메뉴 건너뛰기




Volumn 10, Issue S1, 2013, Pages 17-25

Twenty years of polymers: A personal perspective on alpha-1 antitrypsin deficiency

Author keywords

Cirrhosis; Emphysema; Pathogenesis; Serpin; Serpinopathies; Treatment

Indexed keywords

ALPHA 1 ANTITRYPSIN; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 2C1; POLYMER; UNCLASSIFIED DRUG;

EID: 84875673488     PISSN: 15412555     EISSN: 15412563     Source Type: Journal    
DOI: 10.3109/15412555.2013.764401     Document Type: Review
Times cited : (26)

References (93)
  • 1
    • 46949107890 scopus 로고    scopus 로고
    • Polymers and inflammation: Disease mechanisms of the serpinopathies
    • Gooptu B, Lomas DA. Polymers and inflammation: disease mechanisms of the serpinopathies. J Exp Med 2008; 205:1529- 1534.
    • (2008) J Exp Med , vol.205 , pp. 1529-1534
    • Gooptu, B.1    Lomas, D.A.2
  • 2
    • 67650713938 scopus 로고    scopus 로고
    • Conformational pathology of the serpins - Themes, variations and therapeutic strategies
    • Gooptu B, Lomas DA. Conformational pathology of the serpins - themes, variations and therapeutic strategies. Annu Rev Biochem 2009; 78:147-176.
    • (2009) Annu Rev Biochem , vol.78 , pp. 147-176
    • Gooptu, B.1    Lomas, D.A.2
  • 3
    • 67649246879 scopus 로고    scopus 로고
    • Alpha1-Antitrypsin deficiency, chronic obstructive pulmonary disease and the serpinopathies
    • Ekeowa UI, Gooptu B, Belorgey D, Hagglof P, Karlsson-Li S, Miranda E, et al. alpha1-Antitrypsin deficiency, chronic obstructive pulmonary disease and the serpinopathies. Clin Sci (Lond) 2009; 116(12):837-850.
    • (2009) Clin Sci (Lond) , vol.116 , Issue.12 , pp. 837-850
    • Ekeowa, U.I.1    Gooptu, B.2    Belorgey, D.3    Hagglof, P.4    Karlsson-Li, S.5    Miranda, E.6
  • 5
    • 84856144387 scopus 로고    scopus 로고
    • Why has it been so difficult to prove the efficacy of alpha-1-antitrypsin replacement therapy? Insights from the study of disease pathogenesis
    • Dickens JA, Lomas DA. Why has it been so difficult to prove the efficacy of alpha-1-antitrypsin replacement therapy? Insights from the study of disease pathogenesis. Drug Des Devel Ther 2011; 5:391-405.
    • (2011) Drug des Devel Ther , vol.5 , pp. 391-405
    • Dickens, J.A.1    Lomas, D.A.2
  • 6
    • 84907041622 scopus 로고
    • The electrophoretic a1-globulin pattern of serum in α1-antitrypsin deficiency
    • Laurell C-B, Eriksson S. The electrophoretic a1-globulin pattern of serum in α1-antitrypsin deficiency. Scand J Clin Lab Invest 1963; 15:132-140.
    • (1963) Scand J Clin Lab Invest , vol.15 , pp. 132-140
    • Laurell, C.-B.1    Eriksson, S.2
  • 7
    • 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(6):934-939.
    • (1969) J Lab Clin Med , vol.73 , Issue.6 , pp. 934-939
    • Sharp, H.L.1    Bridges, R.A.2    Krivit, W.3    Freier, E.F.4
  • 8
    • 0021747157 scopus 로고
    • Human α1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function
    • Loebermann H, Tokuoka R, Deisenhofer J, Huber R. Human α1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. J Mol Biol 1984; 177:531-557.
    • (1984) J Mol Biol , vol.177 , pp. 531-557
    • Loebermann, H.1    Tokuoka, R.2    Deisenhofer, J.3    Huber, R.4
  • 10
    • 17744409446 scopus 로고    scopus 로고
    • Wildtype α1-antitrypsin is in the canonical inhibitory conformation
    • Elliott PR, Abrahams J-P, Lomas DA. Wildtype α1-antitrypsin is in the canonical inhibitory conformation. J Mol Biol 1998; 275(3):419-425.
    • (1998) J Mol Biol , vol.275 , Issue.3 , pp. 419-425
    • Elliott, P.R.1    Abrahams, J.-P.2    Lomas, D.A.3
  • 11
    • 0343193210 scopus 로고    scopus 로고
    • Topography of a 2.0A structure of α1-antitrypsin reveals targets for rational drug design to prevent conformational disease
    • Elliott PR, Pei XY, Dafforn TR, Lomas DA. Topography of a 2.0A structure of α1-antitrypsin reveals targets for rational drug design to prevent conformational disease. Protein Sci 2000; 9:1274-1281.
    • (2000) Protein Sci , vol.9 , pp. 1274-1281
    • Elliott, P.R.1    Pei, X.Y.2    Dafforn, T.R.3    Lomas, D.A.4
  • 12
    • 0030587834 scopus 로고    scopus 로고
    • The native strains in the hydrophobic core and flexible reactive loop of a serine protease inhibitor: Crystal structure of an uncleaved α1-antitrypsin at 2.7A
    • Ryu S-E, Choi H-J, Kwon K-S, Lee KN, Yu M-H. The native strains in the hydrophobic core and flexible reactive loop of a serine protease inhibitor: crystal structure of an uncleaved α1-antitrypsin at 2.7A. Structure 1996; 4:1181-1192.
