메뉴 건너뛰기




Volumn 501, Issue , 2011, Pages 421-466

The serpinopathies: Studying serpin polymerization in vivo

Author keywords

Animal models; Antitrypsin; Biochemistry; Cell biology; Cirrhosis; FENIB; Monoclonal antibodies; Neuroserpin; Serpin polymerization; Stem cell technology

Indexed keywords

ALPHA 1 ANTITRYPSIN; MONOCLONAL ANTIBODY; MUTANT PROTEIN; NEUROSERPIN; SERINE PROTEINASE INHIBITOR;

EID: 80955167666     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/B978-0-12-385950-1.00018-3     Document Type: Chapter
Times cited : (31)

References (95)
  • 1
    • 80051635385 scopus 로고    scopus 로고
    • Oxidation of Z alpha-1-antitrypsin by cigarette smoke induces polymerization: A novel mechanism of early-onset emphysema
    • S. Alam, Z. Li, S. Janciauskiene, and R. Mahadeva Oxidation of Z alpha-1-antitrypsin by cigarette smoke induces polymerization: A novel mechanism of early-onset emphysema Am. J. Respir. Cell Mol. Biol. 45 2011 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
  • 3
    • 0020018227 scopus 로고
    • Three-dimensional structure determination by electron microscopy of two-dimensional crystals
    • L.A. Amos, R. Henderson, and P.N. Unwin Three-dimensional structure determination by electron microscopy of two-dimensional crystals Prog. Biophys. Mol. Biol. 39 1982 183 231
    • (1982) Prog. Biophys. Mol. Biol. , vol.39 , pp. 183-231
    • Amos, L.A.1    Henderson, R.2    Unwin, P.N.3
  • 4
    • 11244346111 scopus 로고    scopus 로고
    • Quantitative isolation of 1AT mutant Z protein polymers from human and mouse livers and the effect of heat
    • DOI 10.1002/hep.20508
    • J.K. An, K. Blomenkamp, D. Lindblad, and J.H. Teckman Quantitative isolation of alpha-l-antitrypsin mutant Z protein polymers from human and mouse livers and the effect of heat Hepatology 41 2005 160 167 (Pubitemid 40066394)
    • (2005) Hepatology , vol.41 , Issue.1 , pp. 160-167
    • An, J.-K.1    Blomenkamp, K.2    Lindblad, D.3    Teckman, J.H.4
  • 6
    • 0023886316 scopus 로고
    • 1 -Proteinase inhibitor is a neutrophil chemoattractant after proteolytic inactivation by macrophage elastase
    • 1 - proteinase inhibitor is a neutrophil chemoattractant after proteolytic inactivation by macrophage elastase J. Biol. Chem. 263 1988 4481 4484 (Pubitemid 18096633)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.9 , pp. 4481-4484
    • Banda, M.J.1    Rice, A.G.2    Griffin, G.L.3    Senior, R.M.4
  • 7
    • 0037053323 scopus 로고    scopus 로고
    • Mutant neuroserpin (S49P) that causes familial encephalopathy with neuroserpin inclusion bodies is a poor proteinase inhibitor and readily forms polymers in vitro
    • DOI 10.1074/jbc.M200680200
    • D. Belorgey, D.C. Crowther, R. Mahadeva, and D.A. Lomas Mutant neuroserpin (Ser49Pro) that causes the familial dementia FENIB is a poor proteinase inhibitor and readily forms polymers in vitro J. Biol. Chem. 277 2002 17367 17373 (Pubitemid 34967773)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.19 , pp. 17367-17373
    • Belorgey, D.1    Crowther, D.C.2    Mahadeva, R.3    Lomas, D.A.4
  • 11
    • 0030841343 scopus 로고    scopus 로고
    • Conformational disease
    • DOI 10.1016/S0140-6736(97)02073-4
    • R.W. Carrell, and D.A. Lomas Conformational disease Lancet 350 1997 134 138 (Pubitemid 27313650)
    • (1997) Lancet , vol.350 , Issue.9071 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 16
