메뉴 건너뛰기




Volumn 6, Issue , 2016, Pages

IgE-tailpiece associates with α-1-antitrypsin (A1AT) to protect IgE from proteolysis without compromising its ability to interact with FcεRI

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1 ANTITRYPSIN; IMMUNOGLOBULIN E; IMMUNOGLOBULIN E RECEPTOR; ISOPROTEIN;

EID: 84957580551     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep20509     Document Type: Article
Times cited : (4)

References (77)
  • 1
    • 40049101678 scopus 로고    scopus 로고
    • IgE in allergy and asthma today
    • Gould, H. J. & Sutton, B. J. IgE in allergy and asthma today. Nat. Rev. Immunol. 8, 205-217 (2008).
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 205-217
    • Gould, H.J.1    Sutton, B.J.2
  • 2
    • 84860668874 scopus 로고    scopus 로고
    • IgE and mast cells in allergic disease
    • Galli, S. J. & Tsai, M. IgE and mast cells in allergic disease. Nature Medicine 18, 693-704 (2012).
    • (2012) Nature Medicine , vol.18 , pp. 693-704
    • Galli, S.J.1    Tsai, M.2
  • 3
    • 0032970154 scopus 로고    scopus 로고
    • The high-affinity IgE receptor (Fc epsilon RI): from physiology to pathology
    • Kinet, J. P. The high-affinity IgE receptor (Fc epsilon RI): from physiology to pathology. Annu. Rev. Immunol. 17, 931-972 (1999).
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 931-972
    • Kinet, J.P.1
  • 4
    • 2342510223 scopus 로고    scopus 로고
    • Fcaε RI engagement of Langerhans cell-like dendritic cells and inflammatory dendritic epidermal cell-like dendritic cells induces chemotactic signals and different T-cell phenotypes in vitro
    • Novak, N. et al. Fcaε RI engagement of Langerhans cell-like dendritic cells and inflammatory dendritic epidermal cell-like dendritic cells induces chemotactic signals and different T-cell phenotypes in vitro. J. Allergy Clin. Immunol. 113, 949-957 (2004).
    • (2004) J. Allergy Clin. Immunol. , vol.113 , pp. 949-957
    • Novak, N.1
  • 5
    • 84928885641 scopus 로고    scopus 로고
    • Dendritic cell-bound IgE functions to restrain allergic inflammation at mucosal sites
    • Platzer, B. et al. Dendritic cell-bound IgE functions to restrain allergic inflammation at mucosal sites. Mucosal Immunol. 8, 516-532 (2014).
    • (2014) Mucosal Immunol. , vol.8 , pp. 516-532
    • Platzer, B.1
  • 6
    • 84957429266 scopus 로고    scopus 로고
    • Functions of dendritic-cell-bound IgE in allergy
    • Platzer, B., Stout, M. & Fiebiger, E. Functions of dendritic-cell-bound IgE in allergy. Mol. Immunol. doi: http://dx.doi.org/10.1016/j.molimm.2015.05.016
    • Mol. Immunol.
    • Platzer, B.1    Stout, M.2    Fiebiger, E.3
  • 7
    • 84897521175 scopus 로고    scopus 로고
    • Antigen-Conjugated Human IgE Induces Antigen-Specific T Cell Tolerance in a Humanized Mouse Model
    • Baravalle, G., Greer, A. M., Laflam, T. N. & Shin, J.-S. Antigen-Conjugated Human IgE Induces Antigen-Specific T Cell Tolerance in a Humanized Mouse Model. J. Immunol. 192, 3280-8 (2014).
    • (2014) J. Immunol. , vol.192 , pp. 3280-3288
    • Baravalle, G.1    Greer, A.M.2    Laflam, T.N.3    Shin, J.-S.4
  • 8
    • 84896759705 scopus 로고    scopus 로고
    • Serum IgE clearance is facilitated by human FcepsilonRI internalization
    • Greer, A. M. et al. Serum IgE clearance is facilitated by human FcepsilonRI internalization. J. Clin. Invest. 124, 1187-1198 (2014).
    • (2014) J. Clin. Invest. , vol.124 , pp. 1187-1198
    • Greer, A.M.1
  • 9
    • 0033859578 scopus 로고    scopus 로고
    • The novel human IgE epsilon heavy chain, epsilon tailpiece, is present in plasma as part of a covalent complex
    • Chan, L. A., Lyczak, J. B., Zhang, K., Morrison, S. L. & Saxon, A. The novel human IgE epsilon heavy chain, epsilon tailpiece, is present in plasma as part of a covalent complex. Mol. Immunol. 37, 241-252 (2000).
