메뉴 건너뛰기




Volumn 5, Issue 3, 2005, Pages 249-257

Molecular mousetraps, α1-antitrypsin deficiency and the serpinopathies

Author keywords

Conformational disease; Neuroserpin; Polymerisation; Serpins; 1 antitrypsin

Indexed keywords

ALPHA 1 ANTICHYMOTRYPSIN; ALPHA 1 ANTITRYPSIN; ANTITHROMBIN; COMPLEMENT COMPONENT C1S INHIBITOR; MUTANT PROTEIN; POLYMER; SERINE PROTEINASE INHIBITOR;

EID: 21744457450     PISSN: 14702118     EISSN: None     Source Type: Journal    
DOI: 10.7861/clinmedicine.5-3-249     Document Type: Conference Paper
Times cited : (48)

References (96)
  • 1
    • 0035823595 scopus 로고    scopus 로고
    • The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, novel functions, mechanism of inhibition and a revised nomenclature
    • Silverman GA, Bird PI, Carrell RW, Church FC et al. The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, novel functions, mechanism of inhibition and a revised nomenclature. J Biol Chem 2001;276:33293-6.
    • (2001) J Biol Chem , vol.276 , pp. 33293-33296
    • Silverman, G.A.1    Bird, P.I.2    Carrell, R.W.3    Church, F.C.4
  • 5
    • 0343193210 scopus 로고    scopus 로고
    • 1-antitrypsin reveals targets for rational drug design to prevent conformational disease
    • 1-antitrypsin reveals targets for rational drug design to prevent conformational disease. Protein Science 2000;9:1274-81.
    • (2000) Protein Science , vol.9 , pp. 1274-1281
    • Elliott, P.R.1    Pei, X.Y.2    Dafforn, T.R.3    Lomas, D.A.4
  • 8
    • 0033555837 scopus 로고    scopus 로고
    • The structure of active serpin 1K from Manduca sexta
    • Li J, Wang Z, Canagarajah B, Jiang H et al. The structure of active serpin 1K from Manduca sexta. Structure 1999;7:103-9.
    • (1999) Structure , vol.7 , pp. 103-109
    • Li, J.1    Wang, Z.2    Canagarajah, B.3    Jiang, H.4
  • 9
    • 0029591826 scopus 로고
    • The inhibition mechanism of serpins. Evidence that the mobile reactive centre loop is cleaved in the native protease-inhibitor complex
    • Wilczynska M, Fa M, Ohlsson P-I, Ny T. The inhibition mechanism of serpins. Evidence that the mobile reactive centre loop is cleaved in the native protease-inhibitor complex. J Biol Chem 1995;270:29652-5.
    • (1995) J Biol Chem , vol.270 , pp. 29652-29655
    • Wilczynska, M.1    Fa, M.2    Ohlsson, P.-I.3    Ny, T.4
  • 10
    • 0031134386 scopus 로고    scopus 로고
    • Structural insights into serpin-protease complexes reveal the inhibitory mechanism of serpins
    • Wilczynska M, Fa M, Karolin J, Ohlsson P-I et al. Structural insights into serpin-protease complexes reveal the inhibitory mechanism of serpins. Nat Struc Biol 1997;4:354-7.
    • (1997) Nat Struc Biol , vol.4 , pp. 354-357
    • Wilczynska, M.1    Fa, M.2    Karolin, J.3    Ohlsson, P.-I.4
  • 11
    • 0031036673 scopus 로고    scopus 로고
    • Major proteinase movement upon stable serpin-proteinase complex formation
    • Stratikos E, Gettins PGW. Major proteinase movement upon stable serpin-proteinase complex formation. Proc Natl Acad Sci 1997;4:453-8.
