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Volumn 266, Issue 2, 1999, Pages 403-412

Selection of human elastase inhibitors from a conformationally constrained combinatorial peptide library

Author keywords

Bowman Birk inhibitor; Canonical loop; Combinatorial chemistry; Elastase; Peptide library

Indexed keywords

ALANINE; ALKYL GROUP; BOWMAN BIRK INHIBITOR; CYCLOPEPTIDE; LEUKOCYTE ELASTASE; LEUKOCYTE ELASTASE INHIBITOR; PANCREATIC ELASTASE; PEPTIDE LIBRARY; PROTEINASE INHIBITOR; THREONINE; VALINE; PEPTIDE; PROTEIN;

EID: 0033485402     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00867.x     Document Type: Article
Times cited : (49)

References (73)
  • 1
    • 0002442268 scopus 로고
    • The role of elastase in acute hemorrhagic pancreatitis in man
    • 1. Geokas, M.C., Rinderknecht, H., Swanson, V. & Haverback, B.J. (1968) The role of elastase in acute hemorrhagic pancreatitis in man. Lab. Invest. 19, 235-239.
    • (1968) Lab. Invest. , vol.19 , pp. 235-239
    • Geokas, M.C.1    Rinderknecht, H.2    Swanson, V.3    Haverback, B.J.4
  • 2
    • 0028282060 scopus 로고
    • Synthetic inhibitors of elastase
    • 2. Edwards, P.D. & Bernstein, P.R. (1994) Synthetic inhibitors of elastase. Med. Res. Rev. 14, 127-194.
    • (1994) Med. Res. Rev. , vol.14 , pp. 127-194
    • Edwards, P.D.1    Bernstein, P.R.2
  • 3
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • 3. Laskowski, M. Jr & Kato, I. (1980) Protein inhibitors of proteinases. Annu. Rev. Biochem. 49, 593-626.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 593-626
    • Laskowski M., Jr.1    Kato, I.2
  • 4
    • 0026530977 scopus 로고
    • Natural protein proteinase-inhibitors and their interaction with proteinases
    • 4. Bode, W. & Huber, R. (1992) Natural protein proteinase-inhibitors and their interaction with proteinases. Eut J. Biochem. 204, 433-451.
    • (1992) Eut J. Biochem. , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 5
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • 5. Schechter, I. & Berger, A. (1967) On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157-162.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 6
    • 0001918129 scopus 로고
    • Ligand binding: Proteinase-protein inhibitor interactions
    • 6. Bode, W. & Huber, R. (1991) Ligand binding: proteinase-protein inhibitor interactions. Curr. Opin. Struct. Biol. 1, 45-52.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 45-52
    • Bode, W.1    Huber, R.2
  • 7
    • 0031024397 scopus 로고    scopus 로고
    • Interscaffolding additivity. Association of P-1 variants of eglin C and of turkey ovomucoid third domain with serine proteinases
    • 7. Qasim, M.A., Ganz, P.J., Saunders, C.W., Bateman, K.S., James, M.N.G. & Laskowski, M. (1997) Interscaffolding additivity. Association of P-1 variants of eglin C and of turkey ovomucoid third domain with serine proteinases. Biochemistry 36, 1598-1607.
    • (1997) Biochemistry , vol.36 , pp. 1598-1607
    • Qasim, M.A.1    Ganz, P.J.2    Saunders, C.W.3    Bateman, K.S.4    James, M.N.G.5    Laskowski, M.6
  • 8
    • 0023129864 scopus 로고
    • Chicken ovomucoid: Determination of its amino acid sequence, determination of the trypsin reactive site, and preparation of all 3 of its domains
    • 8. Kato, I., Schrode, J., Kohr, W.J. & Laskowski, M. (1987) Chicken ovomucoid: determination of its amino acid sequence, determination of the trypsin reactive site, and preparation of all 3 of its domains. Biochemistry 26, 193-201.
    • (1987) Biochemistry , vol.26 , pp. 193-201
    • Kato, I.1    Schrode, J.2    Kohr, W.J.3    Laskowski, M.4
  • 9
    • 0028064657 scopus 로고
    • Oxidized mucus proteinase inhibitor: A fairly potent neutrophil elastase inhibitor
    • 9. Boudier, C. & Bieth, J.G. (1994) Oxidized mucus proteinase inhibitor: a fairly potent neutrophil elastase inhibitor. Biochem. J. 303, 61-68.
