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Volumn 56, Issue 9, 2013, Pages 3546-3556

Structure and function of a potent lipopolysaccharide-binding antimicrobial and anti-inflammatory peptide

Author keywords

[No Author keywords available]

Indexed keywords

ANTIFUNGAL AGENT; ANTIINFECTIVE AGENT; ANTIINFLAMMATORY AGENT; CATHELICIDIN; CATHELICIDIN PY; INTERLEUKIN 6; LEVOFLOXACIN; LIPOPOLYSACCHARIDE; MONOCYTE CHEMOTACTIC PROTEIN 1; NATURAL PRODUCT; NITRIC OXIDE; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 84877697409     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm4004158     Document Type: Article
Times cited : (95)

References (31)
  • 1
    • 0036218636 scopus 로고    scopus 로고
    • Cathelicidins: Microbicidal activity, mechanisms of action, and roles in innate immunity
    • Ramanathan, B.; Davis, E. G.; Ross, C. R.; Blecha, F. Cathelicidins: microbicidal activity, mechanisms of action, and roles in innate immunity Microb. Infect. 2002, 4, 361-372
    • (2002) Microb. Infect. , vol.4 , pp. 361-372
    • Ramanathan, B.1    Davis, E.G.2    Ross, C.R.3    Blecha, F.4
  • 2
    • 0036379140 scopus 로고    scopus 로고
    • Cathelicidins, essential gene-encoded mammalian antibiotics
    • Zaiou, M.; Gallo, R. L. Cathelicidins, essential gene-encoded mammalian antibiotics J. Mol. Med. 2002, 80, 549-561
    • (2002) J. Mol. Med. , vol.80 , pp. 549-561
    • Zaiou, M.1    Gallo, R.L.2
  • 3
    • 22944458199 scopus 로고    scopus 로고
    • The role of cathelicidins in the innate host defenses of mammals
    • Zanetti, M. The role of cathelicidins in the innate host defenses of mammals Curr. Issues Mol. Biol. 2005, 7, 179-196
    • (2005) Curr. Issues Mol. Biol. , vol.7 , pp. 179-196
    • Zanetti, M.1
  • 5
    • 0031686776 scopus 로고    scopus 로고
    • Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils
    • Turner, J.; Cho, Y.; Dinh, N. N.; Waring, A. J.; Lehrer, R. I. Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils Antimicrob. Agents Chemother. 1998, 42, 2206-2214
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 2206-2214
    • Turner, J.1    Cho, Y.2    Dinh, N.N.3    Waring, A.J.4    Lehrer, R.I.5
  • 6
    • 33646367203 scopus 로고    scopus 로고
    • Identification and functional characterization of three chicken cathelicidins with potent antimicrobial activity
    • Xiao, Y.; Cai, Y.; Bommineni, Y. R.; Fernando, S. C.; Prakash, O.; Gilliland, S. E.; Zhang, G. Identification and functional characterization of three chicken cathelicidins with potent antimicrobial activity J. Biol. Chem. 2006, 281, 2858-2867
    • (2006) J. Biol. Chem. , vol.281 , pp. 2858-2867
    • Xiao, Y.1    Cai, Y.2    Bommineni, Y.R.3    Fernando, S.C.4    Prakash, O.5    Gilliland, S.E.6    Zhang, G.7
  • 7
    • 52449125862 scopus 로고    scopus 로고
    • Snake cathelicidin from Bungarus fasciatus is a potent peptide antibiotics
    • Wang, Y.; Hong, J.; Liu, X.; Yang, H.; Liu, R.; Wu, J.; Wang, A.; Lin, D.; Lai, R. Snake cathelicidin from Bungarus fasciatus is a potent peptide antibiotics PLoS One 2008, 3, e3217
    • (2008) PLoS One , vol.3 , pp. 3217
    • Wang, Y.1    Hong, J.2    Liu, X.3    Yang, H.4    Liu, R.5    Wu, J.6    Wang, A.7    Lin, D.8    Lai, R.9
  • 8
    • 84864773148 scopus 로고    scopus 로고
    • Amphibian cathelicidin fills the evolutionary gap of cathelicidin in vertebrate
