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Volumn 385, Issue 6, 2004, Pages 547-550

Identification of cysteine protease inhibitors that belong to cystatin family 1 in the cellular slime mold dictyostelium discoideum

Author keywords

Cathepsin B; Development; Inhibition specificity; Papain; Protein expression profile

Indexed keywords

CATHEPSIN B; CYSTATIN; CYSTATIN A1; CYSTATIN A2; CYSTEINE PROTEINASE INHIBITOR; PAPAIN; POLYCLONAL ANTIBODY; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 3242777138     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2004.065     Document Type: Article
Times cited : (6)

References (23)
  • 2
    • 0022896891 scopus 로고
    • The cystatins: A diverse superfamily of cysteine peptidase inhibitors
    • Barrett, A.J. (1986). The cystatins: a diverse superfamily of cysteine peptidase inhibitors. Biomed. Biochim. Acta 45, 1363-1374.
    • (1986) Biomed. Biochim. Acta , vol.45 , pp. 1363-1374
    • Barrett, A.J.1
  • 3
    • 0024066065 scopus 로고
    • The 2.0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases
    • Bode, W., Engh, R., Musil, D., Thiele, U., Huber, R., Karshikov, A., Brzin, J., Kos, J. and Turk, V. (1988). The 2.0 Å X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. EMBO J. 7, 2593-2599.
    • (1988) EMBO J. , vol.7 , pp. 2593-2599
    • Bode, W.1    Engh, R.2    Musil, D.3    Thiele, U.4    Huber, R.5    Karshikov, A.6    Brzin, J.7    Kos, J.8    Turk, V.9
  • 4
    • 0031013054 scopus 로고    scopus 로고
    • Friends and relations of the cystatin superfamily-new members and their evolution
    • Brown, W.M. and Dziegielewska, K.M. (1997). Friends and relations of the cystatin superfamily-new members and their evolution. Protein Sci. 6, 5-12.
    • (1997) Protein Sci. , vol.6 , pp. 5-12
    • Brown, W.M.1    Dziegielewska, K.M.2
  • 5
    • 0003448569 scopus 로고
    • (Cold Spring Harbor, NY, USA: Cold Spring Harbor Laboratory Press)
    • Harlow, E. and Lane, D. (1988). Antibodies: a laboratory manual. (Cold Spring Harbor, NY, USA: Cold Spring Harbor Laboratory Press), pp. 77-81.
    • (1988) Antibodies: A Laboratory Manual , pp. 77-81
    • Harlow, E.1    Lane, D.2
  • 7
    • 0024288519 scopus 로고
    • Multiple cysteine proteinase forms during the life cycle of Dictyostelium discoideum revealed by electrophoretic analysis
    • North, M.J., Scott, K. and Lockwood, B.C. (1988). Multiple cysteine proteinase forms during the life cycle of Dictyostelium discoideum revealed by electrophoretic analysis. Biochem. J. 254, 261-268.
    • (1988) Biochem. J. , vol.254 , pp. 261-268
    • North, M.J.1    Scott, K.2    Lockwood, B.C.3
  • 8
    • 0021676017 scopus 로고
    • Isolation of a human cDNA for alpha 2-thiol proteinase inhibitor and its identity with low molecular weight kininogen
    • Ohkubo, I., Kurachi, K., Takasawa, T., Shiokawa, H. and Sasaki, M. (1984). Isolation of a human cDNA for alpha 2-thiol proteinase inhibitor and its identity with low molecular weight kininogen. Biochemistry 23, 5691-5697.
    • (1984) Biochemistry , vol.23 , pp. 5691-5697
    • Ohkubo, I.1    Kurachi, K.2    Takasawa, T.3    Shiokawa, H.4    Sasaki, M.5
  • 10
    • 0022429825 scopus 로고
    • Characterization of two highly diverged but developmentally coregulated cysteine proteinase genes in Dictyostelium discoideum
    • Pears, C.J., Mahbubani, H.M. and Williams, J.G.(1985). Characterization of two highly diverged but developmentally coregulated cysteine proteinase genes in Dictyostelium discoideum. Nucleic Acids Res. 13, 8853-8866.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 8853-8866
    • Pears, C.J.1    Mahbubani, H.M.2    Williams, J.G.3
  • 12
    • 0344223030 scopus 로고
    • Analysis of the expression of two genes of Dictyostelium discoideum which code for developmentally regulated genes
