메뉴 건너뛰기




Volumn 24, Issue 1, 2009, Pages 279-286

Inhibition of rat liver cathepsins B and L by the peptide aldehyde benzyloxycarbonyl-leucyl-leucyl-leucinal and its analogues

Author keywords

Cathepsin B; Cathepsin L; Cysteine protease inhibitor; IC50; Inhibition; Peptide aldehyde

Indexed keywords

2 FURANCARBONYLLEUCYLLEUCYLLEUCINAL; 4 MORPHOLINYLSUCCINYLLEUCYLLEUCYLLEUCINAL; ACETYLPROLYLLEUCYLLEUCYLLEUCINAL; ACETYLPROLYLPROLYLLEUCYLLEUCYLLEUCINAL; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; CATHEPSIN B; CATHEPSIN L; CYSTEINE PROTEINASE; ISONICOTINYLLEUCYLLEUCYLLEUCINAL; NICOTINYLLEUCYLLEUCYLLEUCINAL; PAPAIN; PROTEINASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 58949086774     PISSN: 14756366     EISSN: 14756374     Source Type: Journal    
DOI: 10.1080/14756360802166921     Document Type: Article
Times cited : (12)

References (23)
  • 1
    • 0343433408 scopus 로고    scopus 로고
    • Cysteine proteases and their inhibitors
    • Otto, H-H and Schirmeister, T. (1997) Cysteine proteases and their inhibitors. Chem Rev, 97, pp. 133-171.
    • (1997) Chem Rev , vol.97 , pp. 133-171
    • Otto, H.-H.1    Schirmeister, T.2
  • 2
    • 0029877917 scopus 로고    scopus 로고
    • Differential inhibition of calpain and proteasome activities by peptidyl aldehydes of di-leucine and tri-leucine
    • Tsubuki, S., Saito, Y., Tomioka, M., Ito, H. and Kawashima, S. (1996) Differential inhibition of calpain and proteasome activities by peptidyl aldehydes of di-leucine and tri-leucine. J Biochem, 119, pp. 572-576.
    • (1996) J Biochem , vol.119 , pp. 572-576
    • Tsubuki, S.1    Saito, Y.2    Tomioka, M.3    Ito, H.4    Kawashima, S.5
  • 4
    • 0025647715 scopus 로고
    • The structure-function relationship between peptide aldehyde derivatives on initiation of neurite outgrowth in PC12h cells
    • Saito, Y., Tsubuki, S., Ito, H. and Kawashima, S. (1990) The structure-function relationship between peptide aldehyde derivatives on initiation of neurite outgrowth in PC12h cells. Neurosci Lett, 120, pp. 1-4.
    • (1990) Neurosci Lett , vol.120 , pp. 1-4
    • Saito, Y.1    Tsubuki, S.2    Ito, H.3    Kawashima, S.4
  • 5
    • 0027421430 scopus 로고
    • Purification and characterization of a Z-Leu-Leu-Leu-MCA degrading protease expected to regulate neurite formation: A nobel catalytic activity in proteasome
    • Tsubuki, S., Kawasaki, H., Saito, Y., Miyashita, N., Inomata, M. and Kawashima, S. (1993) Purification and characterization of a Z-Leu-Leu-Leu-MCA degrading protease expected to regulate neurite formation: A nobel catalytic activity in proteasome. Biochem Biophys Res Commun, 196, pp. 1195-1201.
    • (1993) Biochem Biophys Res Commun , vol.196 , pp. 1195-1201
    • Tsubuki, S.1    Kawasaki, H.2    Saito, Y.3    Miyashita, N.4    Inomata, M.5    Kawashima, S.6
  • 9
    • 0025884209 scopus 로고
    • High-performance liquid chromatographic method for the simultaneous purification of cathepsins B, H and L from human liver
    • Daret-Fumeron, V., Guinec, N. and Pagano, M. (1991) High-performance liquid chromatographic method for the simultaneous purification of cathepsins B, H and L from human liver. J Chromatogr, 568, pp. 55-68.
    • (1991) J Chromatogr , vol.568 , pp. 55-68
    • Daret-Fumeron, V.1    Guinec, N.2    Pagano, M.3
  • 11
    • 12444283342 scopus 로고
    • A new method for forming peptide bonds
    • Sheehan, JC and Hess, GP (1955) A new method for forming peptide bonds. J Am Chem Soc, 77, pp. 1067-1068.
    • (1955) J Am Chem Soc , vol.77 , pp. 1067-1068
    • Sheehan, J.C.1    Hess, G.P.2
  • 12
    • 0016835544 scopus 로고
    • A new method to synthesize new α-aminoaldehydes
    • Ito, A., Takahashi, R. and Baba, Y. (1975) A new method to synthesize new α-aminoaldehydes. Chem Pharm Bull, 23, pp. 3081-3087.
    • (1975) Chem Pharm Bull , vol.23 , pp. 3081-3087
    • Ito, A.1    Takahashi, R.2    Baba, Y.3
