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Volumn 1808, Issue 10, 2011, Pages 2581-2590

Cationic amphipathic peptides accumulate sialylated proteins and lipids in the plasma membrane of eukaryotic host cells

Author keywords

CAMPs; KLK; Plasma membrane accumulation; Sialic acids

Indexed keywords

ANTIMICROBIAL CATIONIC PEPTIDE; CALCIUM RELEASE ACTIVATED CALCIUM CHANNEL 1; CAVEOLIN 1; CD147 ANTIGEN; CD3 ANTIGEN; CD59 ANTIGEN; CD63 ANTIGEN; CD71 ANTIGEN; CHOLERA TOXIN B SUBUNIT; CLATHRIN LIGHT CHAIN; DEOXYRIBODIPYRIMIDINE PHOTOLYASE; FOLATE RECEPTOR; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; K RAS PROTEIN; LEUCINE; LEUKOSIALIN; LIPID; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 3; LYSINE; LYSYLLEUCYLLYSINE; MEMBRANE PROTEIN; PEPTIDE; PROTEIN KINASE FYN; PROTEIN KINASE LCK; PROTEIN TYROSINE KINASE; RAC1 PROTEIN; SIALIC ACID; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND RECEPTOR 3; UNCLASSIFIED DRUG;

EID: 80051787881     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2011.06.007     Document Type: Article
Times cited : (16)

References (72)
  • 1
    • 58149187882 scopus 로고    scopus 로고
    • APD2: The updated antimicrobial peptide database and its application in peptide design
    • G. Wang, X. Li, and Z. Wang APD2: the updated antimicrobial peptide database and its application in peptide design Nucleic Acids Res. 37 2009 D933 D937
    • (2009) Nucleic Acids Res. , vol.37
    • Wang, G.1    Li, X.2    Wang, Z.3
  • 2
    • 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
  • 3
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • DOI 10.1038/nrmicro1098
    • K.A. Brogden Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3 2005 238 250 (Pubitemid 40298223)
    • (2005) Nature Reviews Microbiology , vol.3 , Issue.3 , pp. 238-250
    • Brogden, K.A.1
  • 4
    • 0032006153 scopus 로고    scopus 로고
    • Instruments of microbial warfare: Bacteriocin synthesis, toxicity and immunity
    • DOI 10.1016/S0966-842X(97)01196-7, PII S0966842X97011967
    • T. Baba, and O. Schneewind Instruments of microbial warfare: bacteriocin synthesis, toxicity and immunity Trends Microbiol. 6 1998 66 71 (Pubitemid 28080754)
    • (1998) Trends in Microbiology , vol.6 , Issue.2 , pp. 66-71
    • Baba, T.1    Schneewind, O.2
  • 5
    • 11344267777 scopus 로고    scopus 로고
    • Insect antimicrobial peptides: Structures, properties and gene regulation
    • DOI 10.2174/0929866053406011
    • P. Bulet, and R. Stocklin Insect antimicrobial peptides: structures, properties and gene regulation Protein Pept. Lett. 12 2005 3 11 (Pubitemid 40071927)
    • (2005) Protein and Peptide Letters , vol.12 , Issue.1 , pp. 3-11
    • Bulet, P.1    Stocklin, R.2
  • 6
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: Antimicrobial peptides of innate immunity
    • DOI 10.1038/nri1180
    • T. Ganz Defensins: antimicrobial peptides of innate immunity Nat. Rev. Immunol. 3 2003 710 720 (Pubitemid 41070812)
    • (2003) Nature Reviews Immunology , vol.3 , Issue.9 , pp. 710-720
    • Ganz, T.1
  • 9
    • 0033377813 scopus 로고    scopus 로고
    • Neutrophil antibacterial peptides, multifunctional effector molecules in the mammalian immune system
    • DOI 10.1016/S0022-1759(99)00152-0, PII S0022175999001520
    • G.H. Gudmundsson, and B. Agerberth Neutrophil antibacterial peptides, multifunctional effector molecules in the mammalian immune system J. Immunol. Methods 232 1999 45 54 (Pubitemid 30017764)