    • 0347753712 scopus 로고    scopus 로고
    • Physical characterization of serpins conformations
    • T. Dafforn, R.N. Pike, and S.P. Bottomley Physical characterization of serpins conformations Methods 32 2004 150 158
    • (2004) Methods , vol.32 , pp. 150-158
    • Dafforn, T.1    Pike, R.N.2    Bottomley, S.P.3
  • 17
    • 67650526104 scopus 로고    scopus 로고
    • Neuroserpin polymers activate NF-kappaB by a calcium signalling pathway that is independent of the unfolded protein response
    • M.J. Davies, E. Miranda, B.D. Roussel, R.J. Kaufman, S.J. Marciniak, and D.A. Lomas Neuroserpin polymers activate NF-kappaB by a calcium signalling pathway that is independent of the unfolded protein response J. Biol. Chem. 284 2009 18202 18209
    • (2009) J. Biol. Chem. , vol.284 , pp. 18202-18209
    • Davies, M.J.1    Miranda, E.2    Roussel, B.D.3    Kaufman, R.J.4    Marciniak, S.J.5    Lomas, D.A.6
  • 20
    • 0000668797 scopus 로고
    • Reconstruction of three-dimensional structures from electron micrographs
    • D.J. DeRosier, and A. Klug Reconstruction of three-dimensional structures from electron micrographs Nature 217 1968 130 134
    • (1968) Nature , vol.217 , pp. 130-134
    • Derosier, D.J.1    Klug, A.2
  • 25
    • 0018885287 scopus 로고
    • A 48 well microchemotaxis assembly for rapid and accurate measurement of leukocyte migration
    • W. Falk, R.H. Goodwin Jr., and E.J. Leonard A 48 well microchemotaxis assembly for rapid and accurate measurement of leukocyte migration J. Immunol. Methods 33 1980 239 247
    • (1980) J. Immunol. Methods , vol.33 , pp. 239-247
    • Falk, W.1    Goodwin, Jr.R.H.2    Leonard, E.J.3
  • 27
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • DOI 10.1006/jsbi.1996.0030
    • J. Frank, M. Radermacher, P. Penczek, J. Zhu, Y. Li, M. Ladjadj, and A. Leith SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields J. Struct. Biol. 116 1996 190 199 (Pubitemid 26093143)
    • (1996) Journal of Structural Biology , vol.116 , Issue.1 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 28
    • 1842852975 scopus 로고    scopus 로고
    • Tools for anti-inflammatory drug design: In vitro models of leukocyte migration
    • E.K. Frow, J. Reckless, and D.J. Grainger Tools for anti-inflammatory drug design: In vitro models of leukocyte migration Med. Res. Rev. 24 2004 276 298
    • (2004) Med. Res. Rev. , vol.24 , pp. 276-298
    • Frow, E.K.1    Reckless, J.2    Grainger, D.J.3
  • 29
    • 0022974631 scopus 로고
    • Subcellular location and properties of bactericidal factors from human neutrophils
    • DOI 10.1084/jem.164.5.1407
    • J.E. Gabay, J.M. Heiple, Z.N. Cohn, and C.F. Nathan Subcellular localisation and properties of bactericidal factors from human neutrophils J. Exp. Med. 164 1986 1407 1421 (Pubitemid 17184178)
    • (1986) Journal of Experimental Medicine , vol.164 , Issue.5 , pp. 1407-1421
    • Gabay, J.E.1    Heiple, J.M.2    Cohn, Z.A.3    Nathan, C.F.4
  • 31
    • 67650713938 scopus 로고    scopus 로고
    • Conformational pathology of the serpins - Themes, variations and therapeutic strategies
    • B. Gooptu, and D.A. Lomas Conformational pathology of the serpins - Themes, variations and therapeutic strategies Annu. Rev. Biochem. 78 2009 147 176
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 147-176
    • Gooptu, B.1    Lomas, D.A.2
  • 32
