메뉴 건너뛰기




Volumn 13, Issue 7, 2014, Pages 3131-3143

The role and importance of glycosylation of acute phase proteins with focus on alpha-1 antitrypsin in acute and chronic inflammatory conditions

Author keywords

alpha 1 antitrypsin; glycosylation; inflammation

Indexed keywords

ACUTE PHASE PROTEIN; ALPHA 1 ANTITRYPSIN; BIOLOGICAL MARKER; GLYCAN; SERINE PROTEINASE INHIBITOR; TUMOR MARKER;

EID: 84903697731     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr500146y     Document Type: Review
Times cited : (115)

References (174)
  • 2
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • Gettins, P. G. Serpin structure, mechanism, and function Chem. Rev. 2002, 102 (12) 4751-4804
    • (2002) Chem. Rev. , vol.102 , Issue.12 , pp. 4751-4804
    • Gettins, P.G.1
  • 3
    • 79960638185 scopus 로고    scopus 로고
    • Serpin structure, function and dysfunction
    • Huntington, J. A. Serpin structure, function and dysfunction J. Thromb. Haemostasis 2011, 9 (Suppl 1) 26-34
    • (2011) J. Thromb. Haemostasis , vol.9 , Issue.SUPPL. 1 , pp. 26-34
    • Huntington, J.A.1
  • 4
    • 67650713938 scopus 로고    scopus 로고
    • Conformational pathology of the serpins: Themes, variations, and therapeutic strategies
    • Gooptu, B.; Lomas, D. A. Conformational pathology of the serpins: themes, variations, and therapeutic strategies Ann. Rev. Biochem. 2009, 78, 147-176
    • (2009) Ann. Rev. Biochem. , vol.78 , pp. 147-176
    • Gooptu, B.1    Lomas, D.A.2
  • 5
    • 0029783413 scopus 로고    scopus 로고
    • Inhibitory conformation of the reactive loop of alpha 1-antitrypsin
    • Elliott, P. R.; Lomas, D. A.; Carrell, R. W.; Abrahams, J. P. Inhibitory conformation of the reactive loop of alpha 1-antitrypsin Nat Struct Biol. 1996, 3 (8) 676-681
    • (1996) Nat Struct Biol. , vol.3 , Issue.8 , pp. 676-681
    • Elliott, P.R.1    Lomas, D.A.2    Carrell, R.W.3    Abrahams, J.P.4
  • 6
    • 0343193210 scopus 로고    scopus 로고
    • Topography of a 2.0 A structure of alpha-1-antitrypsin reveals targets for rational drug design to prevent conformational disease
    • Elliott, P. R.; Pei, X. Y.; Dafforn, T. R.; Lomas, D. A. Topography of a 2.0 A structure of alpha-1-antitrypsin reveals targets for rational drug design to prevent conformational disease Protein Sci. 2000, 9 (7) 1274-1281
    • (2000) Protein Sci. , vol.9 , Issue.7 , pp. 1274-1281
    • Elliott, P.R.1    Pei, X.Y.2    Dafforn, T.R.3    Lomas, D.A.4
  • 7
    • 0024423930 scopus 로고
    • Implications of the three-dimensional structure of alpha-1-antitrypsin for structure and function of serpins
    • Huber, R.; Carrell, R. W. Implications of the three-dimensional structure of alpha-1-antitrypsin for structure and function of serpins Biochemistry 1989, 28 (23) 8951-8966
    • (1989) Biochemistry , vol.28 , Issue.23 , pp. 8951-8966
    • Huber, R.1    Carrell, R.W.2
  • 8
    • 4744356921 scopus 로고    scopus 로고
    • Alpha-1-antitrypsin deficiency: Diagnosis and treatment
    • viii-ix - 859
    • Perlmutter, D. H. Alpha-1-antitrypsin deficiency: diagnosis and treatment Clin. Liver Dis. 2004, 8 (4) 839-859 viii-ix
    • (2004) Clin. Liver Dis. , vol.8 , Issue.4 , pp. 839
    • Perlmutter, D.H.1
  • 9
    • 0019984864 scopus 로고
    • Serum levels of acute phase and cardiac proteins after myocardial infarction, surgery, and infection
    • Voulgari, F.; Cummins, P.; Gardecki, T. I.; Beeching, N. J.; Stone, P. C.; Stuart, J. Serum levels of acute phase and cardiac proteins after myocardial infarction, surgery, and infection Br. Heart J. 1982, 48 (4) 352-356
    • (1982) Br. Heart J. , vol.48 , Issue.4 , pp. 352-356
    • Voulgari, F.1    Cummins, P.2    Gardecki, T.I.3    Beeching, N.J.4    Stone, P.C.5    Stuart, J.6
  • 11
    • 84858705230 scopus 로고    scopus 로고
    • Alpha-1 antitrypsin: A potent anti-inflammatory and potential novel therapeutic agent
    • Bergin, D. A.; Hurley, K.; McElvaney, N. G.; Reeves, E. P. Alpha-1 antitrypsin: A potent anti-inflammatory and potential novel therapeutic agent Arch. Immunol. Ther. Exp. (Warsz) 2012, 60 (2) 81-97
    • (2012) Arch. Immunol. Ther. Exp. (Warsz) , vol.60 , Issue.2 , pp. 81-97
    • Bergin, D.A.1    Hurley, K.2    McElvaney, N.G.3    Reeves, E.P.4
  • 12
    • 78649816539 scopus 로고    scopus 로고
    • Alpha-1 Antitrypsin regulates human neutrophil chemotaxis induced by soluble immune complexes and IL-8
    • Bergin, D. A.; Reeves, E. P.; Meleady, P.; Henry, M.; McElvaney, O. J.; Carroll, T. P. Alpha-1 Antitrypsin regulates human neutrophil chemotaxis induced by soluble immune complexes and IL-8 J. Clin Invest. 2010, 120 (12) 4236-4250
    • (2010) J. Clin Invest. , vol.120 , Issue.12 , pp. 4236-4250
    • Bergin, D.A.1    Reeves, E.P.2    Meleady, P.3    Henry, M.4    McElvaney, O.J.5    Carroll, T.P.6
  • 13
    • 33645100367 scopus 로고    scopus 로고
    • Comprehensive glyco-proteomic analysis of human alpha1-antitrypsin and its charge isoforms
    • Kolarich, D.; Weber, A.; Turecek, P. L.; Schwarz, H. P.; Altmann, F. Comprehensive glyco-proteomic analysis of human alpha1-antitrypsin and its charge isoforms Proteomics 2006, 6 (11) 3369-3380
    • (2006) Proteomics , vol.6 , Issue.11 , pp. 3369-3380
    • Kolarich, D.1    Weber, A.2    Turecek, P.L.3    Schwarz, H.P.4    Altmann, F.5
  • 14
    • 0035378754 scopus 로고    scopus 로고
    • Analysis by matrix assisted laser desorption/ionisation-time of flight mass spectrometry of the post-translational modifications of alpha 1-antitrypsin isoforms separated by two-dimensional polyacrylamide gel electrophoresis
    • Mills, P. B.; Mills, K.; Johnson, A. W.; Clayton, P. T.; Winchester, B. G. Analysis by matrix assisted laser desorption/ionisation-time of flight mass spectrometry of the post-translational modifications of alpha 1-antitrypsin isoforms separated by two-dimensional polyacrylamide gel electrophoresis Proteomics 2001, 1 (6) 778-786
    • (2001) Proteomics , vol.1 , Issue.6 , pp. 778-786
    • Mills, P.B.1    Mills, K.2    Johnson, A.W.3    Clayton, P.T.4    Winchester, B.G.5
  • 15
    • 0018122298 scopus 로고
    • Organ cultures of human fetal hepatocytes in the study of extra-and intracellular alpha1-antitrypsin
    • Eriksson, S.; Alm, R.; Astedt, B. Organ cultures of human fetal hepatocytes in the study of extra-and intracellular alpha1-antitrypsin Biochim. Biophys. Acta 1978, 542 (3) 496-505
    • (1978) Biochim. Biophys. Acta , vol.542 , Issue.3 , pp. 496-505
    • Eriksson, S.1    Alm, R.2    Astedt, B.3
  • 16
    • 0017799945 scopus 로고
    • Synthesis of antithrombin III and alpha-1-antitrypsin by the perfused rat liver
    • Koj, A.; Regoeczi, E.; Toews, C. J.; Leveille, R.; Gauldie, J. Synthesis of antithrombin III and alpha-1-antitrypsin by the perfused rat liver Biochim. Biophys. Acta 1978, 539 (4) 496-504
    • (1978) Biochim. Biophys. Acta , vol.539 , Issue.4 , pp. 496-504
    • Koj, A.1    Regoeczi, E.2    Toews, C.J.3    Leveille, R.4    Gauldie, J.5
  • 17
    • 0022472015 scopus 로고
    • Crystal RG. Expression of the alpha-1-antitrypsin gene in mononuclear phagocytes of normal and alpha-1-antitrypsin-deficient individuals
    • Mornex, J. F.; Chytil-Weir, A.; Martinet, Y.; Courtney, M.; LeCocq, J. P. Crystal RG. Expression of the alpha-1-antitrypsin gene in mononuclear phagocytes of normal and alpha-1-antitrypsin-deficient individuals J. Clin. Invest. 1986, 77 (6) 1952-1961
    • (1986) J. Clin. Invest. , vol.77 , Issue.6 , pp. 1952-1961
    • Mornex, J.F.1    Chytil-Weir, A.2    Martinet, Y.3    Courtney, M.4    Lecocq, J.P.5
  • 18
    • 77952770299 scopus 로고    scopus 로고
    • Evidence for unfolded protein response activation in monocytes from individuals with alpha-1 antitrypsin deficiency
    • Carroll, T. P.; Greene, C. M.; OConnor, C. A.; Nolan, A. M.; ONeill, S. J.; McElvaney, N. G. Evidence for unfolded protein response activation in monocytes from individuals with alpha-1 antitrypsin deficiency J. Immunol. 2010, 184 (8) 4538-4546
    • (2010) J. Immunol. , vol.184 , Issue.8 , pp. 4538-4546
    • Carroll, T.P.1    Greene, C.M.2    Oconnor, C.A.3    Nolan, A.M.4    Oneill, S.J.5    McElvaney, N.G.6
  • 20
    • 0030610007 scopus 로고    scopus 로고
    • Biosynthesis of alpha1-proteinase inhibitor by human lung-derived epithelial cells
    • Cichy, J.; Potempa, J.; Travis, J. Biosynthesis of alpha1-proteinase inhibitor by human lung-derived epithelial cells J. Biol. Chem. 1997, 272 (13) 8250-8255
    • (1997) J. Biol. Chem. , vol.272 , Issue.13 , pp. 8250-8255
    • Cichy, J.1    Potempa, J.2    Travis, J.3
  • 21
    • 70350130097 scopus 로고    scopus 로고
    • Proteases and antiproteases in chronic neutrophilic lung disease - Relevance to drug discovery
    • Greene, C. M.; McElvaney, N. G. Proteases and antiproteases in chronic neutrophilic lung disease-relevance to drug discovery Br. J. Pharmacol. 2009, 158 (4) 1048-1058
    • (2009) Br. J. Pharmacol. , vol.158 , Issue.4 , pp. 1048-1058
    • Greene, C.M.1    McElvaney, N.G.2
  • 23
    • 0024397003 scopus 로고
    • Crystal RG. Serum alpha 1-antitrypsin deficiency associated with the common S-type (Glu264 - - Val) mutation results from intracellular degradation of alpha 1-antitrypsin prior to secretion
    • Curiel, D. T.; Chytil, A.; Courtney, M. Crystal RG. Serum alpha 1-antitrypsin deficiency associated with the common S-type (Glu264 - - Val) mutation results from intracellular degradation of alpha 1-antitrypsin prior to secretion J. Biol. Chem. 1989, 264 (18) 10477-10486
