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Volumn 53, Issue , 2014, Pages 79-88

A novel single-domain peptide, anti-LPS factor from prawn: Synthesis of peptide, antimicrobial properties and complete molecular characterization

Author keywords

Anti lipopolysaccharide; Antimicrobial peptide; Hemolysis; Pathogen; Prawn

Indexed keywords

ANTI LIPOPOLYSACCHARIDE FACTOR; CYSTEINE; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; LIPOPOLYSACCHARIDE; PEPTIDE;

EID: 84899442969     PISSN: 01969781     EISSN: 18735169     Source Type: Journal    
DOI: 10.1016/j.peptides.2013.11.008     Document Type: Article
Times cited : (29)

References (61)
  • 1
    • 0001994881 scopus 로고    scopus 로고
    • Susceptibility testing of antimicrobials in liquid media
    • V. Lorian, 4th ed. Williams and Wilkins Baltimore, MD
    • D. Amsterdam Susceptibility testing of antimicrobials in liquid media V. Lorian, Antibiotics in laboratory medicine 4th ed. 1996 Williams and Wilkins Baltimore, MD 52 111
    • (1996) Antibiotics in Laboratory Medicine , pp. 52-111
    • Amsterdam, D.1
  • 2
    • 84881113852 scopus 로고    scopus 로고
    • Fish lily type lectin-1 contains β-prism 2 architecture: Immunological characterization
    • A. Arasu, K. Venkatesh, S. Akila, P. Rajesh, N. Prabha, and B. Prasanth et al. Fish lily type lectin-1 contains β-prism 2 architecture: Immunological characterization Mol Immunol 56 2013 497 506
    • (2013) Mol Immunol , vol.56 , pp. 497-506
    • Arasu, A.1    Venkatesh, K.2    Akila, S.3    Rajesh, P.4    Prabha, N.5    Prasanth, B.6
  • 3
    • 33645751940 scopus 로고    scopus 로고
    • How can a ß-sheet peptide be both a potent antimicrobial and harmfully toxic? Molecular dynamics simulations of protegrin-1 in Micelles
    • A.L. Allison, K. Himanshu, and N.K. Yiannis How can a ß-sheet peptide be both a potent antimicrobial and harmfully toxic? Molecular dynamics simulations of protegrin-1 in Micelles Biopolymers 84 2006 219 231
    • (2006) Biopolymers , vol.84 , pp. 219-231
    • Allison, A.L.1    Himanshu, K.2    Yiannis, N.K.3
  • 5
    • 84871624213 scopus 로고    scopus 로고
    • A WAP domain containing antimicrobial peptide from freshwater prawn M. Rosenbergii: Immune characterization
    • J. Arockiaraj, J.G. Annie, M. Dhanaraj, G. Ranganath, J. Milton, and S. Arun et al. A WAP domain containing antimicrobial peptide from freshwater prawn M. rosenbergii: immune characterization Fish Shellfish Immunol 34 2012 109 118
    • (2012) Fish Shellfish Immunol , vol.34 , pp. 109-118
    • Arockiaraj, J.1    Annie, J.G.2    Dhanaraj, M.3    Ranganath, G.4    Milton, J.5    Arun, S.6
  • 6
    • 84883157872 scopus 로고    scopus 로고
    • Macrobrachium rosenbergii Cathepsin L: Molecular characterization and gene expression in response to viral and bacterial infections
    • J. Arockiaraj, J.G. Annie, M. Dhanaraj, M.K. Thirumalai, P. Mukesh, and J. Milton et al. Macrobrachium rosenbergii Cathepsin L: molecular characterization and gene expression in response to viral and bacterial infections Microbiol Res 168 2013 569 579
    • (2013) Microbiol Res , vol.168 , pp. 569-579
    • Arockiaraj, J.1    Annie, J.G.2    Dhanaraj, M.3    Thirumalai, M.K.4    Mukesh, P.5    Milton, J.6
  • 7
    • 84878667076 scopus 로고    scopus 로고
    • A novel prophenoloxidase, hemocyanin encoded copper containing active enzyme from prawn: Gene characterization
    • J. Arockiaraj, J.G. Annie, P. Gopi, J. Milton, P. Mukesh, and B. Prasanth et al. A novel prophenoloxidase, hemocyanin encoded copper containing active enzyme from prawn: gene characterization Gene 524 2013 139 151
