메뉴 건너뛰기




Volumn 22, Issue 6, 2017, Pages 919-926

The importance of the glycosylation of antimicrobial peptides: natural and synthetic approaches

Author keywords

[No Author keywords available]

Indexed keywords

POLYPEPTIDE ANTIBIOTIC AGENT; ANTIMICROBIAL CATIONIC PEPTIDE;

EID: 85013053172     PISSN: 13596446     EISSN: 18785832     Source Type: Journal    
DOI: 10.1016/j.drudis.2017.02.001     Document Type: Review
Times cited : (73)

References (92)
  • 1
    • 84883140604 scopus 로고    scopus 로고
    • Exploitation of bacterial N-linked glycosylation to develop a novel recombinant glycoconjugate vaccine against Francisella tularensis
    • Cuccui, J., et al. Exploitation of bacterial N-linked glycosylation to develop a novel recombinant glycoconjugate vaccine against Francisella tularensis. Open Biol., 3, 2013, 130002.
    • (2013) Open Biol. , vol.3 , pp. 130002
    • Cuccui, J.1
  • 2
    • 84925670301 scopus 로고    scopus 로고
    • Hijacking bacterial glycosylation for the production of glycoconjugates, from vaccines to humanised glycoproteins
    • Cuccui, J., Wren, B., Hijacking bacterial glycosylation for the production of glycoconjugates, from vaccines to humanised glycoproteins. J. Pharm. Pharmacol 67 (2015), 338–350.
    • (2015) J. Pharm. Pharmacol , vol.67 , pp. 338-350
    • Cuccui, J.1    Wren, B.2
  • 3
    • 84940449986 scopus 로고    scopus 로고
    • Glycosylation in cancer: mechanisms and clinical implications
    • Pinho, S.S., Reis, C.A., Glycosylation in cancer: mechanisms and clinical implications. Nat. Rev. Cancer 15 (2015), 540–555.
    • (2015) Nat. Rev. Cancer , vol.15 , pp. 540-555
    • Pinho, S.S.1    Reis, C.A.2
  • 4
    • 0029003322 scopus 로고
    • Prediction of O-glycosylation of mammalian proteins: specificity patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
    • Hansen, J.E., et al. Prediction of O-glycosylation of mammalian proteins: specificity patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase. Biochem. J. 308 (1995), 801–813.
    • (1995) Biochem. J. , vol.308 , pp. 801-813
    • Hansen, J.E.1
  • 5
    • 30544433136 scopus 로고    scopus 로고
    • Methods in enzymology: O-glycosylation of proteins
    • Peter-Katalinic, J., Methods in enzymology: O-glycosylation of proteins. Methods Enzymol. 405 (2005), 139–171.
    • (2005) Methods Enzymol. , vol.405 , pp. 139-171
    • Peter-Katalinic, J.1
  • 6
    • 77549084289 scopus 로고    scopus 로고
    • C-Glycosylation BT
    • B.O. Fraser-Reid et al. (eds.) Springer
    • Nishikawa, T., et al. C-Glycosylation BT. Fraser-Reid, B.O., et al. (eds.) Glycoscience: Chemistry and Chemical Biology, 2008, Springer, 755–811.
    • (2008) Glycoscience: Chemistry and Chemical Biology , pp. 755-811
    • Nishikawa, T.1
  • 7
    • 0034666159 scopus 로고    scopus 로고
    • Properdin, the positive regulator of complement, is highly C-mannosylated
    • Hartmann, S., Hofsteenge, J., Properdin, the positive regulator of complement, is highly C-mannosylated. J. Biol. Chem. 275 (2000), 28569–28574.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28569-28574
    • Hartmann, S.1    Hofsteenge, J.2
  • 8
    • 0031881719 scopus 로고    scopus 로고
    • Protein C-mannosylation is enzyme-catalysed and uses dolichyl-phosphate-mannose as a precursor
    • Doucey, M.-A., et al. Protein C-mannosylation is enzyme-catalysed and uses dolichyl-phosphate-mannose as a precursor. Mol. Biol. Cell 9 (1998), 291–300.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 291-300
    • Doucey, M.-A.1
  • 9
    • 78751469486 scopus 로고    scopus 로고
    • Sublancin is not a lantibiotic but an S-linked glycopeptide
    • Oman, T.J., et al. Sublancin is not a lantibiotic but an S-linked glycopeptide. Nat. Chem. Biol. 7 (2011), 78–80.
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 78-80
    • Oman, T.J.1
  • 10
    • 79951581591 scopus 로고    scopus 로고
    • Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins
    • Stepper, J., et al. Cysteine S-glycosylation, a new post-translational modification found in glycopeptide bacteriocins. FEBS Lett. 585 (2011), 645–650.
    • (2011) FEBS Lett. , vol.585 , pp. 645-650
    • Stepper, J.1
  • 11
    • 84878402118 scopus 로고    scopus 로고
    • Post-translational modifications of natural antimicrobial peptides and strategies for peptide engineering
    • Wang, G., Post-translational modifications of natural antimicrobial peptides and strategies for peptide engineering. Curr. Biotechnol. 1 (2012), 72–79.