    • (1994) Biochem. J. , vol.303 , pp. 61-68
    • Boudier, C.1    Bieth, J.G.2
  • 11
    • 0025369318 scopus 로고
    • Recombinant chymotrypsin inhibitor-2: Expression, kinetic analysis of inhibition with alpha-chymotrypsin and wild-type and mutant subtilisin Bpn′, and protein engineering to investigate inhibitory specificity and mechanism
    • 11. Longstaff, C., Campbell, A.F. & Fersht, A.R. (1990) Recombinant chymotrypsin inhibitor-2: expression, kinetic analysis of inhibition with alpha-chymotrypsin and wild-type and mutant subtilisin Bpn′, and protein engineering to investigate inhibitory specificity and mechanism. Biochemistry 29, 7339-7347.
    • (1990) Biochemistry , vol.29 , pp. 7339-7347
    • Longstaff, C.1    Campbell, A.F.2    Fersht, A.R.3
  • 13
    • 0017378998 scopus 로고
    • Studies on the synthesis of proteinase inhibitors. I. Synthesis and activity of nonapeptide fragments of soybean Bowman-Birk inhibitor
    • 13. Nishino, N., Aoyagi, H., Kato, T. & Izumiya, N. (1977) Studies on the synthesis of proteinase inhibitors. I. Synthesis and activity of nonapeptide fragments of soybean Bowman-Birk inhibitor. J. Biochem. (Tokyo) 82, 901-909.
    • (1977) J. Biochem. (Tokyo) , vol.82 , pp. 901-909
    • Nishino, N.1    Aoyagi, H.2    Kato, T.3    Izumiya, N.4
  • 14
    • 0024474543 scopus 로고
    • Active-site chemical mutagenesis of ecballium-elaterium trypsin inhibitor-II: New microproteins inhibiting elastase and chymotrypsin
    • 14. Favel, A., Lenguyen, D., Colettipreviero, M.A. & Castro, B. (1989) Active-site chemical mutagenesis of ecballium-elaterium trypsin inhibitor-II: new microproteins inhibiting elastase and chymotrypsin. Biochem. Biophys. Res. Commun. 162, 79-82.
    • (1989) Biochem. Biophys. Res. Commun. , vol.162 , pp. 79-82
    • Favel, A.1    Lenguyen, D.2    Colettipreviero, M.A.3    Castro, B.4
  • 15
    • 36849157571 scopus 로고
    • Therapy by instant evolution
    • 15. Carrell, R. (1984) Therapy by instant evolution. Nature (London) 312, 14.
    • (1984) Nature (London) , vol.312 , pp. 14
    • Carrell, R.1
  • 16
    • 0024373709 scopus 로고
    • Novel inhibitors of human-leukocyte elastase and cathepsin G: Sequence variants of squash seed protease inhibitor with altered protease selectivity
    • 16. McWherter, C.A., Walkenhorst, W.F., Campbell, E.J. & Glover, G.I. (1989) Novel inhibitors of human-leukocyte elastase and cathepsin G: sequence variants of squash seed protease inhibitor with altered protease selectivity. Biochemistry 28, 5708-5714.
    • (1989) Biochemistry , vol.28 , pp. 5708-5714
    • McWherter, C.A.1    Walkenhorst, W.F.2    Campbell, E.J.3    Glover, G.I.4
  • 17
    • 0038902290 scopus 로고    scopus 로고
    • The smallest peptide inhibitors of human leukocyte elastase (HLE): Structural requirements for inhibition of HLE based on Cucurbita maxima trypsin inhibitor III (CMTI-III) analogues
    • 17. Rozycki, J., Kupryszewski, G., Rolka, K., Ragnarsson, U., Zbyryt, T., Watorek, W. & Wilusz, T. (1997) The smallest peptide inhibitors of human leukocyte elastase (HLE): structural requirements for inhibition of HLE based on Cucurbita maxima trypsin inhibitor III (CMTI-III) analogues, Pol. J. Chem. 71, 176-180.