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • H.P. Harding, I. Novoa, Y. Zhang, H. Zeng, R. Wek, M. Schapira, and D. Ron Regulated translation initiation controls stress-induced gene expression in mammalian cells Mol. Cell 6 2000 1099 1108
    • (2000) Mol. Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5    Schapira, M.6    Ron, D.7
  • 33
    • 0021908138 scopus 로고
    • Modulation of multiple neutrophil functions by preparative methods or trace concentrations of bacterial lipopolysaccharide
    • C. Haslett, L.A. Guthrie, M.M. Kopaniak, R.B. Johnston Jr., and P.M. Henson Modulation of multiple neutrophil functions by preparative methods or trace concentrations of bacterial lipopolysaccharide Am. J. Pathol. 119 1985 101 110 (Pubitemid 15088729)
    • (1985) American Journal of Pathology , vol.119 , Issue.1 , pp. 101-110
    • Haslett, C.1    Guthrie, L.A.2    Kopaniak, M.M.3
  • 34
    • 0030823772 scopus 로고    scopus 로고
    • Requirement for macrophage elastase for cigarette smoke-induced emphysema in mice
    • DOI 10.1126/science.277.5334.2002
    • R.D. Hautamaki, D.K. Kobayashi, R.M. Senior, and S. Shapiro Requirement for macrophage elastase for cigarette smoke-induced emphysema in mice Science 277 1997 2002 2004 (Pubitemid 27449144)
    • (1997) Science , vol.277 , Issue.5334 , pp. 2002-2004
    • Hautamaki, R.D.1    Kobayashi, D.K.2    Senior, R.M.3    Shapiro, S.D.4
  • 35
    • 28244499949 scopus 로고    scopus 로고
    • 1 -antitrypsin Z in the endoplasmic reticulum activities caspases-4 and -12, NFB, and BAP31 but not the unfolded protein response
    • DOI 10.1074/jbc.M508652200
    • 1 -antitrypsin Z in the endoplasmic reticulum activates caspases-4 and -12, NFkappaB, and BAP31 but not the unfolded protein response J. Biol. Chem. 280 2005 39002 39015 (Pubitemid 41713850)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.47 , pp. 39002-39015
    • Hidvegi, T.1    Schmidt, B.Z.2    Hale, P.3    Perlmutter, D.H.4
  • 37
    • 0037135563 scopus 로고    scopus 로고
    • Detection of circulating and endothelial cell polymers of Z and wild type 1-antitrypsin by a monoclonal antibody
    • DOI 10.1074/jbc.M203832200
    • S. Janciauskiene, R. Dominaitiene, N.H. Sternby, E. Piitulainen, and S. Eriksson Detection of circulating and endothelial cell polymers of Z and wildtype alpha-1-antitrypsin by a monoclonal antibody J. Biol. Chem. 277 2002 26540 26546 (Pubitemid 34967151)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.29 , pp. 26540-26546
    • Janciauskiene, S.1    Dominaitiene, R.2    Sternby, N.H.3    Piitulainen, E.4    Eriksson, S.5
  • 41
    • 0033773935 scopus 로고    scopus 로고
    • Conformational disease
    • R.R. Kopito, and D. Ron Conformational disease Nat. Cell Biol. 2 2000 207 209
    • (2000) Nat. Cell Biol. , vol.2 , pp. 207-209
    • Kopito, R.R.1    Ron, D.2
  • 42
    • 69249104575 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins
    • H. Kröger, E. Miranda, I. MacLeod, J. Pérez, D.C. Crowther, S.J. Marciniak, and D.A. Lomas Endoplasmic reticulum-associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins J. Biol. Chem. 284 2009 22793 22802
    • (2009) J. Biol. Chem. , vol.284 , pp. 22793-22802
    • Kröger, H.1    Miranda, E.2    MacLeod, I.3    Pérez, J.4    Crowther, D.C.5    Marciniak, S.J.6    Lomas, D.A.7
  • 43
    • 0346493022 scopus 로고    scopus 로고
    • Production, characterization, and use of serpin antibodies
    • DOI 10.1016/S1046-2023(03)00205-6