    • (2012) Curr. Biotechnol. , vol.1 , pp. 72-79
    • Wang, G.1
  • 12
    • 0032412381 scopus 로고    scopus 로고
    • Animal antimicrobial peptides: an overview
    • Andreu, D., Rivas, L., Animal antimicrobial peptides: an overview. Biopolymers 47 (1998), 415–433.
    • (1998) Biopolymers , vol.47 , pp. 415-433
    • Andreu, D.1    Rivas, L.2
  • 13
    • 0028900915 scopus 로고
    • Cells regulate the activities of cytokines by glycosylation
    • Opdenakker, G., et al. Cells regulate the activities of cytokines by glycosylation. FASEB J. 9 (1995), 453–457.
    • (1995) FASEB J. , vol.9 , pp. 453-457
    • Opdenakker, G.1
  • 14
    • 84962256364 scopus 로고    scopus 로고
    • Glycosylation, an effective synthetic strategy to improve the bioavailability of therapeutic peptides
    • Moradi, S.V., et al. Glycosylation, an effective synthetic strategy to improve the bioavailability of therapeutic peptides. Chem. Sci. 7 (2016), 2492–2500.
    • (2016) Chem. Sci. , vol.7 , pp. 2492-2500
    • Moradi, S.V.1
  • 15
    • 70349336181 scopus 로고    scopus 로고
    • Eosinophil cationic protein (ECP) is processed during secretion
    • Woschnagg, C., et al. Eosinophil cationic protein (ECP) is processed during secretion. J. Immunol. 183 (2009), 3949–3954.
    • (2009) J. Immunol. , vol.183 , pp. 3949-3954
    • Woschnagg, C.1
  • 16
    • 84877610166 scopus 로고    scopus 로고
    • Asparagine-linked glycans determine the cytotoxic capacity of eosinophil cationic protein (ECP)
    • Rubin, J., Venge, P., Asparagine-linked glycans determine the cytotoxic capacity of eosinophil cationic protein (ECP). Mol. Immunol. 55 (2013), 372–380.
    • (2013) Mol. Immunol. , vol.55 , pp. 372-380
    • Rubin, J.1    Venge, P.2
  • 17
    • 84916235784 scopus 로고    scopus 로고
    • Protein post-translational modification in host defense: the antimicrobial mechanism of action of human eosinophil cationic protein native forms
    • Salazar, V.A., et al. Protein post-translational modification in host defense: the antimicrobial mechanism of action of human eosinophil cationic protein native forms. FEBS J. 281 (2014), 5432–5446.
    • (2014) FEBS J. , vol.281 , pp. 5432-5446
    • Salazar, V.A.1
  • 18
    • 84921526420 scopus 로고    scopus 로고
    • Understanding the importance of glycosylated threonine and stereospecific action of Drosocin, a Proline rich antimicrobial peptide
    • Lele, D.S., et al. Understanding the importance of glycosylated threonine and stereospecific action of Drosocin, a Proline rich antimicrobial peptide. Eur. J. Med. Chem. 92 (2015), 637–647.
    • (2015) Eur. J. Med. Chem. , vol.92 , pp. 637-647
    • Lele, D.S.1
  • 19
    • 84863800481 scopus 로고    scopus 로고
    • Glycosylated analogs of formaecin I and drosocin exhibit differential pattern of antibacterial activity
    • Talat, S., et al. Glycosylated analogs of formaecin I and drosocin exhibit differential pattern of antibacterial activity. Glycoconj. J. 28 (2011), 537–555.
    • (2011) Glycoconj. J. , vol.28 , pp. 537-555
    • Talat, S.1
  • 20
    • 84931388674 scopus 로고    scopus 로고
    • Enterocin F4-9, a novel O-linked glycosylated bacteriocin
    • Maky, M.A., et al. Enterocin F4-9, a novel O-linked glycosylated bacteriocin. Appl. Env. Microbiol. 81 (2015), 4819–4826.
    • (2015) Appl. Env. Microbiol. , vol.81 , pp. 4819-4826
    • Maky, M.A.1
  • 21
    • 84881171951 scopus 로고    scopus 로고
    • Glycation and transglutaminase mediated glycosylation of fish gelatin peptides with glucosamine enhance bioactivity
    • Hong, P.K., et al. Glycation and transglutaminase mediated glycosylation of fish gelatin peptides with glucosamine enhance bioactivity. Food Chem. 142 (2014), 2852–2893.
    • (2014) Food Chem. , vol.142 , pp. 2852-2893
    • Hong, P.K.1
  • 22
    • 84872006734 scopus 로고    scopus 로고
    • A novel hydroxyproline rich glycopeptide from pericarp of Datura stramonium: proficiently eradicate the biofilm of antifungals resistant Candida albicans
    • Mandal, S.M., A novel hydroxyproline rich glycopeptide from pericarp of Datura stramonium: proficiently eradicate the biofilm of antifungals resistant Candida albicans. Biopo lymers 98 (2012), 332–337.
    • (2012) Biopo lymers , vol.98 , pp. 332-337
    • Mandal, S.M.1
  • 23
    • 33846423842 scopus 로고    scopus 로고
    • The functional heterogeneity of eosinophil cationic protein is determined by a gene polymorphism and post-translational modifications
    • Trulson, A., et al. The functional heterogeneity of eosinophil cationic protein is determined by a gene polymorphism and post-translational modifications. Clin. Exp. Allergy 37 (2007), 208–218.