    • (1996) Structure , vol.4 , pp. 1181-1192
    • Ryu, S.-E.1    Choi, H.-J.2    Kwon, K.-S.3    Lee, K.N.4    Yu, M.-H.5
  • 13
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpinprotease complex shows inhibition by deformation
    • Huntington JA, Read RJ, Carrell RW. Structure of a serpinprotease complex shows inhibition by deformation. Nature 2000; 407:923-926.
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 14
    • 0026755363 scopus 로고
    • The mechanism of Z α1-antitrypsin accumulation in the liver
    • Lomas DA, Evans DL, Finch JT, Carrell RW. The mechanism of Z α1-antitrypsin accumulation in the liver. Nature 1992; 357:605-607.
    • (1992) Nature , vol.357 , pp. 605-607
    • Lomas, D.A.1    Evans, D.L.2    Finch, J.T.3    Carrell, R.W.4
  • 15
    • 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; 32:500-508.
    • (1993) Biochemistry , vol.32 , pp. 500-508
    • Lomas, D.A.1    Evans, D.L.2    Stone, S.R.3    W-Sw, C.4    Carrell, R.W.5
  • 16
    • 0032538299 scopus 로고    scopus 로고
    • Implications for function and therapy of a 2.9A structure of binary-complexed antithrombin
    • Skinner R, Chang W-SW, Jin L, Pei X, Huntington JA, Abrahams J-P, et al. Implications for function and therapy of a 2.9A structure of binary-complexed antithrombin. J Mol Biol 1998; 283(1):9-14.
    • (1998) J Mol Biol , vol.283 , Issue.1 , pp. 9-14
    • Skinner, R.1    W-Sw, C.2    Jin, L.3    Pei, X.4    Huntington, J.A.5    Abrahams, J.-P.6
  • 17
    • 0027295822 scopus 로고
    • α1-antitrypsin Siiyama (Ser53→Phe); Further evidence for intracellular loop-sheet polymerisation
    • Lomas DA, Finch JT, Seyama K, Nukiwa T, Carrell RW. α1-antitrypsin Siiyama (Ser53→Phe); further evidence for intracellular loop-sheet polymerisation. J Biol Chem 1993; 268:15333-15335.
    • (1993) J Biol Chem , vol.268 , pp. 15333-15335
    • Lomas, D.A.1    Finch, J.T.2    Seyama, K.3    Nukiwa, T.4    Carrell, R.W.5
  • 18
    • 0029012309 scopus 로고
    • Alpha1-antitrypsin Mmalton (52Phe deleted) forms loop-sheet polymers in vivo: Evidence for the C sheet mechanism of polymerisation
    • Lomas DA, Elliott PR, Sidhar SK, Foreman RC, Finch JT, Cox DW, et al. Alpha1-antitrypsin Mmalton (52Phe deleted) forms loop-sheet polymers in vivo: evidence for the C sheet mechanism of polymerisation. J Biol Chem 1995; 270(28):16864-16870.
    • (1995) J Biol Chem , vol.270 , Issue.28 , pp. 16864-16870
    • Lomas, D.A.1    Elliott, P.R.2    Sidhar, S.K.3    Foreman, R.C.4    Finch, J.T.5    Cox, D.W.6
  • 19
    • 77956389382 scopus 로고    scopus 로고
    • A novel monoclonal antibody to characterise pathogenic polymers in liver disease associated with α1-antitrypsin deficiency
    • Miranda E, Perez J, Ekeowa UI, Hadzic N, Kalsheker N, Gooptu B, et al. A novel monoclonal antibody to characterise pathogenic polymers in liver disease associated with α1-antitrypsin deficiency. Hepatology 2010; 52:1078-1088.
    • (2010) Hepatology , vol.52 , pp. 1078-1088
    • Miranda, E.1    Perez, J.2    Ekeowa, U.I.3    Hadzic, N.4    Kalsheker, N.5    Gooptu, B.6
  • 23
    • 0034602778 scopus 로고    scopus 로고
    • Inactive conformation of the serpin α1-antichymotrypsin indicates two stage insertion of the reactive loop; Implications for inhibitory function and conformational disease
    • Gooptu B, Hazes B, Chang W-SW, Dafforn TR, Carrell RW, Read R, et al. Inactive conformation of the serpin α1-antichymotrypsin indicates two stage insertion of the reactive loop; implications for inhibitory function and conformational disease. Proc Natl Acad Sci USA 2000; 97(1):67-72.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.1 , pp. 67-72
    • Gooptu, B.1    Hazes, B.2    W-Sw, C.3    Dafforn, T.R.4    Carrell, R.W.5    Read, R.6
  • 24
    • 0029048542 scopus 로고
    • The Z type variation of human α1-antitrypsin causes a protein folding defect
    • Yu M-H, Lee KN, Kim J. The Z type variation of human α1-antitrypsin causes a protein folding defect. Nat Struct Biol 1995; 2(5):363-367.
    • (1995) Nat Struct Biol , vol.2 , Issue.5 , pp. 363-367
    • Yu, M.-H.1    Lee, K.N.2    Kim, J.3
  • 25
    • 0003049256 scopus 로고    scopus 로고
    • Folding and stability of the Z and Siiyama genetic variants of human α1-antitrypsin
    • Kang HA, Lee KN, Yu M-H. Folding and stability of the Z and Siiyama genetic variants of human α1-antitrypsin. J Biol Chem 1997; 272(1):510-516.