    • (2013) Gene , vol.524 , pp. 139-151
    • Arockiaraj, J.1    Annie, J.G.2    Gopi, P.3    Milton, J.4    Mukesh, P.5    Prasanth, B.6
  • 9
    • 84884986921 scopus 로고    scopus 로고
    • An unconventional antimicrobial protein histone from freshwater prawn Macrobrachium rosenbergii: Analysis of immune properties
    • J. Arockiaraj, J.G. Annie, K. Venkatesh, P. Rajesh, B. Prasanth, and M.K. Thirumalai et al. An unconventional antimicrobial protein histone from freshwater prawn Macrobrachium rosenbergii: analysis of immune properties Fish Shellfish Immunol 35 2013 1511 1522
    • (2013) Fish Shellfish Immunol , vol.35 , pp. 1511-1522
    • Arockiaraj, J.1    Annie, J.G.2    Venkatesh, K.3    Rajesh, P.4    Prasanth, B.5    Thirumalai, M.K.6
  • 10
    • 84865746039 scopus 로고    scopus 로고
    • Molecular functions of chaperonin gene, containing tailless complex polypeptide 1 from Macrobrachium rosenbergii
    • J. Arockiaraj, V. Puganeshwaran, E. Sarasvathi, S. Arun, R.Y. Othman, and B. Subha Molecular functions of chaperonin gene, containing tailless complex polypeptide 1 from Macrobrachium rosenbergii Gene 508 2012 241 249
    • (2012) Gene , vol.508 , pp. 241-249
    • Arockiaraj, J.1    Puganeshwaran, V.2    Sarasvathi, E.3    Arun, S.4    Othman, R.Y.5    Subha, B.6
  • 11
    • 0034694378 scopus 로고    scopus 로고
    • Shrimp immunity and disease control
    • E. Bachere Shrimp immunity and disease control Aquaculture 191 2000 3 11
    • (2000) Aquaculture , vol.191 , pp. 3-11
    • Bachere, E.1
  • 12
    • 70349728612 scopus 로고    scopus 로고
    • MultiLoc2: Integrating phylogeny and Gene Ontology terms improves subcellular protein localization prediction
    • T. Blum, S. Briesemeister, and O. Kohlbacher MultiLoc2: integrating phylogeny and Gene Ontology terms improves subcellular protein localization prediction BMC Bioinform 10 2009 274
    • (2009) BMC Bioinform , vol.10 , pp. 274
    • Blum, T.1    Briesemeister, S.2    Kohlbacher, O.3
  • 13
    • 54949120212 scopus 로고    scopus 로고
    • Gram negative bacterial lipopolysaccharide retention by a positively charged new-generation filter
    • I. Bononi, V. Balatti, S. Gaeta, and M. Tognon Gram negative bacterial lipopolysaccharide retention by a positively charged new-generation filter Appl Environ Microbiol 74 2008 6470 6472
    • (2008) Appl Environ Microbiol , vol.74 , pp. 6470-6472
    • Bononi, I.1    Balatti, V.2    Gaeta, S.3    Tognon, M.4
  • 14
    • 1642463826 scopus 로고    scopus 로고
    • The prophenoloxidase-activating system in invertebrates
    • DOI 10.1111/j.0105-2896.2004.00116.x
    • L. Cerenius, and K. Söderhäll The prophenoloxidase-activating system in invertebrates Immunol Rev 198 2004 116 126 (Pubitemid 38406940)
    • (2004) Immunological Reviews , vol.198 , pp. 116-126
    • Cerenius, L.1    Soderhall, K.2
  • 15
    • 34247558656 scopus 로고    scopus 로고
    • Identification and characterization of a cDNA encoding a crustin-like, putative antibacterial protein from the American lobster Homarus americanus
    • DOI 10.1016/j.molimm.2007.02.028, PII S0161589007000934
    • A.E. Christie, S. Rus, C.C. Goiney, C.M. Smith, D.W. Towle, and P.S. Dickinson Identification and characterization of a cDNA encoding a crustin-like, putative antibacterial protein from the American lobster Homarus americanus Mol Immunol 44 2007 3333 3337 (Pubitemid 46678201)
    • (2007) Molecular Immunology , vol.44 , Issue.13 , pp. 3333-3337
    • Christie, A.E.1    Rus, S.2    Goiney, C.C.3    Smith, C.M.4    Towle, D.W.5    Dickinson, P.S.6