    • (2007) Clin. Exp. Allergy , vol.37 , pp. 208-218
    • Trulson, A.1
  • 24
    • 84880940461 scopus 로고    scopus 로고
    • Site-specific N-glycosylation of caprine lysostaphin restricts its bacteriolytic activity toward Staphylococcus aureus
    • Huang, C.Y., et al. Site-specific N-glycosylation of caprine lysostaphin restricts its bacteriolytic activity toward Staphylococcus aureus. Anim. Biotechnol. 24 (2013), 129–147.
    • (2013) Anim. Biotechnol. , vol.24 , pp. 129-147
    • Huang, C.Y.1
  • 25
    • 33748742271 scopus 로고    scopus 로고
    • Protein N‐glycosylation in the baculovirus–insect cell expression system and engineering of insect cells to produce ‘mammalianized’ recombinant glycoproteins
    • Harrison, R.L., Jarvis, D.L., Protein N‐glycosylation in the baculovirus–insect cell expression system and engineering of insect cells to produce ‘mammalianized’ recombinant glycoproteins. Insect Viruses Biotechnol. Appl. 68 (2006), 159–191.
    • (2006) Insect Viruses Biotechnol. Appl. , vol.68 , pp. 159-191
    • Harrison, R.L.1    Jarvis, D.L.2
  • 26
    • 84927143009 scopus 로고    scopus 로고
    • Honey glycoproteins containing antimicrobial peptides, Jelleins of the Major Royal Jelly Protein 1, are responsible for the cell wall lytic and bactericidal activities of honey
    • Brudzynski, K., Sjaarda, C., Honey glycoproteins containing antimicrobial peptides, Jelleins of the Major Royal Jelly Protein 1, are responsible for the cell wall lytic and bactericidal activities of honey. PLoS ONE, 10, 2015, e0120238.
    • (2015) PLoS ONE , vol.10 , pp. e0120238
    • Brudzynski, K.1    Sjaarda, C.2
  • 27
    • 0025782587 scopus 로고
    • The conformational effects of N-glycosylation on the tailpiece from serum IgM
    • Wormald, M.R., et al. The conformational effects of N-glycosylation on the tailpiece from serum IgM. Eur. J. Biochem. 198 (1991), 131–139.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 131-139
    • Wormald, M.R.1
  • 28
    • 0029339153 scopus 로고
    • Conformations and internal mobility of a glycopeptide derived from bromelain using molecular dynamics simulations and NOESY analysis
    • Lommerse, J.P., et al. Conformations and internal mobility of a glycopeptide derived from bromelain using molecular dynamics simulations and NOESY analysis. J. Biomol. NMR 6 (1995), 79–94.
    • (1995) J. Biomol. NMR , vol.6 , pp. 79-94
    • Lommerse, J.P.1
  • 29
    • 0037934610 scopus 로고    scopus 로고
    • The interplay of glycosylation and disulfide formation influences fibrillization in a prion protein fragment
    • Bosques, C.J., Imperiali, B., The interplay of glycosylation and disulfide formation influences fibrillization in a prion protein fragment. Proc. Natl. Acad. Sci. U. S. A. 100 (2003), 7593–7598.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 7593-7598
    • Bosques, C.J.1    Imperiali, B.2
  • 30
    • 0032146060 scopus 로고    scopus 로고
    • A molecular basis for glycosylation-induced conformational switching
    • O'Connor, S.E., Imperiali, B., A molecular basis for glycosylation-induced conformational switching. Chem. Biol. 5 (1998), 427–437.
    • (1998) Chem. Biol. , vol.5 , pp. 427-437
    • O'Connor, S.E.1    Imperiali, B.2
  • 31
    • 0033566020 scopus 로고    scopus 로고
    • Glycoproteins: glycan presentation and protein-fold stability
    • Wormald, M.R., Dwek, R.A., Glycoproteins: glycan presentation and protein-fold stability. Structure 7 (2016), R155–60.
    • (2016) Structure , vol.7 , pp. R155-60
    • Wormald, M.R.1    Dwek, R.A.2
  • 32
    • 46149089907 scopus 로고    scopus 로고
    • Effect of glycosylation on protein folding: a close look at thermodynamic stabilization
    • Shental-Bechor, D., Levy, Y., Effect of glycosylation on protein folding: a close look at thermodynamic stabilization. Proc. Natl. Acad. Sci. U. S. A. 105 (2008), 8256–8261.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 8256-8261
    • Shental-Bechor, D.1    Levy, Y.2
  • 33
    • 70349886556 scopus 로고    scopus 로고
    • Folding of glycoproteins: toward understanding the biophysics of the glycosylation code
    • Shental-Bechor, D., Levy, Y., Folding of glycoproteins: toward understanding the biophysics of the glycosylation code. Curr. Opin. Struct Biol. 19 (2009), 524–533.