    • (1997) J Biol Chem , vol.272 , Issue.1 , pp. 510-516
    • Kang, H.A.1    Lee, K.N.2    Yu, M.-H.3
  • 26
    • 0037816258 scopus 로고    scopus 로고
    • Elucidation of the molecular logic by which misfolded α1-antitrypsin is preferentially selected for degradation
    • Wu Y, Swulius MT, Moremen KW, Sifers RN. Elucidation of the molecular logic by which misfolded α1-antitrypsin is preferentially selected for degradation. Proc Natl Acad Sci USA 2003; 100(14):8229-8234.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.14 , pp. 8229-8234
    • Wu, Y.1    Swulius, M.T.2    Moremen, K.W.3    Sifers, R.N.4
  • 27
    • 0026570248 scopus 로고
    • Soluble aggregates of the human PiZ α1-antitrypsin variant are degraded within the endoplasmic reticulum by a mechanism sensitive to inhibitors of protein synthesis
    • Le A, Ferrell GA, Dishon DS, Quyen-Quyen AL, Sifers RN. Soluble aggregates of the human PiZ α1-antitrypsin variant are degraded within the endoplasmic reticulum by a mechanism sensitive to inhibitors of protein synthesis. J Biol Chem 1992; 267(2):1072-1080.
    • (1992) J Biol Chem , vol.267 , Issue.2 , pp. 1072-1080
    • Le, A.1    Ferrell, G.A.2    Dishon, D.S.3    Quyen-Quyen, A.L.4    Sifers, R.N.5
  • 28
    • 0029788023 scopus 로고    scopus 로고
    • Degradation of a mutant secretory protein, α1-antitrypsin Z, in the endoplasmic reticulum requires proteosome activity
    • Qu D, Teckman JH, Omura S, Perlmutter DH. Degradation of a mutant secretory protein, α1-antitrypsin Z, in the endoplasmic reticulum requires proteosome activity. J Biol Chem 1996; 271(37):22791-22795.
    • (1996) J Biol Chem , vol.271 , Issue.37 , pp. 22791-22795
    • Qu, D.1    Teckman, J.H.2    Omura, S.3    Perlmutter, D.H.4
  • 29
    • 69249104575 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins
    • Kroger H, Miranda E, MacLeod I, Perez J, Crowther DC, Marciniak SJ, et al. Endoplasmic reticulum-associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins. J Biol Chem 2009; 284(34):22793-22802.
    • (2009) J Biol Chem , vol.284 , Issue.34 , pp. 22793-22802
    • Kroger, H.1    Miranda, E.2    Macleod, I.3    Perez, J.4    Crowther, D.C.5    Marciniak, S.J.6
  • 30
    • 0032529612 scopus 로고    scopus 로고
    • The mechanism of α1-antitrypsin polymerization probed by fluorescence spectroscopy
    • James EL, Bottomley SP. The mechanism of α1-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
  • 31
    • 0034721790 scopus 로고    scopus 로고
    • Pathogenic α1-antitrypsin polymers are formed by reactive loop-®-sheet A linkage
    • Sivasothy P, Dafforn TR, Gettins PGW, Lomas DA. Pathogenic α1-antitrypsin polymers are formed by reactive loop-®-sheet A linkage. J Biol Chem. 2000; 275(43):33663-33668.
    • (2000) J Biol Chem. , vol.275 , Issue.43 , pp. 33663-33668
    • Sivasothy, P.1    Dafforn, T.R.2    Pgw, G.3    Lomas, D.A.4
  • 33
    • 3342889562 scopus 로고    scopus 로고
    • Different conformational changes within the F-helix occur during serpin folding, polymerization and proteinase inhibition
    • Cabrita LD, Dai W, Bottomley SP. Different conformational changes within the F-helix occur during serpin folding, polymerization and proteinase inhibition. Biochemistry 2004; 43:9834-9839.
    • (2004) Biochemistry , vol.43 , pp. 9834-9839
    • Cabrita, L.D.1    Dai, W.2    Bottomley, S.P.3
  • 34
    • 34548463041 scopus 로고    scopus 로고
    • Probing the local conformational change of α1-antitrypsin
    • Baek JH, Im H, Kang UB, Seong KM, Lee C, Kim J, et al. Probing the local conformational change of α1-antitrypsin. Protein Sci 2007; 16(9):1842-1850.
    • (2007) Protein Sci , vol.16 , Issue.9 , pp. 1842-1850
    • Baek, J.H.1    Im, H.2    Kang, U.B.3    Seong, K.M.4    Lee, C.5    Kim, J.6
  • 35
    • 62649174885 scopus 로고    scopus 로고
    • Crystallographic and cellular characterisation of two mechanisms stabilising the native fold of alpha-1- antitrypsin: Implications for disease and drug design
    • Gooptu B, Miranda E, Nobeli I, Mallya M, Purkiss A, Leigh Brown SC, et al. Crystallographic and cellular characterisation of two mechanisms stabilising the native fold of alpha-1- antitrypsin: implications for disease and drug design. J Mol Biol 2009; 387(4):857-868.
    • (2009) J Mol Biol , vol.387 , Issue.4 , pp. 857-868
    • Gooptu, B.1    Miranda, E.2    Nobeli, I.3    Mallya, M.4    Purkiss, A.5    Leigh Brown, S.C.6
  • 36
    • 84857926856 scopus 로고    scopus 로고
    • Structural dynamics associated with intermediate formation in an archetypal conformational disease
    • Nyon MP, Segu L, Cabrita LD, Levy GR, Kirkpatrick J, Roussel BD, et al. Structural dynamics associated with intermediate formation in an archetypal conformational disease. Structure 2012; 20(3):504-512.
