메뉴 건너뛰기




Volumn 473, Issue 19, 2016, Pages 3269-3290

An antibody that prevents serpin polymerisation acts by inducing a novel allosteric behavior

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; EPITOPE; LIGAND; PEPTIDE; POLYMER; SERINE PROTEINASE INHIBITOR; ALPHA 1 ANTITRYPSIN; MONOCLONAL ANTIBODY;

EID: 85010004900     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BCJ20160159     Document Type: Article
Times cited : (14)

References (86)
  • 1
    • 85047684827 scopus 로고    scopus 로고
    • Α1-Antitrypsin polymerization and the serpinopathies: Pathobiology and prospects for therapy
    • Lomas, D.A. and Mahadeva, R. (2002) α1-Antitrypsin polymerization and the serpinopathies: pathobiology and prospects for therapy. J. Clin. Invest. 110, 1585-1590 doi:10.1172/JCI0216782.
    • (2002) J. Clin. Invest , vol.110 , pp. 1585-1590
    • Lomas, D.A.1    Mahadeva, R.2
  • 2
    • 0344076056 scopus 로고    scopus 로고
    • Metastability in the inhibitory mechanism of human α1-Antitrypsin
    • Im, H., Seo, E.J. and Yu, M.-H. (1999) Metastability in the inhibitory mechanism of human α1-Antitrypsin. J. Biol. Chem. 274, 11072-11077 doi:10.1074/jbc.274.16.11072.
    • (1999) J. Biol. Chem , vol.274 , pp. 11072-11077
    • Im, H.1    Seo, E.J.2    Yu, M.-H.3
  • 3
    • 0033608984 scopus 로고    scopus 로고
    • Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 A and full insertion of the reactive center loop into β-sheet A
    • Stratikos, E. and Gettins, P.G.W. (1999) Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 A and full insertion of the reactive center loop into β-sheet A. Proc. Natl Acad. Sci. USA 96, 4808-4813 doi:10.1073/pnas.96.9.4808.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 4808-4813
    • Stratikos, E.1    Gettins, P.G.W.2
  • 4
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington, J.A., Read, R.J. and Carrell, R.W. (2000) Structure of a serpin-protease complex shows inhibition by deformation. Nature 407, 923-926 doi:10.1038/35038119.
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 5
    • 67650713938 scopus 로고    scopus 로고
    • Conformational pathology of the serpins: Themes, variations, and therapeutic strategies
    • Gooptu, B. and Lomas, D.A. (2009) Conformational pathology of the serpins: Themes, variations, and therapeutic strategies. Annu. Rev. Biochem. 78, 147-176 doi:10.1146/annurev.biochem.78.082107.133320.
    • (2009) Annu. Rev. Biochem , vol.78 , pp. 147-176
    • Gooptu, B.1    Lomas, D.A.2
  • 6
    • 0026755363 scopus 로고
    • The mechanism of Z α1-Antitrypsin accumulation in the liver
    • Lomas, D.A., Li-Evans, D, Finch, J.T. and Carrell, R.W. (1992) The mechanism of Z α1-Antitrypsin accumulation in the liver. Nature 357, 605-607 doi:10.1038/357605a0.
    • (1992) Nature , vol.357 , pp. 605-607
    • Lomas, D.A.1    Li-Evans, D.2    Finch, J.T.3    Carrell, R.W.4
  • 7
    • 84876803937 scopus 로고    scopus 로고
    • Endoplasmic reticulum polymers impair luminal protein mobility and sensitize to cellular stress in alpha1-Antitrypsin deficiency
    • Ordóñez, A., Snapp, E.L., Tan, L., Miranda, E., Marciniak, S.J. and Lomas, D.A. (2013) Endoplasmic reticulum polymers impair luminal protein mobility and sensitize to cellular stress in alpha1-Antitrypsin deficiency. Hepatology 57, 2049-2060 doi:10.1002/hep.26173.
    • (2013) Hepatology , vol.57 , pp. 2049-2060
    • Ordóñez, A.1    Snapp, E.L.2    Tan, L.3    Miranda, E.4    Marciniak, S.J.5    Lomas, D.A.6
  • 8
    • 28244499949 scopus 로고    scopus 로고
    • Accumulation of mutant α1-Antitrypsin Z in the endoplasmic reticulum activates caspases-4 and -12, NFκB, and BAP31 but not the unfolded protein response
    • Hidvegi, T., Schmidt, B.Z., Hale, P. and Perlmutter, D.H. (2005) Accumulation of mutant α1-Antitrypsin Z in the endoplasmic reticulum activates caspases-4 and -12, NFκB, and BAP31 but not the unfolded protein response. J. Biol. Chem. 280, 39002-39015 doi:10.1074/jbc.M508652200.
    • (2005) J. Biol. Chem , vol.280 , pp. 39002-39015
    • Hidvegi, T.1    Schmidt, B.Z.2    Hale, P.3    Perlmutter, D.H.4
  • 9
    • 0025258970 scopus 로고
    • Accumulation of the insoluble PiZ variant of human alpha 1-Antitrypsin within the hepatic endoplasmic reticulum does not elevate the steady-state level of grp78/BiP
    • PMID:2122976
    • Graham, K.S., Le, A. and Sifers, R.N. (1990) Accumulation of the insoluble PiZ variant of human alpha 1-Antitrypsin within the hepatic endoplasmic reticulum does not elevate the steady-state level of grp78/BiP. J. Biol. Chem. 265, 20463-20468 PMID:2122976.
    • (1990) J. Biol. Chem , vol.265 , pp. 20463-20468
    • Graham, K.S.1    Le, A.2    Sifers, R.N.3
  • 10
    • 0029589824 scopus 로고
    • What do dysfunctional serpins tell us about molecular mobility and disease
    • Stein, P.E. and Carrell, R.W. (1995) What do dysfunctional serpins tell us about molecular mobility and disease? Nat. Struct. Biol. 2, 96-113 doi:10.1038/nsb0295-96.
    • (1995) Nat. Struct. Biol , vol.2 , pp. 96-113
    • Stein, P.E.1    Carrell, R.W.2
  • 11
    • 0034918677 scopus 로고    scopus 로고
    • Alpha-1-Antitrypsin PI phenotypes S and Z in Europe: An analysis of the published surveys
    • Blanco, I., Fernández, E. and Bustillo, E.F. (2001) Alpha-1-Antitrypsin PI phenotypes S and Z in Europe: An analysis of the published surveys. Clin. Genet. 60, 31-41 doi:10.1034/j.1399-0004.2001.600105.x.