    • (2009) Curr. Opin. Struct Biol. , vol.19 , pp. 524-533
    • Shental-Bechor, D.1    Levy, Y.2
  • 34
    • 33947545682 scopus 로고    scopus 로고
    • Sialic acids: carbohydrate moieties that influence the biological and physical properties of biopharmaceutical proteins and living cells
    • Byrne, B., et al. Sialic acids: carbohydrate moieties that influence the biological and physical properties of biopharmaceutical proteins and living cells. Drug Discov. Today 12 (2007), 319–326.
    • (2007) Drug Discov. Today , vol.12 , pp. 319-326
    • Byrne, B.1
  • 35
    • 0033608995 scopus 로고    scopus 로고
    • Protein conjugates of synthetic saccharides elicit higher levels of serum IgG lipopolysaccharide antibodies in mice than do those of the O-specific polysaccharide from Shigella dysenteriae type 1
    • Pozsgay, V., et al. Protein conjugates of synthetic saccharides elicit higher levels of serum IgG lipopolysaccharide antibodies in mice than do those of the O-specific polysaccharide from Shigella dysenteriae type 1. Proc. Natl. Acad. Sci. U. S. A. 96 (1999), 5194–5197.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 5194-5197
    • Pozsgay, V.1
  • 36
    • 84922767939 scopus 로고    scopus 로고
    • Glycosylated enfuvirtide: a long-lasting glycopeptide with potent anti-HIV activity
    • Cheng, S., et al. Glycosylated enfuvirtide: a long-lasting glycopeptide with potent anti-HIV activity. J. Med. Chem. 58 (2015), 1372–1379.
    • (2015) J. Med. Chem. , vol.58 , pp. 1372-1379
    • Cheng, S.1
  • 37
    • 0034871429 scopus 로고    scopus 로고
    • Development of pegylated interferons for the treatment of chronic hepatitis C
    • Kozlowski, A., et al. Development of pegylated interferons for the treatment of chronic hepatitis C. BioDrugs 15 (2001), 419–429.
    • (2001) BioDrugs , vol.15 , pp. 419-429
    • Kozlowski, A.1
  • 38
    • 14544269999 scopus 로고    scopus 로고
    • Synthetic glycopeptides and glycoproteins as tools for biology
    • Pratt, M.R., Bertozzi, C.R., Synthetic glycopeptides and glycoproteins as tools for biology. Chem. Soc. Rev. 34 (2005), 58–68.
    • (2005) Chem. Soc. Rev. , vol.34 , pp. 58-68
    • Pratt, M.R.1    Bertozzi, C.R.2
  • 39
    • 84924370879 scopus 로고    scopus 로고
    • Effects of N-glycosylation on protein conformation and dynamics: Protein Data Bank analysis and molecular dynamics simulation study
    • Lee, H.S., et al. Effects of N-glycosylation on protein conformation and dynamics: Protein Data Bank analysis and molecular dynamics simulation study. Sci. Rep., 5, 2015, 8926.
    • (2015) Sci. Rep. , vol.5 , pp. 8926
    • Lee, H.S.1
  • 40
    • 84880586512 scopus 로고    scopus 로고
    • N-linked protein glycosylation in the ER
    • Aebi, M., N-linked protein glycosylation in the ER. Biochim. Biophys. Acta - Mol. Cell Res. 1833 (2013), 2430–2437.
    • (2013) Biochim. Biophys. Acta - Mol. Cell Res. , vol.1833 , pp. 2430-2437
    • Aebi, M.1
  • 41
    • 80052179739 scopus 로고    scopus 로고
    • Glycosylation of the enhanced aromatic sequon is similarly stabilizing in three distinct reverse turn contexts
    • Price, J.L., et al. Glycosylation of the enhanced aromatic sequon is similarly stabilizing in three distinct reverse turn contexts. Proc. Natl. Acad. Sci. U. S. A. 108 (2011), 14127–14132.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 14127-14132
    • Price, J.L.1
  • 42
    • 64549127326 scopus 로고    scopus 로고
    • Synthesis and antibacterial activities of N-glycosylated derivatives of tyrocidine A, a macrocyclic peptide antibiotic
    • Hu, H., et al. Synthesis and antibacterial activities of N-glycosylated derivatives of tyrocidine A, a macrocyclic peptide antibiotic. J. Med. Chem. 52 (2009), 2052–2059.
    • (2009) J. Med. Chem. , vol.52 , pp. 2052-2059
    • Hu, H.1
  • 43
    • 75149183678 scopus 로고    scopus 로고
    • Glycosylation of therapeutic proteins: an effective strategy to optimize efficacy
    • Solá, R.J., Griebenow, K., Glycosylation of therapeutic proteins: an effective strategy to optimize efficacy. BioDrugs 24 (2010), 9–21.
    • (2010) BioDrugs , vol.24 , pp. 9-21
    • Solá, R.J.1    Griebenow, K.2
  • 44
    • 60549117775 scopus 로고    scopus 로고
    • Activation of dendritic cells by toll-like receptors and C-type lectins
    • Diebold, S.S., Activation of dendritic cells by toll-like receptors and C-type lectins. Handb. Ex. Pharmacol. 188 (2009), 3–30.
