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Volumn 44, Issue 7, 2005, Pages 2642-2649

α1-antitrypsin polymerization: A fluorescence correlation spectroscopic study

Author keywords

[No Author keywords available]

Indexed keywords

CONDENSATION; DIFFUSION; ENZYMES; FLUORESCENCE; OLIGOMERS; POLYMERIZATION; SPECTROSCOPIC ANALYSIS;

EID: 14044279288     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048662e     Document Type: Article
Times cited : (33)

References (57)
  • 1
    • 0001724344 scopus 로고
    • (Eds. Barrett, A. J., and Salvasen, G.), Elsevier, Amsterdam, The Netherlands
    • Carrell, R. W., and Boswell, D. R. (1986) Proteinase Inhibitors (Eds. Barrett, A. J., and Salvasen, G.) pp 403-420, Elsevier, Amsterdam, The Netherlands.
    • (1986) Proteinase Inhibitors , pp. 403-420
    • Carrell, R.W.1    Boswell, D.R.2
  • 2
    • 0027633477 scopus 로고
    • The role of conformational change in serpin structure and function
    • Gettins, P., Patston, P. A., and Schapira, M. (1993) The role of conformational change in serpin structure and function, BioEssays 15, 461-467.
    • (1993) BioEssays , vol.15 , pp. 461-467
    • Gettins, P.1    Patston, P.A.2    Schapira, M.3
  • 3
    • 0030062157 scopus 로고    scopus 로고
    • The biostructural pathology of the serpins: Critical function of sheet opening mechanism
    • Carrell, R. W., and Stein, P. E. (1996) The biostructural pathology of the serpins: critical function of sheet opening mechanism, Biol. Chem. Hoppe-Seyler 377, 1-17.
    • (1996) Biol. Chem. Hoppe-Seyler , vol.377 , pp. 1-17
    • Carrell, R.W.1    Stein, P.E.2
  • 4
    • 0028206262 scopus 로고
    • The serpin superfamily of proteinase inhibitors: Structure, function, and regulation
    • Potempa, J., Korzus, E., and Travis, J. (1994) The serpin superfamily of proteinase inhibitors: structure, function, and regulation, J. Biol. Chem. 269, 15957-15960.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15957-15960
    • Potempa, J.1    Korzus, E.2    Travis, J.3
  • 5
    • 85047684827 scopus 로고    scopus 로고
    • 1-Antitrypsin polymerization and the serpinopathies: Pathobiology and prospects for therapy
    • 1-Antitrypsin polymerization and the serpinopathies: pathobiology and prospects for therapy, J. Clin. Invest. 110, 1585-1590.
    • (2002) J. Clin. Invest. , vol.110 , pp. 1585-1590
    • Lomas, D.A.1    Mahadeva, R.2
  • 7
    • 0027259312 scopus 로고
    • Crystal structure of cleaved bovine antithrombin III at 3-2 Å resolution
    • Mourey, L., Samama, J. P., Delarue, M., Petitou, M., Choay, J., and Moras, D. (1993) Crystal structure of cleaved bovine antithrombin III at 3-2 Å resolution, J. Mol. Biol. 232, 223-241.
    • (1993) J. Mol. Biol. , vol.232 , pp. 223-241
    • Mourey, L.1    Samama, J.P.2    Delarue, M.3    Petitou, M.4    Choay, J.5    Moras, D.6
  • 8
    • 0028407364 scopus 로고
    • Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop
    • Wei, A., Rubin, H., Cooperman, B. S., and Christianson, D. W. (1994) Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop, Nat. Struct. Biol. 1, 251-258.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 251-258
    • Wei, A.1    Rubin, H.2    Cooperman, B.S.3    Christianson, D.W.4
  • 10
    • 0021747157 scopus 로고
    • 1-proteinase inhibitor: Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function
    • 1-proteinase inhibitor: crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function, J. Mol. Biol. 177, 531-557.