    • (1999) Journal of Immunological Methods , vol.232 , Issue.1-2 , pp. 45-54
    • Gudmundsson, G.H.1    Agerberth, B.2
  • 10
    • 0036467390 scopus 로고    scopus 로고
    • Defensins of vertebrate animals
    • DOI 10.1016/S0952-7915(01)00303-X
    • R.I. Lehrer, and T. Ganz Defensins of vertebrate animals Curr. Opin. Immunol. 14 2002 96 102 (Pubitemid 34085112)
    • (2002) Current Opinion in Immunology , vol.14 , Issue.1 , pp. 96-102
    • Lehrer, R.I.1    Ganz, T.2
  • 11
    • 0036379140 scopus 로고    scopus 로고
    • Cathelicidins, essential gene-encoded mammalian antibiotics
    • M. Zaiou, and R.L. Gallo Cathelicidins, essential gene-encoded mammalian antibiotics J. Mol. Med. 80 2002 549 561
    • (2002) J. Mol. Med. , vol.80 , pp. 549-561
    • Zaiou, M.1    Gallo, R.L.2
  • 13
    • 57049185166 scopus 로고    scopus 로고
    • De novo designed synthetic mimics of antimicrobial peptides
    • R.W. Scott, W.F. DeGrado, and G.N. Tew De novo designed synthetic mimics of antimicrobial peptides Curr. Opin. Biotechnol. 19 2008 620 627
    • (2008) Curr. Opin. Biotechnol. , vol.19 , pp. 620-627
    • Scott, R.W.1    Degrado, W.F.2    Tew, G.N.3
  • 14
    • 78649813603 scopus 로고    scopus 로고
    • Optimization and high-throughput screening of antimicrobial peptides
    • S.E. Blondelle, and K. Lohner Optimization and high-throughput screening of antimicrobial peptides Curr. Pharm. Des. 16 2010 3204 3211
    • (2010) Curr. Pharm. Des. , vol.16 , pp. 3204-3211
    • Blondelle, S.E.1    Lohner, K.2
  • 15
    • 0031034840 scopus 로고    scopus 로고
    • Differential scanning microcalorimetry indicates that human defensin, HNP-2, interacts specifically with biomembrane mimetic systems
    • DOI 10.1021/bi961300p
    • K. Lohner, A. Latal, R.I. Lehrer, and T. Ganz Differential scanning microcalorimetry indicates that human defensin, HNP-2, interacts specifically with biomembrane mimetic systems Biochemistry 36 1997 1525 1531 (Pubitemid 27074977)
    • (1997) Biochemistry , vol.36 , Issue.6 , pp. 1525-1531
    • Lohner, K.1    Latal, A.2    Lehrer, R.I.3    Ganz, T.4
  • 16
    • 16844362681 scopus 로고    scopus 로고
    • Molecular mechanisms of membrane perturbation by antimicrobial peptides and the use of biophysical studies in the design of novel peptide antibiotics
    • DOI 10.2174/1386207053764576
    • K. Lohner, and S.E. Blondelle Molecular mechanisms of membrane perturbation by antimicrobial peptides and the use of biophysical studies in the design of novel peptide antibiotics Comb. Chem. High Throughput Screen. 8 2005 241 256 (Pubitemid 40488604)
    • (2005) Combinatorial Chemistry and High Throughput Screening , vol.8 , Issue.3 , pp. 241-256
    • Lohner, K.1    Blondelle, S.E.2
  • 17
    • 0032693639 scopus 로고    scopus 로고
    • Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes
    • K. Matsuzaki Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes Biochim. Biophys. Acta 1462 1999 1 10
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 1-10
    • Matsuzaki, K.1
  • 18
    • 65249190283 scopus 로고    scopus 로고
    • Lantibiotics: Diverse activities and unique modes of action
    • S.M. Asaduzzaman, and K. Sonomoto Lantibiotics: diverse activities and unique modes of action J. Biosci. Bioeng. 107 2009 475 487
    • (2009) J. Biosci. Bioeng. , vol.107 , pp. 475-487
    • Asaduzzaman, S.M.1    Sonomoto, K.2