    • (2000) Mol. Immunol. , vol.37 , pp. 241-252
    • Chan, L.A.1    Lyczak, J.B.2    Zhang, K.3    Morrison, S.L.4    Saxon, A.5
  • 10
    • 0026762983 scopus 로고
    • Two unusual forms of human immunoglobulin E encoded by alternative RNA splicing of epsilon heavy chain membrane exons
    • Zhang, K., Saxon, A. & Max, E. E. Two unusual forms of human immunoglobulin E encoded by alternative RNA splicing of epsilon heavy chain membrane exons. J. Exp. Med. 176, 233-243 (1992).
    • (1992) J. Exp. Med. , vol.176 , pp. 233-243
    • Zhang, K.1    Saxon, A.2    Max, E.E.3
  • 11
    • 0027955556 scopus 로고
    • Complex alternative RNA splicing of ε-immunoglobulin transcripts produces mRNAs encoding four potential secreted protein isoforms
    • Zhang, K., Max, E. E., Cheah, H. K. & Saxon, A. Complex alternative RNA splicing of ε-immunoglobulin transcripts produces mRNAs encoding four potential secreted protein isoforms. J. Biol. Chem. 269, 456-462 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 456-462
    • Zhang, K.1    Max, E.E.2    Cheah, H.K.3    Saxon, A.4
  • 12
    • 0029120113 scopus 로고
    • Differential regulation of alternative 3′ splicing of epsilon messenger RNA variants
    • Diaz-Sanchez, D., Zhang, K., Nutman, T. B. & Saxon, A. Differential regulation of alternative 3′ splicing of epsilon messenger RNA variants. J. Immunol. 155, 1930-1941 (1995).
    • (1995) J. Immunol. , vol.155 , pp. 1930-1941
    • Diaz-Sanchez, D.1    Zhang, K.2    Nutman, T.B.3    Saxon, A.4
  • 13
    • 0029864781 scopus 로고    scopus 로고
    • Characterization of a second secreted IgE isoform and identification of an asymmetric pathway of IgE assembly
    • Batista, F. D., Efremov, D. G. & Burrone, O. R. Characterization of a second secreted IgE isoform and identification of an asymmetric pathway of IgE assembly. Proc. Natl. Acad. Sci. USA 93, 3399-3404 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3399-3404
    • Batista, F.D.1    Efremov, D.G.2    Burrone, O.R.3
  • 14
    • 0032588797 scopus 로고    scopus 로고
    • Functional Fc epsilonRI engagement by a second secretory IgE isoform detected in humans
    • Lorenzi, R., Jouvin, M. H. & Burrone, O. R. Functional Fc epsilonRI engagement by a second secretory IgE isoform detected in humans. Eur. J. Immunol. 29, 936-945 (1999).
    • (1999) Eur. J. Immunol. , vol.29 , pp. 936-945
    • Lorenzi, R.1    Jouvin, M.H.2    Burrone, O.R.3
  • 15
    • 0030022132 scopus 로고    scopus 로고
    • Expression of novel secreted isoforms of human immunoglobulin E proteins
    • Lyczak, J. B., Zhang, K., Saxon, A. & Morrison, S. L. Expression of novel secreted isoforms of human immunoglobulin E proteins. J. Biol. Chem. 271, 3428-3436 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 3428-3436
    • Lyczak, J.B.1    Zhang, K.2    Saxon, A.3    Morrison, S.L.4
  • 17
    • 0025840352 scopus 로고
    • Inhibition of human IgE production via Fc epsilon R-II stimulation results from a decrease in the mRNA for secreted but not membrane epsilon H chains
    • Saxon, A., Kurbe-Leamer, M., Behle, K., Max, E. E. & Zhang, K. Inhibition of human IgE production via Fc epsilon R-II stimulation results from a decrease in the mRNA for secreted but not membrane epsilon H chains. J. Immunol. 147, 4000-4006 (1991).
    • (1991) J. Immunol. , vol.147 , pp. 4000-4006
    • Saxon, A.1    Kurbe-Leamer, M.2    Behle, K.3    Max, E.E.4    Zhang, K.5
  • 18
    • 45149133155 scopus 로고    scopus 로고
    • The secretory tailpiece isoform of IgE is not associated with allergy
    • Aslam, A., Lewis, R. J., Wheatley, A., Pleass, R. J. & Sayers, I. The secretory tailpiece isoform of IgE is not associated with allergy. Allergy 63, 942-3 (2008).