  • 17
    • 51749085388 scopus 로고    scopus 로고
    • HELIQUEST: A web server to screen sequences with specific-helical properties
    • R. Gautier, D. Douguet, B. Antonny, and G. Drin HELIQUEST: a web server to screen sequences with specific-helical properties Bioinformatics 24 2008 2101 2102
    • (2008) Bioinformatics , vol.24 , pp. 2101-2102
    • Gautier, R.1    Douguet, D.2    Antonny, B.3    Drin, G.4
  • 18
    • 0037012956 scopus 로고    scopus 로고
    • Specific interactions of the antimicrobial peptide cyclic β-sheet tachyplesin I with lipopolysaccharides
    • DOI 10.1016/S0005-2736(02)00358-9, PII S0005273602003589
    • Y. Hirakura, S. Kobayashi, and K. Matsuzaki Specific interactions of the antimicrobial peptide cyclic ß-sheet tachyplesin I with lipopolysaccharides Biochim Biophys Acta 1562 2002 32 36 (Pubitemid 34461942)
    • (2002) Biochimica et Biophysica Acta - Biomembranes , vol.1562 , Issue.1-2 , pp. 32-36
    • Hirakura, Y.1    Kobayashi, S.2    Matsuzaki, K.3
  • 19
    • 0027171383 scopus 로고
    • Crystal structure of an endotoxin-neutralizing protein from the horseshoe crab, Limulus anti-LPS factor, at 1.5 A resolution
    • A. Hoess, S. Watson, G.R. Siber, and R. Liddington Crystal structure of an endotoxin-neutralizing protein from the horseshoe crab, Limulus anti-LPS factor, at 1.5 Å resolution EMBO J 12 1993 3351 3356 (Pubitemid 23256421)
    • (1993) EMBO Journal , vol.12 , Issue.9 , pp. 3351-3356
    • Hoess, A.1    Watson, S.2    Siber, G.R.3    Liddington, R.4
  • 20
    • 14544293955 scopus 로고    scopus 로고
    • The interactions of antimicrobial peptides derived from lysozyme with model membrane systems
    • N.H. Howard, J. Weiguo, J.S. David, T. Tony, P. Yup, and C.K. Sun et al. The interactions of antimicrobial peptides derived from lysozyme with model membrane systems Biochim Biophys Acta 1668 2005 175 189
    • (2005) Biochim Biophys Acta , vol.1668 , pp. 175-189
    • Howard, N.H.1    Weiguo, J.2    David, J.S.3    Tony, T.4    Yup, P.5    Sun, C.K.6
  • 21
    • 78650685276 scopus 로고    scopus 로고
    • Molecular cloning, genomic organization and antibacterial activity of a second isoform of antilipopolysaccharide factor (ALF) from the mud crab, Scylla paramamosain
    • C. Imjongjirak, P. Amparyup, and A. Tassanakajon Molecular cloning, genomic organization and antibacterial activity of a second isoform of antilipopolysaccharide factor (ALF) from the mud crab, Scylla paramamosain Fish Shellfish Immunol 30 2011 58 66
    • (2011) Fish Shellfish Immunol , vol.30 , pp. 58-66
    • Imjongjirak, C.1    Amparyup, P.2    Tassanakajon, A.3
  • 22
    • 34247334692 scopus 로고    scopus 로고
    • Antilipopolysaccharide factor (ALF) of mud crab Scylla paramamosain: Molecular cloning, genomic organization and the antimicrobial activity of its synthetic LPS binding domain
    • DOI 10.1016/j.molimm.2007.01.028, PII S0161589007000697
    • C. Imjongjirak, P. Amparyup, A. Tassanakajon, and S. Sittipraneed Antilipopolysaccharide factor (ALF) of mud crab Scylla paramamosain: molecular cloning, genomic organization and the antimicrobial activity of its synthetic LPS binding domain Mol Immunol 44 2007 3195 3203 (Pubitemid 46628664)
    • (2007) Molecular Immunology , vol.44 , Issue.12 , pp. 3195-3203
    • Imjongjirak, C.1    Amparyup, P.2    Tassanakajon, A.3    Sittipraneed, S.4
  • 24
    • 0035958848 scopus 로고    scopus 로고
    • A novel linear amphipathic ß-sheet cationic antimicrobial peptide with enhanced selectivity for bacterial lipids