    • (2012) Structure , vol.20 , Issue.3 , pp. 504-512
    • Nyon, M.P.1    Segu, L.2    Cabrita, L.D.3    Levy, G.R.4    Kirkpatrick, J.5    Roussel, B.D.6
  • 37
    • 0025226070 scopus 로고
    • Structural transition of α1-antitrypsin by a peptide sequentially similar to ®-strand s4A
    • Schulze AJ, Baumann U, Knof S, Jaeger E, Huber R, Laurell C-B. Structural transition of α1-antitrypsin by a peptide sequentially similar to ®-strand s4A. Eur J Biochem 1990; 194:51-56.
    • (1990) Eur J Biochem , vol.194 , pp. 51-56
    • Schulze, A.J.1    Baumann, U.2    Knof, S.3    Jaeger, E.4    Huber, R.5    Laurell, C.-B.6
  • 38
    • 0036882160 scopus 로고    scopus 로고
    • Acid denaturation of α1-antitrypsin: Characterization of a novel mechanism of serpin polymerization
    • Devlin GL, Chow MKM, Howlett GJ, Bottomley SP. Acid denaturation of α1-antitrypsin: characterization of a novel mechanism of serpin polymerization. J Mol Biol 2002; 324:859-870.
    • (2002) J Mol Biol , vol.324 , pp. 859-870
    • Devlin, G.L.1    Chow, M.K.M.2    Howlett, G.J.3    Bottomley, S.P.4
  • 39
    • 0028773279 scopus 로고
    • Biological implications of a 3A structure of dimeric antithrombin
    • Carrell RW, Stein PE, Fermi G, Wardell MR. Biological implications of a 3A structure of dimeric antithrombin. Structure 1994; 2(4):257-270.
    • (1994) Structure , vol.2 , Issue.4 , pp. 257-270
    • Carrell, R.W.1    Stein, P.E.2    Fermi, G.3    Wardell, M.R.4
  • 41
    • 0033081498 scopus 로고    scopus 로고
    • The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion
    • Sharp AM, Stein PE, Pannu NS, Carrell RW, Berkenpas MB, Ginsburg D, et al. The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion. Structure 1999; 7:111-118.
    • (1999) Structure , vol.7 , pp. 111-118
    • Sharp, A.M.1    Stein, P.E.2    Pannu, N.S.3    Carrell, R.W.4    Berkenpas, M.B.5    Ginsburg, D.6
  • 42
    • 33746280757 scopus 로고    scopus 로고
    • X-ray crystal structure of MENT: Evidence for functional loop-sheet polymers in chromatin condensation
    • McGowan S, Buckle AM, Irving JA, Ong PC, Bashtannyk- Puhalovich TA, Kan WT, et al. X-ray crystal structure of MENT: evidence for functional loop-sheet polymers in chromatin condensation. EMBO J 2006; 25(13):3144-3155.
    • (2006) EMBO J , vol.25 , Issue.13 , pp. 3144-3155
    • McGowan, S.1    Buckle, A.M.2    Irving, J.A.3    Ong, P.C.4    Bashtannyk-Puhalovich, T.A.5    Kan, W.T.6
  • 43
    • 55249111481 scopus 로고    scopus 로고
    • Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization
    • Yamasaki M, Li W, Johnson DJ, Huntington JA. Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization. Nature 2008; 455:1255-1258.
    • (2008) Nature , vol.455 , pp. 1255-1258
    • Yamasaki, M.1    Li, W.2    Johnson, D.J.3    Huntington, J.A.4
  • 44
    • 80053561166 scopus 로고    scopus 로고
    • Molecular basis of α1-antitrypsin deficiency revealed by the structure of a domain-swapped trimer
    • Yamasaki M, Sendall TJ, Pearce MC, Whisstock JC, Huntington JA. Molecular basis of α1-antitrypsin deficiency revealed by the structure of a domain-swapped trimer. EMBO Rep 2011; 12(10):1011-1017.
    • (2011) EMBO Rep , vol.12 , Issue.10 , pp. 1011-1017
    • Yamasaki, M.1    Sendall, T.J.2    Pearce, M.C.3    Whisstock, J.C.4    Huntington, J.A.5
  • 45
    • 79551646854 scopus 로고    scopus 로고
    • Dynamic local unfolding in the serpin α1-antitrypsin provides a mechanism for loop insertion and polymerization
    • Krishnan B, Gierasch LM. Dynamic local unfolding in the serpin α1-antitrypsin provides a mechanism for loop insertion and polymerization. Nat Struct Mol Biol 2011; 18(2):222-226.
    • (2011) Nat Struct Mol Biol , vol.18 , Issue.2 , pp. 222-226
    • Krishnan, B.1    Gierasch, L.M.2
  • 48
    • 0023840570 scopus 로고
    • Alpha1 antitrypsin deficiency due to Pi null: Clinical presentation and evidence for molecular heterogeneity
    • Bamforth FJ, Kalsheker NA. Alpha1 antitrypsin deficiency due to Pi null: clinical presentation and evidence for molecular heterogeneity. J Med Genet 1988; 25:83-87.