    • (2008) Allergy , vol.63 , pp. 942-943
    • Aslam, A.1    Lewis, R.J.2    Wheatley, A.3    Pleass, R.J.4    Sayers, I.5
  • 19
    • 0026032975 scopus 로고
    • Human IgE, IgG4 and resistance to reinfection with Schistosoma haematobium
    • Hagan, P., Blumenthal, U. J., Dunn, D., Simpson, A. J. & Wilkins, H. A. Human IgE, IgG4 and resistance to reinfection with Schistosoma haematobium. Nature 349, 243-245 (1991).
    • (1991) Nature , vol.349 , pp. 243-245
    • Hagan, P.1    Blumenthal, U.J.2    Dunn, D.3    Simpson, A.J.4    Wilkins, H.A.5
  • 20
    • 0026563362 scopus 로고
    • Immunity after treatment of human schistosomiasis: Association between IgE antibodies to adult worm antigens and resistance to reinfection
    • Dunne, D. W. et al. Immunity after treatment of human schistosomiasis: Association between IgE antibodies to adult worm antigens and resistance to reinfection. Eur. J. Immunol. 22, 1483-1494 (1992).
    • (1992) Eur. J. Immunol. , vol.22 , pp. 1483-1494
    • Dunne, D.W.1
  • 21
    • 0039820128 scopus 로고
    • High-affinity IgE receptor on eosinophils is involved in defence against parasites
    • Gounni, A. S. et al. High-affinity IgE receptor on eosinophils is involved in defence against parasites. Nature 367, 183-186 (1994).
    • (1994) Nature , vol.367 , pp. 183-186
    • Gounni, A.S.1
  • 24
    • 42249093361 scopus 로고    scopus 로고
    • Nippostrongylus brasiliensis infection leads to the development of emphysema associated with the induction of alternatively activated macrophages
    • Marsland, B. J., Kurrer, M., Reissmann, R., Harris, N. L. & Kopf, M. Nippostrongylus brasiliensis infection leads to the development of emphysema associated with the induction of alternatively activated macrophages. Eur. J. Immunol. 38, 479-488 (2008).
    • (2008) Eur. J. Immunol. , vol.38 , pp. 479-488
    • Marsland, B.J.1    Kurrer, M.2    Reissmann, R.3    Harris, N.L.4    Kopf, M.5
  • 25
    • 0034098248 scopus 로고    scopus 로고
    • Cleavage of human IgE mediated by Schistosoma mansoni
    • Pleass, R. J., Kusel, J. R. & Woof, J. M. Cleavage of human IgE mediated by Schistosoma mansoni. Int. Arch. Allergy Immunol. 121, 194-204 (2000).
    • (2000) Int. Arch. Allergy Immunol. , vol.121 , pp. 194-204
    • Pleass, R.J.1    Kusel, J.R.2    Woof, J.M.3
  • 26
    • 34548214558 scopus 로고    scopus 로고
    • Proteases from Schistosoma mansoni cercariae cleave IgE at solvent exposed interdomain regions
    • Aslam, A. et al. Proteases from Schistosoma mansoni cercariae cleave IgE at solvent exposed interdomain regions. Mol. Immunol. 45, 567-74 (2008).
    • (2008) Mol. Immunol. , vol.45 , pp. 567-574
    • Aslam, A.1
  • 27
    • 30744476751 scopus 로고    scopus 로고
    • Applied and basic research on the epidemiology, morbidity, and immunology of schistosomiasis in fishing communities on Lake Albert, Uganda
    • Dunne, D. W. et al. Applied and basic research on the epidemiology, morbidity, and immunology of schistosomiasis in fishing communities on Lake Albert, Uganda. Trans. R. Soc. Trop. Med. Hyg. 100, 216-223 (2006).
    • (2006) Trans. R. Soc. Trop. Med. Hyg. , vol.100 , pp. 216-223
    • Dunne, D.W.1
  • 28
    • 0016266853 scopus 로고
    • Complexes in plasma between light chain kappa immunoglobulins and alpha 1-antitrypsin respectively prealbumin
    • Laurell, C. B. & Thulin, E. Complexes in plasma between light chain kappa immunoglobulins and alpha 1-antitrypsin respectively prealbumin. Immunochemistry 11, 703-709 (1974).