  • 19
    • 70350435548 scopus 로고    scopus 로고
    • Multifunctional host defense peptides: Intracellular-targeting antimicrobial peptides
    • P. Nicolas Multifunctional host defense peptides: intracellular-targeting antimicrobial peptides FEBS J. 276 2009 6483 6496
    • (2009) FEBS J. , vol.276 , pp. 6483-6496
    • Nicolas, P.1
  • 20
    • 33749006591 scopus 로고    scopus 로고
    • The human beta-defensin-3, an antibacterial peptide with multiple biological functions
    • DOI 10.1016/j.bbamem.2006.07.007, PII S0005273606002690
    • V. Dhople, A. Krukemeyer, and A. Ramamoorthy The human beta-defensin-3, an antibacterial peptide with multiple biological functions Biochim. Biophys. Acta 1758 2006 1499 1512 (Pubitemid 44444831)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.9 , pp. 1499-1512
    • Dhople, V.1    Krukemeyer, A.2    Ramamoorthy, A.3
  • 21
    • 33748935159 scopus 로고    scopus 로고
    • LL-37, the only human member of the cathelicidin family of antimicrobial peptides
    • DOI 10.1016/j.bbamem.2006.03.030, PII S000527360600126X
    • U.H. Durr, U.S. Sudheendra, and A. Ramamoorthy LL-37, the only human member of the cathelicidin family of antimicrobial peptides Biochim. Biophys. Acta 1758 2006 1408 1425 (Pubitemid 44436081)
    • (2006) Biochimica et Biophysica Acta - Biomembranes , vol.1758 , Issue.9 , pp. 1408-1425
    • Durr, U.H.N.1    Sudheendra, U.S.2    Ramamoorthy, A.3
  • 22
    • 58149263244 scopus 로고    scopus 로고
    • The roles of cathelicidin LL-37 in immune defences and novel clinical applications
    • A. Nijnik, and R.E. Hancock The roles of cathelicidin LL-37 in immune defences and novel clinical applications Curr. Opin. Hematol. 16 2009 41 47
    • (2009) Curr. Opin. Hematol. , vol.16 , pp. 41-47
    • Nijnik, A.1    Hancock, R.E.2
  • 23
    • 0028088351 scopus 로고
    • Novel synthetic antimicrobial peptides effective against methicillin-resistant Staphylococcus aureus
    • J. Alvarez-Bravo, S. Kurata, and S. Natori Novel synthetic antimicrobial peptides effective against methicillin-resistant Staphylococcus aureus Biochem. J. 302 Pt 2 1994 535 538 (Pubitemid 24280109)
    • (1994) Biochemical Journal , vol.302 , Issue.2 , pp. 535-538
    • Alvarez-Bravo, J.1    Kurata, S.2    Natori, S.3
  • 25
    • 0033572799 scopus 로고    scopus 로고
    • 2, via cell surface calreticulin
    • DOI 10.1046/j.1432-1327.1999.00920.x
    • J.H. Cho, K. Homma, S. Kanegasaki, and S. Natori Activation of human neutrophils by a synthetic anti-microbial peptide, KLKLLLLLKLK-NH2, via cell surface calreticulin Eur. J. Biochem. 266 1999 878 885 (Pubitemid 30010105)
    • (1999) European Journal of Biochemistry , vol.266 , Issue.3 , pp. 878-885
    • Cho, J.-H.1    Homma, K.-I.2    Kanegasaki, S.3    Natori, S.4
  • 26
    • 0034993230 scopus 로고    scopus 로고
    • Activation of human monocyte cell line U937 via cell surface calreticulin
    • DOI 10.1379/1466-1268(2001)006<0148:AOHMCL>2.0.CO;2
    • J.H. Cho, K.J. Homma, S. Kanegasaki, and S. Natori Activation of human monocyte cell line U937 via cell surface calreticulin Cell Stress Chaperones 6 2001 148 152 (Pubitemid 32522221)
    • (2001) Cell Stress and Chaperones , vol.6 , Issue.2 , pp. 148-152
    • Cho, J.-H.1    Homma, K.J.2    Kanegasaki, S.3    Natori, S.4
  • 27
    • 0030756736 scopus 로고    scopus 로고
