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Volumn 39, Issue 4, 2012, Pages 420-427

Anti-GalNAcβ: A novel anti-glycan autoantibody associated with pregnancy loss in women with antiphospholipid syndrome and in a mouse experimental model

Author keywords

Autoimmunity; Experimental model; Galectins; Metalloproteinase

Indexed keywords

AUTOANTIBODY; GALNACBETA ANTIBODY; GELATINASE A; GELATINASE B; GLYCAN ANTIBODY; N ACETYL BETA DEXTRO GLUCOSAMINE ANTIBODY; UNCLASSIFIED DRUG;

EID: 84869868757     PISSN: 08968411     EISSN: 10959157     Source Type: Journal    
DOI: 10.1016/j.jaut.2012.07.002     Document Type: Article
Times cited : (8)

References (50)
  • 1
    • 28544444249 scopus 로고    scopus 로고
    • Glycomics: an integrated systems approach to structure-function relationships of glycans
    • Raman R., Raguram S., Venkataraman G., Paulson J.C., Sasisekharan R. Glycomics: an integrated systems approach to structure-function relationships of glycans. Nat Methods 2005, 2:817-824.
    • (2005) Nat Methods , vol.2 , pp. 817-824
    • Raman, R.1    Raguram, S.2    Venkataraman, G.3    Paulson, J.C.4    Sasisekharan, R.5
  • 2
    • 0036895610 scopus 로고    scopus 로고
    • Peripheral neuropathies and anti-glycolipid antibodies
    • Willison H.J., Yuki N. Peripheral neuropathies and anti-glycolipid antibodies. Brain 2002, 125:2591-2625.
    • (2002) Brain , vol.125 , pp. 2591-2625
    • Willison, H.J.1    Yuki, N.2
  • 3
    • 0014008734 scopus 로고
    • Blood-group substances
    • Watkins W.M. Blood-group substances. Science 1966, 152:172-181.
    • (1966) Science , vol.152 , pp. 172-181
    • Watkins, W.M.1
  • 4
    • 22944476837 scopus 로고    scopus 로고
    • The alpha-gal epitope and the anti-Gal antibody in xenotransplantation and in cancer immunotherapy
    • Galili U. The alpha-gal epitope and the anti-Gal antibody in xenotransplantation and in cancer immunotherapy. Immunol Cell Biol 2005, 83:674-686.
    • (2005) Immunol Cell Biol , vol.83 , pp. 674-686
    • Galili, U.1
  • 5
    • 0030852709 scopus 로고    scopus 로고
    • Heterogeneity of human anti-pig natural antibodies cross-reactive with the Gal(alpha1,3)Galactose epitope
    • McMorrow I.M., Comrack C.A., Sachs D.H., DerSimonian H. Heterogeneity of human anti-pig natural antibodies cross-reactive with the Gal(alpha1,3)Galactose epitope. Transplantation 1997, 64:501-510.
    • (1997) Transplantation , vol.64 , pp. 501-510
    • McMorrow, I.M.1    Comrack, C.A.2    Sachs, D.H.3    DerSimonian, H.4
  • 6
    • 23244466720 scopus 로고    scopus 로고
    • Antibody responses against galactocerebroside are potential stage-specific biomarkers in multiple sclerosis
    • Menge T., Lalive P.H., von Budingen H.C., Cree B., Hauser S.L., Genain C.P. Antibody responses against galactocerebroside are potential stage-specific biomarkers in multiple sclerosis. J Allergy Clin Immunol 2005, 116:453-459.
    • (2005) J Allergy Clin Immunol , vol.116 , pp. 453-459
    • Menge, T.1    Lalive, P.H.2    von Budingen, H.C.3    Cree, B.4    Hauser, S.L.5    Genain, C.P.6
  • 7
    • 70449632139 scopus 로고    scopus 로고
    • Serum anti-GAGA4 IgM antibodies differentiate relapsing remitting and secondary progressive multiple sclerosis from primary progressive multiple sclerosis and other neurological diseases
    • Brettschneider J., Jaskowski T.D., Tumani H., Abdul S., Husebye D., Seraj H., et al. Serum anti-GAGA4 IgM antibodies differentiate relapsing remitting and secondary progressive multiple sclerosis from primary progressive multiple sclerosis and other neurological diseases. J Neuroimmunol 2009, 217:95-101.