    • (2001) Clin. Genet , vol.60 , pp. 31-41
    • Blanco, I.1    Fernández, E.2    Bustillo, E.F.3
  • 12
    • 0035976919 scopus 로고    scopus 로고
    • The proteasome participates in degradation of mutant alpha 1-Antitrypsin Z in the endoplasmic reticulum of hepatoma-derived hepatocytes
    • Teckman, J.H., Burrows, J., Hidvegi, T., Schmidt, B., Hale, P.D. and Perlmutter, D.H. (2001) The proteasome participates in degradation of mutant alpha 1-Antitrypsin Z in the endoplasmic reticulum of hepatoma-derived hepatocytes. J. Biol. Chem. 276, 44865-44872 doi:10.1074/jbc.M103703200.
    • (2001) J. Biol. Chem , vol.276 , pp. 44865-44872
    • Teckman, J.H.1    Burrows, J.2    Hidvegi, T.3    Schmidt, B.4    Hale, P.D.5    Perlmutter, D.H.6
  • 13
    • 0000461577 scopus 로고
    • Pulmonary emphysema and alpha1-Antitrypsin deficiency
    • Eriksson, S. (1964) Pulmonary emphysema and alpha1-Antitrypsin deficiency. Acta Med. Scand. 175, 197-205 doi:10.1111/j.0954-6820.1964.tb00567.x.
    • (1964) Acta Med. Scand , vol.175 , pp. 197-205
    • Eriksson, S.1
  • 14
    • 49349116007 scopus 로고    scopus 로고
    • Liver disease in alpha 1-Antitrypsin deficiency: A review
    • Fairbanks, K.D. and Tavill, A.S. (2008) Liver disease in alpha 1-Antitrypsin deficiency: A review. Am. J. Gastroenterol. 103, 2136-2142 doi:10.1111/j.1572-0241.2008.01955.x.
    • (2008) Am. J. Gastroenterol , vol.103 , pp. 2136-2142
    • Fairbanks, K.D.1    Tavill, A.S.2
  • 15
    • 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, J.A. and Lomas, D.A. (2011) 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. 5, 391-405 doi:10.2147/DDDT.S14018.
    • (2011) Drug. Des. Devel. Ther , vol.5 , pp. 391-405
    • Dickens, J.A.1    Lomas, D.A.2
  • 16
    • 0033515480 scopus 로고    scopus 로고
    • Probing the unfolding pathway of α1-Antitrypsin
    • James, E.L., Whisstock, J.C., Gore, M.G. and Bottomley, S.P. (1999) Probing the unfolding pathway of α1-Antitrypsin. J. Biol. Chem. 274, 9482-9488 doi:10.1074/jbc.274.14.9482.
    • (1999) J. Biol. Chem , vol.274 , pp. 9482-9488
    • James, E.L.1    Whisstock, J.C.2    Gore, M.G.3    Bottomley, S.P.4
  • 17
    • 0030475698 scopus 로고    scopus 로고
    • Kinetically controlled folding of the serpin plasminogen activator inhibitor 1
    • Wang, Z., Mottonen, J. and Goldsmith, E.J. (1996) Kinetically controlled folding of the serpin plasminogen activator inhibitor 1. Biochemistry 35, 16443-16448 doi:10.1021/bi961214p.
    • (1996) Biochemistry , vol.35 , pp. 16443-16448
    • Wang, Z.1    Mottonen, J.2    Goldsmith, E.J.3
  • 18
    • 0021112571 scopus 로고
    • Demonstration of a two-domain structure of antithrombin III during its denaturation in guanidinium chloride
    • PMID:6885810
    • Villanueva, G.B. and Allen, N. (1983) Demonstration of a two-domain structure of antithrombin III during its denaturation in guanidinium chloride. J. Biol. Chem. 258, 11010-11013 PMID:6885810.
    • (1983) J. Biol. Chem , vol.258 , pp. 11010-11013
    • Villanueva, G.B.1    Allen, N.2
  • 19
    • 0034665989 scopus 로고    scopus 로고
    • Conformational change and intermediates in the unfolding of alpha 1-Antichymotrypsin
    • Pearce, M.C., Rubin, H. and Bottomley, S.P. (2000) Conformational change and intermediates in the unfolding of alpha 1-Antichymotrypsin. J. Biol. Chem. 275, 28513-28518 doi:10.1074/jbc.M004310200.
    • (2000) J. Biol. Chem , vol.275 , pp. 28513-28518
    • Pearce, M.C.1    Rubin, H.2    Bottomley, S.P.3
  • 20
    • 0035834481 scopus 로고    scopus 로고
    • Probing the equilibrium denaturation of the serpin α1-Antitrypsin with single tryptophan mutants; evidence for structure in the urea unfolded state
    • Tew, D.J. and Bottomley, S.P. (2001) Probing the equilibrium denaturation of the serpin α1-Antitrypsin with single tryptophan mutants; evidence for structure in the urea unfolded state. J. Mol. Biol. 313, 1161-1169 doi:10.1006/jmbi.2001.5104.
    • (2001) J. Mol. Biol , vol.313 , pp. 1161-1169
    • Tew, D.J.1    Bottomley, S.P.2
  • 21
    • 0033515559 scopus 로고    scopus 로고
    • A kinetic mechanism for the polymerization of α1-Antitrypsin
    • Dafforn, T.R., Mahadeva, R., Elliott, P.R., Sivasothy, P. and Lomas, D.A. (1999) A kinetic mechanism for the polymerization of α1-Antitrypsin. J. Biol. Chem. 274, 9548-9555 doi:10.1074/jbc.274.14.9548.
    • (1999) J. Biol. Chem , vol.274 , pp. 9548-9555
    • Dafforn, T.R.1    Mahadeva, R.2    Elliott, P.R.3    Sivasothy, P.4    Lomas, D.A.5
  • 22
    • 84934920503 scopus 로고    scopus 로고
    • An antibody raised against a pathogenic serpin variant induces mutant-like behaviour in the wild-Type protein
    • Irving, J.A., Miranda, E., Haq, I., Perez, J., Kotov, V.R., Faull, S.V. et al. (2015) An antibody raised against a pathogenic serpin variant induces mutant-like behaviour in the wild-Type protein. Biochem. J. 468, 99-108 doi:10.1042/BJ20141569.