    • B. Jack, W. Russell, K. Jason, H. Janet, M.E. Richard, and F.E. Raquel et al. A novel linear amphipathic ß-sheet cationic antimicrobial peptide with enhanced selectivity for bacterial lipids J Biol Chem 276 2001 27899 27906
    • (2001) J Biol Chem , vol.276 , pp. 27899-27906
    • Jack, B.1    Russell, W.2    Jason, K.3    Janet, H.4    Richard, M.E.5    Raquel, F.E.6
  • 25
    • 85027949036 scopus 로고    scopus 로고
    • Effect of the anti-lipopolysaccharide factor isoform 3 (ALFPm3) from Penaeus monodon on Vibrio harveyi cells
    • P. Jaree, A. Tassanakajon, and K. Somboonwiwat Effect of the anti-lipopolysaccharide factor isoform 3 (ALFPm3) from Penaeus monodon on Vibrio harveyi cells Dev Comp Immunol 38 2012 554 560
    • (2012) Dev Comp Immunol , vol.38 , pp. 554-560
    • Jaree, P.1    Tassanakajon, A.2    Somboonwiwat, K.3
  • 26
    • 0032993170 scopus 로고    scopus 로고
    • Antimicrobial and cytolytic polypeptides of amoeboid protozoa-effector molecules of primitive phagocytes
    • M. Leippe Antimicrobial and cytolytic polypeptides of amoeboid protozoa-effector molecules of primitive phagocytes Dev Comp Immunol 23 1999 267 269
    • (1999) Dev Comp Immunol , vol.23 , pp. 267-269
    • Leippe, M.1
  • 28
    • 40849102917 scopus 로고    scopus 로고
    • Molecular cloning, genomic organization and functional analysis of an anti-lipopolysaccharide factor from Chinese mitten crab Eriocheir sinensis
    • C. Li, J. Zhao, L. Song, C. Mu, H. Zhang, and Y. Gai et al. Molecular cloning, genomic organization and functional analysis of an anti-lipopolysaccharide factor from Chinese mitten crab Eriocheir sinensis Dev Comp Immunol 32 2008 784 794
    • (2008) Dev Comp Immunol , vol.32 , pp. 784-794
    • Li, C.1    Zhao, J.2    Song, L.3    Mu, C.4    Zhang, H.5    Gai, Y.6
  • 29
    • 33750306792 scopus 로고    scopus 로고
    • Antilipopolysaccharide factor interferes with white spot syndrome virus replication in vitro and in vivo in the crayfish Pacifastacus leniusculus
    • DOI 10.1128/JVI.01101-06
    • H. Liu, P. Jiravanichpaisal, I. Soderhall, L. Cerenius, and K. Soderhall Antilipopolysaccharide factor interferes with white spot syndrome virus replication in vitro and in vivo in the crayfish Pacifastacus leniusculus J Virol 80 2006 10365 10371 (Pubitemid 44628884)
    • (2006) Journal of Virology , vol.80 , Issue.21 , pp. 10365-10371
    • Liu, H.1    Jiravanichpaisal, P.2    Soderhall, I.3    Cerenius, L.4    Soderhall, K.5
  • 30
    • 84861483667 scopus 로고    scopus 로고
    • Characterization of two isoforms of antiliopolysacchride factors (Sp-ALFs) from the mud crab Scylla paramamosain
    • H.P. Liu, R.Y. Chen, Q.X. Zhang, Q.Y. Wang, C.R. Li, and H. Peng et al. Characterization of two isoforms of antiliopolysacchride factors (Sp-ALFs) from the mud crab Scylla paramamosain Fish Shellfish Immunol 33 2012 1 10
    • (2012) Fish Shellfish Immunol , vol.33 , pp. 1-10
    • Liu, H.P.1    Chen, R.Y.2    Zhang, Q.X.3    Wang, Q.Y.4    Li, C.R.5    Peng, H.6
  • 31
    • 0035710746 scopus 로고    scopus 로고
    • -ΔΔCT method
    • DOI 10.1006/meth.2001.1262
    • K.J. Livak, and T.D. Schmittgenm Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C (T)) method Methods 25 2001 402 408 (Pubitemid 34164012)
    • (2001) Methods , vol.25 , Issue.4 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 32
    • 0002755236 scopus 로고
    • Antibiotics in laboratory medicine
    • J.F. Acar, F.W. Goldstein, 4th ed. Williams & Walkins Awaverly London