    • J.A. Kummer, M.C. Strik, B.A. Bladergroen, and C.E. Hack Production, characterization, and use of serpin antibodies Methods 32 2004 141 149 (Pubitemid 38091621)
    • (2004) Methods , vol.32 , Issue.2 , pp. 141-149
    • Kummer, J.A.1    Strik, M.C.M.2    Bladergroen, B.A.3    Hack, C.E.4
  • 44
    • 0025614486 scopus 로고
    • 1 -antichymotrypsin- cathepsin G complexes: Evidence for the involvement of interleukin-6
    • 1 -antichymotrypsin-cathepsin G complexes. Evidence for the involvement of interleukin-6 J. Biol. Chem. 265 1990 21023 21026 (Pubitemid 120014115)
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.34 , pp. 21023-21026
    • Kurdowska, A.1    Travis, J.2
  • 45
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 47
    • 0026570248 scopus 로고
    • 1 -antitrypsin variant are degraded within the endoplasmic reticulum by a mechanism sensitive to inhibitors of protein synthesis
    • 1 -antitrypsin variant are degraded within the endoplasmic reticulum by a mechanism sensitive to inhibitors of protein synthesis J. Biol. Chem. 267 1992 1072 1080
    • (1992) J. Biol. Chem. , vol.267 , pp. 1072-1080
    • Le, A.1    Ferrell, G.A.2    Dishon, D.S.3    Quyen-Quyen, A.L.4    Sifers, R.N.5
  • 48
    • 34548230927 scopus 로고    scopus 로고
    • Getting to the site of inflammation: The leukocyte adhesion cascade updated
    • DOI 10.1038/nri2156, PII NRI2156
    • K. Ley, C. Laudanna, M.I. Cybulsky, and S. Nourshargh Getting to the site of inflammation: The leukocyte adhesion cascade updated Nat. Rev. Immunol. 7 2007 678 689 (Pubitemid 47327397)
    • (2007) Nature Reviews Immunology , vol.7 , Issue.9 , pp. 678-689
    • Ley, K.1    Laudanna, C.2    Cybulsky, M.I.3    Nourshargh, S.4
  • 50
    • 36348957434 scopus 로고    scopus 로고
    • Alpha-1-antitrypsin mutant Z protein content in individual hepatocytes correlates with cell death in a mouse model
    • DOI 10.1002/hep.21822
    • D. Lindblad, K. Blomenkamp, and J. Teckman Alpha-1-antitrypsin mutant Z protein content in individual hepatocytes correlates with cell death in a mouse model Hepatology 46 2007 1228 1235 (Pubitemid 350144787)
    • (2007) Hepatology , vol.46 , Issue.4 , pp. 1228-1235
    • Lindblad, D.1    Blomenkamp, K.2    Teckman, J.3
  • 51
    • 0030898233 scopus 로고    scopus 로고
    • 1 - antitrypsin involves release from calnexin and post-translational trimming of asparagine- linked oligosaccharides
    • DOI 10.1074/jbc.272.12.7946
    • 1 -antitrypsin involves release from calnexin and post-translational trimming of asparagine-linked oligosaccharides J. Biol. Chem. 272 1997 7946 7951 (Pubitemid 27137357)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.12 , pp. 7946-7951
    • Liu, Y.1    Choudhury, P.2    Cabral, C.M.3    Sifers, R.N.4
  • 52
    • 85047684827 scopus 로고    scopus 로고
    • 1 -antitrypsin polymerization and the serpinopathies: Pathobiology and prospects for therapy
    • DOI 10.1172/JCI200216782
    • D.A. Lomas, and R. Mahadeva Alpha-1-antitrypsin polymerisation and the serpinopathies: Pathobiology and prospects for therapy J. Clin. Invest. 110 2002 1585 1590 (Pubitemid 35424233)
    • (2002) Journal of Clinical Investigation , vol.110 , Issue.11 , pp. 1585-1590
    • Lomas, D.A.1    Mahadeva, R.2
  • 56
    • 0029012309 scopus 로고
    • Alpha1-antitrypsin Mmalton (52Phe deleted) forms loop-sheet polymers in vivo: Evidence for the C sheet mechanism of polymerisation