    • (1989) J. Biol. Chem. , vol.264 , Issue.18 , pp. 10477-10486
    • Curiel, D.T.1    Chytil, A.2    Courtney, M.3
  • 24
    • 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 1992, 357 (6379) 605-607
    • (1992) Nature , vol.357 , Issue.6379 , pp. 605-607
    • Lomas, D.A.1    Evans, D.L.2    Finch, J.T.3    Carrell, R.W.4
  • 25
    • 84864018755 scopus 로고    scopus 로고
    • Serum levels and genotype distribution of alpha1-antitrypsin in the general population
    • Ferrarotti, I.; Thun, G. A.; Zorzetto, M.; Ottaviani, S.; Imboden, M.; Schindler, C. Serum levels and genotype distribution of alpha1-antitrypsin in the general population Thorax 2012, 67 (8) 669-674
    • (2012) Thorax , vol.67 , Issue.8 , pp. 669-674
    • Ferrarotti, I.1    Thun, G.A.2    Zorzetto, M.3    Ottaviani, S.4    Imboden, M.5    Schindler, C.6
  • 27
    • 0023898432 scopus 로고
    • Molecular basis of alpha-1-antitrypsin deficiency
    • Brantly, M.; Nukiwa, T.; Crystal, R. G. Molecular basis of alpha-1-antitrypsin deficiency Am. J. Med. 1988, 84 (6A) 13-31
    • (1988) Am. J. Med. , vol.84 , Issue.6 A , pp. 13-31
    • Brantly, M.1    Nukiwa, T.2    Crystal, R.G.3
  • 29
    • 0034743745 scopus 로고    scopus 로고
    • Alpha1-antitrypsin deficiency: A position statement of the Canadian Thoracic Society
    • Abboud, R. T.; Ford, G. T.; Chapman, K. R. Alpha1-antitrypsin deficiency: a position statement of the Canadian Thoracic Society Canadian Respir. J. 2001, 8 (2) 81-88
    • (2001) Canadian Respir. J. , vol.8 , Issue.2 , pp. 81-88
    • Abboud, R.T.1    Ford, G.T.2    Chapman, K.R.3
  • 31
    • 67649407825 scopus 로고    scopus 로고
    • Exploring the role of CT densitometry: A randomised study of augmentation therapy in alpha1-antitrypsin deficiency
    • Dirksen, A.; Piitulainen, E.; Parr, D. G.; Deng, C.; Wencker, M.; Shaker, S. B. Exploring the role of CT densitometry: a randomised study of augmentation therapy in alpha1-antitrypsin deficiency Eur. Respir. J. 2009, 33 (6) 1345-1353
    • (2009) Eur. Respir. J. , vol.33 , Issue.6 , pp. 1345-1353
    • Dirksen, A.1    Piitulainen, E.2    Parr, D.G.3    Deng, C.4    Wencker, M.5    Shaker, S.B.6
  • 33
    • 70350450961 scopus 로고    scopus 로고
    • Augmentation therapy for alpha1 antitrypsin deficiency: A meta-analysis
    • Chapman, K. R.; Stockley, R. A.; Dawkins, C.; Wilkes, M. M.; Navickis, R. J. Augmentation therapy for alpha1 antitrypsin deficiency: A meta-analysis COPD 2009, 6 (3) 177-184
    • (2009) COPD , vol.6 , Issue.3 , pp. 177-184
    • Chapman, K.R.1    Stockley, R.A.2    Dawkins, C.3    Wilkes, M.M.4    Navickis, R.J.5
  • 34
    • 0035095548 scopus 로고    scopus 로고
    • Longitudinal follow-up of patients with alpha(1)-protease inhibitor deficiency before and during therapy with IV alpha(1)-protease inhibitor
    • Wencker, M.; Fuhrmann, B.; Banik, N.; Konietzko, N. Longitudinal follow-up of patients with alpha(1)-protease inhibitor deficiency before and during therapy with IV alpha(1)-protease inhibitor Chest 2001, 119 (3) 737-744
    • (2001) Chest , vol.119 , Issue.3 , pp. 737-744
    • Wencker, M.1    Fuhrmann, B.2    Banik, N.3    Konietzko, N.4
  • 35
    • 0031242842 scopus 로고    scopus 로고
    • Does alpha1-antitrypsin augmentation therapy slow the annual decline in FEV1 in patients with severe hereditary alpha1-antitrypsin deficiency? Wissenschaftliche Arbeitsgemeinschaft zur Therapie von Lungenerkrankungen (WATL) alpha1-AT study group
    • Seersholm, N.; Wencker, M.; Banik, N.; Viskum, K.; Dirksen, A.; Kok-Jensen, A. Does alpha1-antitrypsin augmentation therapy slow the annual decline in FEV1 in patients with severe hereditary alpha1-antitrypsin deficiency? Wissenschaftliche Arbeitsgemeinschaft zur Therapie von Lungenerkrankungen (WATL) alpha1-AT study group Eur. Respir. J. 1997, 10 (10) 2260-2263
    • (1997) Eur. Respir. J. , vol.10 , Issue.10 , pp. 2260-2263
    • Seersholm, N.1    Wencker, M.2    Banik, N.3    Viskum, K.4    Dirksen, A.5    Kok-Jensen, A.6
  • 36
    • 77952806527 scopus 로고    scopus 로고
    • Augmentation therapy for alpha-1 antitrypsin deficiency - Not enough evidence to support its use yet!
    • McCarthy, C.; Dimitrov, B. D. Augmentation therapy for alpha-1 antitrypsin deficiency - not enough evidence to support its use yet! COPD 2010, 7 (3) 234
    • (2010) COPD , vol.7 , Issue.3 , pp. 234
    • McCarthy, C.1    Dimitrov, B.D.2
  • 38
    • 46549087438 scopus 로고    scopus 로고
    • Alpha-1 antitrypsin deficiency: A conformational disease associated with lung and liver manifestations
    • Greene, C. M.; Miller, S. D.; Carroll, T.; McLean, C.; OMahony, M.; Lawless, M. W. Alpha-1 antitrypsin deficiency: a conformational disease associated with lung and liver manifestations J. Inherited Metab. Dis. 2008, 31 (1) 21-34
    • (2008) J. Inherited Metab. Dis. , vol.31 , Issue.1 , pp. 21-34
    • Greene, C.M.1    Miller, S.D.2    Carroll, T.3    McLean, C.4    Omahony, M.5    Lawless, M.W.6
  • 39
    • 79952663591 scopus 로고    scopus 로고
    • Lung disease associated with alpha1-antitrypsin deficiency
    • Tuder, R. M.; Janciauskiene, S. M.; Petrache, I. Lung disease associated with alpha1-antitrypsin deficiency Proc. Am. Thorac. Soc. 2010, 7 (6) 381-386
    • (2010) Proc. Am. Thorac. Soc. , vol.7 , Issue.6 , pp. 381-386
    • Tuder, R.M.1    Janciauskiene, S.M.2    Petrache, I.3
  • 41
    • 34547097491 scopus 로고    scopus 로고
    • Alpha-1-antitrypsin deficiency: Current concepts
    • Mulgrew, A. T.; Taggart, C. C.; McElvaney, N. G. Alpha-1-antitrypsin deficiency: current concepts Lung 2007, 185 (4) 191-201
    • (2007) Lung , vol.185 , Issue.4 , pp. 191-201
    • Mulgrew, A.T.1    Taggart, C.C.2    McElvaney, N.G.3
  • 42
    • 0016592108 scopus 로고
    • Characterization of alpha1-antitrypsin in the inclusion bodies from the liver in alpha 1-antitrypsin deficiency
    • Jeppsson, J. O.; Larsson, C.; Eriksson, S. Characterization of alpha1-antitrypsin in the inclusion bodies from the liver in alpha 1-antitrypsin deficiency New Engl. J. Med. 1975, 293 (12) 576-579
    • (1975) New Engl. J. Med. , vol.293 , Issue.12 , pp. 576-579
    • Jeppsson, J.O.1    Larsson, C.2    Eriksson, S.3
  • 43
    • 21244492343 scopus 로고    scopus 로고
    • A pilot study comparing the purity, functionality and isoform composition of alpha-1-proteinase inhibitor (human) products
    • Cowden, D. I.; Fisher, G. E.; Weeks, R. L. A pilot study comparing the purity, functionality and isoform composition of alpha-1-proteinase inhibitor (human) products Curr. Med. Res. Opin. 2005, 21 (6) 877-883
    • (2005) Curr. Med. Res. Opin. , vol.21 , Issue.6 , pp. 877-883
    • Cowden, D.I.1    Fisher, G.E.2    Weeks, R.L.3
  • 44
    • 33750300517 scopus 로고    scopus 로고
    • Biochemical, molecular characterization, and glycoproteomic analyses of alpha(1)-proteinase inhibitor products used for replacement therapy
    • Kolarich, D.; Turecek, P. L.; Weber, A.; Mitterer, A.; Graninger, M.; Matthiessen, P. Biochemical, molecular characterization, and glycoproteomic analyses of alpha(1)-proteinase inhibitor products used for replacement therapy Transfusion 2006, 46 (11) 1959-1977
    • (2006) Transfusion , vol.46 , Issue.11 , pp. 1959-1977
    • Kolarich, D.1    Turecek, P.L.2    Weber, A.3    Mitterer, A.4    Graninger, M.5    Matthiessen, P.6
  • 45
  • 46
    • 0030937062 scopus 로고    scopus 로고
    • Glycosylation: Heterogeneity and the 3D structure of proteins
    • Rudd, P. M.; Dwek, R. A. Glycosylation: heterogeneity and the 3D structure of proteins Crit. Rev. Biochem. Mol. Biol. 1997, 32 (1) 1-100
    • (1997) Crit. Rev. Biochem. Mol. Biol. , vol.32 , Issue.1 , pp. 1-100
    • Rudd, P.M.1    Dwek, R.A.2
  • 47
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: Nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • Spiro, R. G. Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds Glycobiology 2002, 12 (4) 43R-56R
    • (2002) Glycobiology , vol.12 , Issue.4
    • Spiro, R.G.1
  • 48
    • 0025041029 scopus 로고
    • Protein degradation in the endoplasmic reticulum
    • Klausner, R. D.; Sitia, R. Protein degradation in the endoplasmic reticulum Cell. 1990, 62 (4) 611-614
    • (1990) Cell. , vol.62 , Issue.4 , pp. 611-614
    • Klausner, R.D.1    Sitia, R.2
  • 49
    • 0018853556 scopus 로고
    • Primary structure of glycoprotein glycans: Basis for the molecular biology of glycoproteins
    • Montreuil, J. Primary structure of glycoprotein glycans: Basis for the molecular biology of glycoproteins Adv. carbohydr. chem. biochem. 1980, 37, 157-223
    • (1980) Adv. Carbohydr. Chem. Biochem. , vol.37 , pp. 157-223
    • Montreuil, J.1
  • 50
    • 0009755702 scopus 로고
    • Carbohydrates in protein. 3. The preparation and some of the properties of a glycopeptide from hens-egg albumin
    • Johansen, P. G.; Marshall, R. D.; Neuberger, A. Carbohydrates in protein. 3. The preparation and some of the properties of a glycopeptide from hens-egg albumin Biochem. J. 1961, 78, 518-527
    • (1961) Biochem. J. , vol.78 , pp. 518-527
    • Johansen, P.G.1    Marshall, R.D.2    Neuberger, A.3
  • 51
    • 0029991763 scopus 로고    scopus 로고
    • Biochemistry, molecular biology, and genetics of the oligosaccharyltransferase
    • Silberstein, S.; Gilmore, R. Biochemistry, molecular biology, and genetics of the oligosaccharyltransferase FASEB J. 1996, 10 (8) 849-858
    • (1996) FASEB J. , vol.10 , Issue.8 , pp. 849-858
    • Silberstein, S.1    Gilmore, R.2
  • 52
    • 0019377631 scopus 로고