    • (2009) J Neuroimmunol , vol.217 , pp. 95-101
    • Brettschneider, J.1    Jaskowski, T.D.2    Tumani, H.3    Abdul, S.4    Husebye, D.5    Seraj, H.6
  • 8
    • 63449126296 scopus 로고    scopus 로고
    • Anti-alpha-glucose-based glycan IgM antibodies predict relapse activity in multiple sclerosis after the first neurological event
    • Freedman M.S., Laks J., Dotan N., Altstock R.T., Dukler A., Sindic C.J. Anti-alpha-glucose-based glycan IgM antibodies predict relapse activity in multiple sclerosis after the first neurological event. Mult Scler 2009, 15:422-430.
    • (2009) Mult Scler , vol.15 , pp. 422-430
    • Freedman, M.S.1    Laks, J.2    Dotan, N.3    Altstock, R.T.4    Dukler, A.5    Sindic, C.J.6
  • 9
    • 0035127074 scopus 로고    scopus 로고
    • Comparative study of ASCA (Anti-Saccharomyces cerevisiae antibody) assays in inflammatory bowel disease
    • Vermeire S., Joossens S., Peeters M., Monsuur F., Marien G., Bossuyt X., et al. Comparative study of ASCA (Anti-Saccharomyces cerevisiae antibody) assays in inflammatory bowel disease. Gastroenterology 2001, 120:827-833.
    • (2001) Gastroenterology , vol.120 , pp. 827-833
    • Vermeire, S.1    Joossens, S.2    Peeters, M.3    Monsuur, F.4    Marien, G.5    Bossuyt, X.6
  • 10
    • 0036656503 scopus 로고    scopus 로고
    • Anti-Saccharomyces cerevisiae antibodies-a novel serologic marker for Behcet's disease
    • Krause I., Monselise Y., Milo G., Weinberger A. Anti-Saccharomyces cerevisiae antibodies-a novel serologic marker for Behcet's disease. Clin Exp Rheumatol 2002, 20:S21-S24.
    • (2002) Clin Exp Rheumatol , vol.20
    • Krause, I.1    Monselise, Y.2    Milo, G.3    Weinberger, A.4
  • 11
    • 33745632627 scopus 로고    scopus 로고
    • Overlapping humoral autoimmunity links rheumatic fever and the antiphospholipid syndrome
    • Blank M., Krause I., Magrini L., Spina G., Kalil J., Jacobsen S., et al. Overlapping humoral autoimmunity links rheumatic fever and the antiphospholipid syndrome. Rheumatology (Oxford) 2006, 45:833-841.
    • (2006) Rheumatology (Oxford) , vol.45 , pp. 833-841
    • Blank, M.1    Krause, I.2    Magrini, L.3    Spina, G.4    Kalil, J.5    Jacobsen, S.6
  • 12
    • 0036228886 scopus 로고    scopus 로고
    • Antiphospholipid syndrome: clinical and immunologic manifestations and patterns of disease expression in a cohort of 1,000 patients
    • Cervera R., Piette J.C., Font J., Khamashta M.A., Shoenfeld Y., Camps M.T., et al. Antiphospholipid syndrome: clinical and immunologic manifestations and patterns of disease expression in a cohort of 1,000 patients. Arthritis Rheum 2002, 46:1019-1027.
    • (2002) Arthritis Rheum , vol.46 , pp. 1019-1027
    • Cervera, R.1    Piette, J.C.2    Font, J.3    Khamashta, M.A.4    Shoenfeld, Y.5    Camps, M.T.6
  • 14
    • 0038714974 scopus 로고    scopus 로고
    • Systemic antiphospholipid syndrome
    • Shoenfeld Y. Systemic antiphospholipid syndrome. Lupus 2003, 12:497-498.
    • (2003) Lupus , vol.12 , pp. 497-498
    • Shoenfeld, Y.1
  • 15
    • 70349880351 scopus 로고    scopus 로고
    • Mechanisms of antiphospholipid antibody-associated pregnancy complications
    • Abrahams V.M. Mechanisms of antiphospholipid antibody-associated pregnancy complications. Thromb Res 2009, 124:521-525.
    • (2009) Thromb Res , vol.124 , pp. 521-525
    • Abrahams, V.M.1
  • 16