    • (1997) Pol. J. Chem. , vol.71 , pp. 176-180
    • Rozycki, J.1    Kupryszewski, G.2    Rolka, K.3    Ragnarsson, U.4    Zbyryt, T.5    Watorek, W.6    Wilusz, T.7
  • 18
    • 0026568164 scopus 로고
    • Directed evolution of a protein: Selection of potent neutrophil elastase inhibitors displayed on M13 fusion phage
    • 18. Roberts, B.L., Markland, W., Ley, A.C., Kent, R.B., White, D.W., Guterman, S.K. & Ladner, R.C. (1992) Directed evolution of a protein: selection of potent neutrophil elastase inhibitors displayed on M13 fusion phage. Proc. Natl Acad. Sci. USA 89, 2429-2433.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 2429-2433
    • Roberts, B.L.1    Markland, W.2    Ley, A.C.3    Kent, R.B.4    White, D.W.5    Guterman, S.K.6    Ladner, R.C.7
  • 19
    • 0029953760 scopus 로고    scopus 로고
    • Iterative optimization of high-affinity protease inhibitors using phage display. 1. Plasmin
    • 19. Markland, W., Ley, A.C., Lee, S.W. & Ladner, R.C. (1996) Iterative optimization of high-affinity protease inhibitors using phage display. 1. Plasmin. Biochemistry 35, 8045-8057.
    • (1996) Biochemistry , vol.35 , pp. 8045-8057
    • Markland, W.1    Ley, A.C.2    Lee, S.W.3    Ladner, R.C.4
  • 20
    • 0029894775 scopus 로고    scopus 로고
    • Iterative optimization of high-affinity protease inhibitors using phage display. 2. Plasma kallikrein and thrombin
    • 20. Markland, W., Ley, A.C. & Ladner, R.C. (1996) Iterative optimization of high-affinity protease inhibitors using phage display. 2. Plasma kallikrein and thrombin. Biochemistry 35, 8058-8067.
    • (1996) Biochemistry , vol.35 , pp. 8058-8067
    • Markland, W.1    Ley, A.C.2    Ladner, R.C.3
  • 21
    • 0038089976 scopus 로고    scopus 로고
    • Selection of chymotrypsin inhibitors from a conformationally-constrained combinatorial peptide library
    • 21. McBride, J.D., Freeman, N., Domingo, G.J. & Leatherbarrow, R.J. (1996) Selection of chymotrypsin inhibitors from a conformationally-constrained combinatorial peptide library. J. Mol. Biol. 259, 819-827.
    • (1996) J. Mol. Biol. , vol.259 , pp. 819-827
    • McBride, J.D.1    Freeman, N.2    Domingo, G.J.3    Leatherbarrow, R.J.4
  • 22
    • 0015862558 scopus 로고
    • Scission of soybean Bowman-Birk proteinase inhibitor into two small fragments having either trypsin or chymotrypsin inhibitory activity
    • 22. Odani, S. & Ikenaka, T. (1973) Scission of soybean Bowman-Birk proteinase inhibitor into two small fragments having either trypsin or chymotrypsin inhibitory activity. J. Biochem. (Tokyo) 74, 857-860.
    • (1973) J. Biochem. (Tokyo) , vol.74 , pp. 857-860
    • Odani, S.1    Ikenaka, T.2
  • 23
    • 0017882031 scopus 로고
    • Inhibitory properties of nonapeptide loop structures related to reactive sites of soybean Bowman-Birk inhibitor
    • 23. Terada, S., Sato, K., Kato, T. & Izumiya, N. (1978) Inhibitory properties of nonapeptide loop structures related to reactive sites of soybean Bowman-Birk inhibitor. FEBS Lett. 90, 89-92.
    • (1978) FEBS Lett. , vol.90 , pp. 89-92
    • Terada, S.1    Sato, K.2    Kato, T.3    Izumiya, N.4
  • 25
    • 0025893762 scopus 로고
    • General method for rapid synthesis of multicomponent peptide mixtures
    • 25. Furka, A., Sebestyen, F., Asgedom, M. & Dibo, G. (1991) General method for rapid synthesis of multicomponent peptide mixtures. Int. J. Pept. Protein Res. 37, 487-493.
