메뉴 건너뛰기




Volumn 14, Issue 7, 1996, Pages 852-856

Tumor protease-activated, pore-forming toxins from a combinatorial library

Author keywords

Drug delivery; Immunotoxin; Molecular trigger; Transmembrane pore; Tumor protease

Indexed keywords

ALPHA TOXIN; BACTERIAL PROTEIN; CATHEPSIN B; CYTOTOXIC AGENT; HEMOLYSIN; IMMUNOTOXIN; MUTANT PROTEIN; STAPHYLOCOCCUS TOXIN;

EID: 0029941746     PISSN: 10870156     EISSN: 15461696     Source Type: Journal    
DOI: 10.1038/nbt0796-852     Document Type: Article
Times cited : (61)

References (35)
  • 1
    • 0025787798 scopus 로고
    • Alpha-toxin of Staphylococcus aureus
    • Bhakdi, S. and Tranum-Jensen, J. 1991. Alpha-toxin of Staphylococcus aureus. Microbiol. Rev. 55:733-751.
    • (1991) Microbiol. Rev , vol.55 , pp. 733-751
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 2
    • 0028567173 scopus 로고
    • Subunit stoichiometry of staphylococcal α-hemolysin in crystals and on membranes: A heptameric transmembrane pore
    • Gouaux, J.E., Braha, O., Hobaugh, M.R., Song, L, Cheley, S., Shustak, C, and Bayley, H. 1994. Subunit stoichiometry of staphylococcal α-hemolysin in crystals and on membranes: a heptameric transmembrane pore. Proc. Natl. Acad. Sci. USA 91:12828-12831.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12828-12831
    • Gouaux, J.E.1    Braha, O.2    Hobaugh, M.R.3    Song, L.4    Cheley, S.5    Shustak, C.6    Bayley, H.7
  • 3
    • 0028341551 scopus 로고
    • Identification of a putative membrane-inserted segment in the α-toxin of Staphylococcus aureus
    • Ward, R.J., Palmer, M., Leonard, K., and Bhakdi, S. 1994. Identification of a putative membrane-inserted segment in the α-toxin of Staphylococcus aureus. Biochemistry 33:7477-7484.
    • (1994) Biochemistry , vol.33 , pp. 7477-7484
    • Ward, R.J.1    Palmer, M.2    Leonard, K.3    Bhakdi, S.4
  • 5
    • 0029924449 scopus 로고    scopus 로고
    • Molecular architecture of a toxin pore: A 15-residue sequence lines the transmembrane channel of staphylococcal alpha-toxin
    • Valeva, A., Weisser, A., Walker, B., Kehoe, M., Bayley, H., Bhakdi, S., and Palmer, M. 1996. Molecular architecture of a toxin pore: a 15-residue sequence lines the transmembrane channel of staphylococcal alpha-toxin. EMBO J. 15:1857-1864.
    • (1996) EMBO J , vol.15 , pp. 1857-1864
    • Valeva, A.1    Weisser, A.2    Walker, B.3    Kehoe, M.4    Bayley, H.5    Bhakdi, S.6    Palmer, M.7
  • 6
    • 0029617958 scopus 로고
    • Pore-forming proteins with built-in triggers and switches
    • Bayley, H. 1995. Pore-forming proteins with built-in triggers and switches. Bioorg. Chem. 23:340-345.
    • (1995) Bioorg. Chem , vol.23 , pp. 340-345
    • Bayley, H.1
  • 7
    • 0028181019 scopus 로고
    • A pore-forming protein with a protease-activated trigger
    • Walker, B.J. and Bayley, H. 1994. A pore-forming protein with a protease-activated trigger. Protein Eng. 7:91-97.
    • (1994) Protein Eng , vol.7 , pp. 91-97
    • Walker, B.J.1    Bayley, H.2
  • 8
    • 0019797924 scopus 로고
    • Lysosomal cathepsin B: Correlation with metastatic potential