  • 13
    • 0016805556 scopus 로고
    • Synthetic study of peptide aldehydes
    • Ito, A., Takahashi, R., Miura, C. and Baba, Y. (1975) Synthetic study of peptide aldehydes. Chem Pharm Bull, 23, pp. 3106-3113.
    • (1975) Chem Pharm Bull , vol.23 , pp. 3106-3113
    • Ito, A.1    Takahashi, R.2    Miura, C.3    Baba, Y.4
  • 14
    • 7144261446 scopus 로고
    • The synthesis and properties of tripeptide aldehydes having neurite-extension activity
    • Ito, H., Tsubuki, S., Saito, Y. and Kawashima, S. (1992) The synthesis and properties of tripeptide aldehydes having neurite-extension activity. Nippon Kagaku Kaishi, pp. 1363-1367.
    • (1992) Nippon Kagaku Kaishi , pp. 1363-1367
    • Ito, H.1    Tsubuki, S.2    Saito, Y.3    Kawashima, S.4
  • 16
    • 0028968184 scopus 로고
    • Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex. Implications for structure-based inhibitor design
    • Jia, Z., Hasnain, S., Hirama, T., Lee, X., Mort, JS, To, R. and Huber, CP (1995) Crystal structures of recombinant rat cathepsin B and a cathepsin B-inhibitor complex. Implications for structure-based inhibitor design. J Biol Chem, 270, pp. 5527-5533.
    • (1995) J Biol Chem , vol.270 , pp. 5527-5533
    • Jia, Z.1    Hasnain, S.2    Hirama, T.3    Lee, X.4    Mort, J.S.5    To, R.6    Huber, C.P.7
  • 17
    • 0029976244 scopus 로고    scopus 로고
    • Crystal structures of human procathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide
    • Turk, D., Podobnik, M., Kuhelj, R., Dolinar, M. and Turk, V. (1996) Crystal structures of human procathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide. FEBS Lett, 384, pp. 211-214.
    • (1996) FEBS Lett , vol.384 , pp. 211-214
    • Turk, D.1    Podobnik, M.2    Kuhelj, R.3    Dolinar, M.4    Turk, V.5
  • 18
    • 0030584678 scopus 로고    scopus 로고
    • Structure of rat procathepsin B: Model for inhibition of cysteine protease activity by the proregion
    • Cygler, M., Sivaraman, J., Grochulski, P., Coulombe, R., Storer, AC and Mort, JS (1996) Structure of rat procathepsin B: Model for inhibition of cysteine protease activity by the proregion. Structure, 4, pp. 405-416.
    • (1996) Structure , vol.4 , pp. 405-416
    • Cygler, M.1    Sivaraman, J.2    Grochulski, P.3    Coulombe, R.4    Storer, A.C.5    Mort, J.S.6
  • 20
    • 0034176273 scopus 로고    scopus 로고
    • Probing the specificity of cysteine proteinases at subsites remote from the active site: Analysis of P4, P3, P2' and P3' variations in extended substrates
    • Portaro, FCV, Santos, ABF, Cezari, MHS, Juliano, MA, Juliano, L. and Carmona, E. (2000) Probing the specificity of cysteine proteinases at subsites remote from the active site: Analysis of P4, P3, P2' and P3' variations in extended substrates. Biochem J, 347, pp. 123-129.
    • (2000) Biochem J , vol.347 , pp. 123-129
    • Portaro, F.C.V.1    Santos, A.B.F.2    Cezari, M.H.S.3    Juliano, M.A.4    Juliano, L.5    Carmona, E.6
  • 21
    • 0019199636 scopus 로고
    • Application of the substrate N-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide to a study of the inhibition by leupeptin
    • Human cathepsin, B
    • Knight, CG and Human cathepsin, B (1980) Application of the substrate N-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide to a study of the inhibition by leupeptin. Biochem J, 89, pp. 447-453.
    • (1980) Biochem J , vol.89 , pp. 447-453
    • Knight, C.G.1
  • 22
    • 0027221538 scopus 로고
    • Inhibition studies of some serine and thiol proteinases by new leupeptin analogues
    • McConnell, RM, York, JL, Frizzell, D. and Ezell, C. (1993) Inhibition studies of some serine and thiol proteinases by new leupeptin analogues. J Med Chem, 36, pp. 1084-1089.
    • (1993) J Med Chem , vol.36 , pp. 1084-1089
    • McConnell, R.M.1    York, J.L.2    Frizzell, D.3    Ezell, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.