메뉴 건너뛰기




Volumn 31, Issue 2 I, 2004, Pages 133-139

Inhibiting polymerization: New therapeutic strategies for Z α1-antitrypsin-related emphysema

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1 ANTITRYPSIN; PEPTIDE DERIVATIVE; PHENYLALANYLLEUCYLGLUTAMYLALANYLISOLEUCYLGLYCINE; PROTEINASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 4143133190     PISSN: 10441549     EISSN: None     Source Type: Journal    
DOI: 10.1165/rcmb.2003-0276OC     Document Type: Article
Times cited : (57)

References (35)
  • 2
    • 0029050316 scopus 로고
    • Structural basis for serpin inhibitor activity
    • Wright, H. T., and J. N. Scarsdale. 1995. Structural basis for serpin inhibitor activity. Proteins 22:210-225.
    • (1995) Proteins , vol.22 , pp. 210-225
    • Wright, H.T.1    Scarsdale, J.N.2
  • 3
    • 0021747157 scopus 로고
    • 1-proteinase inhibitor: Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function
    • 1-proteinase inhibitor: crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. J. Mol. Biol. 177:531-556.
    • (1984) J. Mol. Biol. , vol.177 , pp. 531-556
    • Loebermann, H.1    Tokuoka, R.2    Deisenhofer, J.3    Huber, R.4
  • 4
    • 0033608984 scopus 로고    scopus 로고
    • Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70Å and full insertion of the reactive centre loop into β-sheet a
    • Stratikos, E., and P. G. W. Gettins. 1999. Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70Å and full insertion of the reactive centre loop into β-sheet A. Proc. Natl. Acad. Sci. USA 96:4808-4813.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4808-4813
    • Stratikos, E.1    Gettins, P.G.W.2
  • 5
    • 0031134386 scopus 로고    scopus 로고
    • Structural insights into serpin-protease complexes reveal the inhibitory mechanism of serpins
    • Wilczynska, M., M. Fa, J. Karolin, P.-I. Ohlsson, L. B.-A. Johansson, and T. Ny. 1997. Structural insights into serpin-protease complexes reveal the inhibitory mechanism of serpins. Nat. Struct. Biol. 4:354-357.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 354-357
    • Wilczynska, M.1    Fa, M.2    Karolin, J.3    Ohlsson, P.-I.4    Johansson, L.B.-A.5    Ny, T.6
  • 6
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington, J. A., R. J. Read, and R. W. Carrell. 2000. Structure of a serpin-protease complex shows inhibition by deformation. Nature 407:923-926.
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 10
    • 0027999955 scopus 로고
    • Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen VI (187 Asn→Asp)
    • Bruce, D., D. J. Perry, J.-Y. Borg, R. W. Carrell, and M. R. Wardell. 1994. Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen VI (187 Asn→Asp). J. Clin. Invest. 94:2265-2274.
    • (1994) J. Clin. Invest. , vol.94 , pp. 2265-2274
    • Bruce, D.1    Perry, D.J.2    Borg, J.-Y.3    Carrell, R.W.4    Wardell, M.R.5
  • 13
    • 85047684827 scopus 로고    scopus 로고
    • Alpha-1-antitrypsin polymerisation and the serpinopathies: Pathobiology and prospects for therapy
    • Lomas, D. A., and R. Mahadeva. 2002. Alpha-1-antitrypsin polymerisation and the serpinopathies: pathobiology and prospects for therapy. J. Clin. Invest. 110:1585-1590.
    • (2002) J. Clin. Invest. , vol.110 , pp. 1585-1590
    • Lomas, D.A.1    Mahadeva, R.2
  • 14
    • 0023898432 scopus 로고
    • Molecular basis of alpha-1-antitrypsin deficiency
    • Brantly, M., T. Nukiwa, and R. G. Crystal. 1988. Molecular basis of alpha-1-antitrypsin deficiency. Am. J. Med. 84(Suppl. 6A):13-31.
    • (1988) Am. J. Med. , vol.84 , Issue.SUPPL. 6A , pp. 13-31
    • Brantly, M.1    Nukiwa, T.2    Crystal, R.G.3
  • 17
    • 0013828812 scopus 로고
    • 1-antitrypsin deficiency
    • 1-antitrypsin deficiency, Acta Med. Scand. 432:1-85. (Suppl.)
    • (1965) Acta Med. Scand. , vol.432 , Issue.SUPPL. , pp. 1-85
    • Eriksson, S.1
  • 20
    • 0027473016 scopus 로고
    • Effect of the Z mutation on the physical and inhibitory properties of alpha-1-antitrypsin
    • Lomas, D. A., D. L. Evans, S. R. Stone, W.-S. W. Chang, and R. W. Carrell. 1993. Effect of the Z mutation on the physical and inhibitory properties of alpha-1-antitrypsin. Biochemistry 32:500-508.
    • (1993) Biochemistry , vol.32 , pp. 500-508
    • Lomas, D.A.1    Evans, D.L.2    Stone, S.R.3    Chang, W.-S.W.4    Carrell, R.W.5
  • 22
    • 0030819064 scopus 로고    scopus 로고
    • Mechanisms of antithrombin polymerisation and heparin activation probed by insertion of synthetic reactive loop peptides
