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Volumn 45, Issue 9, 2008, Pages 2531-2536

Activation of cathepsin L by the cathelin-like domain of protegrin-3

Author keywords

Antimicrobial peptide; Cathelicidin; Cystatin; Innate immunity

Indexed keywords

CATHELICIDIN; CATHELIN; CATHEPSIN L; CYSTATIN; PROTEGRIN; PROTEGRIN 3; PROTEINASE; UNCLASSIFIED DRUG;

EID: 40849084973     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2008.01.007     Document Type: Article
Times cited : (20)

References (21)
  • 2
    • 0027731168 scopus 로고
    • The structures of native phosphorylated chicken cystatin and of a recombinant unphosphorylated variant in solution
    • Dieckmann T., Mitschang L., Hofmann M., Kos J., Turk V., Auerswald E.V., Jaenicke R., and Oschkinat H. The structures of native phosphorylated chicken cystatin and of a recombinant unphosphorylated variant in solution. J. Mol. Biol. 234 (1993) 1048-1059
    • (1993) J. Mol. Biol. , vol.234 , pp. 1048-1059
    • Dieckmann, T.1    Mitschang, L.2    Hofmann, M.3    Kos, J.4    Turk, V.5    Auerswald, E.V.6    Jaenicke, R.7    Oschkinat, H.8
  • 3
    • 36148983045 scopus 로고    scopus 로고
    • Inducible antibacterial response of scorpion venom gland
    • Gao B., Tian C., and Zhu S. Inducible antibacterial response of scorpion venom gland. Peptides 28 (2007) 2299-2305
    • (2007) Peptides , vol.28 , pp. 2299-2305
    • Gao, B.1    Tian, C.2    Zhu, S.3
  • 4
    • 0037805704 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases regulate antigen presentation
    • Honey K., and Rudensky A.Y. Lysosomal cysteine proteases regulate antigen presentation. Nat. Rev. Immunol. 3 (2003) 472-482
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 472-482
    • Honey, K.1    Rudensky, A.Y.2
  • 5
    • 33750984761 scopus 로고    scopus 로고
    • The role of cystatins in cells of the immune system
    • Kopitar-Jerala N. The role of cystatins in cells of the immune system. FEBS Lett. 580 (2006) 6295-6301
    • (2006) FEBS Lett. , vol.580 , pp. 6295-6301
    • Kopitar-Jerala, N.1
  • 6
    • 77957012032 scopus 로고
    • Spectrophotometric and turbidimetric methods for measuring proteins
    • Layne E. Spectrophotometric and turbidimetric methods for measuring proteins. Methods Enzymol. 10 (1957) 447-455
    • (1957) Methods Enzymol. , vol.10 , pp. 447-455
    • Layne, E.1
  • 10
    • 34347369774 scopus 로고    scopus 로고
    • Localization of hCAP-18 on the surface of chemoattractant-stimulated human granulocytes: analysis using two novel hCAP-18-specific monoclonal antibodies
    • Stie J., Jesaitis A.V., Lord C.I., Gripentrog J.M., Taylor M., Burritt J.B., and Jesaitis A.J. Localization of hCAP-18 on the surface of chemoattractant-stimulated human granulocytes: analysis using two novel hCAP-18-specific monoclonal antibodies. J. Leukoc. Biol. 82 (2007) 161-172
    • (2007) J. Leukoc. Biol. , vol.82 , pp. 161-172
    • Stie, J.1    Jesaitis, A.V.2    Lord, C.I.3    Gripentrog, J.M.4    Taylor, M.5    Burritt, J.B.6    Jesaitis, A.J.7
  • 11
    • 1642536410 scopus 로고    scopus 로고
    • Identification of a novel FcγRIIIaα-associated molecule that contains significant homology to porcine cathelin
    • Sweeney S.E., and Kim Y.B. Identification of a novel FcγRIIIaα-associated molecule that contains significant homology to porcine cathelin. J. Immunol. 172 (2004) 1203-1212
    • (2004) J. Immunol. , vol.172 , pp. 1203-1212
    • Sweeney, S.E.1    Kim, Y.B.2
  • 12
    • 13844322065 scopus 로고    scopus 로고