    • Chemotherapeutic activity of synthetic antimicrobial peptides: Correlation between chemotherapeutic activity and. Neutrophil-activating activity
    • DOI 10.1016/S0014-5793(97)01101-0, PII S0014579397011010
    • Y. Nakajima, J. Alvarez-Bravo, J. Cho, K. Homma, S. Kanegasaki, and S. Natori Chemotherapeutic activity of synthetic antimicrobial peptides: correlation between chemotherapeutic activity and neutrophil-activating activity FEBS Lett. 415 1997 64 66 (Pubitemid 27402050)
    • (1997) FEBS Letters , vol.415 , Issue.1 , pp. 64-66
    • Nakajima, Y.1    Alvarez-Bravo, J.2    Cho, J.-H.3    Homma, K.-I.4    Kanegasaki, S.5    Natori, S.6
  • 28
    • 4043049496 scopus 로고    scopus 로고
    • H2-type immune response to co-injected antigens
    • DOI 10.1016/j.vaccine.2004.03.007, PII S0264410X0400218X
    • J.H. Fritz, S. Brunner, M.L. Birnstiel, M. Buschle, A. Gabain, F. Mattner, and W. Zauner The artificial antimicrobial peptide KLKLLLLLKLK induces predominantly a TH2-type immune response to co-injected antigens Vaccine 22 2004 3274 3284 (Pubitemid 39078743)
    • (2004) Vaccine , vol.22 , Issue.25-26 , pp. 3274-3284
    • Fritz, J.H.1    Brunner, S.2    Birnstiel, M.L.3    Buschle, M.4    Gabain, A.V.5    Mattner, F.6    Zauner, W.7
  • 29
    • 77957309561 scopus 로고    scopus 로고
    • Antimicrobial and immunostimulatory peptide, KLK, induces an increase in cytosolic Ca2+ concentration by mobilizing Ca2+ from intracellular stores
    • J. Weghuber, A.M. Lipp, J. Stadlbauer, M.C. Aichinger, V. Ruprecht, A. Sonnleitner, G.J. Schutz, and T. Henics Antimicrobial and immunostimulatory peptide, KLK, induces an increase in cytosolic Ca2+ concentration by mobilizing Ca2+ from intracellular stores Cell Biol. Int. 34 11 2010 1109 1112
    • (2010) Cell Biol. Int. , vol.34 , Issue.11 , pp. 1109-1112
    • Weghuber, J.1    Lipp, A.M.2    Stadlbauer, J.3    Aichinger, M.C.4    Ruprecht, V.5    Sonnleitner, A.6    Schutz, G.J.7    Henics, T.8
  • 30
    • 78650522411 scopus 로고    scopus 로고
    • Adjuvating the adjuvant: Facilitated delivery of an immunomodulatory oligonucleotide to TLR9 by a cationic antimicrobial peptide in dendritic cells
    • M.C. Aichinger, M. Ginzler, J. Weghuber, L. Zimmermann, K. Riedl, G. Schutz, E. Nagy, G.A. von, R. Schweyen, and T. Henics Adjuvating the adjuvant: facilitated delivery of an immunomodulatory oligonucleotide to TLR9 by a cationic antimicrobial peptide in dendritic cells Vaccine 29 2011 426 436
    • (2011) Vaccine , vol.29 , pp. 426-436
    • Aichinger, M.C.1    Ginzler, M.2    Weghuber, J.3    Zimmermann, L.4    Riedl, K.5    Schutz, G.6    Nagy, E.7    Von, G.A.8    Schweyen, R.9    Henics, T.10
  • 32
    • 60749118913 scopus 로고    scopus 로고
    • Antimicrobial peptides: Linking partition, activity and high membrane-bound concentrations
    • M.N. Melo, R. Ferre, and M.A. Castanho Antimicrobial peptides: linking partition, activity and high membrane-bound concentrations Nat. Rev. Microbiol. 7 2009 245 250
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 245-250
    • Melo, M.N.1    Ferre, R.2    Castanho, M.A.3
  • 33
    • 0035496012 scopus 로고    scopus 로고
    • Cationic peptides: Effectors in innate immunity and novel antimicrobials
    • DOI 10.1016/S1473-3099(01)00092-5, PII S1473309901000925
    • R.E. Hancock Cationic peptides: effectors in innate immunity and novel antimicrobials Lancet Infect. Dis. 1 2001 156 164 (Pubitemid 33586049)