    • (1988) J Med Genet , vol.25 , pp. 83-87
    • Bamforth, F.J.1    Kalsheker, N.A.2
  • 49
    • 0032065494 scopus 로고    scopus 로고
    • Lung polymers in Z α1-antitrypsin related emphysema
    • Elliott PR, Bilton D, Lomas DA. Lung polymers in Z α1-antitrypsin related emphysema. Am J Respir Cell Mol Biol 1998; 18(5):670-674.
    • (1998) Am J Respir Cell Mol Biol , vol.18 , Issue.5 , pp. 670-674
    • Elliott, P.R.1    Bilton, D.2    Lomas, D.A.3
  • 51
    • 25944452730 scopus 로고
    • Proteasecomplexed and polymerised antithrombin and α1-antitrypsin bind low density lipoprotein receptor-related protein
    • Wardell MR, Lomas DA, Brecht WJ, Mahley RW. Proteasecomplexed and polymerised antithrombin and α1-antitrypsin bind low density lipoprotein receptor-related protein. Protein Sci 1994; 3 Suppl. 1:101-S.
    • (1994) Protein Sci , vol.3 , Issue.SUPPL. 1
    • Wardell, M.R.1    Lomas, D.A.2    Brecht, W.J.3    Mahley, R.W.4
  • 52
    • 0023894870 scopus 로고
    • The inhibitory complex of human α1-proteinase inhibitor and human leukocyte elastase is a neutrophil chemoattractant
    • Banda MJ, Rice AG, Griffin GL, Senior RM. The inhibitory complex of human α1-proteinase inhibitor and human leukocyte elastase is a neutrophil chemoattractant. J Exp Med 1988; 167:1608-1615.
    • (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
  • 53
    • 0036014834 scopus 로고    scopus 로고
    • Polymers of α1-antitrypsin are chemotactic for human neutrophils: A new paradigm for the pathogenesis of emphysema
    • Parmar JS, Mahadeva R, Reed BJ, Farahi N, Cadwallader K, Bilton D, et al. Polymers of α1-antitrypsin are chemotactic for human neutrophils: a new paradigm for the pathogenesis of emphysema. Am J Respir Cell Mol Biol 2002; 26:723-730.
    • (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    Cadwallader, K.5    Bilton, D.6
  • 54
    • 19944430698 scopus 로고    scopus 로고
    • Polymers of Z α1-antitrypsin co-localise with neutrophils in emphysematous alveoli and are chemotactic in vivo
    • Mahadeva R, Atkinson C, Li J, Stewart S, Janciauskiene S, Kelley DG, et al. Polymers of Z α1-antitrypsin co-localise with neutrophils in emphysematous alveoli and are chemotactic in vivo. Am J Pathol 2005; 166(2):377-386.
    • (2005) Am J Pathol , vol.166 , Issue.2 , pp. 377-386
    • Mahadeva, R.1    Atkinson, C.2    Li, J.3    Stewart, S.4    Janciauskiene, S.5    Kelley, D.G.6
  • 55
    • 80051635385 scopus 로고    scopus 로고
    • Oxidation of Z alpha-1-antitrypsin by cigarette smoke induces polymerization: A novel mechanism of early-onset emphysema
    • Alam S, Li Z, Janciauskiene S, Mahadeva R. Oxidation of Z alpha-1-antitrypsin by cigarette smoke induces polymerization: a novel mechanism of early-onset emphysema. Am J Respir Cell Mol Biol 2011; 45:261-269.
    • (2011) Am J Respir Cell Mol Biol , vol.45 , pp. 261-269
    • Alam, S.1    Li, Z.2    Janciauskiene, S.3    Mahadeva, R.4
  • 56
    • 77956354416 scopus 로고    scopus 로고
    • Modeling inherited metabolic disorders of the liver using human induced pluripotent stem cells
    • Rashid ST, Corbineau S, Hannan N, Marciniak SJ, Miranda E, Alexander G, et al. Modeling inherited metabolic disorders of the liver using human induced pluripotent stem cells. J Clin Invest 2010; 120(9):3127-3136.
    • (2010) J Clin Invest , vol.120 , Issue.9 , pp. 3127-3136
    • Rashid, S.T.1    Corbineau, S.2    Hannan, N.3    Marciniak, S.J.4    Miranda, E.5    Alexander, G.6
  • 57
    • 0027336667 scopus 로고
    • Alpha1-antitrypsin genetic polymorphism in ANCA-positive systemic vasculitis
    • Esnault VLM, Testa A, Audrain M, Roge C, Hamidou M, Barrier JH, et al. Alpha1-antitrypsin genetic polymorphism in ANCA-positive systemic vasculitis. Kidney Inter 1993; 43(6):1329-1332.
    • (1993) Kidney Inter , vol.43 , Issue.6 , pp. 1329-1332
    • Esnault, V.L.M.1    Testa, A.2    Audrain, M.3    Roge, C.4    Hamidou, M.5    Barrier, J.H.6
  • 59
    • 80052478226 scopus 로고    scopus 로고
    • ANCA-associated vasculitis is linked to carriage of the Z allele of α1-antitrypsin and its polymers
    • Morris H, Morgan MD, Wood AM, Smith SW, Ekeowa UI, Herrmann K, et al. ANCA-associated vasculitis is linked to carriage of the Z allele of α1-antitrypsin and its polymers. Ann Rheum Dis 2011; 70(10):1851-1856.