    • Synthesis and processing of asparagine-linked oligosaccharides
    • Hubbard, S. C.; Ivatt, R. J. Synthesis and processing of asparagine-linked oligosaccharides Annu. Rev. Biochem. 1981, 50, 555-583
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 555-583
    • Hubbard, S.C.1    Ivatt, R.J.2
  • 53
    • 0025883650 scopus 로고
    • Secretion of N-glycosylated interleukin-1 beta in Saccharomyces cerevisiae using a leader peptide from Candida albicans. Effect of N-linked glycosylation on biological activity
    • Livi, G. P.; Lillquist, J. S.; Miles, L. M.; Ferrara, A.; Sathe, G. M.; Simon, P. L. Secretion of N-glycosylated interleukin-1 beta in Saccharomyces cerevisiae using a leader peptide from Candida albicans. Effect of N-linked glycosylation on biological activity J. Biol. Chem. 1991, 266 (23) 15348-15355
    • (1991) J. Biol. Chem. , vol.266 , Issue.23 , pp. 15348-15355
    • Livi, G.P.1    Lillquist, J.S.2    Miles, L.M.3    Ferrara, A.4    Sathe, G.M.5    Simon, P.L.6
  • 54
    • 0029041308 scopus 로고
    • The hydroxy amino acid in an Asn-X-Ser/Thr sequon can influence N-linked core glycosylation efficiency and the level of expression of a cell surface glycoprotein
    • Kasturi, L.; Eshleman, J. R.; Wunner, W. H.; Shakin-Eshleman, S. H. The hydroxy amino acid in an Asn-X-Ser/Thr sequon can influence N-linked core glycosylation efficiency and the level of expression of a cell surface glycoprotein J. Biol. Chem. 1995, 270 (24) 14756-14761
    • (1995) J. Biol. Chem. , vol.270 , Issue.24 , pp. 14756-14761
    • Kasturi, L.1    Eshleman, J.R.2    Wunner, W.H.3    Shakin-Eshleman, S.H.4
  • 55
    • 0020713174 scopus 로고
    • Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes
    • Bause, E. Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes Biochem. J. 1983, 209 (2) 331-336
    • (1983) Biochem. J. , vol.209 , Issue.2 , pp. 331-336
    • Bause, E.1
  • 56
    • 0019888690 scopus 로고
    • Enhancement of protein glycosylation in tissue slices by dolichylphosphate
    • Carson, D. D.; Earles, B. J.; Lennarz, W. J. Enhancement of protein glycosylation in tissue slices by dolichylphosphate J. Biol. Chem. 1981, 256 (22) 11552-11557
    • (1981) J. Biol. Chem. , vol.256 , Issue.22 , pp. 11552-11557
    • Carson, D.D.1    Earles, B.J.2    Lennarz, W.J.3
  • 57
    • 0029585865 scopus 로고
    • Phosphomannomutase deficiency is a cause of carbohydrate-deficient glycoprotein syndrome type i
    • Van Schaftingen, E.; Jaeken, J. Phosphomannomutase deficiency is a cause of carbohydrate-deficient glycoprotein syndrome type I FEBS Lett. 1995, 377 (3) 318-320
    • (1995) FEBS Lett. , vol.377 , Issue.3 , pp. 318-320
    • Van Schaftingen, E.1    Jaeken, J.2
  • 58
    • 0023338172 scopus 로고
    • Tissue-specific N-glycosylation, site-specific oligosaccharide patterns and lentil lectin recognition of rat Thy-1
    • Parekh, R. B.; Tse, A. G.; Dwek, R. A.; Williams, A. F.; Rademacher, T. W. Tissue-specific N-glycosylation, site-specific oligosaccharide patterns and lentil lectin recognition of rat Thy-1 EMBO J. 1987, 6 (5) 1233-1244
    • (1987) EMBO J. , vol.6 , Issue.5 , pp. 1233-1244
    • Parekh, R.B.1    Tse, A.G.2    Dwek, R.A.3    Williams, A.F.4    Rademacher, T.W.5
  • 59
    • 0022462129 scopus 로고
    • Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharides
    • Schachter, H. Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharides Biochem. Cell Biol. 1986, 64 (3) 163-181
    • (1986) Biochem. Cell Biol. , vol.64 , Issue.3 , pp. 163-181
    • Schachter, H.1
  • 60
    • 0018895863 scopus 로고
    • Control of glycoprotein synthesis. Processing of asparagine-linked oligosaccharides by one or more rat liver Golgi alpha-D-mannosidases dependent on the prior action of UDP-N-acetylglucosamine: Alpha-D-mannoside beta 2-N-acetylglucosaminyltransferase i
    • Harpaz, N.; Schachter, H. Control of glycoprotein synthesis. Processing of asparagine-linked oligosaccharides by one or more rat liver Golgi alpha-D-mannosidases dependent on the prior action of UDP-N-acetylglucosamine: alpha-D-mannoside beta 2-N-acetylglucosaminyltransferase I J. Biol. Chem. 1980, 255 (10) 4894-4902
    • (1980) J. Biol. Chem. , vol.255 , Issue.10 , pp. 4894-4902
    • Harpaz, N.1    Schachter, H.2
  • 61
    • 0025048023 scopus 로고
    • Sialosyl-Tn. A novel mucin antigen associated with prognosis in colorectal cancer patients
    • Itzkowitz, S. H.; Bloom, E. J.; Kokal, W. A.; Modin, G.; Hakomori, S.; Kim, Y. S. Sialosyl-Tn. A novel mucin antigen associated with prognosis in colorectal cancer patients Cancer 1990, 66 (9) 1960-1966
    • (1990) Cancer , vol.66 , Issue.9 , pp. 1960-1966
    • Itzkowitz, S.H.1    Bloom, E.J.2    Kokal, W.A.3    Modin, G.4    Hakomori, S.5    Kim, Y.S.6
  • 62
    • 0026446025 scopus 로고
    • Altered glycosylation of membrane glycoproteins associated with human mammary carcinoma
    • Hiraizumi, S; Takasaki, S; Ohuchi, N; Harada, Y; Nose, M; Mori, S Altered glycosylation of membrane glycoproteins associated with human mammary carcinoma Jpn. J. Cancer Res. 1992, 83 (10) 1063-1072
    • (1992) Jpn. J. Cancer Res. , vol.83 , Issue.10 , pp. 1063-1072
    • Hiraizumi, S.1    Takasaki, S.2    Ohuchi, N.3    Harada, Y.4    Nose, M.5    Mori, S.6
  • 63
    • 0027410273 scopus 로고
    • Inflammation-induced expression of sialyl Lewis X-containing glycan structures on alpha 1-acid glycoprotein (orosomucoid) in human sera
    • De Graaf, T. W.; Van der Stelt, M. E.; Anbergen, M. G.; van Dijk, W. Inflammation-induced expression of sialyl Lewis X-containing glycan structures on alpha 1-acid glycoprotein (orosomucoid) in human sera J. Exp. Med. 1993, 177 (3) 657-666
    • (1993) J. Exp. Med. , vol.177 , Issue.3 , pp. 657-666
    • De Graaf, T.W.1    Van Der Stelt, M.E.2    Anbergen, M.G.3    Van Dijk, W.4
  • 64
    • 0027957966 scopus 로고
    • Glycoforms modify the dynamic stability and functional activity of an enzyme
    • Rudd, P. M.; Joao, H. C.; Coghill, E.; Fiten, P.; Saunders, M. R.; Opdenakker, G. Glycoforms modify the dynamic stability and functional activity of an enzyme Biochemistry 1994, 33 (1) 17-22
    • (1994) Biochemistry , vol.33 , Issue.1 , pp. 17-22
    • Rudd, P.M.1    Joao, H.C.2    Coghill, E.3    Fiten, P.4    Saunders, M.R.5    Opdenakker, G.6
  • 65
    • 0021271295 scopus 로고
    • Binding of complement subcomponent C1q to mouse IgG1, IgG2a and IgG2b: A novel C1q binding assay
    • Leatherbarrow, R. J.; Dwek, R. A. Binding of complement subcomponent C1q to mouse IgG1, IgG2a and IgG2b: A novel C1q binding assay Mol. Immunol. 1984, 21 (4) 321-327
    • (1984) Mol. Immunol. , vol.21 , Issue.4 , pp. 321-327
    • Leatherbarrow, R.J.1    Dwek, R.A.2
  • 67
    • 0031028909 scopus 로고    scopus 로고
    • Variations in oligosaccharide-protein interactions in immunoglobulin G determine the site-specific glycosylation profiles and modulate the dynamic motion of the Fc oligosaccharides
    • Wormald, M. R.; Rudd, P. M.; Harvey, D. J.; Chang, S. C.; Scragg, I. G.; Dwek, R. A. Variations in oligosaccharide-protein interactions in immunoglobulin G determine the site-specific glycosylation profiles and modulate the dynamic motion of the Fc oligosaccharides Biochemistry. 1997, 36 (6) 1370-1380
    • (1997) Biochemistry. , vol.36 , Issue.6 , pp. 1370-1380
    • Wormald, M.R.1    Rudd, P.M.2    Harvey, D.J.3    Chang, S.C.4    Scragg, I.G.5    Dwek, R.A.6
  • 68
    • 0028832978 scopus 로고
    • The activation of type 1 and type 2 plasminogen by type i and type II tissue plasminogen activator
    • Mori, K.; Dwek, R. A.; Downing, A. K.; Opdenakker, G.; Rudd, P. M. The activation of type 1 and type 2 plasminogen by type I and type II tissue plasminogen activator J. Biol. Chem. 1995, 270 (7) 3261-3267
    • (1995) J. Biol. Chem. , vol.270 , Issue.7 , pp. 3261-3267
    • Mori, K.1    Dwek, R.A.2    Downing, A.K.3    Opdenakker, G.4    Rudd, P.M.5
  • 69
    • 0026637316 scopus 로고
    • Structure and function of the mannose 6-phosphate/insulinlike growth factor II receptors
    • Kornfeld, S. Structure and function of the mannose 6-phosphate/ insulinlike growth factor II receptors Annu. Rev. Biochem 1992, 61, 307-30
    • (1992) Annu. Rev. Biochem , vol.61 , pp. 307-330
    • Kornfeld, S.1
  • 71
    • 0021099058 scopus 로고
    • Binding of synthetic oligosaccharides to the hepatic Gal/GalNAc lectin. Dependence on fine structural features
    • Lee, Y. C.; Townsend, R. R.; Hardy, M. R.; Lonngren, J.; Arnarp, J.; Haraldsson, M. Binding of synthetic oligosaccharides to the hepatic Gal/GalNAc lectin. Dependence on fine structural features J. Biol. Chem. 1983, 258 (1) 199-202
    • (1983) J. Biol. Chem. , vol.258 , Issue.1 , pp. 199-202
    • Lee, Y.C.1    Townsend, R.R.2    Hardy, M.R.3    Lonngren, J.4    Arnarp, J.5    Haraldsson, M.6
  • 73
    • 0032742944 scopus 로고    scopus 로고
    • Roles for glycosylation of cell surface receptors involved in cellular immune recognition
    • Rudd, P. M.; Wormald, M. R.; Stanfield, R. L.; Huang, M.; Mattsson, N.; Speir, J. A. Roles for glycosylation of cell surface receptors involved in cellular immune recognition J. Mol. biol. 1999, 293 (2) 351-366
    • (1999) J. Mol. Biol. , vol.293 , Issue.2 , pp. 351-366
    • Rudd, P.M.1    Wormald, M.R.2    Stanfield, R.L.3    Huang, M.4    Mattsson, N.5    Speir, J.A.6
  • 74
    • 84883427656 scopus 로고    scopus 로고
    • Changes in serum N-glycosylation profiles: Functional significance and potential for diagnostics
    • In; Rauter, A. P. RSC Publishing: Londoon.