    • (2001) Lancet Infectious Diseases , vol.1 , Issue.3 , pp. 156-164
    • Hancock, R.E.1
  • 35
    • 0032454840 scopus 로고    scopus 로고
    • Structure-function relationships of antimicrobial peptides
    • P.M. Hwang, and H.J. Vogel Structure-function relationships of antimicrobial peptides Biochem. Cell Biol. 76 1998 235 246 (Pubitemid 29102008)
    • (1998) Biochemistry and Cell Biology , vol.76 , Issue.2-3 , pp. 235-246
    • Hwang, P.M.1    Vogel, H.J.2
  • 36
    • 34548650215 scopus 로고    scopus 로고
    • Membrane insertion and bilayer perturbation by antimicrobial peptide CM15
    • DOI 10.1529/biophysj.107.104034
    • S. Pistolesi, R. Pogni, and J.B. Feix Membrane insertion and bilayer perturbation by antimicrobial peptide CM15 Biophys. J. 93 2007 1651 1660 (Pubitemid 47403306)
    • (2007) Biophysical Journal , vol.93 , Issue.5 , pp. 1651-1660
    • Pistolesi, S.1    Pogni, R.2    Feix, J.B.3
  • 37
    • 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
    • S. Thennarasu, R. Huang, D.K. Lee, P. Yang, L. Maloy, Z. Chen, and A. Ramamoorthy Limiting an antimicrobial peptide to the lipid-water interface enhances its bacterial membrane selectivity: a case study of MSI-367 Biochemistry 49 2010 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    Chen, Z.6    Ramamoorthy, A.7
  • 41
    • 65949108219 scopus 로고    scopus 로고
    • Two-stage focus-hold system for rapid ultra-sensitive read-out of large-area biochips
    • C. Hesch, J. Hesse, J. Jacak, and G.J. Schutz Two-stage focus-hold system for rapid ultra-sensitive read-out of large-area biochips J. Microsc. 234 2009 251 254
    • (2009) J. Microsc. , vol.234 , pp. 251-254
    • Hesch, C.1    Hesse, J.2    Jacak, J.3    Schutz, G.J.4
  • 43
    • 45249087468 scopus 로고    scopus 로고
    • Rapid microwave fixation of cell monolayers preserves microtubule- associated cell structures
    • DOI 10.1369/jhc.7A7370.2008
    • S. Reipert, H. Kotisch, B. Wysoudil, and G. Wiche Rapid microwave fixation of cell monolayers preserves microtubule-associated cell structures J. Histochem. Cytochem. 56 2008 697 709 (Pubitemid 351842423)
    • (2008) Journal of Histochemistry and Cytochemistry , vol.56 , Issue.7 , pp. 697-709
    • Reipert, S.1    Kotisch, H.2    Wysoudil, B.3    Wiche, G.4
  • 44
    • 0031764539 scopus 로고    scopus 로고
    • The Roman god Janus: A paradigm for the function of CD43
    • DOI 10.1016/S0167-5699(98)01343-7, PII S0167569998013437
    • J.R. Ostberg, R.K. Barth, and J.G. Frelinger The Roman god Janus: a paradigm for the function of CD43 Immunol. Today 19 1998 546 550 (Pubitemid 28557116)
    • (1998) Immunology Today , vol.19 , Issue.12 , pp. 546-550
    • Ostberg, J.R.1    Barth, R.K.2    Frelinger, J.G.3
  • 45
    • 36349019291 scopus 로고    scopus 로고
    • Enhanced N-glycosylation site analysis of sialoglycopeptides by strong cation exchange prefractionation applied to platelet plasma membranes
    • DOI 10.1074/mcp.M600390-MCP200
    • U. Lewandrowski, R.P. Zahedi, J. Moebius, U. Walter, and A. Sickmann Enhanced N-glycosylation site analysis of sialoglycopeptides by strong cation exchange prefractionation applied to platelet plasma membranes Mol. Cell. Proteomics 6 2007 1933 1941 (Pubitemid 350201869)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.11 , pp. 1933-1941
    • Lewandrowski, U.1    Zahedi, R.P.2    Moebius, J.3    Walter, U.4    Sickmann, A.5
  • 46
    • 0025237554 scopus 로고