    • (1984) J. Mol. Biol. , vol.177 , pp. 531-557
    • Loebermann, H.1    Tokuoka, R.2    Deisenhofer, J.3    Huber, R.4
  • 12
    • 0028773279 scopus 로고
    • Biological implications of a 3 Å structure of dimeric antithrombin
    • Carrell, R. W., Stein, P. E., Wardell, M. R., and Fermi, G. (1994)-Biological implications of a 3 Å structure of dimeric antithrombin, Structure 2, 257-270.
    • (1994) Structure , vol.2 , pp. 257-270
    • Carrell, R.W.1    Stein, P.E.2    Wardell, M.R.3    Fermi, G.4
  • 13
    • 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.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 96-113
    • Stein, P.E.1    Carrell, R.W.2
  • 14
    • 0030448066 scopus 로고    scopus 로고
    • Alpha1-antitrypsin deficiency: A conformational disease
    • Carrell, R. W., Lomas, D. A., Sidhar, S., and Foreman, R. (1996) Alpha1-antitrypsin deficiency: A conformational disease, Chest 110, 243S-247S.
    • (1996) Chest , vol.110
    • Carrell, R.W.1    Lomas, D.A.2    Sidhar, S.3    Foreman, R.4
  • 15
  • 16
    • 0031577721 scopus 로고    scopus 로고
    • The effects of reactive centre loop length upon serpin polymerisation
    • Bottomley, S. P., and Chang, W.-S. W. (1997) The effects of reactive centre loop length upon serpin polymerisation, Biochem. Biophys. Res. Commun. 241, 264-269.
    • (1997) Biochem. Biophys. Res. Commun. , vol.241 , pp. 264-269
    • Bottomley, S.P.1    Chang, W.-S.W.2
  • 17
    • 0026532063 scopus 로고
    • Conformation of the reactive site loop of alpha1-proteinase inhibitor probed by limited proteolysis
    • Mast, A. E., Enghild, J. J., and Salvesen, G. (1992) Conformation of the reactive site loop of alpha1-proteinase inhibitor probed by limited proteolysis, Biochemistry 31, 2720-2728.
    • (1992) Biochemistry , vol.31 , pp. 2720-2728
    • Mast, A.E.1    Enghild, J.J.2    Salvesen, G.3
  • 21
    • 0017099344 scopus 로고
    • Liver disease in alpha1-antitrypsin deficiency detected by screening of 200,000 infants
    • Sveger, T. N. (1976) Liver disease in alpha1-antitrypsin deficiency detected by screening of 200,000 infants, Engl. J. Med. 294, 1316-1321.
    • (1976) Engl. J. Med. , vol.294 , pp. 1316-1321
    • Sveger, T.N.1
  • 22
    • 0022637178 scopus 로고
    • Risk of cirrhosis and primary liver cancer in alpha1-antitrypsin deficiency
    • Eriksson, S., Carlson, J., and Velez, R. N. (1986) Risk of cirrhosis and primary liver cancer in alpha1-antitrypsin deficiency, Engl. J. Med. 314, 736-739.
    • (1986) Engl. J. Med. , vol.314 , pp. 736-739
    • Eriksson, S.1    Carlson, J.2    Velez, R.N.3
  • 24
    • 0013828812 scopus 로고
    • Studies in alpha1-antitrypsin deficiency
    • Eriksson, S. (1965) Studies in alpha1-antitrypsin deficiency, Acta Med. Scand. Suppl. 432, 1-85.
    • (1965) Acta Med. Scand. Suppl. , vol.432 , pp. 1-85
    • Eriksson, S.1
  • 25
    • 0027473016 scopus 로고
    • Effect of the Z mutation on the physical and inhibitory properties of alpha1-antitrypsin
    • Lomas, D. A., Evans, D. L., Stone, S. R., Chang, W.-S. W., and Carrell, R. W. (1993) Effect of the Z mutation on the physical and inhibitory properties of alpha1-antitrypsin, Biochemistry 132, 500-508.