    • Sloane, B.F., Dunn, J.R., and Honn, K.V. 1981. Lysosomal cathepsin B: correlation with metastatic potential. Science 212:1151-1153.
    • (1981) Science , vol.212 , pp. 1151-1153
    • Sloane, B.F.1    Dunn, J.R.2    Honn, K.V.3
  • 9
    • 0020441726 scopus 로고
    • A cysteine protease secreted from human breast tumours is immunologically related to cathepsin B
    • Recklies, A.D., Poole, A.R., and Mort, J.S. 1982. A cysteine protease secreted from human breast tumours is immunologically related to cathepsin B. Biochem. J. 207:633-636.
    • (1982) Biochem. J , vol.207 , pp. 633-636
    • Recklies, A.D.1    Poole, A.R.2    Mort, J.S.3
  • 11
    • 0029021787 scopus 로고
    • Tissue cathepsins as tumor markers
    • Schwartz, M.K. 1995. Tissue cathepsins as tumor markers. Clin. Chim. Acta 237:67-78.
    • (1995) Clin. Chim. Acta , vol.237 , pp. 67-78
    • Schwartz, M.K.1
  • 12
    • 0025845425 scopus 로고
    • Cathepsin B efficiently activates the soluble and the tumor cell receptor-bound form of the proenzyme urokinase-type plasminogen activator (Pro-uPA)
    • Kobayashi, H., Schmitt, M., Goretzki, L, Chucholowski, N., Calvete, J., Kramer, M., Günzler, W.A., Jänicke, P., and Graeff, H. 1991. Cathepsin B efficiently activates the soluble and the tumor cell receptor-bound form of the proenzyme urokinase-type plasminogen activator (pro-uPA). J. Biol. Chem. 266:5147-5152.
    • (1991) J. Biol. Chem , vol.266 , pp. 5147-5152
    • Kobayashi, H.1    Schmitt, M.2    Goretzki, L.3    Chucholowski, N.4    Calvete, J.5    Kramer, M.6    Günzler, W.A.7    Jänicke, P.8    Graeff, H.9
  • 13
    • 14744296273 scopus 로고
    • Optimizing nucleotide mixtures to encode specific subsets of amino acids for semi-random mutagenesis
    • Arkin, A.P. and Youvan, D.C. 1992. Optimizing nucleotide mixtures to encode specific subsets of amino acids for semi-random mutagenesis. Biotechnology 10:297-300.
    • (1992) Biotechnology , vol.10 , pp. 297-300
    • Arkin, A.P.1    Youvan, D.C.2
  • 14
    • 0028583118 scopus 로고
    • Recombinant proteins can be isolated from E. Coll cells by repeated cycles of freezing and thawing
    • Johnson, B.H. and Hecht, M.H. 1994. Recombinant proteins can be isolated from E. coll cells by repeated cycles of freezing and thawing. Biotechnology 12:1357-1360.
    • (1994) Biotechnology , vol.12 , pp. 1357-1360
    • Johnson, B.H.1    Hecht, M.H.2
  • 15
    • 0019765848 scopus 로고
    • Cathepsin B, cathepsin H, and cathepsin L
    • Barrett, A.J. and Kirschke, H. 1981. Cathepsin B, cathepsin H, and cathepsin L. Methods Enzymol. 80:535-561.
    • (1981) Methods Enzymol , vol.80 , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 16
    • 0025802686 scopus 로고
    • A model to explain the pH-dependent specificity of cathepsin B-catalysed hydrolyses
    • Khouri, H.E., Plouffe, C, Hasnain, S., Hirama, T., Storer, A.C., and Ménard, R. 1991. A model to explain the pH-dependent specificity of cathepsin B-catalysed hydrolyses. Biochem. J. 275:751-757.
    • (1991) Biochem. J , vol.275 , pp. 751-757
    • Khouri, H.E.1    Plouffe, C.2    Hasnain, S.3    Hirama, T.4    Storer, A.C.5    Ménard, R.6
  • 17
    • 0028021711 scopus 로고