    • (1997) Proc Natl Acad Sci , vol.4 , pp. 453-458
    • Stratikos, E.1    Gettins, P.G.W.2
  • 13
    • 0033608984 scopus 로고    scopus 로고
    • Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 Å and full insertion of the reactive centre loop into β-sheet A
    • Stratikos E, Gettins PGW. Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 Å and full insertion of the reactive centre loop into β-sheet A. Proc Natl Acad Sci USA 1999;96:4808-13.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4808-4813
    • Stratikos, E.1    Gettins, P.G.W.2
  • 14
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntingdon JA, Read RJ, Carrell RW. Structure of a serpin-protease complex shows inhibition by deformation. Nature 2000;407:923-6.
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntingdon, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 16
    • 0001353920 scopus 로고
    • 2-macroglobulin receptor mediates cellular degradation of urokinase receptor-bound complexes
    • 2-macroglobulin receptor mediates cellular degradation of urokinase receptor-bound complexes. J Biol Chem 1992;267:14543-6.
    • (1992) J Biol Chem , vol.267 , pp. 14543-14546
    • Nykjier, A.1    Petersen, C.M.2    Møller, B.3    Jensen, P.H.4
  • 17
    • 0028158575 scopus 로고
    • Receptor-mediated endocytosis of plasminogen activators and activator/inhibitor complexes
    • Andreasen PA, Sottrup-Jensen L, Kjøller L, Nykjær A et al. Receptor-mediated endocytosis of plasminogen activators and activator/inhibitor complexes. FEBS Lett 1994;338:239-45.
    • (1994) FEBS Lett , vol.338 , pp. 239-245
    • Andreasen, P.A.1    Sottrup-Jensen, L.2    Kjøller, L.3    Nykjær, A.4
  • 18
    • 0036789017 scopus 로고    scopus 로고
    • Serpinopathies and the conformational dementias
    • Lomas DA, Carrell RW. Serpinopathies and the conformational dementias. Nat Rev Genet 2002;3:759-68.
    • (2002) Nat Rev Genet , vol.3 , pp. 759-768
    • Lomas, D.A.1    Carrell, R.W.2
  • 19
    • 85047684827 scopus 로고    scopus 로고
    • Alpha-1-antitrypsin polymerisation and the serpinopathies: Pathobiology and prospects for therapy
    • Lomas DA, Mahadeva R. Alpha-1-antitrypsin polymerisation and the serpinopathies: pathobiology and prospects for therapy. J Clin Invest 2002;110:1585-90.
    • (2002) J Clin Invest , vol.110 , pp. 1585-1590
    • Lomas, D.A.1    Mahadeva, R.2
  • 20
    • 0037011795 scopus 로고    scopus 로고
    • 1-antitrypsin deficiency: A model for conformational diseases
    • 1-antitrypsin deficiency: a model for conformational diseases. N Engl J Med 2002;346:45-53.
    • (2002) N Engl J Med , vol.346 , pp. 45-53
    • Carrell, R.W.1    Lomas, D.A.2
  • 21
    • 0024793406 scopus 로고
    • The fetal liver in PiZZ alpha-1-antitrypsin deficiency: A report of 5 cases
    • Malone M, Mieli-Vergani G, Mowat AP, Portmann B. The fetal liver in PiZZ alpha-1-antitrypsin deficiency: a report of 5 cases. Pediatric Pathology 1989;9:623-31.
    • (1989) Pediatric Pathology , vol.9 , pp. 623-631
    • Malone, M.1    Mieli-Vergani, G.2    Mowat, A.P.3    Portmann, B.4
  • 22
    • 0014530551 scopus 로고
    • Cirrhosis associated with alpha-1-antitrypsin deficiency: A previously unrecognised inherited disorder
    • Sharp HL, Bridges RA, Krivit W, Freier EF. Cirrhosis associated with alpha-1-antitrypsin deficiency: a previously unrecognised inherited disorder. J Lab Clin Med 1969;73:934-9.
    • (1969) J Lab Clin Med , vol.73 , pp. 934-939
    • Sharp, H.L.1    Bridges, R.A.2    Krivit, W.3    Freier, E.F.4
  • 24
    • 0017099344 scopus 로고
    • 1-antitrypsin deficiency detected by screening of 200,000 infants
    • 1-antitrypsin deficiency detected by screening of 200,000 infants. N Engl J Med 1976;294:1316-21.
