메뉴 건너뛰기




Volumn 16, Issue 1, 1999, Pages 136-143

Expression of human plasminogen in Drosophila Schneider S2 cells

Author keywords

[No Author keywords available]

Indexed keywords

PLASMINOGEN; PROTEIN EXPRESSION; PROTEIN FOLDING;

EID: 0033152044     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1999.1045     Document Type: Article
Times cited : (46)

References (30)
  • 1
    • 0023147956 scopus 로고
    • Molecular cloning and characterization of a full-length cDNA clone for human plasminogen
    • Forsgren, M., Raden, B., Israelsson, M., Larsson, K., and Heden, L.-O. (1987) Molecular cloning and characterization of a full-length cDNA clone for human plasminogen. FEBS Lett. 213, 254-260.
    • (1987) FEBS Lett. , vol.213 , pp. 254-260
    • Forsgren, M.1    Raden, B.2    Israelsson, M.3    Larsson, K.4    Heden, L.-O.5
  • 2
    • 0014216684 scopus 로고
    • The peptide chains of human plasmin: Mechanism of activation of human plasminogen to plasmin
    • Robbins, K. C., Summaria, L., Hsieh, B., and Shah, R. J. (1967) The peptide chains of human plasmin: Mechanism of activation of human plasminogen to plasmin. J. Biol. Chem. 242, 2333-2342.
    • (1967) J. Biol. Chem. , vol.242 , pp. 2333-2342
    • Robbins, K.C.1    Summaria, L.2    Hsieh, B.3    Shah, R.J.4
  • 3
    • 0017126764 scopus 로고
    • Mechanism of urokinase-catalyzed activation of human plasminogen
    • Violand, B. N., and Castellino, F. J. (1976) Mechanism of urokinase-catalyzed activation of human plasminogen. J. Biol. Chem. 251, 3906-3912.
    • (1976) J. Biol. Chem. , vol.251 , pp. 3906-3912
    • Violand, B.N.1    Castellino, F.J.2
  • 4
    • 0017617554 scopus 로고
    • Purification and some properties of the Glu- and Lys- human plasmin heavy chains
    • Gonzalez-Gronow, M., Violand, B. N., and Castellino, F. J. (1977) Purification and some properties of the Glu- and Lys- human plasmin heavy chains. J. Biol. Chem. 252, 2175-2177.
    • (1977) J. Biol. Chem. , vol.252 , pp. 2175-2177
    • Gonzalez-Gronow, M.1    Violand, B.N.2    Castellino, F.J.3
  • 5
    • 0000325568 scopus 로고
    • The primary structure of human plasminogen: Isolation of two lysine-binding fragments and one "mini" plasminogen (MW, 38000) by elastase-catalyzed-specific limited proteolysis
    • Sottrup-Jensen, L., Claeys, H., Zajdel, M., Petersen, T. E., and Magnusson, S. (1978) The primary structure of human plasminogen: Isolation of two lysine-binding fragments and one "mini" plasminogen (MW, 38000) by elastase-catalyzed-specific limited proteolysis. Prog. Chem. Fibrinolysis Thrombolysis 3, 191-209.
    • (1978) Prog. Chem. Fibrinolysis Thrombolysis , vol.3 , pp. 191-209
    • Sottrup-Jensen, L.1    Claeys, H.2    Zajdel, M.3    Petersen, T.E.4    Magnusson, S.5
  • 6
    • 0023359594 scopus 로고
    • The reciprocal effects of e-aminohexanoic acid and chloride ion on the activation of human [Glu 1] plasminogen by human urokinase
    • Urano, T., Chibber, B. A. K., and Castellino, F. J. (1987) The reciprocal effects of e-aminohexanoic acid and chloride ion on the activation of human [Glu 1] plasminogen by human urokinase. Proc. Natl. Acad. Sci. USA 84, 4031-4034.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4031-4034
    • Urano, T.1    Chibber, B.A.K.2    Castellino, F.J.3
  • 7
    • 0017878273 scopus 로고
    • Quantitative determination of the binding of e-amino caproic acid to native plasminogen
    • Markus, G., Depasquale, J. L., and Wissler, F. C. (1978) Quantitative determination of the binding of e-amino caproic acid to native plasminogen. J. Biol. Chem. 253, 727-732.
    • (1978) J. Biol. Chem. , vol.253 , pp. 727-732
    • Markus, G.1    Depasquale, J.L.2    Wissler, F.C.3
  • 8
    • 0023737274 scopus 로고
    • The cell binding domains of plasminogen and their function in plasma