    • D.A. Lomas, P.R. Elliott, S.K. Sidhar, R.C. Foreman, J.T. Finch, D.W. Cox, J.C. Whisstock, and R.W. Carrell Alpha1-antitrypsin Mmalton (52Phe deleted) forms loop-sheet polymers in vivo: Evidence for the C sheet mechanism of polymerisation J. Biol. Chem. 270 1995 16864 16870
    • (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    Whisstock, J.C.7    Carrell, R.W.8
  • 57
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • DOI 10.1006/jsbi.1999.4174
    • S.J. Ludtke, P.R. Baldwin, and W. Chiu EMAN: Semiautomated software for high-resolution single-particle reconstructions J. Struct. Biol. 128 1999 82 97 (Pubitemid 30013436)
    • (1999) Journal of Structural Biology , vol.128 , Issue.1 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 59
    • 33749492425 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress signaling in disease
    • DOI 10.1152/physrev.00015.2006
    • S.J. Marciniak, and D. Ron Endoplasmic reticulum stress signaling in disease Physiol. Rev. 86 2006 1133 1149 (Pubitemid 44521649)
    • (2006) Physiological Reviews , vol.86 , Issue.4 , pp. 1133-1149
    • Marciniak, S.J.1    Ron, D.2
  • 62
    • 34547921190 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid inhibits apoptosis induced by Z alpha-1 antitrypsin via inhibition of bad
    • DOI 10.1002/hep.21689
    • S.D. Miller, C.M. Greene, C. McLean, M.W. Lawless, C.C. Taggart, S.J. O'Neill, and N.G. McElvaney Tauroursodeoxycholic acid inhibits apoptosis induced by Z alpha-1 antitrypsin via inhibition of Bad Hepatology 46 2007 496 503 (Pubitemid 47344785)
    • (2007) Hepatology , vol.46 , Issue.2 , pp. 496-503
    • Miller, S.D.W.1    Greene, C.M.2    McLean, C.3    Lawless, M.W.4    Taggart, C.C.5    O'Neill, S.J.6    McElvaney, N.G.7
  • 63
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • DOI 10.1016/S1047-8477(03)00069-8
    • J.A. Mindell, and N. Grigorieff Accurate determination of local defocus and specimen tilt in electron microscopy J. Struct. Biol. 142 2003 334 347 (Pubitemid 36638267)
    • (2003) Journal of Structural Biology , vol.142 , Issue.3 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 64
    • 3142582012 scopus 로고    scopus 로고
    • Mutants of neuroserpin that cause dementia accumulate as polymers within the endoplasmic reticulum
    • DOI 10.1074/jbc.M313166200
    • E. Miranda, K. Römisch, and D.A. Lomas Mutants of neuroserpin that cause dementia accumulate as polymers within the endoplasmic reticulum J. Biol. Chem. 279 2004 28283 28291 (Pubitemid 38900106)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.27 , pp. 28283-28291
    • Miranda, E.1    Romisch, K.2    Lomas, D.A.3
  • 65
    • 44349122437 scopus 로고    scopus 로고
    • The intracellular accumulation of polymeric neuroserpin explains the severity of the dementia FENIB
    • DOI 10.1093/hmg/ddn041
    • E. Miranda, I. McLeod, M.J. Davies, J. Pérez, K. Römisch, D.C. Crowther, and D.A. Lomas The intracellular accumulation of polymeric neuroserpin explains the severity of the dementia FENIB Hum. Mol. Genet. 17 2008 1527 1539 (Pubitemid 351737158)
    • (2008) Human Molecular Genetics , vol.17 , Issue.11 , pp. 1527-1539
    • Miranda, E.1    Macleod, I.2    Davies, M.J.3    Perez, J.4    Romisch, K.5    Crowther, D.C.6    Lomas, D.A.7
  • 68
    • 70350012444 scopus 로고    scopus 로고
    • Polymorphonuclear neutrophils and T lymphocytes: Strange bedfellows or brothers in arms?