    • (1976) N Engl J Med , vol.294 , pp. 1316-1321
    • Sveger, T.1
  • 25
    • 0017888482 scopus 로고
    • 1-antitrypsin deficiency in early childhood
    • 1-antitrypsin deficiency in early childhood. Pediatrics 1978; 62:22-25.
    • (1978) Pediatrics , vol.62 , pp. 22-25
    • Sveger, T.1
  • 26
    • 0024238708 scopus 로고
    • 1-antitrypsin deficient children
    • 1- antitrypsin deficient children. Acta Paed Scand 1988;77:847-51.
    • (1988) Acta Paed Scand , vol.77 , pp. 847-851
    • Sveger, T.1
  • 33
    • 0032529612 scopus 로고    scopus 로고
    • 1-antitrypsin polymerization probed by fluorescence spectroscopy
    • 1-antitrypsin polymerization probed by fluorescence spectroscopy. Arch Biochem Biophys 1998; 356:296-300.
    • (1998) Arch Biochem Biophys , vol.356 , pp. 296-300
    • James, E.L.1    Bottomley, S.P.2
  • 37
    • 0025923680 scopus 로고
    • 1-antitrypsin-deficient variant with mutation on a predicted conserved residue of the serpin backbone
    • 1-antitrypsin-deficient variant with mutation on a predicted conserved residue of the serpin backbone. J Biol Chem 1991;266:12627-32.
    • (1991) J Biol Chem , vol.266 , pp. 12627-12632
    • Seyama, K.1    Nukiwa, T.2    Takabe, K.3    Takahashi, H.4
  • 39
    • 0021151426 scopus 로고
    • Occurrence of alpha-1-antitrypsin deficiency in 155 patients with alcoholic liver disease
    • Roberts EA, Cox DW, Medline A, Wanless IR. Occurrence of alpha-1-antitrypsin deficiency in 155 patients with alcoholic liver disease. Am J Clin Pathol 1984;82:424-7.
    • (1984) Am J Clin Pathol , vol.82 , pp. 424-427
    • Roberts, E.A.1    Cox, D.W.2    Medline, A.3    Wanless, I.R.4
  • 41
    • 0028294879 scopus 로고
    • Immunohistochemical and genetic characterization of the M Cagliari α-1-antitrypsin molecule (M-like α-1-antitrypsin deficiency)
    • Sergi C, Consalez GC, Fabbretti G, Brisigotti M et al. Immunohistochemical and genetic characterization of the M Cagliari α-1-antitrypsin molecule (M-like α-1-antitrypsin deficiency). Lab Invest 1994;70:130-3.
    • (1994) Lab Invest , vol.70 , pp. 130-133
    • Sergi, C.1    Consalez, G.C.2    Fabbretti, G.3    Brisigotti, M.4
  • 42
    • 0038053035 scopus 로고    scopus 로고
    • Serpin polymerisation is prevented by a hydrogen bond network that is centered on His-334 and stabilized by glycereol
    • Zhou A, Stein PE, Huntington JA, Carrell RW. Serpin polymerisation is prevented by a hydrogen bond network that is centered on His-334 and stabilized by glycereol. J Biol Chem 2003;278:15116-122.
    • (2003) J Biol Chem , vol.278 , pp. 15116-15122
    • Zhou, A.1    Stein, P.E.2    Huntington, J.A.3    Carrell, R.W.4
  • 45
    • 0029012309 scopus 로고
    • 52Phe deleted) forms loop-sheet polymers in vivo: Evidence for the C sheet mechanism of polymerisation
    • 52Phe deleted) forms loop-sheet polymers in vivo: evidence for the C sheet mechanism of polymerisation. J Biol Chem 1995; 270:16864-70.
    • (1995) J Biol Chem , vol.270 , pp. 16864-16870
    • Lomas, D.A.1    Elliott, P.R.2    Sidhar, S.K.3    Foreman, R.C.4
  • 49
    • 0015583946 scopus 로고
    • Cirrhosis associated with partial deficiency of alpha-1-antitrypsin in an adult
    • Campra JL, Craig JR, Peters RL, Reynolds TB. Cirrhosis associated with partial deficiency of alpha-1-antitrypsin in an adult. Ann Intern Med 1973;78:233-8.