    • The cathelicidins-structure, function and evolution
    • Tomasinsig L., and Zanetti M. The cathelicidins-structure, function and evolution. Curr. Protein Peptide Sci. 6 (2005) 23-34
    • (2005) Curr. Protein Peptide Sci. , vol.6 , pp. 23-34
    • Tomasinsig, L.1    Zanetti, M.2
  • 13
    • 1042290514 scopus 로고    scopus 로고
    • Hagfish intestinal antimicrobial peptides are ancient cathelicidins
    • Uzzell T., Stolzenberg E.D., Shinnar A.E., and Zasloff M. Hagfish intestinal antimicrobial peptides are ancient cathelicidins. Peptides 24 (2003) 1655-1667
    • (2003) Peptides , vol.24 , pp. 1655-1667
    • Uzzell, T.1    Stolzenberg, E.D.2    Shinnar, A.E.3    Zasloff, M.4
  • 14
  • 15
    • 0037472117 scopus 로고    scopus 로고
    • NMR structure of the cathelin-like domain of the protegrin-3 precursor
    • Yang Y., Sanchez J.F., Strub M.P., Brutscher B., and Aumelas A. NMR structure of the cathelin-like domain of the protegrin-3 precursor. Biochemistry 42 (2003) 4669-4680
    • (2003) Biochemistry , vol.42 , pp. 4669-4680
    • Yang, Y.1    Sanchez, J.F.2    Strub, M.P.3    Brutscher, B.4    Aumelas, A.5
  • 16
    • 0036379140 scopus 로고    scopus 로고
    • Cathelicidins, essential gene-encoded mammalian antibiotics
    • Zaiou M., and Gallo R.L. 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
  • 17
    • 0037960231 scopus 로고    scopus 로고
    • Antimicrobial and protease inhibitory functions of the human cathelicidin (hCAP18/LL37) prosequence
    • Zaiou M., Nizet V., and Gallo R.L. Antimicrobial and protease inhibitory functions of the human cathelicidin (hCAP18/LL37) prosequence. J. Invest. Dermatol. 120 (2003) 810-816
    • (2003) J. Invest. Dermatol. , vol.120 , pp. 810-816
    • Zaiou, M.1    Nizet, V.2    Gallo, R.L.3
  • 18
    • 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. 7 (2005) 179-196
    • (2005) Curr. Issues Mol. Biol. , vol.7 , pp. 179-196
    • Zanetti, M.1
  • 19
    • 0031033223 scopus 로고    scopus 로고
    • p15s (15-kD antimicrobial proteins) are stored in the secondary granules of Rabbit granulocytes: implications for antibacterial synergy with the bactericidal/permeability-increasing protein in inflammatory fluids
    • Zarember K.A., Elsbach P., Shin-Kim K., and Weiss J. p15s (15-kD antimicrobial proteins) are stored in the secondary granules of Rabbit granulocytes: implications for antibacterial synergy with the bactericidal/permeability-increasing protein in inflammatory fluids. Blood 89 (1997) 672-679
    • (1997) Blood , vol.89 , pp. 672-679
    • Zarember, K.A.1    Elsbach, P.2    Shin-Kim, K.3    Weiss, J.4
  • 20
    • 0036149798 scopus 로고    scopus 로고
    • Host defense functions of proteolytically processed and parent (unprocessed cathelicidins of rabbit granulocytes)
    • Zarember K.A., Katz S.S., Tack B.F., Doukhan L., Weiss J., and Elsbach P. Host defense functions of proteolytically processed and parent (unprocessed cathelicidins of rabbit granulocytes). Infect. Immun. 70 (2002) 569-576
    • (2002) Infect. Immun. , vol.70 , pp. 569-576
    • Zarember, K.A.1    Katz, S.S.2    Tack, B.F.3    Doukhan, L.4    Weiss, J.5    Elsbach, P.6
  • 21
    • 2942741244 scopus 로고    scopus 로고
    • Evolutionary epitopes of Hsp90 and p23: implications for their interaction
    • Zhu S., and Tytgat J. Evolutionary epitopes of Hsp90 and p23: implications for their interaction. FABES J. 18 (2004) 940-947
    • (2004) FABES J. , vol.18 , pp. 940-947
    • Zhu, S.1    Tytgat, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.