    • (1974) Immunochemistry , vol.11 , pp. 703-709
    • Laurell, C.B.1    Thulin, E.2
  • 29
    • 0031596106 scopus 로고    scopus 로고
    • Comparison of IgA-alpha1-antitrypsin levels in rheumatoid arthritis and seronegative oligoarthritis: Complex formation is not associated with inflammation per se
    • Scott, L. J., Evans, E. L., Dawes, P. T., Russell, G. I. & Mattey, D. L. Comparison of IgA-alpha1-antitrypsin levels in rheumatoid arthritis and seronegative oligoarthritis: complex formation is not associated with inflammation per se. Br. J. Rheumatol. 37, 398-404 (1998).
    • (1998) Br. J. Rheumatol. , vol.37 , pp. 398-404
    • Scott, L.J.1    Evans, E.L.2    Dawes, P.T.3    Russell, G.I.4    Mattey, D.L.5
  • 30
    • 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. et al. The Shapes of Z-α1-Antitrypsin Polymers in Solution Support the C-Terminal Domain-Swap Mechanism of Polymerization. Biophys. J. 107, 1905-1912 (2014).
    • (2014) Biophys. J , vol.107 , pp. 1905-1912
    • Behrens, M.A.1
  • 31
    • 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. D. & Huntington, J. A. Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization. Nature 455, 1255-1258 (2008).
    • (2008) Nature , vol.455 , pp. 1255-1258
    • Yamasaki, M.1    Li, W.2    Johnson, D.J.D.3    Huntington, J.A.4
  • 32
    • 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. & Huntington, J. A. Molecular basis of α1-antitrypsin deficiency revealed by the structure of a domain-swapped trimer. EMBO reports 12, 1011-1017 (2011).
    • (2011) EMBO Reports , vol.12 , pp. 1011-1017
    • Yamasaki, M.1    Sendall, T.J.2    Pearce, M.C.3    Whisstock, J.C.4    Huntington, J.A.5
  • 33
    • 0023214577 scopus 로고
    • Complexes of albumin and alpha 1-antitrypsin with Fc-fragment of IgA monomer are disulfide-bound to penultimate C-terminal cysteine in the C alpha 3-domain
    • Vaerman, J. P., Hagiwara, K., Kobayashi, K. & Rits, M. Complexes of albumin and alpha 1-antitrypsin with Fc-fragment of IgA monomer are disulfide-bound to penultimate C-terminal cysteine in the C alpha 3-domain. Immunol. Lett. 15, 67-72 (1987).
    • (1987) Immunol. Lett. , vol.15 , pp. 67-72
    • Vaerman, J.P.1    Hagiwara, K.2    Kobayashi, K.3    Rits, M.4
  • 34
    • 0037135563 scopus 로고    scopus 로고
    • Detection of circulating and endothelial cell polymers of Z and wild type alpha 1-antitrypsin by a monoclonal antibody
    • Janciauskiene, S., Dominaitiene, R., Sternby, N. H., Piitulainen, E. & Eriksson, S. Detection of circulating and endothelial cell polymers of Z and wild type alpha 1-antitrypsin by a monoclonal antibody. J. Biol. Chem. 277, 26540-26546 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 26540-26546
    • Janciauskiene, S.1    Dominaitiene, R.2    Sternby, N.H.3    Piitulainen, E.4    Eriksson, S.5
  • 35
    • 84902153645 scopus 로고    scopus 로고
    • Role of alpha-1-antitrypsin in human health and disease
    • De Serres, F. & Blanco, I. Role of alpha-1-antitrypsin in human health and disease. J. Intern. Med. 276, 311-335 (2014).
    • (2014) J. Intern. Med. , vol.276 , pp. 311-335
    • De Serres, F.1    Blanco, I.2
  • 36
    • 0026755363 scopus 로고
    • The mechanism of Z alpha 1-antitrypsin accumulation in the liver
    • Lomas, D. A., Evans, D. L., Finch, J. T. & Carrell, R. W. The mechanism of Z alpha 1-antitrypsin accumulation in the liver. Nature 357, 605-607 (1992).
    • (1992) Nature , vol.357 , pp. 605-607
    • Lomas, D.A.1    Evans, D.L.2    Finch, J.T.3    Carrell, R.W.4
  • 37
    • 0035928739 scopus 로고    scopus 로고
    • The reaction of serpins with proteinases involves important enthalpy changes
    • Boudier, C. & Bieth, J. G. The reaction of serpins with proteinases involves important enthalpy changes. Biochemistry 40, 9962-9967 (2001).