    • (1973) Ann Intern Med , vol.78 , pp. 233-238
    • Campra, J.L.1    Craig, J.R.2    Peters, R.L.3    Reynolds, T.B.4
  • 51
    • 0013828812 scopus 로고
    • 1-antitrypsin deficiency
    • 1-antitrypsin deficiency. Acta Med Scand 1965; suppl.432:1-85.
    • (1965) Acta Med Scand , vol.432 , Issue.SUPPL. , pp. 1-85
    • Eriksson, S.1
  • 52
    • 0015009621 scopus 로고
    • Pathophysiology of the pulmonary circulation in emphysema associated with alpha-1 antitrypsin deficiency
    • Stein PD, Leu JD, Welsh MH, Guenter CA. Pathophysiology of the pulmonary circulation in emphysema associated with alpha-1 antitrypsin deficiency. Circulation 1971;43:227-39.
    • (1971) Circulation , vol.43 , pp. 227-239
    • Stein, P.D.1    Leu, J.D.2    Welsh, M.H.3    Guenter, C.A.4
  • 56
    • 0025151507 scopus 로고
    • Comparative properties of human α-1-proteinase inhibitor glycosylation variants
    • Guzdek A, Potempa J, Dubin A, Travis J. Comparative properties of human α-1-proteinase inhibitor glycosylation variants. FEBS Lett 1990;272:125-7.
    • (1990) FEBS Lett , vol.272 , pp. 125-127
    • Guzdek, A.1    Potempa, J.2    Dubin, A.3    Travis, J.4
  • 57
    • 0027473016 scopus 로고
    • Effect of the Z mutation on the physical and inhibitory properties of α1-antitrypsin
    • Lomas DA, Evans DL, Stone SR, Chang W-SW, Carrell RW. Effect of the Z mutation on the physical and inhibitory properties of α1-antitrypsin. Biochemistry 1993;32:500-8.
    • (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
  • 59
    • 0018128288 scopus 로고
    • 1- antitrypsin deficiency, PiZ
    • 1-antitrypsin deficiency, PiZ. Acta Med Scand 1978;204:345-51.
    • (1978) Acta Med Scand , vol.204 , pp. 345-351
    • Larsson, C.1
  • 62
    • 0036014834 scopus 로고    scopus 로고
    • 1-antitrypsin are chemotactic for human neutrophils: A new paradigm for the pathogenesis of emphysema
    • 1-antitrypsin are chemotactic for human neutrophils: a new paradigm for the pathogenesis of emphysema. Am J Respir Cell Mol Biol 2002;26:723-30.
    • (2002) Am J Respir Cell Mol Biol , vol.26 , pp. 723-730
    • Parmar, J.S.1    Mahadeva, R.2    Reed, B.J.3    Farahi, N.4
  • 63
    • 2442488539 scopus 로고    scopus 로고
    • 1-antitrypsin polymerizes in the lung and acts as a neutrophil chemoattractant
    • 1-antitrypsin polymerizes in the lung and acts as a neutrophil chemoattractant Chest 2004;125:1952-7.
    • (2004) Chest , vol.125 , pp. 1952-1957
    • Mulgrew, A.T.1    Taggart, C.C.2    Lawless, M.W.3    Greene, C.M.4
  • 65
    • 19944430698 scopus 로고    scopus 로고
    • 1-antitrypsin co-localise with neutrophils in emphysematous alveoli and are chemotactic in vivo
    • 1-antitrypsin co-localise with neutrophils in emphysematous alveoli and are chemotactic in vivo. Am J Pathol 2005;166:377-86.
    • (2005) Am J Pathol , vol.166 , pp. 377-386
    • Mahadeva, R.1    Atkinson, C.2    Li, Z.3    Stewart, S.4
  • 66
    • 0023147734 scopus 로고
    • 1-proteinase inhibitor deficiency or chronic obstructive bronchitis: Anti-elastase function and cell profile
    • 1-proteinase inhibitor deficiency or chronic obstructive bronchitis: anti-elastase function and cell profile. Clinical Science 1987;72:373-81.