    • Marino, K; Saldova, R; Adamczyk, B; Rudd, P. M. Changes in serum N-glycosylation profiles: Functional significance and potential for diagnostics. In Carbohydrate Chemistry: Chemical and Biological Approaches; Rauter, A. P., Ed.; RSC Publishing: Londoon, 2012.
    • (2012) Carbohydrate Chemistry: Chemical and Biological Approaches
    • Marino, K.1    Saldova, R.2    Adamczyk, B.3    Rudd, P.M.4
  • 75
    • 41449087577 scopus 로고    scopus 로고
    • HPLC-based analysis of serum N-glycans on a 96-well plate platform with dedicated database software
    • Royle, L.; Campbell, M. P.; Radcliffe, C. M.; White, D. M.; Harvey, D. J.; Abrahams, J. L. HPLC-based analysis of serum N-glycans on a 96-well plate platform with dedicated database software Anal. Biochem. 2008, 376 (1) 1-12
    • (2008) Anal. Biochem. , vol.376 , Issue.1 , pp. 1-12
    • Royle, L.1    Campbell, M.P.2    Radcliffe, C.M.3    White, D.M.4    Harvey, D.J.5    Abrahams, J.L.6
  • 76
    • 61849180382 scopus 로고    scopus 로고
    • Variability, heritability and environmental determinants of human plasma N-glycome
    • Knezevic, A.; Polasek, O.; Gornik, O.; Rudan, I.; Campbell, H.; Hayward, C. Variability, heritability and environmental determinants of human plasma N-glycome J. Proteome Res. 2009, 8 (2) 694-701
    • (2009) J. Proteome Res. , vol.8 , Issue.2 , pp. 694-701
    • Knezevic, A.1    Polasek, O.2    Gornik, O.3    Rudan, I.4    Campbell, H.5    Hayward, C.6
  • 77
    • 0030996004 scopus 로고    scopus 로고
    • Structural changes of immunoglobulin G oligosaccharides with age in healthy human serum
    • Yamada, E.; Tsukamoto, Y.; Sasaki, R.; Yagyu, K.; Takahashi, N. Structural changes of immunoglobulin G oligosaccharides with age in healthy human serum Glycoconjugate J. 1997, 14 (3) 401-405
    • (1997) Glycoconjugate J. , vol.14 , Issue.3 , pp. 401-405
    • Yamada, E.1    Tsukamoto, Y.2    Sasaki, R.3    Yagyu, K.4    Takahashi, N.5
  • 78
    • 77954518174 scopus 로고    scopus 로고
    • Effects of aging, body mass index, plasma lipid profiles, and smoking on human plasma N-glycans
    • Knezevic, A.; Gornik, O.; Polasek, O.; Pucic, M.; Redzic, I.; Novokmet, M. Effects of aging, body mass index, plasma lipid profiles, and smoking on human plasma N-glycans Glycobiology 2010, 20 (8) 959-969
    • (2010) Glycobiology , vol.20 , Issue.8 , pp. 959-969
    • Knezevic, A.1    Gornik, O.2    Polasek, O.3    Pucic, M.4    Redzic, I.5    Novokmet, M.6
  • 80
    • 77957254802 scopus 로고    scopus 로고
    • Genome-wide association study identifies FUT8 and ESR2 as co-regulators of a bi-antennary N-linked glycan A2 (GlcNAc2Man3GlcNAc2) in human plasma proteins
    • 10101/npre.2009.2864.1
    • Lauc, G.; Huffman, J.; Hayward, C.; Knezevic, A.; Polasek, O.; Gornik, O. Genome-wide association study identifies FUT8 and ESR2 as co-regulators of a bi-antennary N-linked glycan A2 (GlcNAc2Man3GlcNAc2) in human plasma proteins Nat. Precedings 2009, 10101/npre.2009.2864.1
    • (2009) Nat. Precedings
    • Lauc, G.1    Huffman, J.2    Hayward, C.3    Knezevic, A.4    Polasek, O.5    Gornik, O.6
  • 81
    • 84975742481 scopus 로고    scopus 로고
    • Genomics meets glycomics: The first GWAS study of human N-Glycome identifies HNF1alpha as a master regulator of plasma protein fucosylation
    • Lauc, G.; Essafi, A.; Huffman, J. E.; Hayward, C.; Knezevic, A.; Kattla, J. J. Genomics meets glycomics: The first GWAS study of human N-Glycome identifies HNF1alpha as a master regulator of plasma protein fucosylation PLoS Genet. 2010, 6 (12) e1001256
    • (2010) PLoS Genet. , vol.6 , Issue.12 , pp. 1001256
    • Lauc, G.1    Essafi, A.2    Huffman, J.E.3    Hayward, C.4    Knezevic, A.5    Kattla, J.J.6
  • 82
    • 33646689560 scopus 로고    scopus 로고
    • Sugar and alcohol molecules provide a therapeutic strategy for the serpinopathies that cause dementia and cirrhosis
    • Sharp, L. K.; Mallya, M.; Kinghorn, K. J.; Wang, Z.; Crowther, D. C.; Huntington, J. A. Sugar and alcohol molecules provide a therapeutic strategy for the serpinopathies that cause dementia and cirrhosis FEBS J. 2006, 273 (11) 2540-2552
    • (2006) FEBS J. , vol.273 , Issue.11 , pp. 2540-2552
    • Sharp, L.K.1    Mallya, M.2    Kinghorn, K.J.3    Wang, Z.4    Crowther, D.C.5    Huntington, J.A.6
  • 84
    • 84867824272 scopus 로고    scopus 로고
    • Smoking and Lung Cancer-induced Changes in N-Glycosylation of Blood Serum Proteins
    • 10.1093/glycob/cws108
    • Vasseur, J. A.; Goetz, J. A.; Alley, W. R., Jr.; Novotny, M. V. Smoking and Lung Cancer-induced Changes in N-Glycosylation of Blood Serum Proteins Glycobiology 2012, 10.1093/glycob/cws108
    • (2012) Glycobiology
    • Vasseur, J.A.1    Goetz, J.A.2    Alley, Jr.W.R.3    Novotny, M.V.4
  • 85
    • 58149391280 scopus 로고    scopus 로고
    • Glycosylation of serum proteins in inflammatory diseases
    • Gornik, O.; Lauc, G. Glycosylation of serum proteins in inflammatory diseases Dis. Markers 2008, 25 (4-5) 267-278
    • (2008) Dis. Markers , vol.25 , Issue.45 , pp. 267-278
    • Gornik, O.1    Lauc, G.2
  • 86
    • 0030686564 scopus 로고    scopus 로고
    • Effect of low to moderate levels of smoking and alcohol consumption on serum immunoglobulin concentrations
    • McMillan, S. A.; Douglas, J. P.; Archbold, G. P.; McCrum, E. E.; Evans, A. E. Effect of low to moderate levels of smoking and alcohol consumption on serum immunoglobulin concentrations J. Clin. Pathol. 1997, 50 (10) 819-822
    • (1997) J. Clin. Pathol. , vol.50 , Issue.10 , pp. 819-822
    • McMillan, S.A.1    Douglas, J.P.2    Archbold, G.P.3    McCrum, E.E.4    Evans, A.E.5
  • 88
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • Arnold, J. N.; Wormald, M. R.; Sim, R. B.; Rudd, P. M.; Dwek, R. A. The impact of glycosylation on the biological function and structure of human immunoglobulins Annu. Rev. Immunol. 2007, 25, 21-50
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 21-50
    • Arnold, J.N.1    Wormald, M.R.2    Sim, R.B.3    Rudd, P.M.4    Dwek, R.A.5
  • 89
    • 0033545342 scopus 로고    scopus 로고
    • Acute-phase proteins and other systemic responses to inflammation
    • Gabay, C.; Kushner, I. Acute-phase proteins and other systemic responses to inflammation New Engl. J. Med. 1999, 340 (6) 448-454
    • (1999) New Engl. J. Med. , vol.340 , Issue.6 , pp. 448-454
    • Gabay, C.1    Kushner, I.2
  • 90
    • 47949099098 scopus 로고    scopus 로고
    • Origin and physiological roles of inflammation
    • Medzhitov, R. Origin and physiological roles of inflammation Nature 2008, 454 (7203) 428-435
    • (2008) Nature , vol.454 , Issue.7203 , pp. 428-435
    • Medzhitov, R.1
  • 92
    • 0030587937 scopus 로고    scopus 로고
    • Immunologic dissonance: A continuing evolution in our understanding of the systemic inflammatory response syndrome (SIRS) and the multiple organ dysfunction syndrome (MODS)
    • Bone, R. C. Immunologic dissonance: a continuing evolution in our understanding of the systemic inflammatory response syndrome (SIRS) and the multiple organ dysfunction syndrome (MODS) Ann. Int. Med. 1996, 125 (8) 680-687
    • (1996) Ann. Int. Med. , vol.125 , Issue.8 , pp. 680-687
    • Bone, R.C.1
  • 93
    • 77956312917 scopus 로고    scopus 로고
    • Identification of N-glycosylation changes in the CSF and serum in patients with schizophrenia
    • Stanta, J. L.; Saldova, R.; Struwe, W. B.; Byrne, J. C.; Leweke, F. M.; Rothermund, M. Identification of N-glycosylation changes in the CSF and serum in patients with schizophrenia J. Proteome Res. 2010, 9 (9) 4476-4489
    • (2010) J. Proteome Res. , vol.9 , Issue.9 , pp. 4476-4489
    • Stanta, J.L.1    Saldova, R.2    Struwe, W.B.3    Byrne, J.C.4    Leweke, F.M.5    Rothermund, M.6
  • 94
    • 53849126845 scopus 로고    scopus 로고
    • Human total serum N-glycome
    • Klein, A. Human total serum N-glycome Adv. Clin Chem. 2008, 46, 51-85
    • (2008) Adv. Clin Chem. , vol.46 , pp. 51-85
    • Klein, A.1
  • 95
    • 1942454310 scopus 로고    scopus 로고
    • Noninvasive diagnosis of liver cirrhosis using DNA sequencer-based total serum protein glycomics
    • Callewaert, N.; Van Vlierberghe, H.; Van Hecke, A.; Laroy, W.; Delanghe, J.; Contreras, R. Noninvasive diagnosis of liver cirrhosis using DNA sequencer-based total serum protein glycomics Nature Med. 2004, 10 (4) 429-434
    • (2004) Nature Med. , vol.10 , Issue.4 , pp. 429-434
    • Callewaert, N.1    Van Vlierberghe, H.2    Van Hecke, A.3    Laroy, W.4    Delanghe, J.5    Contreras, R.6
  • 96
    • 36348983813 scopus 로고    scopus 로고
    • N-glycomic changes in hepatocellular carcinoma patients with liver cirrhosis induced by hepatitis B virus
    • Liu, X. E.; Desmyter, L.; Gao, C. F.; Laroy, W.; Dewaele, S.; Vanhooren, V. N-glycomic changes in hepatocellular carcinoma patients with liver cirrhosis induced by hepatitis B virus Hepatology 2007, 46 (5) 1426-1435
    • (2007) Hepatology , vol.46 , Issue.5 , pp. 1426-1435
    • Liu, X.E.1    Desmyter, L.2    Gao, C.F.3    Laroy, W.4    Dewaele, S.5    Vanhooren, V.6
  • 97