    • (2009) Handb. Ex. Pharmacol. , vol.188 , pp. 3-30
    • Diebold, S.S.1
  • 45
    • 84922978720 scopus 로고    scopus 로고
    • Synthesis of the antimicrobial S-linked glycopeptide, glycocin F
    • Brimble, M.A., et al. Synthesis of the antimicrobial S-linked glycopeptide, glycocin F. Chemistry 21 (2015), 3556–3561.
    • (2015) Chemistry , vol.21 , pp. 3556-3561
    • Brimble, M.A.1
  • 46
    • 84940399119 scopus 로고    scopus 로고
    • Purification, characterization and mode of action of plantaricin K25 produced by Lactobacillus plantarum
    • Wen, L.S., et al. Purification, characterization and mode of action of plantaricin K25 produced by Lactobacillus plantarum. Food Control 60 (2016), 430–439.
    • (2016) Food Control , vol.60 , pp. 430-439
    • Wen, L.S.1
  • 47
    • 84870164388 scopus 로고    scopus 로고
    • Plantaricin A, a cationic peptide produced by Lactobacillus plantarum, permeabilizes eukaryotic cell membranes by a mechanism dependent on negative surface charge linked to glycosylated membrane proteins
    • Sand, S.L., et al. Plantaricin A, a cationic peptide produced by Lactobacillus plantarum, permeabilizes eukaryotic cell membranes by a mechanism dependent on negative surface charge linked to glycosylated membrane proteins. Biochim. Biophys. Acta 1828 (2013), 249–259.
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 249-259
    • Sand, S.L.1
  • 48
    • 33749608085 scopus 로고    scopus 로고
    • The mannose transporter complex: an open door for the macromolecular Invasion of bacteria
    • Erni, B., The mannose transporter complex: an open door for the macromolecular Invasion of bacteria. J. Bacteriol. 188 (2006), 7036–7038.
    • (2006) J. Bacteriol. , vol.188 , pp. 7036-7038
    • Erni, B.1
  • 49
    • 84938244327 scopus 로고    scopus 로고
    • Small molecules from the human microbiota
    • Donia, M.S., Fischbach, M.A., Small molecules from the human microbiota. Science, 349, 2015, 1254766.
    • (2015) Science , vol.349 , pp. 1254766
    • Donia, M.S.1    Fischbach, M.A.2
  • 50
    • 36448952357 scopus 로고    scopus 로고
    • Biosynthetic tailoring of microcin E492m: post-translational modification affords an antibacterial siderophore-peptide conjugate
    • Nolan, E.M., et al. Biosynthetic tailoring of microcin E492m: post-translational modification affords an antibacterial siderophore-peptide conjugate. J. Am. Chem. Soc 129 (2007), 14336–14347.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 14336-14347
    • Nolan, E.M.1
  • 51
    • 0029956552 scopus 로고    scopus 로고
    • Antibacterial activity of glycosylated and phosphorylated chromogranin A-derived peptide 173-194 from bovine adrenal medullary chromaffin granules
    • Strub, J.-M., et al. Antibacterial activity of glycosylated and phosphorylated chromogranin A-derived peptide 173-194 from bovine adrenal medullary chromaffin granules. J. Biol. Chem. 271 (1996), 28533–28540.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28533-28540
    • Strub, J.-M.1
  • 52
    • 84884590595 scopus 로고    scopus 로고
    • Genes involved in protein glycosylation determine the activity and cell internalization of the antifungal peptide PAF26 in Saccharomyces cerevisiae
    • Harries, E., et al. Genes involved in protein glycosylation determine the activity and cell internalization of the antifungal peptide PAF26 in Saccharomyces cerevisiae. Fungal Genet. Biol. 58–59 (2013), 105–115.
    • (2013) Fungal Genet. Biol. , vol.58-59 , pp. 105-115
    • Harries, E.1
  • 53
    • 84887987723 scopus 로고    scopus 로고
    • Adaptive immune activation: glycosylation does matter
    • Wolfert, M.A., Boons, G.-J., Adaptive immune activation: glycosylation does matter. Nat. Chem. Biol. 9 (2013), 776–784.
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 776-784
    • Wolfert, M.A.1    Boons, G.-J.2
  • 54
    • 80051787881 scopus 로고    scopus 로고
    • Cationic amphipathic peptides accumulate sialylated proteins and lipids in the plasma membrane of eukaryotic host cells
    • Weghuber, J., et al. Cationic amphipathic peptides accumulate sialylated proteins and lipids in the plasma membrane of eukaryotic host cells. Biochim. Biophys. Acta 1808 (2011), 2581–2590.
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 2581-2590
    • Weghuber, J.1
  • 55
    • 0036252094 scopus 로고    scopus 로고
    • Pro-rich antimicrobial peptides from animals: structure, biological functions and mechanism of action
    • Gennaro, R., et al. Pro-rich antimicrobial peptides from animals: structure, biological functions and mechanism of action. Curr. Pharm. Des. 8 (2002), 763–778.
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 763-778
    • Gennaro, R.1
  • 56
    • 84984919780 scopus 로고    scopus 로고
    • Cathelicidin PR-39 peptide inhibits hypoxia/reperfusion-induced kidney cell apoptosis by suppression of the endoplasmic reticulum-stress pathway
    • Liu, J., et al. Cathelicidin PR-39 peptide inhibits hypoxia/reperfusion-induced kidney cell apoptosis by suppression of the endoplasmic reticulum-stress pathway. Acta Biochim. Biophys. Sin. 48 (2016), 714–722.