    • (2001) Biochemistry , vol.40 , pp. 9962-9967
    • Boudier, C.1    Bieth, J.G.2
  • 38
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • Gettins, P. G. W. Serpin structure, mechanism, and function. Chem. Rev. 102, 4751-4803 (2002).
    • (2002) Chem. Rev. , vol.102 , pp. 4751-4803
    • Gettins, P.G.W.1
  • 39
    • 0027473016 scopus 로고
    • Effect of the Z mutation on the physical and inhibitory properties of alpha 1-antitrypsin
    • Lomas, D. A., Evans, D. L., Stone, S. R., Chang, W. S. & Carrell, R. W. Effect of the Z mutation on the physical and inhibitory properties of alpha 1-antitrypsin. Biochemistry 32, 500-508 (1993).
    • (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
  • 40
    • 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
    • Belorgey, D., Crowther, D. C., Mahadeva, R. & Lomas, D. A. Mutant neuroserpin (S49P) that causes familial encephalopathy with neuroserpin inclusion bodies is a poor proteinase inhibitor and readily forms polymers in vitro. J. Biol. Chem. 277, 17367-17373 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 17367-17373
    • Belorgey, D.1    Crowther, D.C.2    Mahadeva, R.3    Lomas, D.A.4
  • 41
    • 0026532063 scopus 로고
    • Conformation of the reactive site loop of alpha 1-proteinase inhibitor probed by limited proteolysis
    • Mast, A. E., Enghild, J. J. & Salvesen, G. Conformation of the reactive site loop of alpha 1-proteinase inhibitor probed by limited proteolysis. Biochemistry 31, 2720-2728 (1992).
    • (1992) Biochemistry , vol.31 , pp. 2720-2728
    • Mast, A.E.1    Enghild, J.J.2    Salvesen, G.3
  • 43
    • 0028118817 scopus 로고
    • Expression of functional high affinity immunoglobulin E receptors (Fc epsilon RI) on monocytes of atopic individuals
    • Maurer, D. et al. Expression of functional high affinity immunoglobulin E receptors (Fc epsilon RI) on monocytes of atopic individuals. J. Exp. Med. 179, 745-750 (1994).
    • (1994) J. Exp. Med. , vol.179 , pp. 745-750
    • Maurer, D.1
  • 44
    • 27744472315 scopus 로고    scopus 로고
    • Structural requirements for the interaction of human IgA with the human polymeric Ig receptor
    • Lewis, M. J., Pleass, R. J., Batten, M. R., Atkin, J. D. & Woof, J. M. Structural requirements for the interaction of human IgA with the human polymeric Ig receptor. J. Immunol. 175, 6694-701 (2005).
    • (2005) J. Immunol. , vol.175 , pp. 6694-6701
    • Lewis, M.J.1    Pleass, R.J.2    Batten, M.R.3    Atkin, J.D.4    Woof, J.M.5
  • 45
    • 0030003017 scopus 로고    scopus 로고
    • Mutagenesis of the human IgA1 heavy chain tailpiece that prevents dimer assembly
    • Atkin, J. D., Pleass, R. J., Owens, R. J. & Woof, J. M. Mutagenesis of the human IgA1 heavy chain tailpiece that prevents dimer assembly. J. Immunol. 157, 156-9 (1996).
    • (1996) J. Immunol. , vol.157 , pp. 156-159
    • Atkin, J.D.1    Pleass, R.J.2    Owens, R.J.3    Woof, J.M.4
  • 46
    • 0024546542 scopus 로고
    • IgA-alpha 1 antitrypsin complexes in ankylosing spondylitis
    • Struthers, G. R., Lewin, I. V. & Stanworth, D. R. IgA-alpha 1 antitrypsin complexes in ankylosing spondylitis. Ann. Rheum. Dis. 48, 30-34 (1989).
    • (1989) Ann. Rheum. Dis. , vol.48 , pp. 30-34
    • Struthers, G.R.1    Lewin, I.V.2    Stanworth, D.R.3
  • 47
    • 36348939332 scopus 로고    scopus 로고
    • Dimers Initiate and Propagate Serine Protease Inhibitor Polymerisation
    • Zhou, A. & Carrell, R. W. Dimers Initiate and Propagate Serine Protease Inhibitor Polymerisation. J. Mol. Biol. 375, 36-42 (2008).
    • (2008) J. Mol. Biol. , vol.375 , pp. 36-42
    • Zhou, A.1    Carrell, R.W.2
  • 49
    • 84875673488 scopus 로고    scopus 로고
    • Twenty years of polymers: A personal perspective on alpha-1 antitrypsin deficiency
    • Lomas, D. A. Twenty years of polymers: a personal perspective on alpha-1 antitrypsin deficiency. COPD 10 Suppl 1, 17-25 (2013).