    • 61849122929 scopus 로고    scopus 로고
    • Serum protein N-glycans profiling for the discovery of potential biomarkers for nonalcoholic steatohepatitis
    • Chen, C.; Schmilovitz-Weiss, H.; Liu, X. E.; Pappo, O.; Halpern, M.; Sulkes, J. Serum protein N-glycans profiling for the discovery of potential biomarkers for nonalcoholic steatohepatitis J. Proteome Res. 2009, 8 (2) 463-470
    • (2009) J. Proteome Res. , vol.8 , Issue.2 , pp. 463-470
    • Chen, C.1    Schmilovitz-Weiss, H.2    Liu, X.E.3    Pappo, O.4    Halpern, M.5    Sulkes, J.6
  • 98
    • 0031802899 scopus 로고    scopus 로고
    • Reproducible and sensitive determination of charged oligosaccharides from haptoglobin by PNGase F digestion and HPAEC/PAD analysis: Glycan composition varies with disease
    • Goodarzi, M. T.; Turner, G. A. Reproducible and sensitive determination of charged oligosaccharides from haptoglobin by PNGase F digestion and HPAEC/PAD analysis: glycan composition varies with disease Glycoconjugate J. 1998, 15 (5) 469-75
    • (1998) Glycoconjugate J. , vol.15 , Issue.5 , pp. 469-475
    • Goodarzi, M.T.1    Turner, G.A.2
  • 99
    • 77953697951 scopus 로고    scopus 로고
    • Glycosylation of liver acute-phase proteins in pancreatic cancer and chronic pancreatitis
    • Sarrats, A.; Saldova, R.; Pla, E.; Fort, E.; Harvey, D. J.; Struwe, W. B. Glycosylation of liver acute-phase proteins in pancreatic cancer and chronic pancreatitis Proteomics Clin. Appl. 2010, 4 (4) 432-448
    • (2010) Proteomics Clin. Appl. , vol.4 , Issue.4 , pp. 432-448
    • Sarrats, A.1    Saldova, R.2    Pla, E.3    Fort, E.4    Harvey, D.J.5    Struwe, W.B.6
  • 100
    • 77953796851 scopus 로고    scopus 로고
    • Liver proteins as sensor of human malignancies and inflammation
    • Peracaula, R.; Sarrats, A.; Rudd, P. M. Liver proteins as sensor of human malignancies and inflammation Proteomics Clin. Appl. 2010, 4 (4) 426-431
    • (2010) Proteomics Clin. Appl. , vol.4 , Issue.4 , pp. 426-431
    • Peracaula, R.1    Sarrats, A.2    Rudd, P.M.3
  • 101
    • 10044264455 scopus 로고    scopus 로고
    • Alpha1-acid glycoprotein fucosylation as a marker of carcinoma progression and prognosis
    • Hashimoto, S.; Asao, T.; Takahashi, J.; Yagihashi, Y.; Nishimura, T.; Saniabadi, A. R. alpha1-acid glycoprotein fucosylation as a marker of carcinoma progression and prognosis Cancer 2004, 101 (12) 2825-2836
    • (2004) Cancer , vol.101 , Issue.12 , pp. 2825-2836
    • Hashimoto, S.1    Asao, T.2    Takahashi, J.3    Yagihashi, Y.4    Nishimura, T.5    Saniabadi, A.R.6
  • 102
    • 45549091249 scopus 로고    scopus 로고
    • Plasma glycoprotein profiling for colorectal cancer biomarker identification by lectin glycoarray and lectin blot
    • Qiu, Y.; Patwa, T. H.; Xu, L.; Shedden, K.; Misek, D. E.; Tuck, M. Plasma glycoprotein profiling for colorectal cancer biomarker identification by lectin glycoarray and lectin blot J. Proteome Res.. 2008, 7 (4) 1693-1703
    • (2008) J. Proteome Res. , vol.7 , Issue.4 , pp. 1693-1703
    • Qiu, Y.1    Patwa, T.H.2    Xu, L.3    Shedden, K.4    Misek, D.E.5    Tuck, M.6
  • 103
    • 34948905277 scopus 로고    scopus 로고
    • Comparative profiling of serum glycoproteome by sequential purification of glycoproteins and 2-nitrobenzensulfenyl (NBS) stable isotope labeling: A new approach for the novel biomarker discovery for cancer
    • Ueda, K.; Katagiri, T.; Shimada, T.; Irie, S.; Sato, T. A.; Nakamura, Y. Comparative profiling of serum glycoproteome by sequential purification of glycoproteins and 2-nitrobenzensulfenyl (NBS) stable isotope labeling: a new approach for the novel biomarker discovery for cancer J. Proteome Res. 2007, 6 (9) 3475-3483
    • (2007) J. Proteome Res. , vol.6 , Issue.9 , pp. 3475-3483
    • Ueda, K.1    Katagiri, T.2    Shimada, T.3    Irie, S.4    Sato, T.A.5    Nakamura, Y.6
  • 104
    • 0019321021 scopus 로고
    • Studies on the oligosaccharide chains of human alpha 1-protease inhibitor. II. Structure of oligosaccharides
    • Mega, T.; Lujan, E.; Yoshida, A. Studies on the oligosaccharide chains of human alpha 1-protease inhibitor. II. Structure of oligosaccharides J. Biol. Chem. 1980, 255 (9) 4057-61
    • (1980) J. Biol. Chem. , vol.255 , Issue.9 , pp. 4057-4061
    • Mega, T.1    Lujan, E.2    Yoshida, A.3
  • 105
    • 0018726624 scopus 로고
    • Structure of the oligosaccharide chains in human alpha 1-protease inhibitor
    • Hodges, L. C.; Laine, R.; Chan, S. K. Structure of the oligosaccharide chains in human alpha 1-protease inhibitor J. Biol. Chem. 1979, 254 (17) 8208-12
    • (1979) J. Biol. Chem. , vol.254 , Issue.17 , pp. 8208-8212
    • Hodges, L.C.1    Laine, R.2    Chan, S.K.3
  • 106
    • 0030033101 scopus 로고    scopus 로고
    • Characterization of human plasma glycoproteins separated by two-dimensional gel electrophoresis
    • Packer, N. H.; MR, W. I.; Golaz, O.; Lawson, M. A.; Gooley, A. A.; Hochstrasser, D. F. Characterization of human plasma glycoproteins separated by two-dimensional gel electrophoresis Biotechnology (NY) 1996, 14 (1) 66-70
    • (1996) Biotechnology (NY) , vol.14 , Issue.1 , pp. 66-70
    • Packer, N.H.1    Mr, W.I.2    Golaz, O.3    Lawson, M.A.4    Gooley, A.A.5    Hochstrasser, D.F.6
  • 107
    • 0034775822 scopus 로고    scopus 로고
    • Identification of alpha(1)-antitrypsin variants in plasma with the use of proteomic technology
    • Mills, K.; Mills, P. B.; Clayton, P. T.; Johnson, A. W.; Whitehouse, D. B.; Winchester, B. G. Identification of alpha(1)-antitrypsin variants in plasma with the use of proteomic technology Clin. Chem. 2001, 47 (11) 2012-2022
    • (2001) Clin. Chem. , vol.47 , Issue.11 , pp. 2012-2022
    • Mills, K.1    Mills, P.B.2    Clayton, P.T.3    Johnson, A.W.4    Whitehouse, D.B.5    Winchester, B.G.6
  • 108
    • 33747223673 scopus 로고    scopus 로고
    • Endomannosidase processes oligosaccharides of alpha1-antitrypsin and its naturally occurring genetic variants in the Golgi apparatus
    • Torossi, T.; Fan, J. Y.; Sauter-Etter, K.; Roth, J.; Ziak, M. Endomannosidase processes oligosaccharides of alpha1-antitrypsin and its naturally occurring genetic variants in the Golgi apparatus Cell. Mol. Life Sci. 2006, 63 (16) 1923-1932
    • (2006) Cell. Mol. Life Sci. , vol.63 , Issue.16 , pp. 1923-1932
    • Torossi, T.1    Fan, J.Y.2    Sauter-Etter, K.3    Roth, J.4    Ziak, M.5
  • 109
    • 0023322129 scopus 로고
    • Alpha 1-antitrypsin deficiency - A defect in secretion
    • Foreman, R. C. Alpha 1-antitrypsin deficiency - A defect in secretion Biosci. Rep. 1987, 7 (4) 307-311
    • (1987) Biosci. Rep. , vol.7 , Issue.4 , pp. 307-311
    • Foreman, R.C.1
  • 110
    • 77957887133 scopus 로고    scopus 로고
    • Linkage specific fucosylation of alpha-1-antitrypsin in liver cirrhosis and cancer patients: Implications for a biomarker of hepatocellular carcinoma
    • Comunale, M. A.; Rodemich-Betesh, L.; Hafner, J.; Wang, M.; Norton, P.; Di Bisceglie, A. M. Linkage specific fucosylation of alpha-1-antitrypsin in liver cirrhosis and cancer patients: Implications for a biomarker of hepatocellular carcinoma PloS One 2010, 5 (8) e12419
    • (2010) PloS One , vol.5 , Issue.8 , pp. 12419
    • Comunale, M.A.1    Rodemich-Betesh, L.2    Hafner, J.3    Wang, M.4    Norton, P.5    Di Bisceglie, A.M.6
  • 111
    • 0141730230 scopus 로고    scopus 로고
    • The contribution of N-glycans and their processing in the endoplasmic reticulum to glycoprotein biosynthesis
    • Trombetta, E. S. The contribution of N-glycans and their processing in the endoplasmic reticulum to glycoprotein biosynthesis Glycobiology 2003, 13 (9) 77R-91R
    • (2003) Glycobiology , vol.13 , Issue.9
    • Trombetta, E.S.1
  • 112
    • 0034657712 scopus 로고    scopus 로고
    • Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradation
    • Parodi, A. J. Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradation Biochemical J. 2000, 348 (Pt 1) 1-13
    • (2000) Biochemical J. , vol.348 , Issue.PART 1 , pp. 1-13
    • Parodi, A.J.1
  • 113
    • 0037829617 scopus 로고    scopus 로고
    • Enhancement of endoplasmic reticulum (ER) degradation of misfolded Null Hong Kong alpha1-antitrypsin by human ER mannosidase i
    • Hosokawa, N.; Tremblay, L. O.; You, Z.; Herscovics, A.; Wada, I.; Nagata, K. Enhancement of endoplasmic reticulum (ER) degradation of misfolded Null Hong Kong alpha1-antitrypsin by human ER mannosidase I J. Biol. Chem. 2003, 278 (28) 26287-94
    • (2003) J. Biol. Chem. , vol.278 , Issue.28 , pp. 26287-26294
    • Hosokawa, N.1    Tremblay, L.O.2    You, Z.3    Herscovics, A.4    Wada, I.5    Nagata, K.6
  • 114
    • 0037816258 scopus 로고    scopus 로고
    • Elucidation of the molecular logic by which misfolded alpha 1-antitrypsin is preferentially selected for degradation
    • Wu, Y.; Swulius, M. T.; Moremen, K. W.; Sifers, R. N. Elucidation of the molecular logic by which misfolded alpha 1-antitrypsin is preferentially selected for degradation Proc. Natl. Acad. Sci. U.S.A. 2003, 100 (14) 8229-34
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , Issue.14 , pp. 8229-8234
