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Volumn 360, Issue 1, 2007, Pages 156-162

Recombinant expression, synthesis, purification, and solution structure of arenicin

Author keywords

Hairpin; Antimicrobial activity; Antimicrobial peptide; Arenicin; Arenicola marina; CD; Expression; Folding; Fusion protein; Lugworm; Marine invertebrate; NMR; Purification; Recombinant

Indexed keywords

AMPHOLYTE; DODECYL SULFATE SODIUM; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEIN ARENICIN 2; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 34250891314     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.06.029     Document Type: Article
Times cited : (73)

References (21)
  • 1
    • 0042830450 scopus 로고    scopus 로고
    • Antibacterial peptides: basic facts and emerging concepts
    • Boman H.G. Antibacterial peptides: basic facts and emerging concepts. J. Intern. Med. 254 (2003) 197-215
    • (2003) J. Intern. Med. , vol.254 , pp. 197-215
    • Boman, H.G.1
  • 2
    • 1642545489 scopus 로고    scopus 로고
    • Antimicrobial peptides: from invertebrates to vertebrates
    • Bulet P., Stocklin R., and Menin L. Antimicrobial peptides: from invertebrates to vertebrates. Immunol. Rev. 198 (2004) 169-184
    • (2004) Immunol. Rev. , vol.198 , pp. 169-184
    • Bulet, P.1    Stocklin, R.2    Menin, L.3
  • 4
    • 0033214630 scopus 로고    scopus 로고
    • Myticin, a novel cysteine-rich antimicrobial peptide isolated from haemocytes and plasma of the mussel Mytilus galloprovincialis
    • Mitta G., Hubert F., Noel T., and Roch P. Myticin, a novel cysteine-rich antimicrobial peptide isolated from haemocytes and plasma of the mussel Mytilus galloprovincialis. Eur. J. Biochem. 265 (1999) 71-78
    • (1999) Eur. J. Biochem. , vol.265 , pp. 71-78
    • Mitta, G.1    Hubert, F.2    Noel, T.3    Roch, P.4
  • 5
    • 0024741960 scopus 로고
    • Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusins I and II: chemical structures and biological activity
    • Miyata T., Tokunaga F., Yoneya T., Yoshikawa K., Iwanaga S., Niwa M., Takao T., and Shimonishi Y. Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusins I and II: chemical structures and biological activity. J. Biochem. (Tokyo) 106 (1989) 663-668
    • (1989) J. Biochem. (Tokyo) , vol.106 , pp. 663-668
    • Miyata, T.1    Tokunaga, F.2    Yoneya, T.3    Yoshikawa, K.4    Iwanaga, S.5    Niwa, M.6    Takao, T.7    Shimonishi, Y.8
  • 6
    • 0029020955 scopus 로고
    • A novel big defensin identified in horseshoe crab hemocytes: isolation, amino acid sequence, and antibacterial activity
    • Saito T., Kawabata S., Shigenaga T., Takayenoki Y., Cho J., Nakajima H., Hirata M., and Iwanaga S. A novel big defensin identified in horseshoe crab hemocytes: isolation, amino acid sequence, and antibacterial activity. J. Biochem. (Tokyo) 117 (1995) 1131-1137
    • (1995) J. Biochem. (Tokyo) , vol.117 , pp. 1131-1137
    • Saito, T.1    Kawabata, S.2    Shigenaga, T.3    Takayenoki, Y.4    Cho, J.5    Nakajima, H.6    Hirata, M.7    Iwanaga, S.8
  • 7
    • 0030692830 scopus 로고    scopus 로고
    • Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (Decapoda)
    • Destoumieux D., Bulet P., Loew D., Van D.A., Rodriguez J., and Bachere E. Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (Decapoda). J. Biol. Chem. 272 (1997) 28398-28406
    • (1997) J. Biol. Chem. , vol.272 , pp. 28398-28406
    • Destoumieux, D.1    Bulet, P.2    Loew, D.3    Van, D.A.4    Rodriguez, J.5    Bachere, E.6
  • 8
    • 0001505184 scopus 로고    scopus 로고
    • Styelins, broad-spectrum antimicrobial peptides from the solitary tunicate, Styela clava
    • Lee I.H., Cho Y., and Lehrer R.I. Styelins, broad-spectrum antimicrobial peptides from the solitary tunicate, Styela clava. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 118 (1997) 515-521
    • (1997) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.118 , pp. 515-521
    • Lee, I.H.1    Cho, Y.2    Lehrer, R.I.3
  • 9
    • 0034623953 scopus 로고    scopus 로고
    • Styelin D, an extensively modified antimicrobial peptide from ascidian hemocytes
    • Taylor S.W., Craig A.G., Fischer W.H., Park M., and Lehrer R.I. Styelin D, an extensively modified antimicrobial peptide from ascidian hemocytes. J. Biol. Chem. 275 (2000) 38417-38426
    • (2000) J. Biol. Chem. , vol.275 , pp. 38417-38426
    • Taylor, S.W.1    Craig, A.G.2    Fischer, W.H.3    Park, M.4    Lehrer, R.I.5
  • 13
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H., and von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166 (1987) 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 16
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels C., Xia T., Billiter M., Guntert P., and Wuthrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR 6 (1995) 1-10
    • (1995) J. Biomol. NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.2    Billiter, M.3    Guntert, P.4    Wuthrich, K.5
  • 17
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann T., Guntert P., and Wuthrich K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J. Mol. Biol. 319 (2002) 209-227
    • (2002) J. Mol. Biol. , vol.319 , pp. 209-227
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 18
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 415 (2002) 389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 19
    • 0018339835 scopus 로고
    • The interpretation of near-ultraviolet circular dichroism
    • Kahn P.C. The interpretation of near-ultraviolet circular dichroism. Methods Enzymol. 61 (1979) 339-378
    • (1979) Methods Enzymol. , vol.61 , pp. 339-378
    • Kahn, P.C.1
  • 20
    • 0027768907 scopus 로고
    • Environmental characteristics of residues in proteins: three-dimensional molecular hydrophobicity potential approach
    • Efremov R.G., and Alix A.J. Environmental characteristics of residues in proteins: three-dimensional molecular hydrophobicity potential approach. J. Biomol. Struct. Dyn. 11 (1993) 483-507
    • (1993) J. Biomol. Struct. Dyn. , vol.11 , pp. 483-507
    • Efremov, R.G.1    Alix, A.J.2
  • 21
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., and Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14 (1996) 51-55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3


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