    • Presse, F., Bgadanovsky-Sequeval, D., Mathieu, M. and Felenbok, B. (1986). Analysis of the expression of two genes of Dictyostelium discoideum which code for developmentally regulated genes. Mol. Gen. Genet. 203, 333-340.
    • (1986) Mol. Gen. Genet. , vol.203 , pp. 333-340
    • Presse, F.1    Bgadanovsky-Sequeval, D.2    Mathieu, M.3    Felenbok, B.4
  • 13
    • 0035943517 scopus 로고    scopus 로고
    • The protease inhibitor chagasin of Trypanosoma cruzi adopts an immunoglobulin-type fold and may have arisen by horizontal gene transfer
    • Rigden, D.J., Monteiro, A.C. and Grossi de Sà, M.F. (2001) The protease inhibitor chagasin of Trypanosoma cruzi adopts an immunoglobulin-type fold and may have arisen by horizontal gene transfer. FEBS Lett. 504, 41-44.
    • (2001) FEBS Lett. , vol.504 , pp. 41-44
    • Rigden, D.J.1    Monteiro, A.C.2    Grossi de Sà, M.F.3
  • 14
    • 0022407298 scopus 로고
    • Amino acid sequence of the intracellular cysteine proteinase inhibitor cystatin B from human live
    • Ritonja, A., Machleidt, W. and Barrett, A.J. (1985). Amino acid sequence of the intracellular cysteine proteinase inhibitor cystatin B from human live. Biochem. Biophys. Res. Commun. 131, 1187-1192.
    • (1985) Biochem. Biophys. Res. Commun. , vol.131 , pp. 1187-1192
    • Ritonja, A.1    Machleidt, W.2    Barrett, A.J.3
  • 15
    • 0042565975 scopus 로고    scopus 로고
    • Staphostatins: An expanding new group of proteinase inhibitors with a unique specificity for the regulation of staphopains, Staphylococcus spp. cysteine proteinases
    • Rzychon, M., Sabat, A., Kosowska, K., Potempa, J. and Dubin, A. (2003). Staphostatins: an expanding new group of proteinase inhibitors with a unique specificity for the regulation of staphopains, Staphylococcus spp. cysteine proteinases. Mol. Microbiol. 49, 1051-1066.
    • (2003) Mol. Microbiol. , vol.49 , pp. 1051-1066
    • Rzychon, M.1    Sabat, A.2    Kosowska, K.3    Potempa, J.4    Dubin, A.5
  • 16
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H. and von Jagow, G. (1987). Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 17
    • 0033544857 scopus 로고    scopus 로고
    • The prespore vesicles of Dictyostelium discoideum. Purification, characterization, and developmental regulation
    • Srinivasan, S., Alexander, H. and Alexander, S. (1999). The prespore vesicles of Dictyostelium discoideum. Purification, characterization, and developmental regulation. J. Biol. Chem. 274, 35823-35831.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35823-35831
    • Srinivasan, S.1    Alexander, H.2    Alexander, S.3
  • 19
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F. and Higgins, D.G. (1997). The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25, 4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 20
    • 0030918546 scopus 로고    scopus 로고
    • Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors
    • Turk, B., Turk, V. and Turk, D. (1997). Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors. Biol. Chem. 378, 141-50
    • (1997) Biol. Chem. , vol.378 , pp. 141-150
    • Turk, B.1    Turk, V.2    Turk, D.3
  • 23
    • 0030220996 scopus 로고    scopus 로고
    • Two wound-inducible soybean cysteine proteinase inhibitors have greater insect digestive proteinase inhibitory activities than a constitutive homolog
    • Zhao, Y., Botella, M.A., Subramanian, L., Niu, X., Nielsen, S.S., Bressan, R.A.and Hasegawa, P.M.. (1996). Two wound-inducible soybean cysteine proteinase inhibitors have greater insect digestive proteinase inhibitory activities than a constitutive homolog. Plant Physiol. 111, 1299-1306.
    • (1996) Plant Physiol. , vol.111 , pp. 1299-1306
    • Zhao, Y.1    Botella, M.A.2    Subramanian, L.3    Niu, X.4    Nielsen, S.S.5    Bressan, R.A.6    Hasegawa, P.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.