    • The specificity of clostripain from Clostridium histolyticum. Mapping the S’ subsites via acyl transfer to amino acids
    • Ullman, D. and Jakubke, H.-D. 1994. The specificity of clostripain from Clostridium histolyticum. Mapping the S’ subsites via acyl transfer to amino acids. Eur. J. Biochem. 223:865-872.
    • (1994) Eur. J. Biochem , vol.223 , pp. 865-872
    • Ullman, D.1    Jakubke, H.-D.2
  • 21
    • 0027316004 scopus 로고
    • Substrate phage: Selection of protease substrates by monovalent phage display
    • Matthews, D.J. and Wells, J.A. 1993. Substrate phage: selection of protease substrates by monovalent phage display. Science 260:1113-1117.
    • (1993) Science , vol.260 , pp. 1113-1117
    • Matthews, D.J.1    Wells, J.A.2
  • 22
    • 0027190868 scopus 로고
    • Mapping the S’ subsites of serine proteases using acyl transfer to mixtures of peptide nucleophiles
    • Schellenberger, V., Turck, C.W., Hedstrom, L, and Rutter, W.J. 1993. Mapping the S’ subsites of serine proteases using acyl transfer to mixtures of peptide nucleophiles. Biochemistry 32:4349-4353.
    • (1993) Biochemistry , vol.32 , pp. 4349-4353
    • Schellenberger, V.1    Turck, C.W.2    Hedstrom, L.3    Rutter, W.J.4
  • 23
    • 0029126941 scopus 로고
    • Interactions between residues in staphylococcal α-hemolysin revealed by reversion mutagenesis
    • Panchal, R.G. and Bayley, H. 1995. Interactions between residues in staphylococcal α-hemolysin revealed by reversion mutagenesis. J. Biol. Chem. 270:23072-23076.
    • (1995) J. Biol. Chem , vol.270 , pp. 23072-23076
    • Panchal, R.G.1    Bayley, H.2
  • 24
    • 0015606478 scopus 로고
    • Human cathepsin B1. Purification and some properties of the enzyme
    • Barrett, A.J. 1973. Human cathepsin B1. Purification and some properties of the enzyme. Biochem. J. 131:809-822.
    • (1973) Biochem. J. , vol.131 , pp. 809-822
    • Barrett, A.J.1
  • 25
    • 0029125825 scopus 로고
    • Key residues for membrane binding, oligomerization, and pore-forming activity of staphylococcal α-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification
    • Walker, B. and Bayley, H. 1995. Key residues for membrane binding, oligomerization, and pore-forming activity of staphylococcal α-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification. J. Biol. Chem. 270:23065-23071.
    • (1995) J. Biol. Chem , vol.270 , pp. 23065-23071
    • Walker, B.1    Bayley, H.2
  • 26
    • 0026896029 scopus 로고
    • The matrix-degrading metalloproteinases
    • Matrisian, L.M. 1992. The matrix-degrading metalloproteinases. Bioessays 14:455-463.
    • (1992) Bioessays , vol.14 , pp. 455-463
    • Matrisian, L.M.1
  • 27
    • 0027140406 scopus 로고
    • Role of matrix metalloproteinases in tumor invasion and metastasis
    • Stetler-Stevenson, W.G., Liotta, L.A., and Kleiner, D.E. 1993. Role of matrix metalloproteinases in tumor invasion and metastasis. FASEB J. 7:1434-1441.
    • (1993) FASEB J , vol.7 , pp. 1434-1441
    • Stetler-Stevenson, W.G.1    Liotta, L.A.2    Kleiner, D.E.3
  • 28
    • 0028455028 scopus 로고
    • Tumor targeting: Activation of prodrugs by enzyme-monoclonal antibody conjugates