    • (2015) Biochem. J , vol.468 , pp. 99-108
    • Irving, J.A.1    Miranda, E.2    Haq, I.3    Perez, J.4    Kotov, V.R.5    Faull, S.V.6
  • 24
    • 77956389382 scopus 로고    scopus 로고
    • A novel monoclonal antibody to characterize pathogenic polymers in liver disease associated with α1-Antitrypsin deficiency
    • Miranda, E., Pérez, J., Ekeowa, U.I., Hadzic, N., Kalsheker, N., Gooptu, B. et al. (2010) A novel monoclonal antibody to characterize pathogenic polymers in liver disease associated with α1-Antitrypsin deficiency. Hepatology 52, 1078-1088 doi:10.1002/hep.23760.
    • (2010) Hepatology , vol.52 , pp. 1078-1088
    • Miranda, E.1    Pérez, J.2    Ekeowa, U.I.3    Hadzic, N.4    Kalsheker, N.5    Gooptu, B.6
  • 25
    • 57649219476 scopus 로고    scopus 로고
    • The structural basis of serpin polymerization studied by hydrogen/deuterium exchange and mass spectrometry
    • Tsutsui, Y., Kuri, B., Sengupta, T. and Wintrode, P.L. (2008) The structural basis of serpin polymerization studied by hydrogen/deuterium exchange and mass spectrometry. J. Biol. Chem. 283, 30804-30811 doi:10.1074/jbc.M804048200.
    • (2008) J. Biol. Chem , vol.283 , pp. 30804-30811
    • Tsutsui, Y.1    Kuri, B.2    Sengupta, T.3    Wintrode, P.L.4
  • 26
    • 84857926856 scopus 로고    scopus 로고
    • Structural dynamics associated with intermediate formation in an archetypal conformational disease
    • Nyon, M.P., Segu, L., Cabrita, L.D., Lévy, G.R., Kirkpatrick, J., Roussel, B.D. et al. (2012) Structural dynamics associated with intermediate formation in an archetypal conformational disease. Structure 20, 504-512 doi:10.1016/j.str.2012.01.012.
    • (2012) Structure , vol.20 , pp. 504-512
    • Nyon, M.P.1    Segu, L.2    Cabrita, L.D.3    Lévy, G.R.4    Kirkpatrick, J.5    Roussel, B.D.6
  • 27
    • 84858629624 scopus 로고    scopus 로고
    • Folding mechanism of the metastable serpin α1-Antitrypsin
    • Tsutsui, Y., Dela Cruz, R. and Wintrode, P.L. (2012) Folding mechanism of the metastable serpin α1-Antitrypsin. Proc. Natl Acad. Sci. USA 109, 4467-4472 doi:10.1073/pnas.1109125109.
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 4467-4472
    • Tsutsui, Y.1    Dela Cruz, R.2    Wintrode, P.L.3
  • 28
    • 0027473016 scopus 로고
    • Effect of the Z mutation on the physical and inhibitory properties of α1-Antitrypsin
    • Lomas, D.A., Evans, D.L., Stone, S.R., Chang, W.S. and Carrell, R.W. (1993) Effect of the Z mutation on the physical and inhibitory properties of α1-Antitrypsin. Biochemistry 32, 500-508 doi:10.1021/bi00053a014.
    • (1993) Biochemistry , vol.32 , pp. 500-508
    • Lomas, D.A.1    Evans, D.L.2    Stone, S.R.3    Chang, W.S.4    Carrell, R.W.5
  • 29
    • 55249111481 scopus 로고    scopus 로고
    • Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization
    • Yamasaki, M., Li, W., Johnson, D.J. and Huntington, J.A. (2008) Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization. Nature 455, 1255-1258 doi:10.1038/nature07394.
    • (2008) Nature , vol.455 , pp. 1255-1258
    • Yamasaki, M.1    Li, W.2    Johnson, D.J.3    Huntington, J.A.4
  • 30
    • 80053561166 scopus 로고    scopus 로고
    • Molecular basis of α1-Antitrypsin deficiency revealed by the structure of a domain-swapped trimer
    • Yamasaki, M., Sendall, T.J., Pearce, M.C., Whisstock, J.C. and Huntington, J.A. (2011) Molecular basis of α1-Antitrypsin deficiency revealed by the structure of a domain-swapped trimer. EMBO Rep. 12, 1011-1017 doi:10.1038/embor.2011.171.
    • (2011) EMBO Rep , vol.12 , pp. 1011-1017
    • Yamasaki, M.1    Sendall, T.J.2    Pearce, M.C.3    Whisstock, J.C.4    Huntington, J.A.5
  • 31
    • 0026532063 scopus 로고
    • Conformation of the reactive site loop of .alpha.1-proteinase inhibitor probed by limited proteolysis
    • Mast, A.E., Enghild, J.J. and Salvesen, G. (1992) Conformation of the reactive site loop of .alpha.1-proteinase inhibitor probed by limited proteolysis. Biochemistry 31, 2720-2728 doi:10.1021/bi00125a012.
    • (1992) Biochemistry , vol.31 , pp. 2720-2728
    • Mast, A.E.1    Enghild, J.J.2    Salvesen, G.3
  • 32
    • 69249104575 scopus 로고    scopus 로고
    • Endoplasmic reticulum-Associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins
    • Kroger, H., Miranda, E., MacLeod, I., Pérez, J., Crowther, D.C., Marciniak, S.J. et al. (2009) Endoplasmic reticulum-Associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins. J. Biol. Chem. 284, 22793-22802 doi:10.1074/jbc.M109.027102.
    • (2009) J. Biol. Chem , vol.284 , pp. 22793-22802
    • Kroger, H.1    Miranda, E.2    MacLeod, I.3    Pérez, J.4    Crowther, D.C.5    Marciniak, S.J.6
  • 33
    • 33845976370 scopus 로고    scopus 로고
    • Evidence for a pre-latent form of the serpin plasminogen activator inhibitor-1 with a detached beta-strand 1C
    • Dupont, D.M., Blouse, G.E., Hansen, M., Mathiasen, L., Kjelgaard, S., Jensen, J.K. et al. (2006) Evidence for a pre-latent form of the serpin plasminogen activator inhibitor-1 with a detached beta-strand 1C. J. Biol. Chem. 281, 36071-36081 doi:10.1074/jbc.M606851200.