    • (2011) Ann Rheum Dis , vol.70 , Issue.10 , pp. 1851-1856
    • Morris, H.1    Morgan, M.D.2    Wood, A.M.3    Smith, S.W.4    Ekeowa, U.I.5    Herrmann, K.6
  • 60
    • 67651091349 scopus 로고    scopus 로고
    • New findings in PiZZ alpha (1)-antitrypsin deficiency-related panniculitis. Demonstration of skin polymers and high dosing requirements of intravenous augmentation therapy
    • Gross B, Grebe M, Wencker M, Stoller JK, Bjursten LM, Janciauskiene S. New findings in PiZZ alpha(1)-antitrypsin deficiency-related panniculitis. Demonstration of skin polymers and high dosing requirements of intravenous augmentation therapy. Dermatology 2009; 218(4):370-375.
    • (2009) Dermatology , vol.218 , Issue.4 , pp. 370-375
    • Gross, B.1    Grebe, M.2    Wencker, M.3    Stoller, J.K.4    Bjursten, L.M.5    Janciauskiene, S.6
  • 61
    • 79953858686 scopus 로고    scopus 로고
    • Efficacy of alpha1-antitrypsin augmentation therapy in conditions other than pulmonary emphysema
    • Blanco I, Lara B, de Serres F. Efficacy of alpha1-antitrypsin augmentation therapy in conditions other than pulmonary emphysema. Orphanet J Rare Dis Orphanet J Rare Dis 2011; 6:14.
    • (2011) Orphanet J Rare Dis Orphanet J Rare Dis , vol.6 , pp. 14
    • Blanco, I.1    Lara, B.2    De Serres, F.3
  • 62
    • 33646588338 scopus 로고    scopus 로고
    • The selective advantage of α1-antitrypsin deficiency
    • Lomas DA. The selective advantage of α1-antitrypsin deficiency. Am J Respir Crit Care Med 2006; 173:1072-1077.
    • (2006) Am J Respir Crit Care Med , vol.173 , pp. 1072-1077
    • Lomas, D.A.1
  • 63
    • 32544437550 scopus 로고    scopus 로고
    • Neutrophilic inflammation and IL-8 levels in induced sputum of alpha-1-antitrypsin PiMZ subjects
    • Malerba M, Ricciardolo F, Radaeli A, Torregiani C, Ceriani L, Mori E, et al. Neutrophilic inflammation and IL-8 levels in induced sputum of alpha-1-antitrypsin PiMZ subjects. Thorax 2006; 61(2):129-133.
    • (2006) Thorax , vol.61 , Issue.2 , pp. 129-133
    • Malerba, M.1    Ricciardolo, F.2    Radaeli, A.3    Torregiani, C.4    Ceriani, L.5    Mori, E.6
  • 64
    • 0027923966 scopus 로고
    • A hinge region mutation in C1-inhibitor (Ala436 Thr) results in nonsubstrate-like behavior and in polymerization of the molecule
    • Aulak KS, Eldering E, Hack CE, Lubbers YPT, Harrison RA, Mast A, et al. A hinge region mutation in C1-inhibitor (Ala436 Thr) results in nonsubstrate-like behavior and in polymerization of the molecule. J Biol Chem 1993; 268(24):18088-18094.
    • (1993) J Biol Chem , vol.268 , Issue.24 , pp. 18088-18094
    • Aulak, K.S.1    Eldering, E.2    Hack, C.E.3    Lubbers, Y.P.T.4    Harrison, R.A.5    Mast, A.6
  • 65
    • 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(6):2579-2587.
    • (1995) J Biol Chem , vol.270 , Issue.6 , pp. 2579-2587
    • Eldering, E.1    Verpy, E.2    Roem, D.3    Meo, T.4    Tosi, M.5
  • 66
    • 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; 94:226-2274.
    • (1994) J Clin Invest , vol.94 , pp. 226-2274
    • Bruce, D.1    Perry, D.J.2    Borg, J.-Y.3    Carrell, R.W.4    Wardell, M.R.5
  • 67
    • 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, Alhenc-Gelas M, Aiach M. Antithrombin Phe229Leu: a new homozygous variant leading to spontaneous antithrombin polymerisation in vivo associated with severe childhood thrombosis. Blood 2003; 102(3):919-925.
    • (2003) Blood , vol.102 , Issue.3 , pp. 919-925
    • Picard, V.1    Dautzenberg, M.-D.2    Villoutreix, B.O.3    Orliaguet, G.4    Alhenc-Gelas, M.5    Aiach, M.6
  • 68
    • 0027169598 scopus 로고
    • The molecular basis of α1-antichymotrypsin deficiency in a heterozygote with liver and lung disease
    • Faber J-P, Poller W, Olek K, Baumann U, Carlson J, Lindmark B, et al. The molecular basis of α1-antichymotrypsin deficiency in a heterozygote with liver and lung disease. J Hepatol 1993; 18:313-321.
    • (1993) J Hepatol , vol.18 , pp. 313-321
    • Faber, J.-P.1    Poller, W.2    Olek, K.3    Baumann, U.4    Carlson, J.5    Lindmark, B.6
  • 69
    • 0027328108 scopus 로고
    • A leucine-to-proline substitution causes a defective α1- antichymotrypsin allele associated with familial obstructive lung disease
    • Poller W, Faber J-P, Weidinger S, Tief K, Scholz S, Fischer M, et al. A leucine-to-proline substitution causes a defective α1-antichymotrypsin allele associated with familial obstructive lung disease. Genomics 1993; 17:740-743.