    • I. Müller, M. Munder, P. Kropf, and G.M. Hänsch Polymorphonuclear neutrophils and T lymphocytes: Strange bedfellows or brothers in arms? Trends Immunol. 30 2009 522 530
    • (2009) Trends Immunol. , vol.30 , pp. 522-530
    • Müller, I.1    Munder, M.2    Kropf, P.3    Hänsch, G.M.4
  • 70
    • 0035947778 scopus 로고    scopus 로고
    • Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha
    • I. Novoa, H. Zeng, H.P. Harding, and D. Ron Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha J. Cell Biol. 153 2001 1011 1022
    • (2001) J. Cell Biol. , vol.153 , pp. 1011-1022
    • Novoa, I.1    Zeng, H.2    Harding, H.P.3    Ron, D.4
  • 71
    • 17144431759 scopus 로고    scopus 로고
    • Latent S49P neuroserpin forms polymers in the dementia familial encephalopathy with neuroserpin inclusion bodies
    • DOI 10.1074/jbc.M413282200
    • M. Onda, D. Belorgey, L.K. Sharp, and D.A. Lomas Latent S49P neuroserpin spontaneously forms polymers: Identification of a novel pathway of polymerization and implications for the dementia FENIB J. Biol. Chem. 280 2005 13735 13741 (Pubitemid 40517269)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.14 , pp. 13735-13741
    • Onda, M.1    Belorgey, D.2    Sharp, L.K.3    Lomas, D.A.4
  • 72
    • 0030948848 scopus 로고    scopus 로고
    • Cytokines regulate membrane-bound leukocyte elastase on neutrophils: A novel mechanism for effector activity
    • C.A. Owen, M.A. Campbell, S.S. Boukedes, and E.J. Campbell Cytokines regulate membrane-bound leukocyte elastase on neutrophils: A novel mechanism for effector activity Am. J. Physiol. 272 3 Pt. 1 1997 L385 L393
    • (1997) Am. J. Physiol. , vol.272 , Issue.3 PART. 1
    • Owen, C.A.1    Campbell, M.A.2    Boukedes, S.S.3    Campbell, E.J.4
  • 73
    • 0029001576 scopus 로고
    • A novel signal transduction pathway from the endoplasmic reticulum to the nucleus is mediated by transcription factor NF-kappa B
    • H.L. Pahl, and P.A. Baeuerle A novel signal transduction pathway from the endoplasmic reticulum to the nucleus is mediated by transcription factor NF-kappa B EMBO J. 14 1995 2580 2588
    • (1995) EMBO J. , vol.14 , pp. 2580-2588
    • Pahl, H.L.1    Baeuerle, P.A.2
  • 76
    • 0033369168 scopus 로고    scopus 로고
    • Lung glutathione and oxidative stress: Implications in cigarette smoke-induced airway disease
    • I. Rahman, and W. MacNee Lung glutathione and oxidative stress: Implications in cigarette smoke-induced airway disease Am. J. Physiol. 277 6 Pt 1 1999 L1067 L1088
    • (1999) Am. J. Physiol. , vol.277 , Issue.6 PART. 1
    • Rahman, I.1    MacNee, W.2
  • 78
    • 0037375602 scopus 로고    scopus 로고
    • Particle finding in electron micrographs using a fast local correlation algorithm
    • DOI 10.1016/S0304-3991(02)00333-9, PII S0304399102003339
    • A.M. Roseman Particle finding in electron micrographs using a fast local correlation algorithm Ultramicroscopy 94 2003 225 236 (Pubitemid 36057119)
    • (2003) Ultramicroscopy , vol.94 , Issue.3-4 , pp. 225-236
    • Roseman, A.M.1
  • 80
    • 0005425213 scopus 로고
    • The development of the electron microscope and of electron microscopy
    • E. Ruska The development of the electron microscope and of electron microscopy Rev. Mod. Phys. 59 1987 627 638