    • (2006) J. Biol. Chem , vol.281 , pp. 36071-36081
    • Dupont, D.M.1    Blouse, G.E.2    Hansen, M.3    Mathiasen, L.4    Kjelgaard, S.5    Jensen, J.K.6
  • 34
    • 0037623683 scopus 로고    scopus 로고
    • Elucidation of the epitope of a latency-inducing antibody: Identification of a new molecular target for PAI-1 inhibition
    • PMID:12876625
    • Naessens, D., Gils, A., Compernolle, G. and Declerck, P.J. (2003) Elucidation of the epitope of a latency-inducing antibody: identification of a new molecular target for PAI-1 inhibition. Thromb. Haemost. 90, 52-58 PMID:12876625.
    • (2003) Thromb. Haemost , vol.90 , pp. 52-58
    • Naessens, D.1    Gils, A.2    Compernolle, G.3    Declerck, P.J.4
  • 35
    • 0042191343 scopus 로고    scopus 로고
    • Elucidation of a novel epitope of a substrate-inducing monoclonal antibody against the serpin PAI-1
    • Naessens, D., Gils, A., Compernolle, G. and Declerck, P.J. (2003) Elucidation of a novel epitope of a substrate-inducing monoclonal antibody against the serpin PAI-1. J. Thromb. Haemost. 1, 1028-1033 doi:10.1046/j.1538-7836.2003.00206.x.
    • (2003) J. Thromb. Haemost , vol.1 , pp. 1028-1033
    • Naessens, D.1    Gils, A.2    Compernolle, G.3    Declerck, P.J.4
  • 36
    • 0038071502 scopus 로고    scopus 로고
    • Mapping of the epitope of a monoclonal antibody protecting plasminogen activator inhibitor-1 against inactivating agents
    • Bodker, J.S., Wind, T., Jensen, J.K., Hansen, M., Pedersen, K.E. and Andreasen, P.A. (2003) Mapping of the epitope of a monoclonal antibody protecting plasminogen activator inhibitor-1 against inactivating agents. Eur. J. Biochem. 270, 1672-1679 doi:10.1046/j.1432-1033.2003.03523.x.
    • (2003) Eur. J. Biochem , vol.270 , pp. 1672-1679
    • Bodker, J.S.1    Wind, T.2    Jensen, J.K.3    Hansen, M.4    Pedersen, K.E.5    Andreasen, P.A.6
  • 37
    • 84891879068 scopus 로고    scopus 로고
    • Three monoclonal antibodies against the serpin protease nexin-1 prevent protease translocation
    • Kousted, T.M., Skjoedt, K., Petersen, S.V., Koch, C., Vitved, L., Sochalska, M. et al. (2014) Three monoclonal antibodies against the serpin protease nexin-1 prevent protease translocation. Thromb. Haemost. 111, 29-40 doi:10.1160/TH13-04-0340.
    • (2014) Thromb. Haemost , vol.111 , pp. 29-40
    • Kousted, T.M.1    Skjoedt, K.2    Petersen, S.V.3    Koch, C.4    Vitved, L.5    Sochalska, M.6
  • 38
    • 0035059744 scopus 로고    scopus 로고
    • Epitope mapping for four monoclonal antibodies against human plasminogen activator inhibitor type-1: Implications for antibody-mediated PAI-1-neutralization and vitronectin-binding
    • Wind, T., Jensen, M.A. and Andreasen, P.A. (2001) Epitope mapping for four monoclonal antibodies against human plasminogen activator inhibitor type-1: implications for antibody-mediated PAI-1-neutralization and vitronectin-binding. Eur. J. Biochem. 268, 1095-1106 doi:10.1046/j.1432-1327.2001.2680041095.x.
    • (2001) Eur. J. Biochem , vol.268 , pp. 1095-1106
    • Wind, T.1    Jensen, M.A.2    Andreasen, P.A.3
  • 39
    • 84899424699 scopus 로고    scopus 로고
    • Altered native stability is the dominant basis for susceptibility of α1-Antitrypsin mutants to polymerization
    • Irving, J.A., Haq, I., Dickens, J.A., Faull, S.V. and Lomas, D.A. (2014) Altered native stability is the dominant basis for susceptibility of α1-Antitrypsin mutants to polymerization. Biochem. J. 460, 103-119 doi:10.1042/BJ20131650.
    • (2014) Biochem. J , vol.460 , pp. 103-119
    • Irving, J.A.1    Haq, I.2    Dickens, J.A.3    Faull, S.V.4    Lomas, D.A.5
  • 40
    • 33750725161 scopus 로고    scopus 로고
    • Identification of a 4-mer peptide inhibitor that effectively blocks the polymerization of pathogenic Z α1-Antitrypsin
    • Chang, Y.-P., Mahadeva, R., Chang, W.-S., Shukla, A., Dafforn, T.R. and Chu, Y.-H. (2006) Identification of a 4-mer peptide inhibitor that effectively blocks the polymerization of pathogenic Z α1-Antitrypsin. Am. J. Resp. Cell Mol. 35, 540-548 doi:10.1165/rcmb.2005-0207OC.
    • (2006) Am. J. Resp. Cell Mol , vol.35 , pp. 540-548
    • Chang, Y.-P.1    Mahadeva, R.2    Chang, W.-S.3    Shukla, A.4    Dafforn, T.R.5    Chu, Y.-H.6
  • 41
    • 0036510604 scopus 로고    scopus 로고
    • 6-mer peptide selectively anneals to a pathogenic serpin conformation and blocks polymerization. Implications for the prevention of Z α1-Antitrypsin-related cirrhosis
    • Mahadeva, R., Dafforn, T.R., Carrell, R.W. and Lomas, D.A. (2002) 6-mer peptide selectively anneals to a pathogenic serpin conformation and blocks polymerization. Implications for the prevention of Z α1-Antitrypsin-related cirrhosis. J. Biol. Chem. 277, 6771-6774 doi:10.1074/jbc.C100722200.