    • (2016) Acta Biochim. Biophys. Sin. , vol.48 , pp. 714-722
    • Liu, J.1
  • 57
    • 0032875198 scopus 로고    scopus 로고
    • Proline-rich antimicrobial peptide, PR-39 gene transduction altered invasive activity and actin structure in human hepatocellular carcinoma cells
    • Ohtake, T., et al. Proline-rich antimicrobial peptide, PR-39 gene transduction altered invasive activity and actin structure in human hepatocellular carcinoma cells. Br. J. Cancer 81 (1999), 393–403.
    • (1999) Br. J. Cancer , vol.81 , pp. 393-403
    • Ohtake, T.1
  • 58
    • 0037162503 scopus 로고    scopus 로고
    • Processing of glycans on glycoprotein and glycopeptide antigens in antigen-presenting cells
    • Werdelin, O., et al. Processing of glycans on glycoprotein and glycopeptide antigens in antigen-presenting cells. Proc. Natl. Acad. Sci. U. S. A. 99 (2002), 9611–9613.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 9611-9613
    • Werdelin, O.1
  • 59
    • 84964389619 scopus 로고    scopus 로고
    • The immunology of host defence peptides: beyond antimicrobial activity
    • Hancock, R.E., et al. The immunology of host defence peptides: beyond antimicrobial activity. Nat. Rev. Immunol. 16 (2016), 321–334.
    • (2016) Nat. Rev. Immunol. , vol.16 , pp. 321-334
    • Hancock, R.E.1
  • 60
    • 2542507286 scopus 로고    scopus 로고
    • Polysaccharide processing and presentation by the MHCII pathway
    • Cobb, B.A., et al. Polysaccharide processing and presentation by the MHCII pathway. Cell 117 (2004), 677–687.
    • (2004) Cell , vol.117 , pp. 677-687
    • Cobb, B.A.1
  • 61
    • 0033024354 scopus 로고    scopus 로고
    • Crystal structure of an MHC class I presented glycopeptide that generates carbohydrate-specific CTL
    • Speir, J.A., et al. Crystal structure of an MHC class I presented glycopeptide that generates carbohydrate-specific CTL. Immunity 10 (1999), 51–61.
    • (1999) Immunity , vol.10 , pp. 51-61
    • Speir, J.A.1
  • 62
    • 84892375230 scopus 로고    scopus 로고
    • gammadelta T cells and their potential for immunotherapy
    • Wu, Y.L., et al. gammadelta T cells and their potential for immunotherapy. Int. J. Biol. Sci. 10 (2014), 119–135.
    • (2014) Int. J. Biol. Sci. , vol.10 , pp. 119-135
    • Wu, Y.L.1
  • 63
    • 84859354949 scopus 로고    scopus 로고
    • B-cell receptor: from resting state to activate
    • Treanor, B., B-cell receptor: from resting state to activate. Immunology 136 (2012), 21–27.
    • (2012) Immunology , vol.136 , pp. 21-27
    • Treanor, B.1
  • 64
    • 84922887966 scopus 로고    scopus 로고
    • Glycans in the immune system and the altered glycan theory of autoimmunity: a critical review
    • Maverakis, E., et al. Glycans in the immune system and the altered glycan theory of autoimmunity: a critical review. J. Autoimmun. 57 (2015), 1–13.
    • (2015) J. Autoimmun. , vol.57 , pp. 1-13
    • Maverakis, E.1
  • 65
    • 54949106904 scopus 로고    scopus 로고
    • Mammalian glycosylation in immunity
    • Marth, J.D., Grewal, P.K., Mammalian glycosylation in immunity. Nat. Rev. Immunol. 8 (2008), 874–887.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 874-887
    • Marth, J.D.1    Grewal, P.K.2
  • 66
    • 68149118066 scopus 로고    scopus 로고
    • Increasing the sialylation of therapeutic glycoproteins: the potential of the sialic acid biosynthetic pathway
    • Bork, K., et al. Increasing the sialylation of therapeutic glycoproteins: the potential of the sialic acid biosynthetic pathway. J. Pharm. Sci. 98 (2009), 3499–3508.
    • (2009) J. Pharm. Sci. , vol.98 , pp. 3499-3508
    • Bork, K.1
  • 67
    • 84959223142 scopus 로고    scopus 로고
    • Glycans as vaccine antigens and adjuvants: immunological considerations
    • Zimmermann, S., Lepenies, B., Glycans as vaccine antigens and adjuvants: immunological considerations. Methods Mol. Biol. 1331 (2015), 11–26.
    • (2015) Methods Mol. Biol. , vol.1331 , pp. 11-26
    • Zimmermann, S.1    Lepenies, B.2
  • 68
    • 1542283702 scopus 로고    scopus 로고
    • Designer glycopeptides for cytotoxic T cell-based elimination of carcinomas
    • Xu, Y., et al. Designer glycopeptides for cytotoxic T cell-based elimination of carcinomas. J. Exp. Med. 199 (2004), 707–716.