    • Interaction of the unique N-terminal region of tyrosine kinase p56lck with cytoplasmic domains of CD4 and CD8 is mediated by cysteine motifs
    • J.M. Turner, M.H. Brodsky, B.A. Irving, S.D. Levin, R.M. Perlmutter, and D.R. Littman Interaction of the unique N-terminal region of tyrosine kinase p56lck with cytoplasmic domains of CD4 and CD8 is mediated by cysteine motifs Cell 60 1990 755 765
    • (1990) Cell , vol.60 , pp. 755-765
    • Turner, J.M.1    Brodsky, M.H.2    Irving, B.A.3    Levin, S.D.4    Perlmutter, R.M.5    Littman, D.R.6
  • 47
    • 7944231534 scopus 로고    scopus 로고
    • Function of the Src-family kinases, Lck and Fyn, in T-cell development and activation
    • DOI 10.1038/sj.onc.1208074
    • E.H. Palacios, and A. Weiss Function of the Src-family kinases, Lck and Fyn, in T-cell development and activation Oncogene 23 2004 7990 8000 (Pubitemid 39468856)
    • (2004) Oncogene , vol.23 , Issue.48 REV. ISS. 7 , pp. 7990-8000
    • Palacios, E.H.1    Weiss, A.2
  • 48
    • 34250851923 scopus 로고    scopus 로고
    • Coassembly of Flotillins Induces Formation of Membrane Microdomains, Membrane Curvature, and Vesicle Budding
    • DOI 10.1016/j.cub.2007.05.078, PII S0960982207015138
    • M. Frick, N.A. Bright, K. Riento, A. Bray, C. Merrified, and B.J. Nichols Coassembly of flotillins induces formation of membrane microdomains, membrane curvature, and vesicle budding Curr. Biol. 17 2007 1151 1156 (Pubitemid 46990891)
    • (2007) Current Biology , vol.17 , Issue.13 , pp. 1151-1156
    • Frick, M.1    Bright, N.A.2    Riento, K.3    Bray, A.4    Merrified, C.5    Nichols, B.J.6
  • 50
    • 3242824311 scopus 로고
    • Transferrin receptor and its recycling in HeLa cells
    • J.D. Bleil, and M.S. Bretscher Transferrin receptor and its recycling in HeLa cells EMBO J. 1 1982 351 355
    • (1982) EMBO J. , vol.1 , pp. 351-355
    • Bleil, J.D.1    Bretscher, M.S.2
  • 52
    • 21644447229 scopus 로고    scopus 로고
    • Basigin (EMMPRIN/CD147) interacts with integrin to affect cellular architecture
    • DOI 10.1242/jcs.02408
    • K.D. Curtin, I.A. Meinertzhagen, and R.J. Wyman Basigin (EMMPRIN/CD147) interacts with integrin to affect cellular architecture J. Cell Sci. 118 2005 2649 2660 (Pubitemid 40932890)
    • (2005) Journal of Cell Science , vol.118 , Issue.12 , pp. 2649-2660
    • Curtin, K.D.1    Meinertzhagen, I.A.2    Wyman, R.J.3
  • 53
    • 0033295671 scopus 로고    scopus 로고
    • Class B scavenger receptors, caveolae and cholesterol homeostasis
    • G.A. Graf, S.V. Matveev, and E.J. Smart Class B scavenger receptors, caveolae and cholesterol homeostasis Trends Cardiovasc. Med. 9 1999 221 225
    • (1999) Trends Cardiovasc. Med. , vol.9 , pp. 221-225
    • Graf, G.A.1    Matveev, S.V.2    Smart, E.J.3
  • 54
    • 70350350296 scopus 로고    scopus 로고
    • Hierarchical role of CD3 chains in thymocyte development
    • V.P. Dave Hierarchical role of CD3 chains in thymocyte development Immunol. Rev. 232 2009 22 33
    • (2009) Immunol. Rev. , vol.232 , pp. 22-33
    • Dave, V.P.1
  • 55
    • 0037318863 scopus 로고    scopus 로고
    • CD45 ectodomain controls interaction with GEMs and Lck activity for optimal TCR signaling
    • DOI 10.1038/ni877
    • C. Irles, A. Symons, F. Michel, T.R. Bakker, P.A. van der Merwe, and O. Acuto CD45 ectodomain controls interaction with GEMs and Lck activity for optimal TCR signaling Nat. Immunol. 4 2003 189 197 (Pubitemid 36193022)