    • (1987) Clinical Science , vol.72 , pp. 373-381
    • Morrison, H.M.1    Kramps, J.A.2    Burnett, D.3    Stockley, R.A.4
  • 68
    • 0023894870 scopus 로고
    • 1-proteinase inhibitor and human leukocyte elastase is a neutrophil chemoattractant
    • 1-proteinase inhibitor and human leukocyte elastase is a neutrophil chemoattractant. J Exp Med 1988;167:1608-15.
    • (1988) J Exp Med , vol.167 , pp. 1608-1615
    • Banda, M.J.1    Rice, A.G.2    Griffin, G.L.3    Senior, R.M.4
  • 69
    • 0018893350 scopus 로고
    • Chemotactic activity of elastin derived peptides
    • Senior RM, Griffin GL, Mecham RP. Chemotactic activity of elastin derived peptides. J Clin Invest 1980;66:859-62.
    • (1980) J Clin Invest , vol.66 , pp. 859-862
    • Senior, R.M.1    Griffin, G.L.2    Mecham, R.P.3
  • 71
    • 0027923966 scopus 로고
    • 436→Thr) results in nonsubstrate-like behavior and in polymerization of the molecule
    • 436→Thr) results in nonsubstrate-like behavior and in polymerization of the molecule. J Biol Chem 1993;268:18088-94.
    • (1993) J Biol Chem , vol.268 , pp. 18088-18094
    • Aulak, K.S.1    Eldering, E.2    Hack, C.E.3    Lubbers, Y.P.4
  • 72
    • 0028855465 scopus 로고
    • COOH-terminal substitutions in the serpin C1 inhibitor that cause loop overinsertion and subsequent multimerization
    • Eldering E, Verpy E, Roem D, Meo T, Tosi M. COOH-terminal substitutions in the serpin C1 inhibitor that cause loop overinsertion and subsequent multimerization. J Biol Chem 1995;270:2579-87.
    • (1995) J Biol Chem , vol.270 , pp. 2579-2587
    • Eldering, E.1    Verpy, E.2    Roem, D.3    Meo, T.4    Tosi, M.5
  • 73
    • 0027999955 scopus 로고
    • Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen VI (187 Asn→Asp)
    • Bruce D, Perry DJ, Borg J-Y, Carrell RW, Wardell MR. Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen VI (187 Asn→Asp). J Clin Invest 1994;94:2265-74.
    • (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
  • 74
    • 0043245935 scopus 로고    scopus 로고
    • Antithrombin Phe229Leu: A new homozygous variant leading to spontaneous antithrombin polymerisation in vivo associated with severe childhood thrombosis
    • Picard V, Dautzenberg M-D, Villoutreix BO, Orliaguet G et al. Antithrombin Phe229Leu: a new homozygous variant leading to spontaneous antithrombin polymerisation in vivo associated with severe childhood thrombosis. Blood 2003;102:919-25.
    • (2003) Blood , vol.102 , pp. 919-925
    • Picard, V.1    Dautzenberg, M.-D.2    Villoutreix, B.O.3    Orliaguet, G.4
  • 75
    • 0027169598 scopus 로고
    • 1-antichymotrypsin deficiency in a heterozygote with liver and lung disease
    • 1-antichymotrypsin deficiency in a heterozygote with liver and lung disease. J Hepatology 1993;18:313-21.
    • (1993) J Hepatology , vol.18 , pp. 313-321
    • Faber, J.-P.1    Poller, W.2    Olek, K.3    Bauman, U.4
  • 76
    • 0027328108 scopus 로고
    • 1- antichymotrypsin allele associated with familial obstructive lung disease
    • 1-antichymotrypsin allele associated with familial obstructive lung disease. Genomics 1993;17:740-3.