    • (1993) Biochemistry , vol.132 , pp. 500-508
    • Lomas, D.A.1    Evans, D.L.2    Stone, S.R.3    Chang, W.-S.W.4    Carrell, R.W.5
  • 27
    • 0027295822 scopus 로고
    • Alpha1-antitrypsin Siiyama (Ser53→Phe). Further evidence for intracellular loop-sheet polymerization
    • Lomas, D. A., Finch, J. T., Seyama, K., Nukiwa, T., and Carrell, R. W. (1993) Alpha1-antitrypsin Siiyama (Ser53→Phe). Further evidence for intracellular loop-sheet polymerization, J. Biol. Chem. 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
  • 28
    • 0032529612 scopus 로고    scopus 로고
    • 1-antitrypsin polymerization probed by fluorescence spectroscopy
    • 1-antitrypsin polymerization probed by fluorescence spectroscopy, Arch. Biochem. Biophys. 356, 296-300.
    • (1998) Arch. Biochem. Biophys. , vol.356 , pp. 296-300
    • James, E.L.1    Bottomley, S.P.2
  • 32
    • 0031871740 scopus 로고    scopus 로고
    • Detection of single amyloid beta-protein aggregates in the cerebrospinal fluid of Alzheimer's patients by fluorescence correlation spectroscopy
    • Pitschke, M., Prior, R., Haupt, M., and Riesner, D. (1998) Detection of single amyloid beta-protein aggregates in the cerebrospinal fluid of Alzheimer's patients by fluorescence correlation spectroscopy, Nature Med. 4, 832-834.
    • (1998) Nature Med. , vol.4 , pp. 832-834
    • Pitschke, M.1    Prior, R.2    Haupt, M.3    Riesner, D.4
  • 33
    • 35949038838 scopus 로고
    • Thermodynamic fluctuations in a reacting system-measurement by fluorescence correlation spectroscopy
    • Magde, D., Elson, E. L., and Webb, W. W. (1972) Thermodynamic fluctuations in a reacting system-measurement by fluorescence correlation spectroscopy, Phys. Rev. Lett. 29, 705-711.
    • (1972) Phys. Rev. Lett. , vol.29 , pp. 705-711
    • Magde, D.1    Elson, E.L.2    Webb, W.W.3
  • 34
    • 0016366591 scopus 로고
    • Fluorescence correlation spectroscopy. II. An experimental realization
    • Magde, D., Elson, E. L., and Webb, W. W. (1974) Fluorescence correlation spectroscopy. II. An experimental realization, Biopolymers 13, 29-61.
    • (1974) Biopolymers , vol.13 , pp. 29-61
    • Magde, D.1    Elson, E.L.2    Webb, W.W.3
  • 35
    • 0037064049 scopus 로고    scopus 로고
    • DNA-induced polymerization of HIV-1 integrase analyzed with fluorescence fluctuation spectroscopy
    • Vercammen, J., Maertens, G., Gerard, M., De Clercq, E., Debyser, Z., and Engelborghs, Y. (2002) DNA-induced polymerization of HIV-1 integrase analyzed with fluorescence fluctuation spectroscopy, J. Biol. Chem. 277, 38045-38052.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38045-38052
    • Vercammen, J.1    Maertens, G.2    Gerard, M.3    De Clercq, E.4    Debyser, Z.5    Engelborghs, Y.6
  • 36
    • 0345188654 scopus 로고    scopus 로고
    • The incipient stage in thrombin-induced fibrin polymerization detected by FCS at the single molecule level
    • Bark, N., Földes-Papp, Z., and Rigler, R. (1999) The incipient stage in thrombin-induced fibrin polymerization detected by FCS at the single molecule level, Biochem. Biophys. Res. Commun. 260, 35-41.
    • (1999) Biochem. Biophys. Res. Commun. , vol.260 , pp. 35-41
    • Bark, N.1    Földes-Papp, Z.2    Rigler, R.3
  • 38
    • 0000445751 scopus 로고    scopus 로고
    • Millisecond intensity fluctuations of single molecules at room temperature
    • Weston, K. D., and Buratto, S. K. (1998) Millisecond intensity fluctuations of single molecules at room temperature, J. Phys. Chem. A 102, 3635-3638.
    • (1998) J. Phys. Chem. A , vol.102 , pp. 3635-3638
    • Weston, K.D.1    Buratto, S.K.2
  • 39
    • 0037154114 scopus 로고    scopus 로고
    • Biological and chemical applications of fluorescence correlation spectroscopy: A review
    • Hess, S. T., Huang, S., Heikal, A. A., and Webb, W. W. (2002) Biological and chemical applications of fluorescence correlation spectroscopy: A review, Biochemistry 41, 697-705.