    • (2003) Nature Immunology , vol.4 , Issue.2 , pp. 189-197
    • Irles, C.1    Symons, A.2    Michel, F.3    Bakker, T.R.4    Van Der Merwe, P.A.5    Acuto, O.6
  • 56
    • 0001481450 scopus 로고
    • The sialic acids. VI. Purification and properties of sialidase from Clostridium perfringens
    • J.T. Cassidy, G.W. Jourdian, and S. Roseman The sialic acids. VI. Purification and properties of sialidase from Clostridium perfringens J. Biol. Chem. 240 1965 3501 3506
    • (1965) J. Biol. Chem. , vol.240 , pp. 3501-3506
    • Cassidy, J.T.1    Jourdian, G.W.2    Roseman, S.3
  • 57
    • 38149094836 scopus 로고    scopus 로고
    • Membrane phosphatidylserine regulates surface charge and protein localization
    • T. Yeung, G.E. Gilbert, J. Shi, J. Silvius, A. Kapus, and S. Grinstein Membrane phosphatidylserine regulates surface charge and protein localization Science 319 2008 210 213
    • (2008) Science , vol.319 , pp. 210-213
    • Yeung, T.1    Gilbert, G.E.2    Shi, J.3    Silvius, J.4    Kapus, A.5    Grinstein, S.6
  • 59
    • 33748994545 scopus 로고    scopus 로고
    • Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking
    • DOI 10.1016/j.tcb.2006.08.006, PII S0962892406002236, Membrane Dynamics
    • A.J. Ridley Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking Trends Cell Biol. 16 2006 522 529 (Pubitemid 44444995)
    • (2006) Trends in Cell Biology , vol.16 , Issue.10 , pp. 522-529
    • Ridley, A.J.1
  • 60
    • 0034682560 scopus 로고    scopus 로고
    • Mutational and biochemical analysis of plasma membrane targeting mediated by the farnesylated, polybasic carboxy terminus of K-ras4B
    • DOI 10.1021/bi000512q
    • M.O. Roy, R. Leventis, and J.R. Silvius Mutational and biochemical analysis of plasma membrane targeting mediated by the farnesylated, polybasic carboxy terminus of K-ras4B Biochemistry 39 2000 8298 8307 (Pubitemid 30460982)
    • (2000) Biochemistry , vol.39 , Issue.28 , pp. 8298-8307
    • Roy, M.-O.1    Leventis, R.2    Silvius, J.R.3
  • 61
    • 33845313646 scopus 로고    scopus 로고
    • 2 lipids target proteins with polybasic clusters to the plasma membrane
    • DOI 10.1126/science.1134389
    • W.D. Heo, T. Inoue, W.S. Park, M.L. Kim, B.O. Park, T.J. Wandless, and T. Meyer PI(3,4,5)P3 and PI(4,5)P2 lipids target proteins with polybasic clusters to the plasma membrane Science 314 2006 1458 1461 (Pubitemid 44871952)
    • (2006) Science , vol.314 , Issue.5804 , pp. 1458-1461
    • Won, D.H.1    Inoue, T.2    Wei, S.P.3    Man, L.K.4    Byung, O.P.5    Wandless, T.J.6    Meyer, T.7
  • 62
    • 22144463880 scopus 로고    scopus 로고
    • Metabolism and functions of phosphatidylserine
    • DOI 10.1016/j.plipres.2005.05.001, PII S0163782705000214
    • J.E. Vance, and R. Steenbergen Metabolism and functions of phosphatidylserine Prog. Lipid Res. 44 2005 207 234 (Pubitemid 40973811)
    • (2005) Progress in Lipid Research , vol.44 , Issue.4 , pp. 207-234
    • Vance, J.E.1    Steenbergen, R.2
  • 63
    • 59249083736 scopus 로고    scopus 로고
    • Expression, purification and structural studies of a short antimicrobial peptide
    • M. Zorko, B. Japelj, I. Hafner-Bratkovic, and R. Jerala Expression, purification and structural studies of a short antimicrobial peptide Biochim. Biophys. Acta 1788 2009 314 323
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 314-323