    • (1993) Genomics , vol.17 , pp. 740-743
    • Poller, W.1    Faber, J.-P.2    Weidjnger, S.3    Tief, K.4
  • 77
    • 0034602778 scopus 로고    scopus 로고
    • 1-antichymotrypsin indicates two stage insertion of the reactive loop; implications for inhibitory function and conformational disease
    • 1-antichymotrypsin indicates two stage insertion of the reactive loop; implications for inhibitory function and conformational disease. Proc Natl Acad Sci USA 2000;97:67-72.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 67-72
    • Gooptu, B.1    Hazes, B.2    Chang, W.-S.W.3    Daffron, T.R.4
  • 78
    • 4444233600 scopus 로고    scopus 로고
    • Homozygous deficiency of heparin cofactor II: Relevance of P17 glutamate residue in serpins, relationship with conformational diseases, and role in thrombosis
    • Corral J, Aznar J, Gonzalez-Conejero R, del Key ML et al. Homozygous deficiency of heparin cofactor II: relevance of P17 glutamate residue in serpins, relationship with conformational diseases, and role in thrombosis. Circulation 2004;110:1303-7.
    • (2004) Circulation , vol.110 , pp. 1303-1307
    • Corral, J.1    Aznar, J.2    Gonzalez-Conejero, R.3    Del Key, M.L.4
  • 79
    • 0037385352 scopus 로고    scopus 로고
    • Mutations in the Drosophila serpin: Necrotic mirror disease-associated mutations of human serpins
    • Green C, Brown G, Dafforn TR, Morley T et al. Mutations in the Drosophila serpin: Necrotic mirror disease-associated mutations of human serpins. Development 2003;130:1473-8.
    • (2003) Development , vol.130 , pp. 1473-1478
    • Green, C.1    Brown, G.2    Dafforn, T.R.3    Morley, T.4
  • 80
    • 0032794402 scopus 로고    scopus 로고
    • Familial encephalopathy with neuroserpin inclusion bodies (FENIB)
    • Davis RL, Holohan PD, Shrimpton AE, Tatum AH et al. Familial encephalopathy with neuroserpin inclusion bodies (FENIB). Am J Pathol 1999;155:1901-13.
    • (1999) Am J Pathol , vol.155 , pp. 1901-1913
    • Davis, R.L.1    Holohan, P.D.2    Shrimpton, A.E.3    Tatum, A.H.4
  • 81
    • 0033598346 scopus 로고    scopus 로고
    • Familial dementia caused by polymerisation of mutant neuroserpin
    • Davis RL, Shrimpton AE, Holohan PD, Bradshaw C et al. Familial dementia caused by polymerisation of mutant neuroserpin. Nature 1999;401:376-9.
    • (1999) Nature , vol.401 , pp. 376-379
    • Davis, R.L.1    Shrimpton, A.E.2    Holohan, P.D.3    Bradshaw, C.4
  • 82
    • 0034857852 scopus 로고    scopus 로고
    • Cognitive deficits associated with a recently reported familial neurodegenerative disease
    • Bradshaw CB, Davis RL, Shrimpton AE, Holohan PD et al. Cognitive deficits associated with a recently reported familial neurodegenerative disease. Arch Neurol 2001;58:1429-34.
    • (2001) Arch Neurol , vol.58 , pp. 1429-1434
    • Bradshaw, C.B.1    Davis, R.L.2    Shrimpton, A.E.3    Holohan, P.D.4
  • 83
    • 0037193809 scopus 로고    scopus 로고
    • Association between conformational mutations in neuroserpin and onset and severity of dementia
    • Davis RL, Shrimpton AE, Carrell RW, Lomas DA et al. Association between conformational mutations in neuroserpin and onset and severity of dementia. Lancet 2002;359:2242-7.
    • (2002) Lancet , vol.359 , pp. 2242-2247
    • Davis, R.L.1    Shrimpton, A.E.2    Carrell, R.W.3    Lomas, D.A.4
  • 84
    • 0037053323 scopus 로고    scopus 로고
    • Mutant neuroserpin (Ser49Pro) that causes the familial dementia FENIB is a poor proteinase inhibitor and readily forms polymers in vitro
    • Belorgey D, Crowther DC, Mahadeva R, Lomas DA. Mutant neuroserpin (Ser49Pro) that causes the familial dementia FENIB is a poor proteinase inhibitor and readily forms polymers in vitro. J Biol Chem 2002;277:17367-73.