    • (1993) Genomics , vol.17 , pp. 740-743
    • Poller, W.1    Faber, J.-P.2    Weidinger, S.3    Tief, K.4    Scholz, S.5    Et Al., F.M.6
  • 70
    • 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, Villa P, Minano A, Vaya A, 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(10):1303-1307.
    • (2004) Circulation , vol.110 , Issue.10 , pp. 1303-1307
    • Corral, J.1    Aznar, J.2    Gonzalez-Conejero, R.3    Villa, P.4    Minano, A.5    Vaya, A.6
  • 71
    • 0031452755 scopus 로고    scopus 로고
    • Neuroserpin, a brain-associated inhibitor of tissue plasminogen activator is localized primarily in neurones
    • Hastings GA, Coleman TA, Haudenschild CC, Stefansson S, Smith EP, Barthlow R, et al. Neuroserpin, a brain-associated inhibitor of tissue plasminogen activator is localized primarily in neurones. J Biol Chem 1997; 272(52):33062-33067.
    • (1997) J Biol Chem , vol.272 , Issue.52 , pp. 33062-33067
    • Hastings, G.A.1    Coleman, T.A.2    Haudenschild, C.C.3    Stefansson, S.4    Smith, E.P.5    Barthlow, R.6
  • 74
    • 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, Gerhard L, Baumann B, et al. Association between conformational mutations in neuroserpin and onset and severity of dementia. Lancet 2002; 359:2242-2247.
    • (2002) Lancet , vol.359 , pp. 2242-2247
    • Davis, R.L.1    Shrimpton, A.E.2    Carrell, R.W.3    Lomas, D.A.4    Gerhard, L.5    Baumann, B.6
  • 76
    • 80052033433 scopus 로고    scopus 로고
    • Encephalopathy with neuroserpin inclusion bodies presenting as progressive myoclonus epilepsy and associated with a novel mutation in the proteinase inhibitor 12 gene
    • Hagen M, Murrell JR, Delisle MB, Andermann E, Andermann F, Guiot MC, et al. Encephalopathy with neuroserpin inclusion bodies presenting as progressive myoclonus epilepsy and associated with a novel mutation in the proteinase inhibitor 12 Gene. Brain Pathol 2011; 21(5):575-582.
    • (2011) Brain Pathol , vol.21 , Issue.5 , pp. 575-582
    • Hagen, M.1    Murrell, J.R.2    Delisle, M.B.3    Andermann, E.4    Andermann, F.5    Guiot, M.C.6
  • 77
    • 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; 277:17367-17373.
    • (2002) J Biol Chem , vol.277 , pp. 17367-17373
    • Belorgey, D.1    Crowther, D.C.2    Mahadeva, R.3    Lomas, D.A.4
  • 78
    • 3142582012 scopus 로고    scopus 로고
    • Mutants of neuroserpin that cause dementia accumulate as polymers within the endoplasmic reticulum
    • Miranda E, Romisch K, Lomas DA. Mutants of neuroserpin that cause dementia accumulate as polymers within the endoplasmic reticulum. J Biol Chem 2004; 279(27):28283- 28291.
    • (2004) J Biol Chem , vol.279 , Issue.27 , pp. 28283-28291
    • Miranda, E.1    Romisch, K.2    Lomas, D.A.3
  • 79
    • 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, Johansson J, Lomas DA. 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(16):3360-3367.
    • (2004) Eur J Biochem , vol.271 , Issue.16 , pp. 3360-3367
    • Belorgey, D.1    Sharp, L.K.2    Crowther, D.C.3    Onda, M.4    Johansson, J.5    Lomas, D.A.6
  • 80
    • 44349122437 scopus 로고    scopus 로고
    • The intracellular accumulation of polymeric neuroserpin explains the severity of the dementia FENIB
    • Miranda E, McLeod I, Davies MJ, Perez J, Romisch K, Crowther DC, et al. The intracellular accumulation of polymeric neuroserpin explains the severity of the dementia FENIB. Hum Mol Genet 2008; 17:1527-1539.
    • (2008) Hum Mol Genet , vol.17 , pp. 1527-1539
    • Miranda, E.1    McLeod, I.2    Davies, M.J.3    Perez, J.4    Romisch, K.5    Crowther, D.C.6
  • 81
    • 63449091253 scopus 로고    scopus 로고
    • The 2.1-A crystal structure of native neuroserpin reveals unique structural elements that contribute to conformational instability
    • Takehara S, Onda M, Zhang J, Nishiyama M, Yang X, Mikami B, et al. The 2.1-A crystal structure of native neuroserpin reveals unique structural elements that contribute to conformational instability. J Mol Biol 2009; 388(1):11-20.
    • (2009) J Mol Biol , vol.388 , Issue.1 , pp. 11-20
    • Takehara, S.1    Onda, M.2    Zhang, J.3    Nishiyama, M.4    Yang, X.5    Mikami, B.6
  • 82
    • 76749090946 scopus 로고    scopus 로고
    • PH dependent stability of neuroserpin is mediated by Histidines 119 and 138; Implications for the control of ®-sheet a and polymerization
    • Belorgey D, Hagglof P, Onda M, Lomas DA. pH dependent stability of neuroserpin is mediated by Histidines 119 and 138; implications for the control of ®-sheet A and polymerisation. Protein Sci 2010; 19(2):220-228.