    • Zorko, M.1    Japelj, B.2    Hafner-Bratkovic, I.3    Jerala, R.4
  • 64
    • 0033369108 scopus 로고    scopus 로고
    • Candidacidal activity of shortened synthetic analogs of amoebapores and NK-lysin
    • DOI 10.1007/s004300050113
    • J. Andra, and M. Leippe Candidacidal activity of shortened synthetic analogs of amoebapores and NK-lysin Med. Microbiol. Immunol. 188 1999 117 124 (Pubitemid 30085357)
    • (1999) Medical Microbiology and Immunology , vol.188 , Issue.3 , pp. 117-124
    • Andra, J.1    Leippe, M.2
  • 66
    • 68149169568 scopus 로고    scopus 로고
    • Beyond glycosylation: Sialic acid precursors act as signaling molecules and are involved in cellular control of differentiation of PC12 cells
    • M. Kontou, W. Weidemann, K. Bork, and R. Horstkorte Beyond glycosylation: sialic acid precursors act as signaling molecules and are involved in cellular control of differentiation of PC12 cells Biol. Chem. 390 2009 575 579
    • (2009) Biol. Chem. , vol.390 , pp. 575-579
    • Kontou, M.1    Weidemann, W.2    Bork, K.3    Horstkorte, R.4
  • 67
    • 36049013008 scopus 로고    scopus 로고
    • Polysialic acid-neural cell adhesion molecule in brain plasticity: From synapses to integration of new neurons
    • DOI 10.1016/j.brainresrev.2007.05.014, PII S0165017307000999
    • E. Gascon, L. Vutskits, and J.Z. Kiss Polysialic acid-neural cell adhesion molecule in brain plasticity: from synapses to integration of new neurons Brain Res. Rev. 56 2007 101 118 (Pubitemid 350100865)
    • (2007) Brain Research Reviews , vol.56 , Issue.1 , pp. 101-118
    • Gascon, E.1    Vutskits, L.2    Kiss, J.Z.3
  • 68
    • 33947602811 scopus 로고    scopus 로고
    • Siglecs and their roles in the immune system
    • DOI 10.1038/nri2056, PII NRI2056
    • P.R. Crocker, J.C. Paulson, and A. Varki Siglecs and their roles in the immune system Nat. Rev. Immunol. 7 2007 255 266 (Pubitemid 46480955)
    • (2007) Nature Reviews Immunology , vol.7 , Issue.4 , pp. 255-266
    • Crocker, P.R.1    Paulson, J.C.2    Varki, A.3
  • 69
    • 71649106024 scopus 로고    scopus 로고
    • Sialic acids in T cell development and function
    • S. Bi, and L.G. Baum Sialic acids in T cell development and function Biochim. Biophys. Acta 1790 2009 1599 1610
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 1599-1610
    • Bi, S.1    Baum, L.G.2
  • 70
    • 33846207546 scopus 로고    scopus 로고
    • Deregulated Ras signaling in developmental disorders: new tricks for an old dog
    • DOI 10.1016/j.gde.2006.12.004, PII S0959437X06002395, Genetic and Cellular mechanisms of oncogenesis
    • S. Schubbert, G. Bollag, and K. Shannon Deregulated Ras signaling in developmental disorders: new tricks for an old dog Curr. Opin. Genet. Dev. 17 2007 15 22 (Pubitemid 46109294)
    • (2007) Current Opinion in Genetics and Development , vol.17 , Issue.1 , pp. 15-22
    • Schubbert, S.1    Bollag, G.2    Shannon, K.3
  • 71
    • 40849102416 scopus 로고    scopus 로고
    • Membrane curvature stress and antibacterial activity of lactoferricin derivatives
    • D. Zweytick, S. Tumer, S.E. Blondelle, and K. Lohner Membrane curvature stress and antibacterial activity of lactoferricin derivatives Biochem. Biophys. Res. Commun. 369 2008 395 400
    • (2008) Biochem. Biophys. Res. Commun. , vol.369 , pp. 395-400
    • Zweytick, D.1    Tumer, S.2    Blondelle, S.E.3    Lohner, K.4


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