    • Hao, X.; Yang, H.; Wei, L.; Yang, S.; Zhu, W.; Ma, D.; Yu, H.; Lai, R. Amphibian cathelicidin fills the evolutionary gap of cathelicidin in vertebrate Amino Acids 2012, 43, 677-685
    • (2012) Amino Acids , vol.43 , pp. 677-685
    • Hao, X.1    Yang, H.2    Wei, L.3    Yang, S.4    Zhu, W.5    Ma, D.6    Yu, H.7    Lai, R.8
  • 9
    • 23444437935 scopus 로고    scopus 로고
    • A review of antimicrobial peptides and their therapeutic potential as anti-infective drugs
    • Gordon, Y. J.; Romanowski, E. G.; McDermott, A. M. A review of antimicrobial peptides and their therapeutic potential as anti-infective drugs Curr. Eye Res. 2005, 30, 505-515
    • (2005) Curr. Eye Res. , vol.30 , pp. 505-515
    • Gordon, Y.J.1    Romanowski, E.G.2    McDermott, A.M.3
  • 12
    • 0031566434 scopus 로고    scopus 로고
    • Automated NOESY interpretation with ambiguous distance restraints: The refined NMR solution structure of the pleckstrin homology domain from beta-spectrin
    • Nilges, M.; Macias, M. J.; O'Donoghue, S. I.; Oschkinat, H. Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from beta-spectrin J. Mol. Biol. 1997, 269, 408-422
    • (1997) J. Mol. Biol. , vol.269 , pp. 408-422
    • Nilges, M.1    MacIas, M.J.2    O'Donoghue, S.I.3    Oschkinat, H.4
  • 15
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R.; Billeter, M.; Wüthrich, K. MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graphics Modell. 1996, 14, 51-55
    • (1996) J. Mol. Graphics Modell. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 16
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • Laskowski, R. A.; Moss, D. S.; Thornton, J. M. Main-chain bond lengths and bond angles in protein structures J. Mol. Biol. 1993, 231, 1049-1067
    • (1993) J. Mol. Biol. , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 17
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou, N.; Nei, M. The neighbor-joining method: a new method for reconstructing phylogenetic trees Mol. Biol. Evol. 1987, 4, 406-425
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 18
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular Evolutionary Genetics Analysis Using Maximum Likelihood, Evolutionary Distance, and Maximum Parsimony Methods
    • Tamura, K.; Peterson, D.; Peterson, N.; Stecher, G.; Nei, M.; Kumar, S. MEGA5: Molecular Evolutionary Genetics Analysis Using Maximum Likelihood, Evolutionary Distance, and Maximum Parsimony Methods Mol. Biol. Evol. 2011, 28, 2731-2739
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 22
    • 69949111622 scopus 로고    scopus 로고
    • NO generation from inorganic nitrate and nitrite: Role in physiology, nutrition and the rapeutics
    • Lundberg, J. O.; Weitzberg, E. NO generation from inorganic nitrate and nitrite: role in physiology, nutrition and the rapeutics Arch. Pharm. Res. 2009, 32, 1119-1126
    • (2009) Arch. Pharm. Res. , vol.32 , pp. 1119-1126
    • Lundberg, J.O.1    Weitzberg, E.2
  • 23
    • 77952766239 scopus 로고    scopus 로고
    • Two immunoregulatory peptides with antioxidant activity from tick salivary glands
    • Wu, J.; Wang, Y.; Liu, H.; Yang, H.; Ma, D.; Li, J.; Li, D.; Lai, R.; Yu, H. Two immunoregulatory peptides with antioxidant activity from tick salivary glands J. Biol. Chem. 2010, 285, 16606-16613