    • (2013) COPD , vol.10 , pp. 17-25
    • Lomas, D.A.1
  • 52
    • 33646588338 scopus 로고    scopus 로고
    • The selective advantage of alpha-1-antitrypsin deficiency
    • Lomas, D. A. The selective advantage of alpha-1-antitrypsin deficiency. Am. J. Respir. Crit. Care Med. 173, 1072-1077 (2006).
    • (2006) Am. J. Respir. Crit. Care Med. , vol.173 , pp. 1072-1077
    • Lomas, D.A.1
  • 53
    • 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. & Bustillo, E. F. Alpha-1-antitrypsin PI phenotypes S and Z in Europe: an analysis of the published surveys. Clin. Genet. 60, 31-41 (2001).
    • (2001) Clin. Genet. , vol.60 , pp. 31-41
    • Blanco, I.1    Fernández, E.2    Bustillo, E.F.3
  • 54
    • 84923580569 scopus 로고    scopus 로고
    • DNA Typing of Ancient Parasite Eggs from Environmental Samples Identifies Human and Animal Worm Infections in Viking-Age Settlement
    • Søe, M. J., Nejsum, P., Fredensborg, B. L. & Kapel, C. M. O. DNA Typing of Ancient Parasite Eggs from Environmental Samples Identifies Human and Animal Worm Infections in Viking-Age Settlement. J. Parasitol. 101, 57-63 (2015).
    • (2015) J. Parasitol. , vol.101 , pp. 57-63
    • Søe, M.J.1    Nejsum, P.2    Fredensborg, B.L.3    Kapel, C.M.O.4
  • 55
    • 32544437550 scopus 로고    scopus 로고
    • Neutrophilic inflammation and IL-8 levels in induced sputum of alpha-1-antitrypsin PiMZ subjects
    • Malerba, M. et al. Neutrophilic inflammation and IL-8 levels in induced sputum of alpha-1-antitrypsin PiMZ subjects. Thorax 61, 129-133 (2006).
    • (2006) Thorax , vol.61 , pp. 129-133
    • Malerba, M.1
  • 56
    • 27644501820 scopus 로고    scopus 로고
    • Immune responses following experimental human hookworm infection
    • Wright, V. & Bickle, Q. Immune responses following experimental human hookworm infection. Clin. Exp. Immunol. 142, 398-403 (2005).
    • (2005) Clin. Exp. Immunol. , vol.142 , pp. 398-403
    • Wright, V.1    Bickle, Q.2
  • 57
    • 0027997433 scopus 로고
    • Complex formation of human alpha-1-antitrypsin with components in Schistosoma mansoni cercariae
    • Modha, J. & Doenhoff, M. J. Complex formation of human alpha-1-antitrypsin with components in Schistosoma mansoni cercariae. Parasite Immunol. 16, 447-450 (1994).
    • (1994) Parasite Immunol. , vol.16 , pp. 447-450
    • Modha, J.1    Doenhoff, M.J.2
  • 58
    • 0023872622 scopus 로고
    • Detection of alpha 2-macroglobulin, alpha 1-protease inhibitor, and neutral protease-antiprotease complexes within liver granulomas of Schistosoma mansoni-infected mice
    • Truden, J. L. & Boros, D. L. Detection of alpha 2-macroglobulin, alpha 1-protease inhibitor, and neutral protease-antiprotease complexes within liver granulomas of Schistosoma mansoni-infected mice. Am. J. Pathol. 130, 281-288 (1988).
    • (1988) Am. J. Pathol. , vol.130 , pp. 281-288
    • Truden, J.L.1    Boros, D.L.2
  • 59
    • 84921324746 scopus 로고    scopus 로고
    • Schistosome infection aggravates HCV-related liver disease and induces changes in the regulatory T-cell phenotype
    • Loffredo-Verde, E. et al. Schistosome infection aggravates HCV-related liver disease and induces changes in the regulatory T-cell phenotype. Parasite Immunol. 37, 97-104 (2015).
    • (2015) Parasite Immunol. , vol.37 , pp. 97-104
    • Loffredo-Verde, E.1
  • 60
    • 80054739270 scopus 로고    scopus 로고
    • Acquired alpha 1-antitrypsin deficiency in tropical pulmonary eosinophilia
    • Ray, D. et al. Acquired alpha 1-antitrypsin deficiency in tropical pulmonary eosinophilia. Indian J. Med. Res. 134, 79-82 (2011).