    • V. Lorian Antibiotics in laboratory medicine J.F. Acar, F.W. Goldstein, Disk susceptibility test 4th ed. 1995 Williams & Walkins Awaverly London 1
    • (1995) Disk Susceptibility Test , pp. 1
    • Lorian, V.1
  • 34
    • 43049179999 scopus 로고    scopus 로고
    • LPS/TLR4 signal transduction pathway
    • Y.C. Lu, W.C. Yeh, and P.S. Ohashi LPS/TLR4 signal transduction pathway Cytokine 42 2 2008 145 151
    • (2008) Cytokine , vol.42 , Issue.2 , pp. 145-151
    • Lu, Y.C.1    Yeh, W.C.2    Ohashi, P.S.3
  • 35
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • DOI 10.1038/nature01511
    • M. Mann, and R. Aebersold Mass spectrometry-based proteomics Nature 422 2003 198 207 (Pubitemid 36362757)
    • (2003) Nature , vol.422 , Issue.6928 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 36
    • 0021799698 scopus 로고
    • Isolation and biological activities of limulus anticoagulant (anti-LPS factor) which interacts with lipopolysaccharide (LPS)
    • T. Morita, S. Ohtsubo, T. Nakamura, S. Tanaka, S. Iwanaga, and K. Ohashi Isolation and biological activities of limulus anticoagulant (anti-LPS factor) which interacts with lipopolysaccharide (LPS) J Biochem 97 1985 1611 1620 (Pubitemid 15008056)
    • (1985) Journal of Biochemistry , vol.97 , Issue.6 , pp. 1611-1620
    • Morita, T.1    Ohtsubo, S.2    Nakamura, T.3
  • 37
    • 0023352436 scopus 로고
    • Primary structure of anti-lipopolysaccharide factor from American horseshoe crab, Limulus polyphemus
    • T. Muta, T. Miyata, F. Tokunaga, T. Nakamura, and S. Iwanaga Primary structure of anti-lipopolysaccharide factor from American horseshoe crab, Limulus polyphemus J Biochem 101 1987 1321 1330
    • (1987) J Biochem , vol.101 , pp. 1321-1330
    • Muta, T.1    Miyata, T.2    Tokunaga, F.3    Nakamura, T.4    Iwanaga, S.5
  • 38
    • 33645883237 scopus 로고    scopus 로고
    • Cloning and characterization of a LPS-regulatory gene having an LPS binding domain in kuruma prawn Marsupenaeus japonicus
    • H. Nagoshi, H. Inagawa, K. Morii, H. Harada, C. Kohchi, and T. Nishizawa et al. Cloning and characterization of a LPS-regulatory gene having an LPS binding domain in kuruma prawn Marsupenaeus japonicus Mol Immunol 43 2006 2061 2069
    • (2006) Mol Immunol , vol.43 , pp. 2061-2069
    • Nagoshi, H.1    Inagawa, H.2    Morii, K.3    Harada, H.4    Kohchi, C.5    Nishizawa, T.6
  • 40
    • 0032489294 scopus 로고    scopus 로고
    • Mechanism of action of the antimicrobial peptide buforin II: Buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions
    • DOI 10.1006/bbrc.1998.8159
    • C.B. Park, H.S. Kim, and S.C. Kim Mechanism of action of the antimicrobial peptide buforin II: buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions Biochem Biophys Res Commun 244 1998 253 257 (Pubitemid 28419934)
    • (1998) Biochemical and Biophysical Research Communications , vol.244 , Issue.1 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 41
    • 84860601877 scopus 로고    scopus 로고
    • Antimicrobial peptides: A key component of innate immunity
    • M. Pasupuleti, M. Malmsten, and A. Schmidtchen Antimicrobial peptides: a key component of innate immunity Crit Rev Biotechnol 32 2011 143 171
    • (2011) Crit Rev Biotechnol , vol.32 , pp. 143-171
    • Pasupuleti, M.1    Malmsten, M.2    Schmidtchen, A.3
  • 42
    • 0033753732 scopus 로고    scopus 로고
    • DNAssist: The integrated editing and analysis of molecular biology sequences in windows
    • H.G. Patterton, and S. Graves DNAssist: the integrated editing and analysis of molecular biology sequences in windows Bioinform Appl Note 16 2000 652 653