    • Huennekens, F.M. 1994. Tumor targeting: activation of prodrugs by enzyme-monoclonal antibody conjugates. Trends Biotechnol. 12:239-245.
    • (1994) Trends Biotechnol , vol.12 , pp. 239-245
    • Huennekens, F.M.1
  • 29
    • 0029257531 scopus 로고
    • Biochemical and cytotoxic properties of conjugates of transferrin with equinatoxin II, a cytolysin from a sea anemone
    • Pederzolli, C, Belmonte, G., Serra, M.D., Macek, P., and Menestrina, G. 1995. Biochemical and cytotoxic properties of conjugates of transferrin with equinatoxin II, a cytolysin from a sea anemone. Bioconjugate Chem. 6:166-173.
    • (1995) Bioconjugate Chem , vol.6 , pp. 166-173
    • Pederzolli, C.1    Belmonte, G.2    Serra, M.D.3    Macek, P.4    Menestrina, G.5
  • 31
    • 0026641089 scopus 로고
    • Functional expression of the α-hemolysin of Staphylococcus aureus in intact Escherichia coll and in cell lysates
    • Walker, B.J., Krishnasastry, M., Zorn, L., Kasianowicz, J.J., and Bayley, H. 1992. Functional expression of the α-hemolysin of Staphylococcus aureus in intact Escherichia coll and in cell lysates. J. Biol. Chem. 267:10902-10909.
    • (1992) J. Biol. Chem , vol.267 , pp. 10902-10909
    • Walker, B.J.1    Krishnasastry, M.2    Zorn, L.3    Kasianowicz, J.J.4    Bayley, H.5
  • 32
    • 0026785678 scopus 로고
    • Assembly of the oligomeric membrane pore formed by staphylococcal α-hemolysin examined by truncation mutagenesis
    • Walker, B.J., Krishnasastry, M., Zorn, L, and Bayley, H. 1992. Assembly of the oligomeric membrane pore formed by staphylococcal α-hemolysin examined by truncation mutagenesis. J. Biol. Chem. 267:21782-21786.
    • (1992) J. Biol. Chem , vol.267 , pp. 21782-21786
    • Walker, B.J.1    Krishnasastry, M.2    Zorn, L.3    Bayley, H.4
  • 33
    • 0025145229 scopus 로고
    • Optimization of routine transformation of Escherichia coli with plasmid DNA
    • Huff, J.R, Grant, B.J., Penning, C.A., and Sullivan, K.F 1990. Optimization of routine transformation of Escherichia coli with plasmid DNA. BioTechniques 9:570-576.
    • (1990) Biotechniques , vol.9 , pp. 570-576
    • Huff, J.R.1    Grant, B.J.2    Penning, C.A.3    Sullivan, K.F.4
  • 34
    • 0024558335 scopus 로고
    • One-step preparation of competent Escherichia coli: Transformation and storage of bacterial cells in the same solution
    • Chung, C.T., Niemela, S.L., and Miller, R.H. 1989. One-step preparation of competent Escherichia coli: transformation and storage of bacterial cells in the same solution. Proc. Watt. Acad. Sci. USA 86:2172-2175.
    • (1989) Proc. Watt. Acad. Sci. USA , vol.86 , pp. 2172-2175
    • Chung, C.T.1    Niemela, S.L.2    Miller, R.H.3
  • 35
    • 0018786290 scopus 로고
    • α-Clostripain: Chemical characterization, activity, and thiol content of the highly active form of clostripain
    • Gilles, A.-M., Imhoff, J.-M., and Keil, B. 1979. α-Clostripain: chemical characterization, activity, and thiol content of the highly active form of clostripain. J. Biol. Chem. 254:1462-1468.
    • (1979) J. Biol. Chem , vol.254 , pp. 1462-1468
    • Gilles, A.-M.1    Imhoff, J.-M.2    Keil, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.