    • (1991) Int. J. Pept. Protein Res. , vol.37 , pp. 487-493
    • Furka, A.1    Sebestyen, F.2    Asgedom, M.3    Dibo, G.4
  • 26
    • 0024571818 scopus 로고
    • Human leukocyte and porcine pancreatic elastase: X-ray crystal structures, mechanism, substrate-specificity, and mechanism-based inhibitors
    • 26. Bode, W., Meyer, E. & Powers, J.C. (1989) Human leukocyte and porcine pancreatic elastase: X-ray crystal structures, mechanism, substrate-specificity, and mechanism-based inhibitors. Biochemistry 28, 1951-1963.
    • (1989) Biochemistry , vol.28 , pp. 1951-1963
    • Bode, W.1    Meyer, E.2    Powers, J.C.3
  • 28
    • 12044255356 scopus 로고
    • Disulfide bond formation in peptides by dimethyl sulfoxide: Scope and applications
    • 28. Tam, J.P., Wu, C.R., Liu, W. & Zhang, J.W. (1991) Disulfide bond formation in peptides by dimethyl sulfoxide: scope and applications. J. Am. Chem. Soc. 113, 6657-6662.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 6657-6662
    • Tam, J.P.1    Wu, C.R.2    Liu, W.3    Zhang, J.W.4
  • 30
    • 50549163362 scopus 로고
    • The preparation and properties of two new chromogenic substrates of trypsin
    • 30. Erlanger, B., Kokowski, N. & Cohen, W. (1961) The preparation and properties of two new chromogenic substrates of trypsin. Arch. Biochem. Biophys. 95, 271-278.
    • (1961) Arch. Biochem. Biophys. , vol.95 , pp. 271-278
    • Erlanger, B.1    Kokowski, N.2    Cohen, W.3
  • 31
    • 0018747530 scopus 로고
    • Mapping the extended substrate binding site of cathepsin G and human leukocyte elastase. Studies with peptide substrates related to the alpha 1-protease inhibitor reactive site
    • 31. Nakajima, K., Powers, J.C., Ashe, B.M. & Zimmerman, M. (1979) Mapping the extended substrate binding site of cathepsin G and human leukocyte elastase. Studies with peptide substrates related to the alpha 1-protease inhibitor reactive site. J. Biol Chem. 254, 4027-4032.
    • (1979) J. Biol Chem. , vol.254 , pp. 4027-4032
    • Nakajima, K.1    Powers, J.C.2    Ashe, B.M.3    Zimmerman, M.4
  • 32
    • 0016363174 scopus 로고
    • The synthesis and analytical use of a highly sensitive and convenient substrate of elastase
    • 32. Bieth, J., Spiess, B. & Wermuth, C.G. (1974) The synthesis and analytical use of a highly sensitive and convenient substrate of elastase. Biochem. Med. 11, 350-357.
    • (1974) Biochem. Med. , vol.11 , pp. 350-357
    • Bieth, J.1    Spiess, B.2    Wermuth, C.G.3
  • 33
    • 0004124047 scopus 로고
    • Erithacus Software Ltd, Staines, UK
    • 33. Leatherbarrow, R.J. (1992) GraFit 3.0. Erithacus Software Ltd, Staines, UK.
    • (1992) GraFit 3.0
    • Leatherbarrow, R.J.1
  • 34
    • 0025205262 scopus 로고
    • Using linear and nonlinear-regression to fit biochemical data
    • 34. Leatherbarrow, R.J. (1990) Using linear and nonlinear-regression to fit biochemical data. Trends Biochem. Sci. 15, 455-458.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 455-458
    • Leatherbarrow, R.J.1
  • 35
    • 0027409046 scopus 로고
    • The 0.25-nm X-ray structure of the Bowman-Birk-type inhibitor from mung bean in ternary complex with porcine trypsin
    • 35. Lin, G.D., Bode, W., Huber, R., Chi, C.W. & Engh, R.A. (1993) The 0.25-nm X-ray structure of the Bowman-Birk-type inhibitor from mung bean in ternary complex with porcine trypsin. Eur. J. Biochem. 212, 549-555.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 549-555
    • Lin, G.D.1    Bode, W.2    Huber, R.3    Chi, C.W.4    Engh, R.A.5
  • 36
    • 0032544235 scopus 로고    scopus 로고
    • The role of threonine in the P-2 position of Bowman-Birk proteinase inhibitors: Studies on P-2 variation in cyclic peptides encompassing the reactive site loop
    • 36. McBride, J.D., Brauer, A.B.E., Nievo, M. & Leatherbarrow, R.J. (1998) The role of threonine in the P-2 position of Bowman-Birk proteinase inhibitors: studies on P-2 variation in cyclic peptides encompassing the reactive site loop. J. Mol. Biol. 282, 447-457.