    • Miles, L. A., Dahlberg, C. M., and Plow, E. F. (1988) The cell binding domains of plasminogen and their function in plasma. J. Biol. Chem. 263, 11928-11934.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11928-11934
    • Miles, L.A.1    Dahlberg, C.M.2    Plow, E.F.3
  • 9
    • 0027451350 scopus 로고
    • PAM, a novel plasminogenbinding protein from Streptococcus pyogenes
    • Berge, A., and Sjobring, U. (1993) PAM, a novel plasminogenbinding protein from Streptococcus pyogenes. J. Biol. Chem. 268, 25417-25424.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25417-25424
    • Berge, A.1    Sjobring, U.2
  • 10
    • 0020596647 scopus 로고
    • The binding of human plasminogen to fibrin and fibrinogen
    • Lucas, M. A., Fretto, L. J., and McKee, P. A. (1983) The binding of human plasminogen to fibrin and fibrinogen. J. Biol. Chem. 258, 4249-4256.
    • (1983) J. Biol. Chem. , vol.258 , pp. 4249-4256
    • Lucas, M.A.1    Fretto, L.J.2    McKee, P.A.3
  • 11
    • 0015373803 scopus 로고
    • Measurement of the binding of antifibrinolytic amino acids to various plasminogens
    • Brockway, W. J., and Castellino, F. J. (1972) Measurement of the binding of antifibrinolytic amino acids to various plasminogens. Arch. Biochem. Biophys. 151, 194-199.
    • (1972) Arch. Biochem. Biophys. , vol.151 , pp. 194-199
    • Brockway, W.J.1    Castellino, F.J.2
  • 12
    • 0023627578 scopus 로고
    • The control of the urokinase-catalyzed activation of human glutamic acid 1-plasminogen by positive and negative effectors
    • Urano, T., De Serrano, V. S., Chibber, B. A. K., and Castellino, F. J. (1987) The control of the urokinase-catalyzed activation of human glutamic acid 1-plasminogen by positive and negative effectors. J. Biol. Chem. 262, 15959-15964.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15959-15964
    • Urano, T.1    De Serrano, V.S.2    Chibber, B.A.K.3    Castellino, F.J.4
  • 13
    • 0016594066 scopus 로고
    • The effect of epsilon amino caproic acid on the gross conformation of plasminogen and plasmin
    • Violand, B. N., Sodetz, J. M., and Castellino, F. J. (1975) The effect of epsilon amino caproic acid on the gross conformation of plasminogen and plasmin. Arch. Biochem. Biophys. 170, 300-305.
    • (1975) Arch. Biochem. Biophys. , vol.170 , pp. 300-305
    • Violand, B.N.1    Sodetz, J.M.2    Castellino, F.J.3
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.) 227, 680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 85030357338 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof.
  • 19
    • 0025269262 scopus 로고
    • Synthesis, purification and properties of a peptide that enhances the activation of human [glu]1plasminogen by tissue plasminogen activator and retards fibrin polymerization
    • Chibber, B. A. K., Urano, S., and Castellino, F. J. (1990) Synthesis, purification and properties of a peptide that enhances the activation of human [glu]1plasminogen by tissue plasminogen activator and retards fibrin polymerization. Int. J. Peptide Protein Res. 35, 73-80.
    • (1990) Int. J. Peptide Protein Res. , vol.35 , pp. 73-80
    • Chibber, B.A.K.1    Urano, S.2    Castellino, F.J.3
  • 21
    • 0028943590 scopus 로고
    • Roles of individual kringle domains in the functioning of positive and negative effectors of human plasminogen activation
    • Menhart, N., Hoover, G. J., McCance, S. G., and Castellino, F. J. (1995) Roles of individual kringle domains in the functioning of positive and negative effectors of human plasminogen activation. Biochemistry 34, 1482-1488.
    • (1995) Biochemistry , vol.34 , pp. 1482-1488
    • Menhart, N.1    Hoover, G.J.2    McCance, S.G.3    Castellino, F.J.4
  • 22
    • 0015328565 scopus 로고
