, de la Torre BG, Nogues VM, Andreu D, Boix E, (2009) Bactericidal and membrane disruption activities of the eosinophil cationic protein are largely retained in an N-terminal fragment. Biochem J 421: 425-434.
    • (2009) Biochem J , vol.421 , pp. 425-434
    • Torrent, M.1    de la Torre, B.G.2    Nogues, V.M.3    Andreu, D.4    Boix, E.5
  • 47
    • 78650903471 scopus 로고    scopus 로고
    • Eosinophil cationic protein (ECP) can bind heparin and other glycosaminoglycans through its RNase active site
    • Torrent M, Nogues MV, Boix E, (2011) Eosinophil cationic protein (ECP) can bind heparin and other glycosaminoglycans through its RNase active site. J Mol Recognit 24: 90-100.
    • (2011) J Mol Recognit , vol.24 , pp. 90-100
    • Torrent, M.1    Nogues, M.V.2    Boix, E.3
  • 48
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • Kayed R, Sokolov Y, Edmonds B, McIntire TM, Milton SC, et al. (2004) Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. J Biol Chem 279: 46363-46366.
    • (2004) J Biol Chem , vol.279 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Edmonds, B.3    McIntire, T.M.4    Milton, S.C.5
  • 49
    • 22144455300 scopus 로고    scopus 로고
    • Surface behavior and lipid interaction of Alzheimer beta-amyloid peptide 1-42: a membrane-disrupting peptide
    • Ambroggio EE, Kim DH, Separovic F, Barrow CJ, Barnham KJ, et al. (2005) Surface behavior and lipid interaction of Alzheimer beta-amyloid peptide 1-42: a membrane-disrupting peptide. Biophys J 88: 2706-2713.
    • (2005) Biophys J , vol.88 , pp. 2706-2713
    • Ambroggio, E.E.1    Kim, D.H.2    Separovic, F.3    Barrow, C.J.4    Barnham, K.J.5
  • 50
    • 48249143665 scopus 로고    scopus 로고
    • Structural requirements for antimicrobial versus chemoattractant activities for dermaseptin S9
    • Auvynet C, El Amri C, Lacombe C, Bruston F, Bourdais J, et al. (2008) Structural requirements for antimicrobial versus chemoattractant activities for dermaseptin S9. FEBS J 275: 4134-4151.
    • (2008) FEBS J , vol.275 , pp. 4134-4151
    • Auvynet, C.1    El Amri, C.2    Lacombe, C.3    Bruston, F.4    Bourdais, J.5
  • 51
    • 84862693569 scopus 로고    scopus 로고
    • Systemic immune challenges trigger and drive Alzheimer-like neuropathology in mice
    • Krstic D, Madhusudan A, Doehner J, Vogel P, Notter T, et al. (2012) Systemic immune challenges trigger and drive Alzheimer-like neuropathology in mice. J Neuroinflammation 9: 151.
    • (2012) J Neuroinflammation , vol.9 , pp. 151
    • Krstic, D.1    Madhusudan, A.2    Doehner, J.3    Vogel, P.4    Notter, T.5
  • 52
    • 84856390353 scopus 로고    scopus 로고
    • Emerging roles of pathogens in Alzheimer disease
    • Miklossy J, (2011) Emerging roles of pathogens in Alzheimer disease. Expert Rev Mol Med 13: e30.
    • (2011) Expert Rev Mol Med , vol.13
    • Miklossy, J.1
  • 53
    • 33644816697 scopus 로고    scopus 로고
    • Dementia associated with infectious diseases
    • Almeida OP, Lautenschlager NT, (2005) Dementia associated with infectious diseases. Int Psychogeriatr 17 (Suppl 1):: S65-77.
    • (2005) Int Psychogeriatr , vol.17 , Issue.SUPPL. 1
    • Almeida, O.P.1    Lautenschlager, N.T.2
  • 54
    • 77956647384 scopus 로고    scopus 로고
    • Eosinophil-induced neurotoxicity: the role of eosinophil cationic protein/RNase 3
    • Navarro S, Boix E, Cuchillo CM, Nogues MV, (2010) Eosinophil-induced neurotoxicity: the role of eosinophil cationic protein/RNase 3. J Neuroimmunol 227: 60-70.
    • (2010) J Neuroimmunol , vol.227 , pp. 60-70
    • Navarro, S.1    Boix, E.2    Cuchillo, C.M.3    Nogues, M.V.4
  • 55
    • 0020419578 scopus 로고
    • The Gordon phenomenon induced by the eosinophil cationic protein and eosinophil protein X
    • Fredens K, Dahl R, Venge P, (1982) The Gordon phenomenon induced by the eosinophil cationic protein and eosinophil protein X. J Allergy Clin Immunol 70: 361-366.
    • (1982) J Allergy Clin Immunol , vol.70 , pp. 361-366
    • Fredens, K.1    Dahl, R.2    Venge, P.3
  • 56
    • 33846384399 scopus 로고    scopus 로고
    • Topography studies on the membrane interaction mechanism of the eosinophil cationic protein
    • Torrent M, Cuyas E, Carreras E, Navarro S, Lopez O, et al. (2007) Topography studies on the membrane interaction mechanism of the eosinophil cationic protein. Biochemistry 46: 720-733.
    • (2007) Biochemistry , vol.46 , pp. 720-733
    • Torrent, M.1    Cuyas, E.2    Carreras, E.3    Navarro, S.4    Lopez, O.5
  • 57
    • 65249140613 scopus 로고    scopus 로고
    • Comparison of the membrane interaction mechanism of two antimicrobial RNases: RNase 3/ECP and RNase 7
    • Torrent M, Sanchez D, Buzon V, Nogues MV, Cladera J, et al. (2009) Comparison of the membrane interaction mechanism of two antimicrobial RNases: RNase 3/ECP and RNase 7. Biochim Biophys Acta 1788: 1116-1125.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 1116-1125
    • Torrent, M.1    Sanchez, D.2    Buzon, V.3    Nogues, M.V.4    Cladera, J.5


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