    • (2010) Protein Sci , vol.19 , Issue.2 , pp. 220-228
    • Belorgey, D.1    Hagglof, P.2    Onda Lomas, M.D.A.3
  • 83
    • 0036510604 scopus 로고    scopus 로고
    • Sixmer peptide selectively anneals to a pathogenic serpin conformation and blocks polymerisation: Implications for the prevention of Z α1-antitrypsin related cirrhosis
    • Mahadeva R, Dafforn TR, Carrell RW, Lomas DA. Sixmer peptide selectively anneals to a pathogenic serpin conformation and blocks polymerisation: implications for the prevention of Z α1-antitrypsin related cirrhosis. J Biol Chem 2002; 277(9):6771-6774.
    • (2002) J Biol Chem , vol.277 , Issue.9 , pp. 6771-6774
    • Mahadeva, R.1    Dafforn, T.R.2    Carrell, R.W.3    Lomas, D.A.4
  • 84
  • 86
    • 0034969249 scopus 로고    scopus 로고
    • Prevention of polymerization of M and Z α1-antitrypsin (a1- AT) with Trimethylamine N-Oxide. Implications for the treatment of α1-AT deficiency
    • Devlin GL, Parfrey H, Tew DJ, Lomas DA, Bottomley SP. Prevention of polymerization of M and Z α1-antitrypsin (a1- AT) with Trimethylamine N-Oxide. Implications for the treatment of α1-AT deficiency. Am J Respir Cell Mol Biol 2001; 24(6):727-732.
    • (2001) Am J Respir Cell Mol Biol , vol.24 , Issue.6 , pp. 727-732
    • Devlin, G.L.1    Parfrey, H.2    Tew, D.J.3    Lomas, D.A.4    Bottomley, S.P.5
  • 87
    • 0034652248 scopus 로고    scopus 로고
    • Chemical chaperones mediate increased secretion of mutant α1-antitrypsin (α1- AT) Z: A potential pharmacologcial strategy for prevention of liver injury and emphysema
    • Burrows JAJ, Willis LK, Perlmutter DH. Chemical chaperones mediate increased secretion of mutant α1-antitrypsin (α1- AT) Z: a potential pharmacologcial strategy for prevention of liver injury and emphysema. Proc Natl Acad Sci USA 2000; 97:1796-1801.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1796-1801
    • Burrows, J.A.J.1    Willis, L.K.2    Perlmutter, D.H.3
  • 88
    • 16544381001 scopus 로고    scopus 로고
    • Lack of effect of oral 4-phenylbutyrate on serum alpha-1-antitrypsin in patients with alpha-1-antitrypsin deficiency: A preliminary study
    • Teckman JH. Lack of effect of oral 4-phenylbutyrate on serum alpha-1-antitrypsin in patients with alpha-1-antitrypsin deficiency: a preliminary study. J Pediatr Gastroenterol Nutr 2004; 39(1):34-37.
    • (2004) J Pediatr Gastroenterol Nutr , vol.39 , Issue.1 , pp. 34-37
    • Teckman, J.H.1
  • 89
    • 77954597127 scopus 로고    scopus 로고
    • An autophagy-enhancing drug promotes degradation of mutant alpha1-antitrypsin Z and reduces hepatic fibrosis
    • Hidvegi T, Ewing M, Hale P, Dippold C, Beckett C, Kemp C, et al. An autophagy-enhancing drug promotes degradation of mutant alpha1-antitrypsin Z and reduces hepatic fibrosis. Science 2010; 329:229-232.
    • (2010) Science , vol.329 , pp. 229-232
    • Hidvegi, T.1    Ewing, M.2    Hale, P.3    Dippold, C.4    Beckett, C.5    Kemp, C.6
  • 90
    • 0042858320 scopus 로고    scopus 로고
    • Targeting a surface cavity of α1-antitrypsin to prevent conformational disease
    • Parfrey H, Mahadeva R, Ravenhill NA, Zhou A, Dafforn TR, Foreman RC, et al. Targeting a surface cavity of α1-antitrypsin to prevent conformational disease. J Biol Chem 2003;278(35):33060-33066.
    • (2003) J Biol Chem , vol.278 , Issue.35 , pp. 33060-33066
    • Parfrey, H.1    Mahadeva, R.2    Ravenhill, N.A.3    Zhou, A.4    Dafforn, T.R.5    Foreman, R.C.6
  • 91
    • 35848929750 scopus 로고    scopus 로고
    • Small molecules block the polymerisation of Z α1-antitrypsin and increase the clearance of intracellular aggregates
    • Mallya M, Phillips RL, Saldanha SA, Gooptu B, Leigh Brown SC, Termine DJ, et al. Small molecules block the polymerisation of Z α1-antitrypsin and increase the clearance of intracellular aggregates. J Med Chem 2007; 50(22):5357-5363.
    • (2007) J Med Chem , vol.50 , Issue.22 , pp. 5357-5363
    • Mallya, M.1    Phillips, R.L.2    Saldanha, S.A.3    Gooptu, B.4    Leigh Brown, S.C.5    Termine, D.J.6
  • 92
    • 80054987997 scopus 로고    scopus 로고
    • Targeted gene correction of α1-antitrypsin deficiency in induced pluripotent stem cells
    • Yusa K, Rashid ST, Strick-Marchand H, Varela I, Liu PQ, Paschon DE, et al. Targeted gene correction of α1-antitrypsin deficiency in induced pluripotent stem cells. Nature 2011; 478:391-394.
    • (2011) Nature , vol.478 , pp. 391-394
    • Yusa, K.1    Rashid, S.T.2    Strick-Marchand, H.3    Varela, I.4    Liu, P.Q.5    Paschon, D.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.