    • (2011) Indian J. Med. Res. , vol.134 , pp. 79-82
    • Ray, D.1
  • 61
    • 0027165959 scopus 로고
    • Alpha1-antitrypsin in tropical pulmonary eosinophilia
    • Ray, D. & Krishna, K. S. Alpha1-antitrypsin in tropical pulmonary eosinophilia. Chest 104, 487-492 (1993).
    • (1993) Chest , vol.104 , pp. 487-492
    • Ray, D.1    Krishna, K.S.2
  • 62
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington, J. A., Read, R. J. & Carrell, R. W. Structure of a serpin-protease complex shows inhibition by deformation. Nature 407, 923-926 (2000).
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 63
    • 0018276853 scopus 로고
    • Structural evidence for methionine at the reactive site of human alpha-1-proteinase inhibitor
    • Johnson, D. & Travis, J. Structural evidence for methionine at the reactive site of human alpha-1-proteinase inhibitor. J. Biol. Chem. 253, 7142-7144 (1978).
    • (1978) J. Biol. Chem. , vol.253 , pp. 7142-7144
    • Johnson, D.1    Travis, J.2
  • 64
    • 0034836428 scopus 로고    scopus 로고
    • LRP: A multifunctional scavenger and signaling receptor
    • Herz, J. & Strickland, D. K. LRP: A multifunctional scavenger and signaling receptor. J. Clin. Invest. 108, 779-784 (2001).
    • (2001) J. Clin. Invest. , vol.108 , pp. 779-784
    • Herz, J.1    Strickland, D.K.2
  • 65
    • 84894557027 scopus 로고    scopus 로고
    • Low-density lipoprotein receptor-related protein-1: Role in the regulation of vascular integrity
    • Strickland, D. K., Au, D. T., Cunfer, P. & Muratoglu, S. C. Low-density lipoprotein receptor-related protein-1: Role in the regulation of vascular integrity. Arterioscler. Thromb. Vasc. Biol. 34, 487-498 (2014).
    • (2014) Arterioscler. Thromb. Vasc. Biol. , vol.34 , pp. 487-498
    • Strickland, D.K.1    Au, D.T.2    Cunfer, P.3    Muratoglu, S.C.4
  • 66
    • 2142758108 scopus 로고    scopus 로고
    • Sterol regulation of scavenger receptor class B type I in macrophages
    • Yu, L., Cao, G., Repa, J. & Stangl, H. Sterol regulation of scavenger receptor class B type I in macrophages. J. Lipid Res. 45, 889-899 (2004).
    • (2004) J. Lipid Res. , vol.45 , pp. 889-899
    • Yu, L.1    Cao, G.2    Repa, J.3    Stangl, H.4
  • 67
    • 26844540763 scopus 로고    scopus 로고
    • Regulation and splicing of scavenger receptor class B type I in human macrophages and atherosclerotic plaques
    • Svensson, P.-A. et al. Regulation and splicing of scavenger receptor class B type I in human macrophages and atherosclerotic plaques. BMC Cardiovasc. Disord. 5, 25 (2005).
    • (2005) BMC Cardiovasc. Disord , vol.5 , pp. 25
    • Svensson, P.-A.1
  • 68
    • 0009627006 scopus 로고
    • Binding site on macrophages that mediates uptake and degradation of acetylated low density lipoprotein, producing massive cholesterol deposition
    • Goldstein, J. L., Ho, Y. K., Basu, S. K. & Brown, M. S. Binding site on macrophages that mediates uptake and degradation of acetylated low density lipoprotein, producing massive cholesterol deposition. Proc. Natl. Acad. Sci. USA 76, 333-337 (1979).
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 333-337
    • Goldstein, J.L.1    Ho, Y.K.2    Basu, S.K.3    Brown, M.S.4
  • 69
    • 70349694399 scopus 로고    scopus 로고
    • Alpha1-Antitrypsin deficiency: Best clinical practice
    • Kalsheker, N. a. alpha1-Antitrypsin deficiency: best clinical practice. J. Clin. Pathol. 62, 865-869 (2009).
    • (2009) J. Clin. Pathol. , vol.62 , pp. 865-869
    • Kalsheker, N.A.1
  • 70
    • 0023195781 scopus 로고
    • Metabolism of immunoglobulin E in patients with markedly elevated serum immunoglobulin E levels
    • Dreskin, S. C., Goldsmith, P. K., Strober, W., Zech, L. A. & Gallin, J. I. Metabolism of immunoglobulin E in patients with markedly elevated serum immunoglobulin E levels. J. Clin. Invest. 79, 1764-1772 (1987).