    • (2002) J. Biol. Chem , vol.277 , pp. 6771-6774
    • Mahadeva, R.1    Dafforn, T.R.2    Carrell, R.W.3    Lomas, D.A.4
  • 43
    • 35848929750 scopus 로고    scopus 로고
    • Small molecules block the polymerization of Z α1-Antitrypsin and increase the clearance of intracellular aggregates
    • Mallya, M., Phillips, R.L., Saldanha, S.A., Gooptu, B., Leigh Brown, S.C., Termine, D.J. et al. (2007) Small molecules block the polymerization of Z α1-Antitrypsin and increase the clearance of intracellular aggregates. J. Med. Chem. 50, 5357-5363 doi:10.1021/jm070687z.
    • (2007) J. Med. Chem , vol.50 , 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
  • 44
    • 84933567270 scopus 로고    scopus 로고
    • A single-chain variable fragment intrabody prevents intracellular polymerization of Z α1-Antitrypsin while allowing its antiproteinase activity
    • Ordonez, A., Perez, J., Tan, L., Dickens, J.A., Motamedi-Shad, N., Irving, J.A. et al. (2015) A single-chain variable fragment intrabody prevents intracellular polymerization of Z α1-Antitrypsin while allowing its antiproteinase activity. FASEB J. 29, 2667-2678 doi:10.1096/fj.14-267351.
    • (2015) FASEB J , vol.29 , pp. 2667-2678
    • Ordonez, A.1    Perez, J.2    Tan, L.3    Dickens, J.A.4    Motamedi-Shad, N.5    Irving, J.A.6
  • 45
    • 0035920162 scopus 로고    scopus 로고
    • The serpin inhibitory mechanism is critically dependent on the length of the reactive center loop
    • Zhou, A., Carrell, R.W. and Huntington, J.A. (2001) The serpin inhibitory mechanism is critically dependent on the length of the reactive center loop. J. Biol. Chem. 276, 27541-27547 doi:10.1074/jbc.M102594200.
    • (2001) J. Biol. Chem , vol.276 , pp. 27541-27547
    • Zhou, A.1    Carrell, R.W.2    Huntington, J.A.3
  • 46
    • 0031033206 scopus 로고    scopus 로고
    • Importance of the release of strand 1C to the polymerization mechanism of inhibitory serpins
    • Chang, W.-S., Whisstock, J., Hopkins, P.C., Lesk, A.M., Carrell, R.W. and Wardell, M.R. (1997) Importance of the release of strand 1C to the polymerization mechanism of inhibitory serpins. Protein Sci. 6, 89-98 doi:10.1002/pro.5560060110.
    • (1997) Protein Sci , vol.6 , pp. 89-98
    • Chang, W.-S.1    Whisstock, J.2    Hopkins, P.C.3    Lesk, A.M.4    Carrell, R.W.5    Wardell, M.R.6
  • 47
    • 0031041451 scopus 로고    scopus 로고
    • Inhibitory mechanism of serpins Mobility of the C-Terminal region of The reactive-site loop
    • Hopkins, P.C.R., Chang, W.-S.W., Wardell, M.R. and Stone, S.R. (1997) Inhibitory mechanism of serpins MOBILITY OF THE C-TERMINAL REGION OF THE REACTIVE-SITE LOOP. J. Biol. Chem. 272, 3905-3909 doi:10.1074/jbc.272.7.3905.
    • (1997) J. Biol. Chem , vol.272 , pp. 3905-3909
    • Hopkins, P.C.R.1    Chang, W.-S.W.2    Wardell, M.R.3    Stone, S.R.4
  • 48
    • 0034721790 scopus 로고    scopus 로고
    • Pathogenic α1-Antitrypsin polymers are formed by reactive loop-β-sheet A linkage
    • Sivasothy, P., Dafforn, T.R., Gettins, P.G.W. and Lomas, D.A. (2000) Pathogenic α1-Antitrypsin polymers are formed by reactive loop-β-sheet A linkage. J. Biol. Chem. 275, 33663-33668 doi:10.1074/jbc.M004054200.
    • (2000) J. Biol. Chem , vol.275 , pp. 33663-33668
    • Sivasothy, P.1    Dafforn, T.R.2    Gettins, P.G.W.3    Lomas, D.A.4
  • 49
    • 84879633515 scopus 로고    scopus 로고
    • Reactive centre loop mutants of α-1antitrypsin reveal position-specific effects on intermediate formation along the polymerization pathway
    • Haq, I., Irving, J.A., Faull, S.V., Dickens, J.A., Ordonez, A., Belorgey, D. et al. (2013) Reactive centre loop mutants of α-1antitrypsin reveal position-specific effects on intermediate formation along the polymerization pathway. Biosci. Rep. 33, e00046 doi:10.1042/BSR20130038.
    • (2013) Biosci. Rep , vol.33 , pp. e00046
    • Haq, I.1    Irving, J.A.2    Faull, S.V.3    Dickens, J.A.4    Ordonez, A.5    Belorgey, D.6
  • 50
    • 80955167666 scopus 로고    scopus 로고
    • The serpinopathies: Studying serpin polymerization in vivo
    • Irving, J.A., Ekeowa, U.I., Belorgey, D., Haq, I., Gooptu, B., Miranda, E. et al. (2011) The serpinopathies: Studying serpin polymerization in vivo. Methods Enzymol. 501, 421-466 doi:10.1016/B978-0-12-385950-1.00018-3.
    • (2011) Methods Enzymol , vol.501 , pp. 421-466
    • Irving, J.A.1    Ekeowa, U.I.2    Belorgey, D.3    Haq, I.4    Gooptu, B.5    Miranda, E.6
  • 51
    • 84876572656 scopus 로고    scopus 로고
    • The stability of 2-state, 3-state and more-state proteins from simple spectroscopic techniques... Plus the structure of the equilibrium intermediates at the same time
    • Sancho, J. (2013) The stability of 2-state, 3-state and more-state proteins from simple spectroscopic techniques... plus the structure of the equilibrium intermediates at the same time. Arch. Biochem. Biophys. 531, 4-13 doi:10.1016/j.abb.2012.10.014.
    • (2013) Arch. Biochem. Biophys. , vol.531 , pp. 4-13
    • Sancho, J.1
  • 52
    • 78650485354 scopus 로고    scopus 로고
    • Thermodynamic analysis of ligand-induced changes in protein thermal unfolding applied to high-Throughput determination of ligand affinities with extrinsic fluorescent dyes
    • Layton, C.J. and Hellinga, H.W. (2010) Thermodynamic analysis of ligand-induced changes in protein thermal unfolding applied to high-Throughput determination of ligand affinities with extrinsic fluorescent dyes. Biochemistry 49, 10831-10841 doi:10.1021/bi101414z.