    • (2000) Bioinform Appl Note , vol.16 , pp. 652-653
    • Patterton, H.G.1    Graves, S.2
  • 43
    • 84864284822 scopus 로고    scopus 로고
    • Cloning and expression analysis of an anti-lipopolysaccharide factor from giant freshwater prawn, Macrobrachium rosenbergii
    • Q. Ren, Z.Q. Du, M. Li, C.Y. Zhang, and K.P. Chen Cloning and expression analysis of an anti-lipopolysaccharide factor from giant freshwater prawn, Macrobrachium rosenbergii Mol Biol Rep 39 2012 7673 7680
    • (2012) Mol Biol Rep , vol.39 , pp. 7673-7680
    • Ren, Q.1    Du, Z.Q.2    Li, M.3    Zhang, C.Y.4    Chen, K.P.5
  • 44
    • 0029902934 scopus 로고    scopus 로고
    • High affinity endotoxin-binding and neutralizing peptides based on the crystal structure of recombinant Limulus anti-lipopolysaccharide factor
    • DOI 10.1074/jbc.271.45.28120
    • C. Ried, C. Wahl, T. Miethke, G. Wellnhofer, C. Landgraf, and J. Schneider-Mergener High affinity endotoxin-binding and neutralizing peptides based on the crystal structure of recombinant Limulus anti-lipopolysaccharide factor J Biol Chem 271 1996 28120 28127 (Pubitemid 26374620)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.45 , pp. 28120-28127
    • Ried, C.1    Wahl, C.2    Miethke, T.3    Wellnhofer, G.4    Landgraf, C.5    Schneider-Mergener, J.6    Hoess, A.7
  • 45
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: A unified platform for automated protein structure and function prediction
    • A. Roy, A. Kucukural, and Y. Zhang I-TASSER: a unified platform for automated protein structure and function prediction Nat Prot 5 2010 725 738
    • (2010) Nat Prot , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 46
    • 84864460609 scopus 로고    scopus 로고
    • COFACTOR: An accurate comparative algorithm for structure-based protein function annotation
    • A. Roy, J. Yang, and Y. Zhang COFACTOR: an accurate comparative algorithm for structure-based protein function annotation Nucl Acids Res 0 2012 W471 W477
    • (2012) Nucl Acids Res , vol.0
    • Roy, A.1    Yang, J.2    Zhang, Y.3
  • 47
    • 0032752132 scopus 로고    scopus 로고
    • Interaction of cationic peptides with lipoteichoic acid and gram-positive bacteria
    • M.G. Scott, M.R. Gold, and R.E. Hancock Interaction of cationic peptides with lipoteichoic acid and gram-positive bacteria Infect Immun 67 1999 6445 6453
    • (1999) Infect Immun , vol.67 , pp. 6445-6453
    • Scott, M.G.1    Gold, M.R.2    Hancock, R.E.3
  • 48
    • 33749578940 scopus 로고    scopus 로고
    • Statistical potential for assessment and prediction of protein structures
    • DOI 10.1110/ps.062416606
    • M.Y. Shen, and A. Sali Statistical potential for assessment and prediction of protein structures Protein Sci 15 2006 2507 2524 (Pubitemid 44771688)
    • (2006) Protein Science , vol.15 , Issue.11 , pp. 2507-2524
    • Shen, M.-Y.1    Sali, A.2
  • 49
    • 46549083956 scopus 로고    scopus 로고
    • Localization of anti-lipopolysaccharide factor (ALFPm3) in tissues of the black tiger shrimp, Penaeus monodon and characterization of its binding properties
    • K. Somboonwiwat, E. Bachere, V. Rimphanitchayakit, and A. Tassanakajon Localization of anti-lipopolysaccharide factor (ALFPm3) in tissues of the black tiger shrimp, Penaeus monodon and characterization of its binding properties Dev Comp Immunol 32 2008 1170 1176
    • (2008) Dev Comp Immunol , vol.32 , pp. 1170-1176
    • Somboonwiwat, K.1    Bachere, E.2    Rimphanitchayakit, V.3    Tassanakajon, A.4
  • 52
    • 39149087407 scopus 로고    scopus 로고