    • (1998) J. Mol. Biol. , vol.282 , pp. 447-457
    • McBride, J.D.1    Brauer, A.B.E.2    Nievo, M.3    Leatherbarrow, R.J.4
  • 37
    • 0029658121 scopus 로고    scopus 로고
    • Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution: Structural peculiarities in a folded protein conformation
    • 37. Voss, R.H., Ermler, U., Essen, L.O., Wenzl, G., Kim, Y.M. & Flecker, P. (1996) Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution: structural peculiarities in a folded protein conformation. Eur. J. Biochem. 242, 122-131.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 122-131
    • Voss, R.H.1    Ermler, U.2    Essen, L.O.3    Wenzl, G.4    Kim, Y.M.5    Flecker, P.6
  • 38
    • 0019160999 scopus 로고
    • Studies on reactivity of human leukocyte elastase, cathepsin G, and porcine pancreatic elastase toward peptides including sequences related to the reactive site of alpha I-protease inhibitor (alpha 1-antitrypsin)
    • 38. McRae, B., Nakajima, K., Travis, J. & Powers, J.C. (1980) Studies on reactivity of human leukocyte elastase, cathepsin G, and porcine pancreatic elastase toward peptides including sequences related to the reactive site of alpha I-protease inhibitor (alpha 1-antitrypsin). Biochemistry 19, 3973-3978.
    • (1980) Biochemistry , vol.19 , pp. 3973-3978
    • McRae, B.1    Nakajima, K.2    Travis, J.3    Powers, J.C.4
  • 39
    • 0021142713 scopus 로고
    • Active-site mapping of the serine proteases human-leukocyte elastase, cathepsin g, porcine pancreatic elastase, rat mast-cell protease-I and protease-Ii, bovine chymotrypsin-α and Staphylococcus aureus protease V-8 using tripeptide thiobenzyl ester substrates
    • 39. Harper, J.W., Cook, R.R., Roberts, C.J., McLaughlin, B.J. & Powers, J.C. (1984) Active-site mapping of the serine proteases human-leukocyte elastase, cathepsin g, porcine pancreatic elastase, rat mast-cell protease-I and protease-Ii, bovine chymotrypsin-α and Staphylococcus aureus protease V-8 using tripeptide thiobenzyl ester substrates. Biochemistry 23, 2995-3002.
    • (1984) Biochemistry , vol.23 , pp. 2995-3002
    • Harper, J.W.1    Cook, R.R.2    Roberts, C.J.3    McLaughlin, B.J.4    Powers, J.C.5
  • 42
    • 0029078878 scopus 로고
    • Isolation and characterization of guamerin, a new human-leukocyte elastase inhibitor from Hirudo-Nipponia
    • 42. Jung, H.I., Kim, S.I., Ha, K.S., Joe, C.O. & Kang, K.W. (1995) Isolation and characterization of guamerin, a new human-leukocyte elastase inhibitor from Hirudo-Nipponia. J. Biol. Chem. 270, 13879-13884.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13879-13884
    • Jung, H.I.1    Kim, S.I.2    Ha, K.S.3    Joe, C.O.4    Kang, K.W.5
  • 43
    • 0026668735 scopus 로고
    • Changing the inhibitory specificity and function of the proteinase inhibitor eglin-c by site-directed mutagenesis: Functional and structural investigation
    • 43. Heinz, D.W., Hyberts, S.G., Peng, J.W., Priestle, J.P., Wagner, G. amp; Grutter, M.G. (1992) Changing the inhibitory specificity and function of the proteinase inhibitor eglin-c by site-directed mutagenesis: functional and structural investigation. Biochemistry 31, 8755-8766.
    • (1992) Biochemistry , vol.31 , pp. 8755-8766
    • Heinz, D.W.1    Hyberts, S.G.2    Peng, J.W.3    Priestle, J.P.4    Wagner, G.5    Grutter, M.G.6
  • 44
    • 0027406841 scopus 로고
    • Kinetics of the inhibition of human-leukocyte elastase by elafin, a 6-kilodalton elastase-specific inhibitor from human skin
    • 44. Ying, Q.L. & Simon, S.R. (1993) Kinetics of the inhibition of human-leukocyte elastase by elafin, a 6-kilodalton elastase-specific inhibitor from human skin. Biochemistry 32, 1866-1874.