    • (2010) Biochemistry , vol.49 , pp. 10831-10841
    • Layton, C.J.1    Hellinga, H.W.2
  • 53
    • 0027182969 scopus 로고
    • Effects of mutations in the hinge region of serpins
    • Hopkins, P.C.R., Carrell, R.W. and Stone, S.R. (1993) Effects of mutations in the hinge region of serpins. Biochemistry 32, 7650-7657 doi:10.1021/bi00081a008.
    • (1993) Biochemistry , vol.32 , pp. 7650-7657
    • Hopkins, P.C.R.1    Carrell, R.W.2    Stone, S.R.3
  • 54
    • 0014517882 scopus 로고
    • Comparison of the esterase activities of trypsin, plasmin, and thrombin on guanidinobenzoate esters
    • Chase, Jr T. and Shaw, E. (1969) Comparison of the esterase activities of trypsin, plasmin, and thrombin on guanidinobenzoate esters. Titration of the enzymes. Biochemistry 8, 2212-2224 doi:10.1021/bi00833a063.
    • (1969) Titration of the Enzymes. Biochemistry , vol.8 , pp. 2212-2224
    • Chase, J.T.1    Shaw, E.2
  • 55
    • 0035980118 scopus 로고    scopus 로고
    • The pH dependence of serpin-proteinase complex dissociation reveals a mechanism of complex stabilization involving inactive and active conformational states of the proteinase which are perturbable by calcium
    • Calugaru, S.V., Swanson, R. and Olson, S.T. (2001) The pH dependence of serpin-proteinase complex dissociation reveals a mechanism of complex stabilization involving inactive and active conformational states of the proteinase which are perturbable by calcium. J. Biol. Chem. 276, 32446-32455 doi:10.1074/jbc.M104731200.
    • (2001) J. Biol. Chem , vol.276 , pp. 32446-32455
    • Calugaru, S.V.1    Swanson, R.2    Olson, S.T.3
  • 57
    • 0037117718 scopus 로고    scopus 로고
    • Evidence that serpin architecture intrinsically supports papain-like cysteine protease inhibition: Engineering α1-Antitrypsin to inhibit cathepsin proteases
    • Irving, J.A., Pike, R.N., Dai, W., Brömme, D., Worrall, D.M., Silverman, G.A. et al. (2002) Evidence that serpin architecture intrinsically supports papain-like cysteine protease inhibition: Engineering α1-Antitrypsin to inhibit cathepsin proteases. Biochemistry 41, 4998-5004 doi:10.1021/bi0159985.
    • (2002) Biochemistry , vol.41 , pp. 4998-5004
    • Irving, J.A.1    Pike, R.N.2    Dai, W.3    Brömme, D.4    Worrall, D.M.5    Silverman, G.A.6
  • 58
    • 0034090934 scopus 로고    scopus 로고
    • Partitioning of serpin-proteinase reactions between stable inhibition and substrate cleavage is regulated by the rate of serpin reactive center loop insertion into β-sheet A
    • Lawrence, D.A., Olson, S.T., Muhammad, S., Day, D.E., Kvassman, J.O., Ginsburg, D. et al. (2000) Partitioning of serpin-proteinase reactions between stable inhibition and substrate cleavage is regulated by the rate of serpin reactive center loop insertion into β-sheet A. J. Biol. Chem. 275, 5839-5844 doi:10.1074/jbc.275.8.5839.
    • (2000) J. Biol. Chem , vol.275 , pp. 5839-5844
    • Lawrence, D.A.1    Olson, S.T.2    Muhammad, S.3    Day, D.E.4    Kvassman, J.O.5    Ginsburg, D.6
  • 59
    • 0037039329 scopus 로고    scopus 로고
    • Heterogeneity in serpin-protease complexes as demonstrated by differences in the mechanism of complex breakdown
    • Plotnick, M.I., Samakur, M., Wang, Z.M., Liu, X., Rubin, H., Schechter, N.M. et al. (2002) Heterogeneity in serpin-protease complexes as demonstrated by differences in the mechanism of complex breakdown. Biochemistry 41, 334-342 doi:10.1021/bi015650+.
    • (2002) Biochemistry , vol.41 , pp. 334-342
    • Plotnick, M.I.1    Samakur, M.2    Wang, Z.M.3    Liu, X.4    Rubin, H.5    Schechter, N.M.6
  • 60
    • 84915758694 scopus 로고    scopus 로고
    • Characterising the association of latency with α1-Antitrypsin polymerisation using a novel monoclonal antibody
    • Tan, L., Perez, J., Mela, M., Miranda, E., Burling, K.A., Rouhani, F.N. et al. (2015) Characterising the association of latency with α1-Antitrypsin polymerisation using a novel monoclonal antibody. Int. J. Biochem. Cell Biol. 58, 81-91 doi:10.1016/j.biocel.2014.11.005.
    • (2015) Int. J. Biochem. Cell Biol , vol.58 , pp. 81-91
    • Tan, L.1    Perez, J.2    Mela, M.3    Miranda, E.4    Burling, K.A.5    Rouhani, F.N.6
  • 61
  • 62
    • 84963865259 scopus 로고    scopus 로고
    • Deficiency mutations of alpha-1 antitrypsin. Effects on folding, function, and polymerization
    • Haq, I., Irving, J.A., Saleh, A.D., Dron, L., Regan-Mochrie, G.L., Motamedi-Shad, N. et al. (2016) Deficiency mutations of alpha-1 antitrypsin. Effects on folding, function, and polymerization. Am. J. Resp. Cell Mol. 54, 71-80 doi:10.1165/rcmb.2015-0154OC.
    • (2016) Am. J. Resp. Cell Mol , vol.54 , pp. 71-80
    • Haq, I.1    Irving, J.A.2    Saleh, A.D.3    Dron, L.4    Regan-Mochrie, G.L.5    Motamedi-Shad, N.6
  • 63
    • 17744409446 scopus 로고    scopus 로고
    • Wild-Type α1-Antitrypsin is in the canonical inhibitory conformation
    • Elliott, P.R., Abrahams, J.-P. and Lomas, D.A. (1998) Wild-Type α1-Antitrypsin is in the canonical inhibitory conformation. J. Mol. Biol. 275, 419-425 doi:10.1006/jmbi.1997.1458.