    • (2010) J. Biol. Chem. , vol.285 , pp. 16606-16613
    • Wu, J.1    Wang, Y.2    Liu, H.3    Yang, H.4    Ma, D.5    Li, J.6    Li, D.7    Lai, R.8    Yu, H.9
  • 24
    • 33745835454 scopus 로고    scopus 로고
    • Cyanobacterial lipopolysaccharides and human health-A review
    • Stewart, I.; Schluter, P.; Shaw, G. Cyanobacterial lipopolysaccharides and human health-a review Environ. Health 2006, 5, 7
    • (2006) Environ. Health , vol.5 , pp. 7
    • Stewart, I.1    Schluter, P.2    Shaw, G.3
  • 25
    • 0030689711 scopus 로고    scopus 로고
    • The natural history of amphibian skin secretions, their normal functioning and potential medical applications
    • Clarke, B. T. The natural history of amphibian skin secretions, their normal functioning and potential medical applications Biol. Rev. Cambridge Philos. Soc. 1997, 72, 365-379
    • (1997) Biol. Rev. Cambridge Philos. Soc. , vol.72 , pp. 365-379
    • Clarke, B.T.1
  • 26
    • 33847078068 scopus 로고    scopus 로고
    • Structure of the antimicrobial beta-hairpin peptide protegrin-1 in a DLPC lipid bilayer investigated by molecular dynamics simulation
    • Khandelia, H.; Kaznessis, Y. N. Structure of the antimicrobial beta-hairpin peptide protegrin-1 in a DLPC lipid bilayer investigated by molecular dynamics simulation Biochim. Biophys. Acta 2007, 1768, 509-520
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 509-520
    • Khandelia, H.1    Kaznessis, Y.N.2
  • 27
    • 0028844134 scopus 로고
    • Cathelicidins: A novel protein family with a common proregion and a variable C-terminal antimicrobial domain
    • Zanetti, M.; Gennaro, R.; Romeo, D. Cathelicidins: a novel protein family with a common proregion and a variable C-terminal antimicrobial domain FEBS Lett. 1995, 374, 1-5
    • (1995) FEBS Lett. , vol.374 , pp. 1-5
    • Zanetti, M.1    Gennaro, R.2    Romeo, D.3
  • 28
    • 0030704248 scopus 로고    scopus 로고
    • Modulation of tryptophan environment in membrane-bound melittin by negatively charged phospholipids: Implications in membrane organization and function
    • Ghosh, A. K.; Rukmini, R.; Chattopadhyay, A. Modulation of tryptophan environment in membrane-bound melittin by negatively charged phospholipids: implications in membrane organization and function Biochemistry 1997, 36, 14291-14305
    • (1997) Biochemistry , vol.36 , pp. 14291-14305
    • Ghosh, A.K.1    Rukmini, R.2    Chattopadhyay, A.3
  • 30
    • 0033166472 scopus 로고    scopus 로고
    • Unresponsiveness of MyD88-deficient mice to endotoxin
    • Kawai, T.; Adachi, O.; Ogawa, T.; Takeda, K.; Akira, S. Unresponsiveness of MyD88-deficient mice to endotoxin Immunity 1999, 11, 115-122
    • (1999) Immunity , vol.11 , pp. 115-122
    • Kawai, T.1    Adachi, O.2    Ogawa, T.3    Takeda, K.4    Akira, S.5
  • 31
    • 33644978944 scopus 로고    scopus 로고
    • Endotoxin (lipopolysaccharide) neutralization by innate immunity host-defense peptides. Peptide properties and plausible modes of action
    • Rosenfeld, Y.; Papo, N.; Shai, Y. Endotoxin (lipopolysaccharide) neutralization by innate immunity host-defense peptides. Peptide properties and plausible modes of action J. Biol. Chem. 2006, 281, 1636-1643
    • (2006) J. Biol. Chem. , vol.281 , pp. 1636-1643
    • Rosenfeld, Y.1    Papo, N.2    Shai, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.