    • (1993) Biochemistry , vol.32 , pp. 1866-1874
    • Ying, Q.L.1    Simon, S.R.2
  • 45
    • 0023740057 scopus 로고
    • Preparation of chemically mutated aprotinin homologs by semisynthesis: P1 substitutions change inhibitory specificity
    • 45. Beckmann, J., Mehlich, A., Schroder, W., Wenzel, H.R. & Tschesche, H. (1988) Preparation of chemically mutated aprotinin homologs by semisynthesis: P1 substitutions change inhibitory specificity. Eur. J. Biochem. 176, 675-682.
    • (1988) Eur. J. Biochem. , vol.176 , pp. 675-682
    • Beckmann, J.1    Mehlich, A.2    Schroder, W.3    Wenzel, H.R.4    Tschesche, H.5
  • 48
    • 0030033356 scopus 로고    scopus 로고
    • Inhibitory properties of separate recombinant Kunitz-type-protease-inhibitor domains from tissue-factor-pathway inhibitor
    • 48. Petersen, L.C., Bjorn, S.E., Olsen, O.H., Nordfang, O., Norris, F. & Norris, K. (1996) Inhibitory properties of separate recombinant Kunitz-type-protease-inhibitor domains from tissue-factor-pathway inhibitor. Eur. J. Biochem. 235, 310-316.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 310-316
    • Petersen, L.C.1    Bjorn, S.E.2    Olsen, O.H.3    Nordfang, O.4    Norris, F.5    Norris, K.6
  • 50
    • 0019793958 scopus 로고
    • Reactivity of human-leukocyte elastase and porcine pancreatic elastase toward peptide 4-nitroanilides containing model desmosine residues: Evidence that human-leukocyte elastase is selective for cross-linked regions of elastin
    • 50. Yasutake, A. & Powers, J.C. (1981) Reactivity of human-leukocyte elastase and porcine pancreatic elastase toward peptide 4-nitroanilides containing model desmosine residues: evidence that human-leukocyte elastase is selective for cross-linked regions of elastin. Biochemistry 20, 3675-3679.
    • (1981) Biochemistry , vol.20 , pp. 3675-3679
    • Yasutake, A.1    Powers, J.C.2
  • 51
    • 0022801412 scopus 로고
    • X-ray crystal structure of the complex of human-leukocyte elastase (PMN elastase) and the 3rd domain of the turkey ovomucoid inhibitor
    • 51. Bode, W., Wei, A.Z., Huber, R., Meyer, E., Travis, J. & Neumann, S. (1986) X-ray crystal structure of the complex of human-leukocyte elastase (PMN elastase) and the 3rd domain of the turkey ovomucoid inhibitor. EMBO J. 5, 2453-2458.
    • (1986) EMBO J. , vol.5 , pp. 2453-2458
    • Bode, W.1    Wei, A.Z.2    Huber, R.3    Meyer, E.4    Travis, J.5    Neumann, S.6
  • 54
    • 0020480240 scopus 로고
    • Thermodynamics and kinetics of single residue replacements in avian ovomucoid 3rd domains: Effect on inhibitor interactions with serine proteinases
    • 54. Empie, M.W. & Laskowski, M. (1982) Thermodynamics and kinetics of single residue replacements in avian ovomucoid 3rd domains: effect on inhibitor interactions with serine proteinases. Biochemistry 21, 2274-2284.
    • (1982) Biochemistry , vol.21 , pp. 2274-2284
    • Empie, M.W.1    Laskowski, M.2
  • 55
    • 0025168332 scopus 로고
    • Elafin - An elastase-specific inhibitor of human skin: Purification, characterization, and complete amino acid sequence
    • 55. Wiedow, O., Schroder, J.M., Gregory, H., Young, J.A. & Christophers, E. (1990) Elafin - an elastase-specific inhibitor of human skin: purification, characterization, and complete amino acid sequence. J. Biol. Chem. 265, 14791-14795.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14791-14795
    • Wiedow, O.1    Schroder, J.M.2    Gregory, H.3    Young, J.A.4    Christophers, E.5
  • 56
    • 0029811088 scopus 로고    scopus 로고
    • Crystal structure of an elastase-specific inhibitor elafin complexed with porcine pancreatic elastase determined at 1.9 angstrom resolution
    • 56. Tsunemi, M., Matsuura, Y., Sakakibara, S. & Katsube, Y. (1996) Crystal structure of an elastase-specific inhibitor elafin complexed with porcine pancreatic elastase determined at 1.9 angstrom resolution. Biochemistry 35, 11570-11576.