    • (1998) J. Mol. Biol , vol.275 , pp. 419-425
    • Elliott, P.R.1    Abrahams, J.-P.2    Lomas, D.A.3
  • 64
    • 84875791872 scopus 로고    scopus 로고
    • Homogeneous antibody fragment conjugation by disulfide bridging introduces 'spinostics'
    • Schumacher, F.F., Sanchania, V.A., Tolner, B., Wright, Z.V., Ryan, C.P., Smith, M.E.B. et al. (2013) Homogeneous antibody fragment conjugation by disulfide bridging introduces 'spinostics'. Sci. Rep. 3, Article No. 1525 doi:10.1038/srep01525.
    • (2013) Sci. Rep , vol.3 , pp. 1525
    • Schumacher, F.F.1    Sanchania, V.A.2    Tolner, B.3    Wright, Z.V.4    Ryan, C.P.5    Smith, M.E.B.6
  • 65
    • 34548463041 scopus 로고    scopus 로고
    • Probing the local conformational change of α1-Antitrypsin
    • Baek, J.-H., Im, H., Kang, U.-B., Seong, K.M., Lee, C., Kim, J. et al. (2007) Probing the local conformational change of α1-Antitrypsin. Protein Sci. 16, 1842-1850 doi:10.1110/ps.072911607.
    • (2007) Protein Sci. , vol.16 , pp. 1842-1850
    • Baek, J.-H.1    Im, H.2    Kang, U.-B.3    Seong, K.M.4    Lee, C.5    Kim, J.6
  • 66
    • 79551646854 scopus 로고    scopus 로고
    • Dynamic local unfolding in the serpin α-1 antitrypsin provides a mechanism for loop insertion and polymerization
    • Krishnan, B. and Gierasch, L.M. (2011) Dynamic local unfolding in the serpin α-1 antitrypsin provides a mechanism for loop insertion and polymerization. Nat. Struct. Mol. Biol. 18, 222-226 doi:10.1038/nsmb.1976.
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 222-226
    • Krishnan, B.1    Gierasch, L.M.2
  • 67
    • 84873839238 scopus 로고    scopus 로고
    • The roles of helix I and strand 5A in the folding, function and misfolding of α1-Antitrypsin
    • Knaupp, A.S., Keleher, S., Yang, L., Dai, W., Bottomley, S.P. and Pearce, M.C. (2013) The roles of helix I and strand 5A in the folding, function and misfolding of α1-Antitrypsin. PLoS ONE 8, e54766 doi:10.1371/journal.pone.0054766.
    • (2013) PLoS ONE , vol.8 , pp. e54766
    • Knaupp, A.S.1    Keleher, S.2    Yang, L.3    Dai, W.4    Bottomley, S.P.5    Pearce, M.C.6
  • 68
    • 0025226070 scopus 로고
    • Structural transition of α1-Antitrypsin by a peptide sequentially similar to beta-strand s4A
    • Schulze, A.J., Baumann, U., Knof, S., Jaeger, E., Huber, R. and Laurell, C.-B. (1990) Structural transition of α1-Antitrypsin by a peptide sequentially similar to beta-strand s4A. Eur. J. Biochem. 194, 51-56 doi:10.1111/j.1432-1033.1990.tb19425.x.
    • (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
  • 70
    • 0026690347 scopus 로고
    • Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement
    • PMID:1618758
    • Olson, S.T., Bjork, I., Sheffer, R., Craig, P.A., Shore, J.D. and Choay, J. (1992) Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement. J. Biol. Chem. 267, 12528-12538 PMID:1618758.
    • (1992) J. Biol. Chem , vol.267 , pp. 12528-12538
    • Olson, S.T.1    Bjork, I.2    Sheffer, R.3    Craig, P.A.4    Shore, J.D.5    Choay, J.6
  • 71
    • 0026527693 scopus 로고
    • Antibody assisted protein refolding
    • Carlson, J.D. and Yarmush, M.L. (1992) Antibody assisted protein refolding. Nat. Biotechnol. 10, 86-91 doi:10.1038/nbt0192-86.
    • (1992) Nat. Biotechnol , vol.10 , pp. 86-91
    • Carlson, J.D.1    Yarmush, M.L.2
  • 72
    • 0015496403 scopus 로고
    • Alpha-1 antitrypsin in the livers of patients with emphysema
    • Lieberman, J., Mittman, C. and Gordon, H.W. (1972) Alpha-1 antitrypsin in the livers of patients with emphysema. Science 175, 63-65 doi:10.1126/science.175.4017.63.
    • (1972) Science , vol.175 , pp. 63-65
    • Lieberman, J.1    Mittman, C.2    Gordon, H.W.3
  • 73
    • 0027295822 scopus 로고
    • Alpha 1-Antitrypsin Siiyama (Ser53->Phe). Further evidence for intracellular loop-sheet polymerization
    • PMID:8340361
    • Lomas, D.A., Finch, J.T., Seyama, K., Nukiwa, T. and Carrell, R.W. (1993) Alpha 1-Antitrypsin Siiyama (Ser53->Phe). Further evidence for intracellular loop-sheet polymerization. J. Biol. Chem. 268, 15333-15335 PMID:8340361.
    • (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
  • 74
    • 0034681281 scopus 로고    scopus 로고
    • Conformational changes in serpins: I. The native and cleaved conformations of α1-Antitrypsin
    • Whisstock, J.C., Skinner, R., Carrell, R.W. and Lesk, A.M. (2000) Conformational changes in serpins: I. The native and cleaved conformations of α1-Antitrypsin. J. Mol. Biol. 296, 685-699 doi:10.1006/jmbi.1999.3520.
    • (2000) J. Mol. Biol , vol.296 , pp. 685-699
    • Whisstock, J.C.1    Skinner, R.2    Carrell, R.W.3    Lesk, A.M.4
  • 75
    • 3342889562 scopus 로고    scopus 로고
    • Different conformational changes within the F-helix occur during serpin folding, polymerization, and proteinase inhibition
    • Cabrita, L.D., Dai, W. and Bottomley, S.P. (2004) Different conformational changes within the F-helix occur during serpin folding, polymerization, and proteinase inhibition. Biochemistry 43, 9834-9839 doi:10.1021/bi0491346.