    • Wu, Y.1    Swulius, M.T.2    Moremen, K.W.3    Sifers, R.N.4
  • 115
    • 0034681281 scopus 로고    scopus 로고
    • Conformational changes in serpins: I. The native and cleaved conformations of alpha(1)-antitrypsin
    • Whisstock, J. C.; Skinner, R.; Carrell, R. W.; Lesk, A. M. Conformational changes in serpins: I. The native and cleaved conformations of alpha(1)-antitrypsin J. Mol. Biol. 2000, 296 (2) 685-699
    • (2000) J. Mol. Biol. , vol.296 , Issue.2 , pp. 685-699
    • Whisstock, J.C.1    Skinner, R.2    Carrell, R.W.3    Lesk, A.M.4
  • 116
    • 77955960141 scopus 로고    scopus 로고
    • Molecular contortionism - On the physical limits of serpin loop-sheet polymers
    • Huntington, J. A.; Whisstock, J. C. Molecular contortionism-on the physical limits of serpin loop-sheet polymers Biological Chem. 2010, 391 (8) 973-982
    • (2010) Biological Chem. , vol.391 , Issue.8 , pp. 973-982
    • Huntington, J.A.1    Whisstock, J.C.2
  • 117
    • 79954632232 scopus 로고    scopus 로고
    • Effects of glycosylation on the stability and flexibility of a metastable protein: The human serpin alpha(1)-antitrypsin
    • Sarkar, A.; Wintrode, P. L. Effects of glycosylation on the stability and flexibility of a metastable protein: the human serpin alpha(1)-antitrypsin Int. J. Mass Spectrom. 2011, 302 (1-3) 69-75
    • (2011) Int. J. Mass Spectrom. , vol.302 , Issue.13 , pp. 69-75
    • Sarkar, A.1    Wintrode, P.L.2
  • 118
    • 70349886556 scopus 로고    scopus 로고
    • Folding of glycoproteins: Toward understanding the biophysics of the glycosylation code
    • Shental-Bechor, D.; Levy, Y. Folding of glycoproteins: toward understanding the biophysics of the glycosylation code Curr. Opin. Struct. Biol. 2009, 19 (5) 524-33
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , Issue.5 , pp. 524-533
    • Shental-Bechor, D.1    Levy, Y.2
  • 119
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki, A. Biological roles of oligosaccharides: All of the theories are correct Glycobiology 1993, 3 (2) 97-130
    • (1993) Glycobiology , vol.3 , Issue.2 , pp. 97-130
    • Varki, A.1
  • 120
    • 0023588232 scopus 로고
    • Augmentation of lung antineutrophil elastase capacity with recombinant human alpha-1-antitrypsin
    • Casolaro, M. A.; Fells, G.; Wewers, M.; Pierce, J. E.; Ogushi, F.; Hubbard, R. Augmentation of lung antineutrophil elastase capacity with recombinant human alpha-1-antitrypsin J. Appl. Physiol 1987, 63 (5) 2015-23
    • (1987) J. Appl. Physiol , vol.63 , Issue.5 , pp. 2015-2023
    • Casolaro, M.A.1    Fells, G.2    Wewers, M.3    Pierce, J.E.4    Ogushi, F.5    Hubbard, R.6
  • 121
    • 0031008063 scopus 로고    scopus 로고
    • Effect of glycosylation on the stability of alpha1-antitrypsin toward urea denaturation and thermal deactivation
    • Kwon, K. S.; Yu, M. H. Effect of glycosylation on the stability of alpha1-antitrypsin toward urea denaturation and thermal deactivation Biochim. Biophys. Acta 1997, 1335 (3) 265-72
    • (1997) Biochim. Biophys. Acta , vol.1335 , Issue.3 , pp. 265-272
    • Kwon, K.S.1    Yu, M.H.2
  • 122
    • 0025278926 scopus 로고
    • Biosynthesis and secretion of M- and Z-type alpha 1-proteinase inhibitor by human monocytes. Effect of inhibitors of glycosylation and of oligosaccharide processing on secretion and function
    • Gross, V.; vom Berg, D.; Kreuzkamp, J.; Ganter, U.; Bauer, J.; Wurtemberger, G. Biosynthesis and secretion of M- and Z-type alpha 1-proteinase inhibitor by human monocytes. Effect of inhibitors of glycosylation and of oligosaccharide processing on secretion and function Biol. Chem. Hoppe-Seyler 1990, 371 (3) 231-238
    • (1990) Biol. Chem. Hoppe-Seyler , vol.371 , Issue.3 , pp. 231-238
    • Gross, V.1    Vom Berg, D.2    Kreuzkamp, J.3    Ganter, U.4    Bauer, J.5    Wurtemberger, G.6
  • 123
    • 84893876340 scopus 로고    scopus 로고
    • Increased Outer Arm and Core Fucose Residues on the N-Glycans of Mutated Alpha-1 Antitrypsin Protein from Alpha-1 Antitrypsin Deficient Individuals
    • McCarthy, C.; Saldova, R.; OBrien, M. E.; Bergin, D. A.; Carroll, T. P.; Keenan, J. Increased Outer Arm and Core Fucose Residues on the N-Glycans of Mutated Alpha-1 Antitrypsin Protein from Alpha-1 Antitrypsin Deficient Individuals J. Proteome Res. 2014, 13 (2) 596-605
    • (2014) J. Proteome Res. , vol.13 , Issue.2 , pp. 596-605
    • McCarthy, C.1    Saldova, R.2    Obrien, M.E.3    Bergin, D.A.4    Carroll, T.P.5    Keenan, J.6
  • 124
    • 84903751169 scopus 로고    scopus 로고
    • Antitrypsin inhibits leukotriene B4 neutrophil signalling through a mechanism that involves direct complexation of the two molecules
    • ODwyer, C. A. M.; Reeves, N. G.; Alpha-1, E. P. antitrypsin inhibits leukotriene B4 neutrophil signalling through a mechanism that involves direct complexation of the two molecules Am. J. Respir. Crit. Care Med. 2013, 187, A2741
    • (2013) Am. J. Respir. Crit. Care Med. , vol.187 , pp. 2741
    • Odwyer, C.A.M.1    Reeves, N.G.2    Alpha, E.P.3
  • 125
    • 84892546029 scopus 로고    scopus 로고
    • The Circulating Proteinase Inhibitor alpha-1 Antitrypsin Regulates Neutrophil Degranulation and Autoimmunity
    • Bergin, D. A.; Reeves, E. P.; Hurley, K.; Wolfe, R.; Jameel, R.; Fitzgerald, S. The Circulating Proteinase Inhibitor alpha-1 Antitrypsin Regulates Neutrophil Degranulation and Autoimmunity Sci. Transl. Med. 2014, 6 (217) 217ra1
    • (2014) Sci. Transl. Med. , vol.6 , Issue.217
    • Bergin, D.A.1    Reeves, E.P.2    Hurley, K.3    Wolfe, R.4    Jameel, R.5    Fitzgerald, S.6
  • 126
    • 33846907545 scopus 로고    scopus 로고
    • Alpha 1-antitrypsin inhalation reduces airway inflammation in cystic fibrosis patients
    • Griese, M.; Latzin, P.; Kappler, M.; Weckerle, K.; Heinzlmaier, T.; Bernhardt, T. Alpha 1-antitrypsin inhalation reduces airway inflammation in cystic fibrosis patients Eur. Respir. J. 2007, 29 (2) 240-250
    • (2007) Eur. Respir. J. , vol.29 , Issue.2 , pp. 240-250
    • Griese, M.1    Latzin, P.2    Kappler, M.3    Weckerle, K.4    Heinzlmaier, T.5    Bernhardt, T.6
  • 127
    • 79953250407 scopus 로고    scopus 로고
    • Alpha 1-antitrypsin enhances insulin secretion and prevents cytokine-mediated apoptosis in pancreatic beta-cells
    • Kalis, M.; Kumar, R.; Janciauskiene, S.; Salehi, A.; Cilio, C. M. Alpha 1-antitrypsin enhances insulin secretion and prevents cytokine-mediated apoptosis in pancreatic beta-cells Islets 2010, 2 (3) 185-189
    • (2010) Islets , vol.2 , Issue.3 , pp. 185-189
    • Kalis, M.1    Kumar, R.2    Janciauskiene, S.3    Salehi, A.4    Cilio, C.M.5
  • 128
    • 84858699084 scopus 로고    scopus 로고
    • Acute-phase protein alpha1-antitrypsin inhibits neutrophil calpain i and induces random migration
    • Al-Omari, M.; Korenbaum, E.; Ballmaier, M.; Lehmann, U.; Jonigk, D.; Manstein, D. J. Acute-phase protein alpha1-antitrypsin inhibits neutrophil calpain I and induces random migration Mol. Med. 2011, 17 (9-10) 865-874
    • (2011) Mol. Med. , vol.17 , Issue.910 , pp. 865-874
    • Al-Omari, M.1    Korenbaum, E.2    Ballmaier, M.3    Lehmann, U.4    Jonigk, D.5    Manstein, D.J.6
  • 130
    • 31544470902 scopus 로고    scopus 로고
    • Safety and efficacy of recombinant alpha(1)-antitrypsin therapy in cystic fibrosis
    • Martin, S. L.; Downey, D.; Bilton, D.; Keogan, M. T.; Edgar, J.; Elborn, J. S. Safety and efficacy of recombinant alpha(1)-antitrypsin therapy in cystic fibrosis Pediatr. Pulmonol. 2006, 41 (2) 177-183
    • (2006) Pediatr. Pulmonol. , vol.41 , Issue.2 , pp. 177-183
    • Martin, S.L.1    Downey, D.2    Bilton, D.3    Keogan, M.T.4    Edgar, J.5    Elborn, J.S.6
  • 132
    • 0024417082 scopus 로고
    • Crystal RG. Recombinant DNA-produced alpha 1-antitrypsin administered by aerosol augments lower respiratory tract antineutrophil elastase defenses in individuals with alpha 1-antitrypsin deficiency
    • Hubbard, R. C.; McElvaney, N. G.; Sellers, S. E.; Healy, J. T.; Czerski, D. B. Crystal RG. Recombinant DNA-produced alpha 1-antitrypsin administered by aerosol augments lower respiratory tract antineutrophil elastase defenses in individuals with alpha 1-antitrypsin deficiency J. Clin. Invest. 1989, 84 (4) 1349-1354
    • (1989) J. Clin. Invest. , vol.84 , Issue.4 , pp. 1349-1354
    • Hubbard, R.C.1    McElvaney, N.G.2    Sellers, S.E.3    Healy, J.T.4    Czerski, D.B.5
  • 133
    • 0024334846 scopus 로고
    • Interferon beta 2/interleukin 6 modulates synthesis of alpha 1-antitrypsin in human mononuclear phagocytes and in human hepatoma cells
    • Perlmutter, D. H.; May, L. T.; Sehgal, P. B. Interferon beta 2/interleukin 6 modulates synthesis of alpha 1-antitrypsin in human mononuclear phagocytes and in human hepatoma cells J. Clin. Invest. 1989, 84 (1) 138-144
    • (1989) J. Clin. Invest. , vol.84 , Issue.1 , pp. 138-144
    • Perlmutter, D.H.1    May, L.T.2    Sehgal, P.B.3
  • 135
    • 0023911386 scopus 로고
    • Elastase regulates the synthesis of its inhibitor, alpha 1-proteinase inhibitor, and exaggerates the defect in homozygous PiZZ alpha 1 PI deficiency