    • (1996) Biochemistry , vol.35 , pp. 11570-11576
    • Tsunemi, M.1    Matsuura, Y.2    Sakakibara, S.3    Katsube, Y.4
  • 58
    • 0021188622 scopus 로고
    • Synthesis in yeast of a functional oxidation-resistant mutant of human alpha-1-antitrypsin
    • 58. Rosenberg, S., Barr, P.J., Najarian, R.C. & Hallewell, R.A. (1984) Synthesis in yeast of a functional oxidation-resistant mutant of human alpha-1-antitrypsin. Nature (London) 312, 77-80.
    • (1984) Nature (London) , vol.312 , pp. 77-80
    • Rosenberg, S.1    Barr, P.J.2    Najarian, R.C.3    Hallewell, R.A.4
  • 59
    • 0001828581 scopus 로고
    • Reversible inhibitors of serine proteinases
    • Gutte, B., ed. Academic Press, San Diego, CA
    • 59. Wenzel, H.R. & Tschesche, H. (1995) Reversible inhibitors of serine proteinases. In Peptides Synthesis, Structures, and Applications (Gutte, B., ed.), pp. 321-362. Academic Press, San Diego, CA.
    • (1995) Peptides Synthesis, Structures, and Applications , pp. 321-362
    • Wenzel, H.R.1    Tschesche, H.2
  • 60
    • 0015911769 scopus 로고
    • Dependence of the kinetic parameters for elastase-catalyzed amide hydrolysis on the length of peptide substrates
    • 60. Thompson, R.C. & Blout, E.R. (1973) Dependence of the kinetic parameters for elastase-catalyzed amide hydrolysis on the length of peptide substrates. Biochemistry 12, 57-65.
    • (1973) Biochemistry , vol.12 , pp. 57-65
    • Thompson, R.C.1    Blout, E.R.2
  • 61
    • 0023553577 scopus 로고
    • Anti-chymotrypsin and anti-elastase activities of a synthetic bicyclic fragment containing a chymotrypsin-reactive site of soybean Bowman-Birk inhibitor
    • 61. Ando, S., Yasutake, A., Waki, M., Nishino, N., Kato, T. & Izumiya, N. (1987) Anti-chymotrypsin and anti-elastase activities of a synthetic bicyclic fragment containing a chymotrypsin-reactive site of soybean Bowman-Birk inhibitor. Biochim. Biophys. Acta 916, 527-531.
    • (1987) Biochim. Biophys. Acta , vol.916 , pp. 527-531
    • Ando, S.1    Yasutake, A.2    Waki, M.3    Nishino, N.4    Kato, T.5    Izumiya, N.6
  • 62
    • 0030795530 scopus 로고    scopus 로고
    • Stability of protease inhibitors based on the Bowman-Birk reactive site loop to hydrolysis by proteases
    • 62. Gariani, T. & Leatherbarrow, R.J. (1997) Stability of protease inhibitors based on the Bowman-Birk reactive site loop to hydrolysis by proteases. J. Pept. Res. 49, 467-475.
    • (1997) J. Pept. Res. , vol.49 , pp. 467-475
    • Gariani, T.1    Leatherbarrow, R.J.2
  • 63
    • 0009476961 scopus 로고
    • Synthetic elastase inhibitors and their role in the treatment of disease
    • Rich, D.H. & Gross, E., eds. Pierce Chemical Co., Rockford, IL
    • 63. Powers, J.C., Yasutake, A., Nishino, N, Gupton, B.F. & Kam, C.M. (1981) Synthetic elastase inhibitors and their role in the treatment of disease. In Peptides: Synthesis, Structure, Function (Rich, D.H. & Gross, E., eds), pp. 391-399. Pierce Chemical Co., Rockford, IL.