    • (1987) J. Clin. Invest. , vol.79 , pp. 1764-1772
    • Dreskin, S.C.1    Goldsmith, P.K.2    Strober, W.3    Zech, L.A.4    Gallin, J.I.5
  • 71
    • 84879725035 scopus 로고    scopus 로고
    • Development and analysis of alpha 1-antitrypsin neoglycoproteins: The impact of additional N-glycosylation sites on serum half-life
    • Lusch, A. et al. Development and analysis of alpha 1-antitrypsin neoglycoproteins: The impact of additional N-glycosylation sites on serum half-life. Mol. Pharm. 10, 2616-2629 (2013).
    • (2013) Mol. Pharm. , vol.10 , pp. 2616-2629
    • Lusch, A.1
  • 72
    • 0030882075 scopus 로고    scopus 로고
    • Expression and functions of the high-affinity IgE receptor on human platelets and megakaryocyte precursors
    • Joseph, M. et al. Expression and functions of the high-affinity IgE receptor on human platelets and megakaryocyte precursors. Eur. J. Immunol. 27, 2212-2218 (1997).
    • (1997) Eur. J. Immunol. , vol.27 , pp. 2212-2218
    • Joseph, M.1
  • 73
    • 84929659585 scopus 로고    scopus 로고
    • A Human Platelet Receptor Protein Microarray Identifies the High Affinity Immunoglobulin E Receptor Subunit α (FcεR1α) as an Activating Platelet Endothelium Aggregation Receptor 1 (PEAR1) Ligand
    • Sun, Y. et al. A Human Platelet Receptor Protein Microarray Identifies the High Affinity Immunoglobulin E Receptor Subunit α (FcεR1α) as an Activating Platelet Endothelium Aggregation Receptor 1 (PEAR1) Ligand. Mol. Cell. Proteomics 14, 1265-1274 (2015).
    • (2015) Mol. Cell. Proteomics , vol.14 , pp. 1265-1274
    • Sun, Y.1
  • 74
    • 84862545173 scopus 로고    scopus 로고
    • Assessing the association between omalizumab and arteriothrombotic events through spontaneous adverse event reporting
    • Ali, A. Assessing the association between omalizumab and arteriothrombotic events through spontaneous adverse event reporting. J. Asthma Allergy 5, 1-9 (2012).
    • (2012) J. Asthma Allergy , vol.5 , pp. 1-9
    • Ali, A.1
  • 75
    • 79959237123 scopus 로고    scopus 로고
    • The discovery of α1-antitrypsin and its role in health and disease
    • Janciauskiene, S. M. et al. The discovery of α1-antitrypsin and its role in health and disease. Respiratory Medicine 105, 1129-1139 (2011).
    • (2011) Respiratory Medicine , vol.105 , pp. 1129-1139
    • Janciauskiene, S.M.1
  • 76
    • 84859104213 scopus 로고    scopus 로고
    • The generation and evaluation of two panels of epitope-matched mouse IgG1, IgG2a, IgG2b and IgG3 antibodies specific for Plasmodium falciparum and Plasmodium yoelii merozoite surface protein 1-19 (MSP1(19))
    • Adame-Gallegos, J. R., Shi, J., McIntosh, R. S. & Pleass, R. J. The generation and evaluation of two panels of epitope-matched mouse IgG1, IgG2a, IgG2b and IgG3 antibodies specific for Plasmodium falciparum and Plasmodium yoelii merozoite surface protein 1-19 (MSP1(19)). Exp. Parasitol. 130, 384-93 (2012).
    • (2012) Exp. Parasitol. , vol.130 , pp. 384-393
    • Adame-Gallegos, J.R.1    Shi, J.2    McIntosh, R.S.3    Pleass, R.J.4
  • 77
    • 0032950307 scopus 로고    scopus 로고
    • Adult resistance to schistosomiasis mansoni: Age-dependence of reinfection remains constant in communities with diverse exposure patterns
    • Kabatereine, N. B. et al. Adult resistance to schistosomiasis mansoni: age-dependence of reinfection remains constant in communities with diverse exposure patterns. Parasitology 118 (Pt 1), 101-105 (1999).
    • (1999) Parasitology , vol.118 , pp. 101-105
    • Kabatereine, N.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.