    • (2002) J Biol Chem , vol.277 , pp. 17367-17373
    • Belorgey, D.1    Crowther, D.C.2    Mahadeva, R.3    Lomas, D.A.4
  • 85
    • 4344586923 scopus 로고    scopus 로고
    • Neuroserpin Portland (Ser52Arg) is trapped as an inactive intermediate that rapidly forms polymers: Implications for the epilepsy seen in the dementia FENIB
    • Belorgey D, Sharp LK, Crowther DC, Onda M et al. Neuroserpin Portland (Ser52Arg) is trapped as an inactive intermediate that rapidly forms polymers: implications for the epilepsy seen in the dementia FENIB. Eur J Biochem 2004;271:3360-7.
    • (2004) Eur J Biochem , vol.271 , pp. 3360-3367
    • Belorgey, D.1    Sharp, L.K.2    Crowther, D.C.3    Onda, M.4
  • 86
    • 17144431759 scopus 로고    scopus 로고
    • Latent S49P neuroserpin spontaneously forms polymers: Identification of a novel pathway of polymerization and implications for the dementia FENIB
    • Onda M, Belorgey D, Sharp LK, Lomas DA. Latent S49P neuroserpin spontaneously forms polymers: identification of a novel pathway of polymerization and implications for the dementia FENIB. J Biol Chem 2005;280:13735-41.
    • (2005) J Biol Chem , vol.280 , pp. 13735-13741
    • Onda, M.1    Belorgey, D.2    Sharp, L.K.3    Lomas, D.A.4
  • 87
    • 3142582012 scopus 로고    scopus 로고
    • Mutants of neuroserpin that cause dementia accumulate as polymers within the endoplasmic reticulum
    • Miranda E, Römisch K, Lomas DA. Mutants of neuroserpin that cause dementia accumulate as polymers within the endoplasmic reticulum. J Biol Chem 2004;279:28283-91.
    • (2004) J Biol Chem , vol.279 , pp. 28283-28291
    • Miranda, E.1    Römisch, K.2    Lomas, D.A.3
  • 90
    • 0032538299 scopus 로고    scopus 로고
    • Implications for function and therapy of a 2.9 Å structure of binary-complexed antithrombin
    • Skinner R, Chang W-SW, Jin L, Pei X et al. Implications for function and therapy of a 2.9 Å structure of binary-complexed antithrombin. J Mol Biol 1998;283:9-14.
    • (1998) J Mol Biol , vol.283 , pp. 9-14
    • Skinner, R.1    Chang, W.-S.W.2    Jin, L.3    Pei, X.4
  • 91
    • 0030819064 scopus 로고    scopus 로고
    • Mechanisms of antithrombin polymerisation and heparin activation probed by insertion of synthetic reactive loop peptides
    • Fitton HL, Pike RN, Carrell RW, Chang W-SW. Mechanisms of antithrombin polymerisation and heparin activation probed by insertion of synthetic reactive loop peptides. Biol Chem 1997;378:1059-63.
    • (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
  • 92
    • 0029866947 scopus 로고    scopus 로고
    • Probing serpin reactive loop conformations by proteolytic cleavage
    • Chang W-SW, Wardell MR, Lomas DA, Carrell RW. Probing serpin reactive loop conformations by proteolytic cleavage. Biochem J 1996;314:647-53.
    • (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
  • 95
    • 4444332086 scopus 로고    scopus 로고
    • How small peptides block and reverse serpin polymerization
    • Zhou A, Stein PE, Huntington JA, Sivasothy P et al. How small peptides block and reverse serpin polymerization. J Mol Biol 2004;342:931-41.
    • (2004) J Mol Biol , vol.342 , pp. 931-941
    • Zhou, A.1    Stein, P.E.2    Huntington, J.A.3    Sivasothy, P.4
  • 96


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.