    • (2002) Biochemistry , vol.41 , pp. 697-705
    • Hess, S.T.1    Huang, S.2    Heikal, A.A.3    Webb, W.W.4
  • 40
    • 0030744965 scopus 로고    scopus 로고
    • Number analysis of fluorescence correlation spectroscopy for the cleaving process of fluorescence labeled DNA
    • Nishimura, G., Rigler, R., and Kinjo, M. (1997) Number analysis of fluorescence correlation spectroscopy for the cleaving process of fluorescence labeled DNA, Bioimaging 5, 129-133.
    • (1997) Bioimaging , vol.5 , pp. 129-133
    • Nishimura, G.1    Rigler, R.2    Kinjo, M.3
  • 41
    • 0036106455 scopus 로고    scopus 로고
    • Analysis of ligand binding by two-colour fluorescence cross-correlation spectroscopy
    • Weidemann, T., Wachsmuth, M., Tewes, M., Rippe, K., and Langowski, J. (2002) Analysis of ligand binding by two-colour fluorescence cross-correlation spectroscopy, Single Mol. 3, 49-61.
    • (2002) Single Mol. , vol.3 , pp. 49-61
    • Weidemann, T.1    Wachsmuth, M.2    Tewes, M.3    Rippe, K.4    Langowski, J.5
  • 42
    • 0037195077 scopus 로고    scopus 로고
    • Measurement of microsecond dynamic motion in the intestinal fatty acid binding protein by using fluorescence correlation spectroscopy
    • Chattopadhyay, K., Saffarian, S., Elson, E. L., and Frieden, C. (2002) Measurement of microsecond dynamic motion in the intestinal fatty acid binding protein by using fluorescence correlation spectroscopy, Proc. Natl. Acad. Sci. U.S.A. 99, 14171-14176.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 14171-14176
    • Chattopadhyay, K.1    Saffarian, S.2    Elson, E.L.3    Frieden, C.4
  • 43
    • 37049075338 scopus 로고
    • Synthesis and characterization of pure isomers of iodoacetamidotetramethylrhodamme
    • Corrie, J. E. T., and Craik, J. S. (1994) Synthesis and characterization of pure isomers of iodoacetamidotetramethylrhodamme, J. Chem. Soc., Perkin Trans. 1, 2967-2973.
    • (1994) J. Chem. Soc., Perkin Trans. , vol.1 , pp. 2967-2973
    • Corrie, J.E.T.1    Craik, J.S.2
  • 44
    • 0034924454 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy as a method for assessment of interactions between phage displaying antibodies and soluble antigen
    • Lagerkvist, A. C., Földes-Papp, Z., Persson, M. A. A., and Rigler, R. (2001) Fluorescence correlation spectroscopy as a method for assessment of interactions between phage displaying antibodies and soluble antigen, Protein Sci. 10, 1522-1528.
    • (2001) Protein Sci. , vol.10 , pp. 1522-1528
    • Lagerkvist, A.C.1    Földes-Papp, Z.2    Persson, M.A.A.3    Rigler, R.4
  • 45
    • 36749107042 scopus 로고
    • Fluorescence correlation spectroscopy as a probe of molecular dynamics
    • Aragón, S. R., and Pecora, R. (1976) Fluorescence correlation spectroscopy as a probe of molecular dynamics, J. Chem. Phys. 64, 1791-1803.