    • Cell lines derived from late embryonic stages of Drosophila melanogaster
    • Schneider, I. (1972) Cell lines derived from late embryonic stages of Drosophila melanogaster. J. Embryol. Exp. Morphol. 27, 353-365.
    • (1972) J. Embryol. Exp. Morphol. , vol.27 , pp. 353-365
    • Schneider, I.1
  • 24
    • 0029925960 scopus 로고    scopus 로고
    • Functional interactions between the pelle kinase, toll receptor, and tube suggest a mechanism for activation of dorsal
    • Norris, J. L., and Manley, J. L. (1996) Functional interactions between the pelle kinase, toll receptor, and tube suggest a mechanism for activation of dorsal. Genes Dev. 10, 862-872.
    • (1996) Genes Dev. , vol.10 , pp. 862-872
    • Norris, J.L.1    Manley, J.L.2
  • 25
    • 0028556694 scopus 로고
    • Stable expression of a functional homo-oligomeric Drosophila GABA receptor in a Drosophila cell line
    • Millar, N. S., Buckingham, S. D., and Sattelle, D. B. (1994) Stable expression of a functional homo-oligomeric Drosophila GABA receptor in a Drosophila cell line. Proc. R Soc. Lond. B Biol. Sci. 258, 307-314.
    • (1994) Proc. R Soc. Lond. B Biol. Sci. , vol.258 , pp. 307-314
    • Millar, N.S.1    Buckingham, S.D.2    Sattelle, D.B.3
  • 26
    • 0027986667 scopus 로고
    • Drosophila PS1 integrin is a laminin receptor and differs in ligand specificity from PS2
    • Gotwals, P. J., Fessler, L. I., Wehrli, M., and Hynes, R. O. (1994) Drosophila PS1 integrin is a laminin receptor and differs in ligand specificity from PS2. Proc. Natl. Acad. Sci. USA 91, 11447-11451.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11447-11451
    • Gotwals, P.J.1    Fessler, L.I.2    Wehrli, M.3    Hynes, R.O.4
  • 27
    • 0018102544 scopus 로고
    • The effect of α-ω-amino acids on human plasminogen structure and activation
    • Violand, B. N., Byrne, R., and Castellino, F. J. (1978) The effect of α-ω-amino acids on human plasminogen structure and activation. J. Biol. Chem. 253, 5395-5401.
    • (1978) J. Biol. Chem. , vol.253 , pp. 5395-5401
    • Violand, B.N.1    Byrne, R.2    Castellino, F.J.3
  • 28
    • 0025774601 scopus 로고
    • Construction, expression and purification of recombinant kringle 1 of human plasminogen and analysis of its interaction with w-amino acids
    • Menhart, N., Sehl, L. C., Kelley, R. F., and Castellino, F. J. (1991) Construction, expression and purification of recombinant kringle 1 of human plasminogen and analysis of its interaction with w-amino acids. Biochemistry 30, 1948-1957.
    • (1991) Biochemistry , vol.30 , pp. 1948-1957
    • Menhart, N.1    Sehl, L.C.2    Kelley, R.F.3    Castellino, F.J.4
  • 29
    • 0025217903 scopus 로고
    • Thermodynamic properties of the binding of α-, ω-amino acids to the isolated kringle 4 region of human plasminogen as determined by high sensitivity titration calorimetry
    • Sehl, L. C., and Castellino, F. J. (1990) Thermodynamic properties of the binding of α-, ω-amino acids to the isolated kringle 4 region of human plasminogen as determined by high sensitivity titration calorimetry. J. Biol. Chem. 265, 5482-5486.
    • (1990) J. Biol. Chem. , vol.265 , pp. 5482-5486
    • Sehl, L.C.1    Castellino, F.J.2
  • 30
    • 0032502267 scopus 로고    scopus 로고
    • Structure and ligand binding determinants of the recombinant kringle 5 domain of human plasminogen
    • Chang, Y., Mochalkin, I., McCance, S. G., Cheng, B. S., Tulinsky, A., and Castellino, F. J. (1998) Structure and ligand binding determinants of the recombinant kringle 5 domain of human plasminogen. Biochemistry 37, 3258-3271.
    • (1998) Biochemistry , vol.37 , pp. 3258-3271
    • Chang, Y.1    Mochalkin, I.2    McCance, S.G.3    Cheng, B.S.4    Tulinsky, A.5    Castellino, F.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.