    • (2004) J. Exp. Med. , vol.199 , pp. 707-716
    • Xu, Y.1
  • 69
    • 0032995748 scopus 로고    scopus 로고
    • Inhibitory effect of free sialic acid on complement activation and its significance in hypocomplementemic glomerulonephritis
    • Fujita, T., et al. Inhibitory effect of free sialic acid on complement activation and its significance in hypocomplementemic glomerulonephritis. J. Clin. Lab. Anal. 13 (1999), 173–179.
    • (1999) J. Clin. Lab. Anal. , vol.13 , pp. 173-179
    • Fujita, T.1
  • 70
    • 0035200718 scopus 로고    scopus 로고
    • Improved blood-brain barrier penetration and enhanced analgesia of an opioid peptide by glycosylation
    • Egleton, R.D., et al. Improved blood-brain barrier penetration and enhanced analgesia of an opioid peptide by glycosylation. J. Pharmacol. Exp. Ther. 299 (2001), 967–972.
    • (2001) J. Pharmacol. Exp. Ther. , vol.299 , pp. 967-972
    • Egleton, R.D.1
  • 71
    • 0035748363 scopus 로고    scopus 로고
    • Peptide drug modifications to enhance bioavailability and blood-brain barrier permeability
    • Witt, K.A., et al. Peptide drug modifications to enhance bioavailability and blood-brain barrier permeability. Peptides 22 (2001), 2329–2343.
    • (2001) Peptides , vol.22 , pp. 2329-2343
    • Witt, K.A.1
  • 72
    • 84945551910 scopus 로고    scopus 로고
    • Promising approaches to circumvent the blood-brain barrier: progress, pitfalls and clinical prospects in brain cancer
    • Papademetriou, I.T., Porter, T., Promising approaches to circumvent the blood-brain barrier: progress, pitfalls and clinical prospects in brain cancer. Ther. Deliv. 6 (2015), 989–1016.
    • (2015) Ther. Deliv. , vol.6 , pp. 989-1016
    • Papademetriou, I.T.1    Porter, T.2
  • 73
    • 85011843832 scopus 로고    scopus 로고
    • Design and application of antimicrobial peptide conjugates
    • Reinhardt, A., Neundorf, I., Design and application of antimicrobial peptide conjugates. Int. J. Mol. Sci., 17, 2016, 701.
    • (2016) Int. J. Mol. Sci. , vol.17 , pp. 701
    • Reinhardt, A.1    Neundorf, I.2
  • 74
    • 84888368664 scopus 로고    scopus 로고
    • Expression of asialoglycoprotein receptor 1 in human hepatocellular carcinoma
    • Shi, B., et al. Expression of asialoglycoprotein receptor 1 in human hepatocellular carcinoma. J. Histochem. Cytochem. 61 (2013), 901–909.
    • (2013) J. Histochem. Cytochem. , vol.61 , pp. 901-909
    • Shi, B.1
  • 75
    • 1142309575 scopus 로고    scopus 로고
    • Lectins and glycoconjugates in drug delivery and targeting
    • Lehr, C.-M., Gabor, F., Lectins and glycoconjugates in drug delivery and targeting. Adv. Drug Deliv. Rev. 56 (2004), 419–420.
    • (2004) Adv. Drug Deliv. Rev. , vol.56 , pp. 419-420
    • Lehr, C.-M.1    Gabor, F.2
  • 76
    • 0036199682 scopus 로고    scopus 로고
    • The pulmonary collectins, SP-A and SP-D, orchestrate innate immunity in the lung
    • McCormack, F.X., Whitsett, J.A., The pulmonary collectins, SP-A and SP-D, orchestrate innate immunity in the lung. J. Clin. Invest. 109 (2002), 707–712.
    • (2002) J. Clin. Invest. , vol.109 , pp. 707-712
    • McCormack, F.X.1    Whitsett, J.A.2
  • 77
    • 80051546187 scopus 로고    scopus 로고
    • Will new generations of modified antimicrobial peptides improve their potential as pharmaceuticals?
    • Brogden, N.K., Brogden, K.A., Will new generations of modified antimicrobial peptides improve their potential as pharmaceuticals?. Int. J. Antimicrob Agents 38 (2011), 217–225.
    • (2011) Int. J. Antimicrob Agents , vol.38 , pp. 217-225
    • Brogden, N.K.1    Brogden, K.A.2
  • 78
    • 84870515227 scopus 로고    scopus 로고
    • Asialoglycoprotein receptor (ASGPR): a peculiar target of liver-specific autoimmunity
    • Roggenbuck, D., et al. Asialoglycoprotein receptor (ASGPR): a peculiar target of liver-specific autoimmunity. Auto-Immunity Highlights 3 (2012), 119–125.
    • (2012) Auto-Immunity Highlights , vol.3 , pp. 119-125
    • Roggenbuck, D.1
  • 79
    • 85015136039 scopus 로고    scopus 로고
    • Reinventing cell penetrating peptides using glycosylated methionine sulfonium ion sequences
    • Kramer, J.R., et al. Reinventing cell penetrating peptides using glycosylated methionine sulfonium ion sequences. ACS Cent. Sci. 1 (2015), 83–88.