    • Fitton, H. L., R. N. Pike, R. W. Carrell, and W.-S. W. Chang. 1997. Mechanisms of antithrombin polymerisation and heparin activation probed by insertion of synthetic reactive loop peptides. Biol. Chem. 378:1059-1063.
    • (1997) Biol. Chem. , vol.378 , pp. 1059-1063
    • Fitton, H.L.1    Pike, R.N.2    Carrell, R.W.3    Chang, W.-S.W.4
  • 23
    • 0029866947 scopus 로고    scopus 로고
    • Probing serpin reactive loop conformations by proteolytic cleavage
    • Chang, W.-S. W., M. R. Wardell, D. A. Lomas, and R. W. Carrell. 1996. Probing serpin reactive loop conformations by proteolytic cleavage. Biochem. J. 314:647-653.
    • (1996) Biochem. J. , vol.314 , pp. 647-653
    • Chang, W.-S.W.1    Wardell, M.R.2    Lomas, D.A.3    Carrell, R.W.4
  • 24
    • 0019321009 scopus 로고
    • Kinetics of association of serine proteinases with native and oxidized α-1-proteinase inhibitor and α-1-antichymotrypsin
    • Beatty, K., J. Bieth, and J. Travis. 1980. Kinetics of association of serine proteinases with native and oxidized α-1-proteinase inhibitor and α-1-antichymotrypsin. J. Biol. Chem. 255:3931-3934.
    • (1980) J. Biol. Chem. , vol.255 , pp. 3931-3934
    • Beatty, K.1    Bieth, J.2    Travis, J.3
  • 25
    • 0002799574 scopus 로고
    • Principles of active site titration of proteolytic enzymes
    • Kezdy, F. J., and E. T. Kaiser. 1970. Principles of active site titration of proteolytic enzymes. Methods Enzymol. 19:3-20.
    • (1970) Methods Enzymol. , vol.19 , pp. 3-20
    • Kezdy, F.J.1    Kaiser, E.T.2
  • 27
    • 0023728105 scopus 로고
    • The behavior and significance of slow-binding enzyme inhibitors
    • Morrison, J. F., and C. T. Walsh. 1988. The behavior and significance of slow-binding enzyme inhibitors. Adv. Enzymol. Relat. Areas Mol. Biol. 61:201-301.
    • (1988) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.61 , pp. 201-301
    • Morrison, J.F.1    Walsh, C.T.2
  • 28
    • 0029003409 scopus 로고
    • Theoretical and practical aspects of proteinase inhibition kinetics
    • Bieth, J. G. 1995. Theoretical and practical aspects of proteinase inhibition kinetics. Methods Enzymol. 248:59-84.
    • (1995) Methods Enzymol. , vol.248 , pp. 59-84
    • Bieth, J.G.1
  • 29
    • 0030044487 scopus 로고    scopus 로고
    • Inhibition of human pancreatic proteinases by mucus proteinase inhibitor, eglin C and aprotinin
    • Belorgey, D., S. Dirrig, M. Amouric, C. Figarella, and J. G. Bieth. 1996. Inhibition of human pancreatic proteinases by mucus proteinase inhibitor, eglin C and aprotinin. Biochem. J. 313:555-560.
    • (1996) Biochem. J. , vol.313 , pp. 555-560
    • Belorgey, D.1    Dirrig, S.2    Amouric, M.3    Figarella, C.4    Bieth, J.G.5
  • 30
    • 0032524769 scopus 로고    scopus 로고
    • Interfering with the inhibitory mechanism of serpins: Crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide
    • Xue, Y., P. Björquist, T. Inghardt, M. Linschoten, D. Musil, L. Sjölin, and J. Deinum. 1998. Interfering with the inhibitory mechanism of serpins: crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide. Structure 6:627-636.
    • (1998) Structure , vol.6 , pp. 627-636
    • Xue, Y.1    Björquist, P.2    Inghardt, T.3    Linschoten, M.4    Musil, D.5    Sjölin, L.6    Deinum, J.7
  • 32
    • 0028773279 scopus 로고
    • Biological implications of a 3Å structure of dimeric antithrombin
    • Carrell, R. W., P. E. Stein, G. Fermi, and M. R. Wardell. 1994. Biological implications of a 3Å structure of dimeric antithrombin. Structure 2:257-270.
    • (1994) Structure , vol.2 , pp. 257-270
    • Carrell, R.W.1    Stein, P.E.2    Fermi, G.3    Wardell, M.R.4
  • 34
    • 0036518616 scopus 로고    scopus 로고
    • Targeting hepatocytes for drug and gene delivery: Emerging novel approaches and applications
    • Wu, J., M. H. Nantz, and M. A. Zern. 2002. Targeting hepatocytes for drug and gene delivery: emerging novel approaches and applications. Front. Biosci. 7:717-725.
    • (2002) Front. Biosci. , vol.7 , pp. 717-725
    • Wu, J.1    Nantz, M.H.2    Zern, M.A.3
  • 35
    • 0035325257 scopus 로고    scopus 로고
    • Peptide-based targeting of fluorophores to organelles in living cells
    • Pap, E. H., T. B. Dansen, R. van Summeren, and K. W. Wirtz. 2001. Peptide-based targeting of fluorophores to organelles in living cells. Exp. Cell Res. 265:288-293.
    • (2001) Exp. Cell Res. , vol.265 , pp. 288-293
    • Pap, E.H.1    Dansen, T.B.2    Van Summeren, R.3    Wirtz, K.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.