    • Anti-lipopolysaccharide factor in Litopenaeus vannamei (LvALF): A broad spectrum antimicrobial peptide essential for shrimp immunity against bacterial and fungal infection
    • E. Vega, N.A. Leary, J.E. Shockey, J. Robalino, C. Payne, and C.L. Browdy Anti-lipopolysaccharide factor in Litopenaeus vannamei (LvALF): a broad spectrum antimicrobial peptide essential for shrimp immunity against bacterial and fungal infection Mol Immunol 45 2008 1916 1925
    • (2008) Mol Immunol , vol.45 , pp. 1916-1925
    • Vega, E.1    Leary, N.A.2    Shockey, J.E.3    Robalino, J.4    Payne, C.5    Browdy, C.L.6
  • 53
    • 0036224089 scopus 로고    scopus 로고
    • Cloning of anti-LPS factor cDNA from Tachypleus tridentatus, expression in Bombyx mori larvae and its biological activity in vitro
    • D.N. Wang, J.W. Liu, G.Z. Yang, W.J. Zhang, and X.F. Wu Cloning of anti-LPS factor cDNA from Tachypleus tridentatus, expression in Bombyx mori larvae and its biological activity in vitro Mol Biotechnol 21 2002 1 7
    • (2002) Mol Biotechnol , vol.21 , pp. 1-7
    • Wang, D.N.1    Liu, J.W.2    Yang, G.Z.3    Zhang, W.J.4    Wu, X.F.5
  • 54
    • 82955247061 scopus 로고    scopus 로고
    • A new anti-lipopolysaccharide factor (EsALF-3) from Eriocheir sinensis with antimicrobial activity
    • L. Wang, Y. Zhang, L. Wang, J. Yang, Z. Zhou, and Y. Gai et al. A new anti-lipopolysaccharide factor (EsALF-3) from Eriocheir sinensis with antimicrobial activity Afr J Biotechnol 10 2011 17678 17689
    • (2011) Afr J Biotechnol , vol.10 , pp. 17678-17689
    • Wang, L.1    Zhang, Y.2    Wang, L.3    Yang, J.4    Zhou, Z.5    Gai, Y.6
  • 58
    • 0006558813 scopus 로고    scopus 로고
    • A Phase Transition for the Minimum Free Energy of Secondary Structures of a Random RNA
    • DOI 10.1006/aama.1996.0502, PII S0196885896905023
    • M. Xiong, and M.S. Waterman A phase transition for the minimum free energy of secondary structures of a random RNA Adv Appl Math 18 1997 111 132 (Pubitemid 127341274)
    • (1997) Advances in Applied Mathematics , vol.18 , Issue.2 , pp. 111-132
    • Xiong, M.1    Waterman, M.S.2
  • 59
    • 65249136556 scopus 로고    scopus 로고
    • NMR structure of rALF-Pm3, an anti-lipopolysaccharide factor from shrimp: Model of the possible lipid A-binding site
    • Y. Yang, H. Boze, P. Chemardin, A. Padilla, G. Moulin, and A. Tassanakajon et al. NMR structure of rALF-Pm3, an anti-lipopolysaccharide factor from shrimp: model of the possible lipid A-binding site Biopolymers 91 2009 207 220
    • (2009) Biopolymers , vol.91 , pp. 207-220
    • Yang, Y.1    Boze, H.2    Chemardin, P.3    Padilla, A.4    Moulin, G.5    Tassanakajon, A.6
  • 60
    • 3042581007 scopus 로고    scopus 로고
    • Flexible structure alignment by chaining aligned fragment pairs allowing twists
    • Y. Ye, and A. Godzik Flexible structure alignment by chaining aligned fragment pairs allowing twists Bioinformatics 9 2003 II246 II255
    • (2003) Bioinformatics , vol.9
    • Ye, Y.1    Godzik, A.2
  • 61
    • 67650376043 scopus 로고    scopus 로고
    • Identification, cloning, characterization and recombinant expression of an antilipopolysaccharide factor from the hemocytes of Indian mud crab, Scylla serrata
    • R.D. Yedery, and K.V.R. Reddy Identification, cloning, characterization and recombinant expression of an antilipopolysaccharide factor from the hemocytes of Indian mud crab, Scylla serrata Fish Shellfish Immunol 27 2009 275 284
    • (2009) Fish Shellfish Immunol , vol.27 , pp. 275-284
    • Yedery, R.D.1    Reddy, K.V.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.