    • (2015) ACS Cent. Sci. , vol.1 , pp. 83-88
    • Kramer, J.R.1
  • 80
    • 84877318780 scopus 로고    scopus 로고
    • Antimicrobial peptides stage a comeback
    • Fox, J.L., Antimicrobial peptides stage a comeback. Nat. Biotechnol. 31 (2013), 379–382.
    • (2013) Nat. Biotechnol. , vol.31 , pp. 379-382
    • Fox, J.L.1
  • 81
    • 84879570321 scopus 로고    scopus 로고
    • The innate defense regulator peptides IDR-HH2, IDR-1002, and IDR-1018 modulate human neutrophil functions
    • Niyonsaba, F., et al. The innate defense regulator peptides IDR-HH2, IDR-1002, and IDR-1018 modulate human neutrophil functions. J. Leukoc. Biol. 94 (2013), 159–170.
    • (2013) J. Leukoc. Biol. , vol.94 , pp. 159-170
    • Niyonsaba, F.1
  • 82
    • 34147147029 scopus 로고    scopus 로고
    • An anti-infective peptide that selectively modulates the innate immune response
    • Scott, M.G., et al. An anti-infective peptide that selectively modulates the innate immune response. Nat. Biotechnol. 25 (2007), 465–472.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 465-472
    • Scott, M.G.1
  • 83
    • 77950795510 scopus 로고    scopus 로고
    • Generating heparan sulfate saccharide libraries for glycomics applications
    • Powell, A.K., et al. Generating heparan sulfate saccharide libraries for glycomics applications. Nat. Protoc. 5 (2010), 821–833.
    • (2010) Nat. Protoc. , vol.5 , pp. 821-833
    • Powell, A.K.1
  • 84
    • 84855265950 scopus 로고    scopus 로고
    • Integrating bioinformatics tools to handle glycosylation
    • Mazola, Y., et al. Integrating bioinformatics tools to handle glycosylation. PLoS Comput. Biol., 7, 2011, e1002285.
    • (2011) PLoS Comput. Biol. , vol.7 , pp. e1002285
    • Mazola, Y.1
  • 85
    • 84867299668 scopus 로고    scopus 로고
    • GlycoCD: a repository for carbohydrate-related CD antigens
    • Kumar, S., et al. GlycoCD: a repository for carbohydrate-related CD antigens. Bioinformatics 28 (2012), 2553–2555.
    • (2012) Bioinformatics , vol.28 , pp. 2553-2555
    • Kumar, S.1
  • 86
    • 84862953864 scopus 로고    scopus 로고
    • How hydrophobicity and the glycosylation site of glycans affect protein folding and stability: a molecular dynamics simulation
    • Lu, D., et al. How hydrophobicity and the glycosylation site of glycans affect protein folding and stability: a molecular dynamics simulation. J. Phys. Chem. B 116 (2012), 390–400.
    • (2012) J. Phys. Chem. B , vol.116 , pp. 390-400
    • Lu, D.1
  • 87
    • 11144304794 scopus 로고    scopus 로고
    • W3-SWEET: carbohydrate modeling by internet
    • Bohne, A., et al. W3-SWEET: carbohydrate modeling by internet. Mol. Model. Annu. 4 (1998), 33–43.
    • (1998) Mol. Model. Annu. , vol.4 , pp. 33-43
    • Bohne, A.1
  • 88
    • 84899881824 scopus 로고    scopus 로고
    • QSAR Modeling: where have you been? Where are you going to?
    • Cherkasov, A., et al. QSAR Modeling: where have you been? Where are you going to?. J. Med. Chem., 57, 2014, 4977.
    • (2014) J. Med. Chem. , vol.57 , pp. 4977
    • Cherkasov, A.1
  • 89
    • 0036455954 scopus 로고    scopus 로고
    • Rapid generation of a representative ensemble of N-glycan conformations
    • Frank, M., et al. Rapid generation of a representative ensemble of N-glycan conformations. Silico Biol. 2 (2002), 427–439.
    • (2002) Silico Biol. , vol.2 , pp. 427-439
    • Frank, M.1
  • 90
    • 84896537748 scopus 로고    scopus 로고
    • Site-specific antibody–drug conjugation through glycoengineering
    • Zhou, Q., et al. Site-specific antibody–drug conjugation through glycoengineering. Bioconjug. Chem. 25 (2014), 510–520.
    • (2014) Bioconjug. Chem. , vol.25 , pp. 510-520
    • Zhou, Q.1
  • 91
    • 84957597082 scopus 로고    scopus 로고
    • One-pot peptide and protein conjugation: a combination of enzymatic transamidation and click chemistry
    • Rachel, N.M., Pelletier, J.N., One-pot peptide and protein conjugation: a combination of enzymatic transamidation and click chemistry. Chem. Commun. 52 (2016), 2541–2544.
    • (2016) Chem. Commun. , vol.52 , pp. 2541-2544
    • Rachel, N.M.1    Pelletier, J.N.2
  • 92
    • 68749110765 scopus 로고    scopus 로고
    • Optimal and consistent protein glycosylation in mammalian cell culture
    • Hossler, P., et al. Optimal and consistent protein glycosylation in mammalian cell culture. Glycobiology 19 (2009), 936–949.
    • (2009) Glycobiology , vol.19 , pp. 936-949
    • Hossler, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.