    • (2004) Biochemistry , vol.43 , pp. 9834-9839
    • Cabrita, L.D.1    Dai, W.2    Bottomley, S.P.3
  • 76
    • 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.-S.W., Dafforn, T.R., Carrell, R.W., Read, R.J. et al. (2000) 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 97, 67-72 doi:10.1073/pnas.97.1.67.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 67-72
    • Gooptu, B.1    Hazes, B.2    Chang, W.-S.W.3    Dafforn, T.R.4    Carrell, R.W.5    Read, R.J.6
  • 77
    • 84862651054 scopus 로고    scopus 로고
    • Conformational properties of the disease-causing Z variant of α1-Antitrypsin revealed by theory and experiment
    • Kass, I., Knaupp, A.S., Bottomley, S.P. and Buckle, A.M. (2012) Conformational properties of the disease-causing Z variant of α1-Antitrypsin revealed by theory and experiment. Biophys. J. 102, 2856-2865 doi:10.1016/j.bpj.2012.05.023.
    • (2012) Biophys. J , vol.102 , pp. 2856-2865
    • Kass, I.1    Knaupp, A.S.2    Bottomley, S.P.3    Buckle, A.M.4
  • 78
    • 0019866346 scopus 로고
    • Thermal denaturation of antithrombin III. Stabilization by heparin and lyotropic anions
    • PMID:7298649
    • Busby, T.F., Atha, D.H. and Ingham, K.C. (1981) Thermal denaturation of antithrombin III. stabilization by heparin and lyotropic anions. J. Biol. Chem. 256, 12140-12147 PMID:7298649.
    • (1981) J. Biol. Chem , vol.256 , pp. 12140-12147
    • Busby, T.F.1    Atha, D.H.2    Ingham, K.C.3
  • 79
    • 0028958184 scopus 로고
    • Peptide-mediated inactivation of recombinant and platelet plasminogen activator inhibitor-1 in vitro
    • Eitzman, D.T., Fay, W.P., Lawrence, D.A., Francis-Chmura, A.M., Shore, J.D., Olson, S.T. et al. (1995) Peptide-mediated inactivation of recombinant and platelet plasminogen activator inhibitor-1 in vitro. J. Clin. Invest. 95, 2416-2420 doi:10.1172/JCI117937.
    • (1995) J. Clin. Invest , vol.95 , pp. 2416-2420
    • Eitzman, D.T.1    Fay, W.P.2    Lawrence, D.A.3    Francis-Chmura, A.M.4    Shore, J.D.5    Olson, S.T.6
  • 80
    • 0029012309 scopus 로고
    • Α1-Antitrypsin Mmalton (Phe52-deleted) forms loop-sheet polymers in vivo. Evidence for the C sheet mechanism of polymerization
    • Lomas, D.A., Elliott, P.R., Sidhar, S.K., Foreman, R.C., Finch, J.T., Cox, D.W. et al. (1995) α1-Antitrypsin Mmalton (Phe52-deleted) forms loop-sheet polymers in vivo. Evidence for the C sheet mechanism of polymerization. J. Biol. Chem. 270, 16864-16870 doi:10.1074/jbc.270.28.16864.
    • (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    Finch, J.T.5    Cox, D.W.6
  • 81
    • 84908231015 scopus 로고    scopus 로고
    • The shapes of Z-α1-Antitrypsin polymers in solution support the C-Terminal domain-swap mechanism of polymerization
    • Behrens, M.A., Sendall, T.J., Pedersen, J.S., Kjeldgaard, M., Huntington, J.A. and Jensen, J.K. (2014) The shapes of Z-α1-Antitrypsin polymers in solution support the C-Terminal domain-swap mechanism of polymerization. Biophys. J. 107, 1905-1912 doi:10.1016/j.bpj.2014.08.030.
    • (2014) Biophys. J , vol.107 , pp. 1905-1912
    • Behrens, M.A.1    Sendall, T.J.2    Pedersen, J.S.3    Kjeldgaard, M.4    Huntington, J.A.5    Jensen, J.K.6
  • 82
    • 84939164437 scopus 로고    scopus 로고
    • Novel allosteric modulators of G protein-coupled receptors
    • Gentry, P.R., Sexton, P.M. and Christopoulos, A. (2015) Novel allosteric modulators of G protein-coupled receptors. J. Biol. Chem. 290, 19478-19488 doi:10.1074/jbc.R115.662759.
    • (2015) J. Biol. Chem , vol.290 , pp. 19478-19488
    • Gentry, P.R.1    Sexton, P.M.2    Christopoulos, A.3
  • 83
    • 79952261716 scopus 로고    scopus 로고
    • GSK1120212 ( JTP-74057) is an inhibitor of MEK activity and activation with favorable pharmacokinetic properties for sustained in vivo pathway inhibition
    • Gilmartin, A.G., Bleam, M.R., Groy, A., Moss, K.G., Minthorn, E.A., Kulkarni, S.G. et al. (2011) GSK1120212 ( JTP-74057) is an inhibitor of MEK activity and activation with favorable pharmacokinetic properties for sustained in vivo pathway inhibition. Clin. Cancer Res. 17, 989-1000 doi:10.1158/1078-0432.CCR-10-2200.
    • (2011) Clin. Cancer Res , vol.17 , pp. 989-1000
    • Gilmartin, A.G.1    Bleam, M.R.2    Groy, A.3    Moss, K.G.4    Minthorn, E.A.5    Kulkarni, S.G.6
  • 85
    • 0037225278 scopus 로고    scopus 로고
    • In vitro and in silico design of α1-Antitrypsin mutants with different conformational stabilities
    • Gilis, D., McLennan, H.R., Dehouck, Y., Cabrita, L.D., Rooman, M. and Bottomley, S.P. (2003) In vitro and in silico design of α1-Antitrypsin mutants with different conformational stabilities. J. Mol. Biol. 325, 581-589 doi:10.1016/S0022-2836(02)01221-4.
    • (2003) J. Mol. Biol , vol.325 , pp. 581-589
    • Gilis, D.1    McLennan, H.R.2    Dehouck, Y.3    Cabrita, L.D.4    Rooman, M.5    Bottomley, S.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.