    • (1976) J. Chem. Phys. , vol.64 , pp. 1791-1803
    • Aragón, S.R.1    Pecora, R.2
  • 46
    • 0028229903 scopus 로고
    • Sorting single molecules: Application to diagnostics and evolutionary biotechnology
    • Eigen, M., and Rigler, R. (1994) Sorting single molecules: application to diagnostics and evolutionary biotechnology, Proc. Natl. Acad. Sci. U.S.A. 91, 5740-5747.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 5740-5747
    • Eigen, M.1    Rigler, R.2
  • 47
    • 0033580925 scopus 로고    scopus 로고
    • Antichymotrypsin interaction with chymotrypsin. Intermediates on the way to inhibited complex formation
    • Luo, Y., Zhou, Y., and Cooperman, B. S. (1999) Antichymotrypsin interaction with chymotrypsin. Intermediates on the way to inhibited complex formation, J. Biol. Chem. 274, 17733-17741.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17733-17741
    • Luo, Y.1    Zhou, Y.2    Cooperman, B.S.3
  • 48
    • 1542467586 scopus 로고    scopus 로고
    • The selective inhibition of serpin aggregation by the molecular chaperone, α-Crystallin, indicates a nucleation-dependent specificity
    • Devlin, G. L., Carver, J. A., and Bottomley, S. P. (2003) The selective inhibition of serpin aggregation by the molecular chaperone, α-Crystallin, indicates a nucleation-dependent specificity, J. Biol. Chem. 278, 48644-48650.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48644-48650
    • Devlin, G.L.1    Carver, J.A.2    Bottomley, S.P.3
  • 49
    • 0033554852 scopus 로고    scopus 로고
    • Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques
    • Wilkins, D. K., Grimshaw, S. B., Receveur, V., Dobson, C. M., Jones, J. A., and Smith, L. J. (1999) Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques, Biochemistry 38, 16424-16431.
    • (1999) Biochemistry , vol.38 , pp. 16424-16431
    • Wilkins, D.K.1    Grimshaw, S.B.2    Receveur, V.3    Dobson, C.M.4    Jones, J.A.5    Smith, L.J.6
  • 51
    • 0344252790 scopus 로고
    • A theory of the linear viscoelastic properties of dilute solutions of coiling polymers
    • Rouse, P. E. (1953) A theory of the linear viscoelastic properties of dilute solutions of coiling polymers, J. Chem. Phys. 21, 1272-1280.
    • (1953) J. Chem. Phys. , vol.21 , pp. 1272-1280
    • Rouse, P.E.1
  • 52
    • 36849141559 scopus 로고
    • Dynamics of polymer molecules in dilute solution: Viscoelasticity flow birefringence and dielectric loss
    • Zimm, B. H. (1956) Dynamics of polymer molecules in dilute solution: viscoelasticity flow birefringence and dielectric loss, J. Chem. Phys. 24, 269-278.
    • (1956) J. Chem. Phys. , vol.24 , pp. 269-278
    • Zimm, B.H.1
  • 53
    • 35148860246 scopus 로고
    • Reptation of a polymer chain in the presence of fixed obstacles
    • de Gennes, P. G. (1971) Reptation of a polymer chain in the presence of fixed obstacles, J. Chem. Phys. 55, 572-579.
    • (1971) J. Chem. Phys. , vol.55 , pp. 572-579
    • De Gennes, P.G.1
  • 54
    • 0942268369 scopus 로고    scopus 로고
    • Long-time tails in the dynamics of Rouse polymers
    • Tothova, J., Lisy, V., and Zatovsky, A. V. (2003) Long-time tails in the dynamics of Rouse polymers, J. Chem. Phys. 119, 13135-13137.
    • (2003) J. Chem. Phys. , vol.119 , pp. 13135-13137
    • Tothova, J.1    Lisy, V.2    Zatovsky, A.V.3
  • 55
    • 0000660577 scopus 로고    scopus 로고
    • Chain dynamics in steady shear flow
    • Dua, A., and Cherayil, B. J. (2000) Chain dynamics in steady shear flow, J. Chem. Phys. 112, 8707-8714.
    • (2000) J. Chem. Phys. , vol.112 , pp. 8707-8714
    • Dua, A.1    Cherayil, B.J.2
  • 56
    • 0142227240 scopus 로고    scopus 로고
    • Nucleation-elongation: A mechanism for cooperative supramolecular polymerization
    • Zhao, D., and Moore, J. S. (2003) Nucleation-elongation: a mechanism for cooperative supramolecular polymerization, Org. Biomol. Chem. 1, 3471-3491.
    • (2003) Org. Biomol. Chem. , vol.1 , pp. 3471-3491
    • Zhao, D.1    Moore, J.S.2


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