    • (1981) Peptides: Synthesis, Structure, Function , pp. 391-399
    • Powers, J.C.1    Yasutake, A.2    Nishino, N.3    Gupton, B.F.4    Kam, C.M.5
  • 64
    • 0031041505 scopus 로고    scopus 로고
    • Human leukocyte elastase inhibition by Bowman-Birk soybean inhibitor; discrimination of the inhibition mechanisms
    • 64. Larionova, N.I., Gladysheva, I.P. & Gladyshev, D.P. (1997) Human leukocyte elastase inhibition by Bowman-Birk soybean inhibitor; discrimination of the inhibition mechanisms. FEBS Lett. 404, 245-248.
    • (1997) FEBS Lett. , vol.404 , pp. 245-248
    • Larionova, N.I.1    Gladysheva, I.P.2    Gladyshev, D.P.3
  • 67
    • 0020974247 scopus 로고
    • Interaction of protein substrate and inhibitors with alpha-2-macroglobulin-bound proteinases
    • 67. Bieth, J.G., Kandel, M.J., Zreika, M. & Pochon, F. (1983) Interaction of protein substrate and inhibitors with alpha-2-macroglobulin-bound proteinases. Ann. N.Y. Acad. Sci. 421, 209-217.
    • (1983) Ann. N.Y. Acad. Sci. , vol.421 , pp. 209-217
    • Bieth, J.G.1    Kandel, M.J.2    Zreika, M.3    Pochon, F.4
  • 68
    • 0031942060 scopus 로고    scopus 로고
    • Peptides derived from human C-reactive protein inhibit the enzymatic activities of human leukocyte elastase and cathepsin G: Use of overlapping peptide sequences to identify a unique inhibitor
    • 68. Yavin, E.J. & Fridkin, M. (1998) Peptides derived from human C-reactive protein inhibit the enzymatic activities of human leukocyte elastase and cathepsin G: use of overlapping peptide sequences to identify a unique inhibitor. J. Pept. Res. 51, 282-289.
    • (1998) J. Pept. Res. , vol.51 , pp. 282-289
    • Yavin, E.J.1    Fridkin, M.2
  • 69
    • 0001296785 scopus 로고
    • Catalysis by human-leukocyte elastase. 4. Role of secondary-subsite interactions
    • 69. Stein, R.L. (1985) Catalysis by human-leukocyte elastase. 4. Role of secondary-subsite interactions. J. Am. Chem. Soc. 107, 5767-5775.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 5767-5775
    • Stein, R.L.1
  • 70
    • 0016232066 scopus 로고
    • Catalysis, binding and enzyme-substrate complementarity
    • 70. Fersht, A.R. (1974) Catalysis, binding and enzyme-substrate complementarity. Proc. R. Soc. Lond. B. Biol. Sci. 187, 397-407.
    • (1974) Proc. R. Soc. Lond. B. Biol. Sci. , vol.187 , pp. 397-407
    • Fersht, A.R.1
  • 71
    • 0021986979 scopus 로고
    • Catalysis by human-leukocyte elastase. 3. Steady-state kinetics for the hydrolysis of para-nitrophenyl esters
    • 71. Stein, R.L. (1985) Catalysis by human-leukocyte elastase. 3. Steady-state kinetics for the hydrolysis of para-nitrophenyl esters. Arch. Biochem. Biophys. 236, 677-680.
    • (1985) Arch. Biochem. Biophys. , vol.236 , pp. 677-680
    • Stein, R.L.1
  • 72
    • 0017324044 scopus 로고
    • Serine proteases: Structure and mechanism of catalysis
    • 72. Kraut, J. (1977) Serine proteases: structure and mechanism of catalysis. Annu. Rev. Biochem. 46, 331-358.
    • (1977) Annu. Rev. Biochem. , vol.46 , pp. 331-358
    • Kraut, J.1
  • 73
    • 0023721908 scopus 로고
    • The refined 2.3 Å crystal-structure of human-leukocyte elastase in a complex with a valine chloromethyl ketone inhibitor
    • 73. Wei, A.Z., Mayr, I. & Bode, W. (1988) The refined 2.3 Å crystal-structure of human-leukocyte elastase in a complex with a valine chloromethyl ketone inhibitor. FEBS Lett. 234, 367-373.
    • (1988) FEBS Lett. , vol.234 , pp. 367-373
    • Wei, A.Z.1    Mayr, I.2    Bode, W.3


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