    • Perlmutter, D. H.; Travis, J.; Punsal, P. I. Elastase regulates the synthesis of its inhibitor, alpha 1-proteinase inhibitor, and exaggerates the defect in homozygous PiZZ alpha 1 PI deficiency J. Clin. Invest. 1988, 81 (6) 1774-1780
    • (1988) J. Clin. Invest. , vol.81 , Issue.6 , pp. 1774-1780
    • Perlmutter, D.H.1    Travis, J.2    Punsal, P.I.3
  • 136
    • 0031893793 scopus 로고    scopus 로고
    • Alpha 1-antitrypsin and protease complexation is induced by lipopolysaccharide, interleukin-1beta, and tumor necrosis factor-alpha in monocytes
    • Knoell, D. L.; Ralston, D. R.; Coulter, K. R.; Wewers, M. D. Alpha 1-antitrypsin and protease complexation is induced by lipopolysaccharide, interleukin-1beta, and tumor necrosis factor-alpha in monocytes Am. J. Resp. Crit. Care Med. 1998, 157 (1) 246-255
    • (1998) Am. J. Resp. Crit. Care Med. , vol.157 , Issue.1 , pp. 246-255
    • Knoell, D.L.1    Ralston, D.R.2    Coulter, K.R.3    Wewers, M.D.4
  • 137
    • 0032037476 scopus 로고    scopus 로고
    • Oncostatin M is a potent stimulator of alpha1-antitrypsin secretion in lung epithelial cells: Modulation by transforming growth factor-beta and interferon-gamma
    • Boutten, A.; Venembre, P.; Seta, N.; Hamelin, J.; Aubier, M.; Durand, G. Oncostatin M is a potent stimulator of alpha1-antitrypsin secretion in lung epithelial cells: modulation by transforming growth factor-beta and interferon-gamma Am. J. Respir. Cell Mol. Biol. 1998, 18 (4) 511-520
    • (1998) Am. J. Respir. Cell Mol. Biol. , vol.18 , Issue.4 , pp. 511-520
    • Boutten, A.1    Venembre, P.2    Seta, N.3    Hamelin, J.4    Aubier, M.5    Durand, G.6
  • 138
    • 0026557212 scopus 로고
    • Different capabilities of monocytes from patients with systemic lupus erythematosus and rheumatoid arthritis to induce glycosylation alterations of acute phase proteins in vitro
    • Mackiewicz, A.; Sobieska, M.; Kapcinska, M.; Mackiewicz, S. H.; Wiktorowicz, K. E.; Pawlowski, T. Different capabilities of monocytes from patients with systemic lupus erythematosus and rheumatoid arthritis to induce glycosylation alterations of acute phase proteins in vitro Ann. Rheum. Dis. 1992, 51 (1) 67-72
    • (1992) Ann. Rheum. Dis. , vol.51 , Issue.1 , pp. 67-72
    • Mackiewicz, A.1    Sobieska, M.2    Kapcinska, M.3    Mackiewicz, S.H.4    Wiktorowicz, K.E.5    Pawlowski, T.6
  • 139
    • 0025201215 scopus 로고
    • Changes in the serum concentration and the glycosylation of human alpha 1-acid glycoprotein and alpha 1-protease inhibitor in severely burned persons: Relation to interleukin-6 levels
    • Pos, O.; van der Stelt, M. E.; Wolbink, G. J.; Nijsten, M. W.; van der Tempel, G. L.; van Dijk, W. Changes in the serum concentration and the glycosylation of human alpha 1-acid glycoprotein and alpha 1-protease inhibitor in severely burned persons: relation to interleukin-6 levels Clin. Exp. Immunol. 1990, 82 (3) 579-582
    • (1990) Clin. Exp. Immunol. , vol.82 , Issue.3 , pp. 579-582
    • Pos, O.1    Van Der Stelt, M.E.2    Wolbink, G.J.3    Nijsten, M.W.4    Van Der Tempel, G.L.5    Van Dijk, W.6
  • 140
    • 0026632640 scopus 로고
    • Soluble human interleukin-6-receptor modulates interleukin-6-dependent N-glycosylation of alpha 1-protease inhibitor secreted by HepG2 cells
    • Mackiewicz, A.; Rose-John, S.; Schooltink, H.; Laciak, M.; Gorny, A.; Heinrich, P. C. Soluble human interleukin-6-receptor modulates interleukin-6-dependent N-glycosylation of alpha 1-protease inhibitor secreted by HepG2 cells FEBS Lett. 1992, 306 (2-3) 257-261
    • (1992) FEBS Lett. , vol.306 , Issue.23 , pp. 257-261
    • Mackiewicz, A.1    Rose-John, S.2    Schooltink, H.3    Laciak, M.4    Gorny, A.5    Heinrich, P.C.6
  • 141
    • 0032429592 scopus 로고    scopus 로고
    • Changes of glycosylation of serum proteins in psoriatic arthritis, studied by enzyme-linked lectin assay (ELLA), using concanavalin A
    • Saso, L.; Valentini, G.; Giardino, A. M.; Spadaro, A.; Riccieri, V.; Zoppini, A. Changes of glycosylation of serum proteins in psoriatic arthritis, studied by enzyme-linked lectin assay (ELLA), using concanavalin A Biochem. Mol. Biol. Int. 1998, 46 (5) 867-875
    • (1998) Biochem. Mol. Biol. Int. , vol.46 , Issue.5 , pp. 867-875
    • Saso, L.1    Valentini, G.2    Giardino, A.M.3    Spadaro, A.4    Riccieri, V.5    Zoppini, A.6
  • 142
    • 0027280688 scopus 로고
    • Leukemia inhibitory factor, interferon gamma and dexamethasone regulate N-glycosylation of alpha 1-protease inhibitor in human hepatoma cells
    • Mackiewicz, A.; Laciak, M.; Gorny, A.; Baumann, H. Leukemia inhibitory factor, interferon gamma and dexamethasone regulate N-glycosylation of alpha 1-protease inhibitor in human hepatoma cells Eur. J. Cell Biol. 1993, 60 (2) 331-336
    • (1993) Eur. J. Cell Biol. , vol.60 , Issue.2 , pp. 331-336
    • Mackiewicz, A.1    Laciak, M.2    Gorny, A.3    Baumann, H.4
  • 143
    • 20144384634 scopus 로고    scopus 로고
    • Acute phase mediator oncostatin M regulates affinity of alpha1-protease inhibitor for concanavalin A in hepatoma-derived but not lung-derived epithelial cells
    • Kulig, P.; Cichy, J. Acute phase mediator oncostatin M regulates affinity of alpha1-protease inhibitor for concanavalin A in hepatoma-derived but not lung-derived epithelial cells Cytokine 2005, 30 (5) 269-274
    • (2005) Cytokine , vol.30 , Issue.5 , pp. 269-274
    • Kulig, P.1    Cichy, J.2
  • 144
    • 0027326640 scopus 로고
    • Properties of alpha 1-antitrypsin secreted by human adenocarcinoma cell lines
    • Kataoka, H.; Seguchi, K.; Inoue, T.; Koono, M. Properties of alpha 1-antitrypsin secreted by human adenocarcinoma cell lines FEBS Lett. 1993, 328 (3) 291-295
    • (1993) FEBS Lett. , vol.328 , Issue.3 , pp. 291-295
    • Kataoka, H.1    Seguchi, K.2    Inoue, T.3    Koono, M.4
  • 145
    • 50449083310 scopus 로고    scopus 로고
    • Evaluation of the serum N-linked glycome for the diagnosis of cancer and chronic inflammation
    • Arnold, J. N.; Saldova, R.; Hamid, U. M.; Rudd, P. M. Evaluation of the serum N-linked glycome for the diagnosis of cancer and chronic inflammation Proteomics 2008, 8 (16) 3284-3293
    • (2008) Proteomics , vol.8 , Issue.16 , pp. 3284-3293
    • Arnold, J.N.1    Saldova, R.2    Hamid, U.M.3    Rudd, P.M.4
  • 146
    • 0018120654 scopus 로고
    • Altered carbohydrate content of alpha1-antitrypsin in patients with cancer
    • Rostenberg, I.; Guizar-Vazquez, J.; Penaloza, R. Altered carbohydrate content of alpha1-antitrypsin in patients with cancer J. Natl. Cancer Inst. 1978, 61 (4) 961-965
    • (1978) J. Natl. Cancer Inst. , vol.61 , Issue.4 , pp. 961-965
    • Rostenberg, I.1    Guizar-Vazquez, J.2    Penaloza, R.3
  • 147
    • 57049137606 scopus 로고    scopus 로고
    • A strategy to reveal potential glycan markers from serum glycoproteins associated with breast cancer progression
    • Abd Hamid, U. M.; Royle, L.; Saldova, R.; Radcliffe, C. M.; Harvey, D. J.; Storr, S. J. A strategy to reveal potential glycan markers from serum glycoproteins associated with breast cancer progression Glycobiology 2008, 18 (12) 1105-1118
    • (2008) Glycobiology , vol.18 , Issue.12 , pp. 1105-1118
    • Abd Hamid, U.M.1    Royle, L.2    Saldova, R.3    Radcliffe, C.M.4    Harvey, D.J.5    Storr, S.J.6
  • 148
    • 1342287837 scopus 로고    scopus 로고
    • Role of imbalance between neutrophil elastase and alpha 1-antitrypsin in cancer development and progression
    • Sun, Z.; Yang, P. Role of imbalance between neutrophil elastase and alpha 1-antitrypsin in cancer development and progression Lancet Oncol. 2004, 5 (3) 182-190
    • (2004) Lancet Oncol. , vol.5 , Issue.3 , pp. 182-190
    • Sun, Z.1    Yang, P.2
  • 149
    • 22244461873 scopus 로고    scopus 로고
    • Alpha1-antitrypsin and neutrophil elastase imbalance and lung cancer risk
    • Yang, P.; Bamlet, W. R.; Sun, Z.; Ebbert, J. O.; Aubry, M. C.; Krowka, M. J. Alpha1-antitrypsin and neutrophil elastase imbalance and lung cancer risk Chest 2005, 128 (1) 445-452
    • (2005) Chest , vol.128 , Issue.1 , pp. 445-452
    • Yang, P.1    Bamlet, W.R.2    Sun, Z.3    Ebbert, J.O.4    Aubry, M.C.5    Krowka, M.J.6
  • 152
    • 83055196734 scopus 로고    scopus 로고
    • Therapeutic target-site variability in alpha1-antitrypsin characterized at high resolution
    • Patschull, A. O.; Segu, L.; Nyon, M. P.; Lomas, D. A.; Nobeli, I.; Barrett, T. E. Therapeutic target-site variability in alpha1-antitrypsin characterized at high resolution Acta Crystallogr. Sect. F 2011, 67 (Pt 12) 1492-7
    • (2011) Acta Crystallogr. Sect. F , vol.67 , Issue.PART 12 , pp. 1492-1497
    • Patschull, A.O.1    Segu, L.2    Nyon, M.P.3    Lomas, D.A.4    Nobeli, I.5    Barrett, T.E.6
  • 153
    • 0036462598 scopus 로고    scopus 로고
    • Conformational studies of oligosaccharides and glycopeptides: Complementarity of NMR, X-ray crystallography, and molecular modelling