    • (1987) Rev. Mod. Phys. , vol.59 , pp. 627-638
    • Ruska, E.1
  • 81
    • 0032815040 scopus 로고    scopus 로고
    • Ximdisp - A visualization tool to aid structure determination from electron microscope images
    • DOI 10.1006/jsbi.1998.4073
    • J.M. Smith XIMDISP - A visualization tool to aid structure determination from electron microscope images J. Struct. Biol. 125 1999 223 228 (Pubitemid 29402607)
    • (1999) Journal of Structural Biology , vol.125 , Issue.2-3 , pp. 223-228
    • Smith, J.M.1
  • 82
    • 0017099344 scopus 로고
    • 1 -antitrypsin deficiency detected by screening of 200,000 infants
    • 1 -antitrypsin deficiency detected by screening of 200,000 infants N. Engl. J. Med. 294 1976 1316 1321
    • (1976) N. Engl. J. Med. , vol.294 , pp. 1316-1321
    • Sveger, T.1
  • 83
    • 39149086020 scopus 로고    scopus 로고
    • Induction of pluripotent stem cells from fibroblast cultures
    • K. Takahashi, K. Okita, M. Nakagawa, and S. Yamanaka Induction of pluripotent stem cells from fibroblast cultures Nat. Protoc. 2 2007 3081 3089
    • (2007) Nat. Protoc. , vol.2 , pp. 3081-3089
    • Takahashi, K.1    Okita, K.2    Nakagawa, M.3    Yamanaka, S.4
  • 85
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • DOI 10.1016/j.jsb.2006.05.009, PII S1047847706001894, Software Tools for Macromolecular Microscopy
    • G. Tang, L. Peng, P.R. Baldwin, D.S. Mann, W. Jiang, I. Rees, and S.J. Ludtke EMAN2: An extensible image processing suite for electron microscopy J. Struct. Biol. 147 2007 38 46 (Pubitemid 44880785)
    • (2007) Journal of Structural Biology , vol.157 , Issue.1 , pp. 38-46
    • Tang, G.1    Peng, L.2    Baldwin, P.R.3    Mann, D.S.4    Jiang, W.5    Rees, I.6    Ludtke, S.J.7
  • 89
    • 0036155403 scopus 로고    scopus 로고
    • Evaluation of oxidized alpha-1-antitrypsin in blood as an oxidative stress marker using anti-oxidative 1-AT monoclonal antibody
    • DOI 10.1016/S0009-8981(01)00765-3, PII S0009898101007653
    • M. Ueda, S. Mashiba, and K. Uchida Evaluation of oxidized alpha-1-antitrypsin in blood as an oxidative stress marker using anti-oxidative alpha1-AT monoclonal antibody Clin. Chim. Acta 317 1-2 2002 125 131 (Pubitemid 34114027)
    • (2002) Clinica Chimica Acta , vol.317 , Issue.1-2 , pp. 125-131
    • Ueda, M.1    Mashiba, S.2    Uchida, K.3
  • 90
    • 57549095977 scopus 로고    scopus 로고
    • Differentiation of human embryonic stem cells in adherent and in chemically defined culture conditions
    • Chapter 1: Unit 1D.4.1-1D.4.7
    • L. Vallier, and R. Pedersen Differentiation of human embryonic stem cells in adherent and in chemically defined culture conditions Curr. Protoc. Stem Cell Biol. 2008 Chapter 1: p. Unit 1D.4.1-1D.4.7
    • (2008) Curr. Protoc. Stem Cell Biol.
    • Vallier, L.1    Pedersen, R.2
  • 95
    • 55249111481 scopus 로고    scopus 로고
    • Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization
    • M. Yamasaki, W. Li, D.J. Johnson, and J.A. Huntington Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization Nature 455 2008 1255 1258
    • (2008) Nature , vol.455 , pp. 1255-1258
    • Yamasaki, M.1    Li, W.2    Johnson, D.J.3    Huntington, J.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.