    • Wormald, M. R.; Petrescu, A. J.; Pao, Y. L.; Glithero, A.; Elliott, T.; Dwek, R. A. Conformational studies of oligosaccharides and glycopeptides: complementarity of NMR, X-ray crystallography, and molecular modelling Chem. Rev. 2002, 102 (2) 371-86
    • (2002) Chem. Rev. , vol.102 , Issue.2 , pp. 371-386
    • Wormald, M.R.1    Petrescu, A.J.2    Pao, Y.L.3    Glithero, A.4    Elliott, T.5    Dwek, R.A.6
  • 154
    • 1342327544 scopus 로고    scopus 로고
    • Statistical analysis of the protein environment of N-glycosylation sites: Implications for occupancy, structure, and folding
    • Petrescu, A. J.; Milac, A. L.; Petrescu, S. M.; Dwek, R. A.; Wormald, M. R. Statistical analysis of the protein environment of N-glycosylation sites: implications for occupancy, structure, and folding Glycobiology 2004, 14 (2) 103-14
    • (2004) Glycobiology , vol.14 , Issue.2 , pp. 103-114
    • Petrescu, A.J.1    Milac, A.L.2    Petrescu, S.M.3    Dwek, R.A.4    Wormald, M.R.5
  • 157
    • 23844520619 scopus 로고    scopus 로고
    • Glycosylation of site-specific glycans of alpha1-acid glycoprotein and alterations in acute and chronic inflammation
    • Higai, K.; Aoki, Y.; Azuma, Y.; Matsumoto, K. Glycosylation of site-specific glycans of alpha1-acid glycoprotein and alterations in acute and chronic inflammation Biochim. Biophys. Acta 2005, 1725 (1) 128-35
    • (2005) Biochim. Biophys. Acta , vol.1725 , Issue.1 , pp. 128-135
    • Higai, K.1    Aoki, Y.2    Azuma, Y.3    Matsumoto, K.4
  • 158
    • 0037365579 scopus 로고    scopus 로고
    • Altered glycosylation of alpha1-acid glycoprotein in patients with inflammation and diabetes mellitus
    • Higai, K.; Azuma, Y.; Aoki, Y.; Matsumoto, K. Altered glycosylation of alpha1-acid glycoprotein in patients with inflammation and diabetes mellitus Clin. Chim. Acta 2003, 329 (1-2) 117-125
    • (2003) Clin. Chim. Acta , vol.329 , Issue.12 , pp. 117-125
    • Higai, K.1    Azuma, Y.2    Aoki, Y.3    Matsumoto, K.4
  • 159
    • 0031809628 scopus 로고    scopus 로고
    • Inflammation-induced expression of sialyl LewisX is not restricted to alpha1-acid glycoprotein but also occurs to a lesser extent on alpha1-antichymotrypsin and haptoglobin
    • Brinkman-van der Linden, E. C.; de Haan, P. F.; Havenaar, E. C.; van Dijk, W. Inflammation-induced expression of sialyl LewisX is not restricted to alpha1-acid glycoprotein but also occurs to a lesser extent on alpha1-antichymotrypsin and haptoglobin Glycoconjugate J. 1998, 15 (2) 177-182
    • (1998) Glycoconjugate J. , vol.15 , Issue.2 , pp. 177-182
    • Brinkman-Van Der Linden, E.C.1    De Haan, P.F.2    Havenaar, E.C.3    Van Dijk, W.4
  • 161
    • 36248972262 scopus 로고    scopus 로고
    • Ovarian cancer is associated with changes in glycosylation in both acute-phase proteins and IgG
    • Saldova, R.; Royle, L.; Radcliffe, C. M.; Abd Hamid, U. M.; Evans, R.; Arnold, J. N. Ovarian cancer is associated with changes in glycosylation in both acute-phase proteins and IgG Glycobiology 2007, 17 (12) 1344-1356
    • (2007) Glycobiology , vol.17 , Issue.12 , pp. 1344-1356
    • Saldova, R.1    Royle, L.2    Radcliffe, C.M.3    Abd Hamid, U.M.4    Evans, R.5    Arnold, J.N.6
  • 163
    • 36749058881 scopus 로고    scopus 로고
    • Glycosylation status of haptoglobin in sera of patients with prostate cancer vs benign prostate disease or normal subjects
    • Fujimura, T.; Shinohara, Y.; Tissot, B.; Pang, P. C.; Kurogochi, M.; Saito, S. Glycosylation status of haptoglobin in sera of patients with prostate cancer vs. benign prostate disease or normal subjects Int. J. Cancer 2008, 122 (1) 39-49
    • (2008) Int. J. Cancer , vol.122 , Issue.1 , pp. 39-49
    • Fujimura, T.1    Shinohara, Y.2    Tissot, B.3    Pang, P.C.4    Kurogochi, M.5    Saito, S.6
  • 164
    • 36049038546 scopus 로고    scopus 로고
    • Haptoglobin and posttranslational glycan-modified derivatives as serum biomarkers for the diagnosis of nonsmall cell lung cancer
    • Hoagland, L., 4th; Campa, M. J.; Gottlin, E. B.; Herndon, J. E., 2nd; Patz, E. F., Jr. Haptoglobin and posttranslational glycan-modified derivatives as serum biomarkers for the diagnosis of nonsmall cell lung cancer Cancer 2007, 110 (10) 2260-8
    • (2007) Cancer , vol.110 , Issue.10 , pp. 2260-2268
    • Hoagland IV, H.L.1    Campa, M.J.2    Gottlin, E.B.3    Herndon II, E.H.J.4    Patz Jr., E.F.5
  • 165
    • 33646343959 scopus 로고    scopus 로고
    • Fucosylated haptoglobin is a novel marker for pancreatic cancer: A detailed analysis of the oligosaccharide structure and a possible mechanism for fucosylation
    • Okuyama, N.; Ide, Y.; Nakano, M.; Nakagawa, T.; Yamanaka, K.; Moriwaki, K. Fucosylated haptoglobin is a novel marker for pancreatic cancer: A detailed analysis of the oligosaccharide structure and a possible mechanism for fucosylation Int. J. Cancer 2006, 118 (11) 2803-2808
    • (2006) Int. J. Cancer , vol.118 , Issue.11 , pp. 2803-2808
    • Okuyama, N.1    Ide, Y.2    Nakano, M.3    Nakagawa, T.4    Yamanaka, K.5    Moriwaki, K.6
  • 166
    • 42149132652 scopus 로고    scopus 로고
    • Site-specific analysis of N-glycans on haptoglobin in sera of patients with pancreatic cancer: A novel approach for the development of tumor markers
    • Nakano, M.; Nakagawa, T.; Ito, T.; Kitada, T.; Hijioka, T.; Kasahara, A. Site-specific analysis of N-glycans on haptoglobin in sera of patients with pancreatic cancer: A novel approach for the development of tumor markers Int. J. Cancer 2008, 122 (10) 2301-2309
    • (2008) Int. J. Cancer , vol.122 , Issue.10 , pp. 2301-2309
    • Nakano, M.1    Nakagawa, T.2    Ito, T.3    Kitada, T.4    Hijioka, T.5    Kasahara, A.6
  • 167
    • 0026664939 scopus 로고
    • Increased fucosylation and other carbohydrate changes in haptoglobin in ovarian cancer
    • Thompson, S.; Dargan, E.; Turner, G. A. Increased fucosylation and other carbohydrate changes in haptoglobin in ovarian cancer Cancer Lett. 1992, 66 (1) 43-48
    • (1992) Cancer Lett. , vol.66 , Issue.1 , pp. 43-48
    • Thompson, S.1    Dargan, E.2    Turner, G.A.3
  • 168
    • 0023640202 scopus 로고
    • Elevated levels of abnormally-fucosylated haptoglobins in cancer sera
    • Thompson, S.; Turner, G. A. Elevated levels of abnormally-fucosylated haptoglobins in cancer sera Br J. Cancer. 1987, 56 (5) 605-610
    • (1987) Br J. Cancer. , vol.56 , Issue.5 , pp. 605-610
    • Thompson, S.1    Turner, G.A.2
  • 169
    • 0028827236 scopus 로고
    • Haptoglobin. A potential reporter molecule for glycosylation changes in disease
    • Turner, G. A. Haptoglobin. A potential reporter molecule for glycosylation changes in disease Adv. Exp. Med. Biol. 1995, 376, 231-238
    • (1995) Adv. Exp. Med. Biol. , vol.376 , pp. 231-238
    • Turner, G.A.1
  • 170
    • 0029001779 scopus 로고
    • Decreased branching, increased fucosylation and changed sialylation of alpha-1-proteinase inhibitor in breast and ovarian cancer
    • Goodarzi, M. T.; Turner, G. A. Decreased branching, increased fucosylation and changed sialylation of alpha-1-proteinase inhibitor in breast and ovarian cancer Clin. Chim. Acta 1995, 236 (2) 161-171
    • (1995) Clin. Chim. Acta , vol.236 , Issue.2 , pp. 161-171
    • Goodarzi, M.T.1    Turner, G.A.2
  • 172
    • 0028292786 scopus 로고
    • Differential recognition by conglutinin and mannan-binding protein of N -glycans presented on neoglycolipids and glycoproteins with special reference to complement glycoprotein C3 and ribonuclease B
    • Solis, D.; Feizi, T.; Yuen, C. T.; Lawson, A. M.; Harrison, R. A.; Loveless, R. W. Differential recognition by conglutinin and mannan-binding protein of N -glycans presented on neoglycolipids and glycoproteins with special reference to complement glycoprotein C3 and ribonuclease B J. Biol. Chem. 1994, 269 (15) 11555-62
    • (1994) J. Biol. Chem. , vol.269 , Issue.15 , pp. 11555-11562
    • Solis, D.1    Feizi, T.2    Yuen, C.T.3    Lawson, A.M.4    Harrison, R.A.5    Loveless, R.W.6
  • 173
    • 2442487932 scopus 로고    scopus 로고
    • Monoglucosylated glycans in the secreted human complement component C3: Implications for protein biosynthesis and structure
    • Crispin, M. D.; Ritchie, G. E.; Critchley, A. J.; Morgan, B. P.; Wilson, I. A.; Dwek, R. A. Monoglucosylated glycans in the secreted human complement component C3: Implications for protein biosynthesis and structure FEBS Lett. 2004, 566 (1-3) 270-274
    • (2004) FEBS Lett. , vol.566 , Issue.13 , pp. 270-274
    • Crispin, M.D.1    Ritchie, G.E.2    Critchley, A.J.3    Morgan, B.P.4    Wilson, I.A.5    Dwek, R.A.6
  • 174
    • 84859862380 scopus 로고    scopus 로고
    • Human urinary glycoproteomics; Attachment site specific analysis of N- and O-linked glycosylations by CID and ECD
    • 013649
    • Halim, A.; Nilsson, J.; Ruetschi, U.; Hesse, C.; Larson, G. Human urinary glycoproteomics; attachment site specific analysis of N- and O-linked glycosylations by CID and ECD Mol. Cell. Proteomics 2012, 11 (4) M111 013649
    • (2012) Mol. Cell. Proteomics , vol.11 , Issue.4 , pp. 111
    • Halim, A.1    Nilsson, J.2    Ruetschi, U.3    Hesse, C.4    Larson, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.