    • 73949110131 scopus 로고    scopus 로고
    • Is obstetric antiphospholipid syndrome a primary nonthrombotic, proinflammatory, complement-mediated disorder related to antiphospholipid antibodies?
    • Alijotas-Reig J., Vilardell-Tarres M. Is obstetric antiphospholipid syndrome a primary nonthrombotic, proinflammatory, complement-mediated disorder related to antiphospholipid antibodies?. Obstet Gynecol Surv 2010, 65:39-45.
    • (2010) Obstet Gynecol Surv , vol.65 , pp. 39-45
    • Alijotas-Reig, J.1    Vilardell-Tarres, M.2
  • 17
    • 79958086576 scopus 로고    scopus 로고
    • Pathogenesis of antiphospholipid syndrome: understanding the antibodies
    • Meroni P.L., Borghi M.O., Raschi E., Tedesco F. Pathogenesis of antiphospholipid syndrome: understanding the antibodies. Nat Rev Rheumatol 2011, 7:330-339.
    • (2011) Nat Rev Rheumatol , vol.7 , pp. 330-339
    • Meroni, P.L.1    Borghi, M.O.2    Raschi, E.3    Tedesco, F.4
  • 18
    • 84871100965 scopus 로고    scopus 로고
    • Anti-phospholipid induced murine fetal loss: novel protective effect of a peptide targeting the beta2 glycoprotein I phospholipid-binding site. Implications for human fetal loss
    • [Epub ahead of print]
    • Martinez de la Torre Y., Pregnolato F., D'Amelio F., Grossi C., Di Simone N., Pasqualini F., et al. Anti-phospholipid induced murine fetal loss: novel protective effect of a peptide targeting the beta2 glycoprotein I phospholipid-binding site. Implications for human fetal loss. J Autoimmun 2011, [Epub ahead of print].
    • (2011) J Autoimmun
    • Martinez de la Torre, Y.1    Pregnolato, F.2    D'Amelio, F.3    Grossi, C.4    Di Simone, N.5    Pasqualini, F.6
  • 19
    • 14144253793 scopus 로고    scopus 로고
    • Pathogenic role of anti-beta 2-glycoprotein I antibodies in antiphospholipid associated fetal loss: characterisation of beta 2-glycoprotein I binding to trophoblast cells and functional effects of anti-beta 2-glycoprotein I antibodies in vitro
    • Di Simone N., Raschi E., Testoni C., Castellani R., D'Asta M., Shi T., et al. Pathogenic role of anti-beta 2-glycoprotein I antibodies in antiphospholipid associated fetal loss: characterisation of beta 2-glycoprotein I binding to trophoblast cells and functional effects of anti-beta 2-glycoprotein I antibodies in vitro. Ann Rheum Dis 2005, 64:462-467.
    • (2005) Ann Rheum Dis , vol.64 , pp. 462-467
    • Di Simone, N.1    Raschi, E.2    Testoni, C.3    Castellani, R.4    D'Asta, M.5    Shi, T.6
  • 21
    • 0034121236 scopus 로고    scopus 로고
    • Antiphospholipid antibodies affect trophoblast gonadotropin secretion and invasiveness by binding directly and through adhered beta2-glycoprotein I
    • Di Simone N., Meroni P.L., de Papa N., Raschi E., Caliandro D., De Carolis C.S., et al. Antiphospholipid antibodies affect trophoblast gonadotropin secretion and invasiveness by binding directly and through adhered beta2-glycoprotein I. Arthritis Rheum 2000, 43:140-150.
    • (2000) Arthritis Rheum , vol.43 , pp. 140-150
    • Di Simone, N.1    Meroni, P.L.2    de Papa, N.3    Raschi, E.4    Caliandro, D.5    De Carolis, C.S.6
  • 23
    • 34948873645 scopus 로고    scopus 로고
    • Cross reactive epitopes on beta2-glycoprotein-I and Saccharomyces cerevisiae in patients with the antiphospholipid syndrome
    • Krause I., Blank M., Cervera R., Font J., Matthias T., Pfeiffer S., et al. Cross reactive epitopes on beta2-glycoprotein-I and Saccharomyces cerevisiae in patients with the antiphospholipid syndrome. Ann N Y Acad Sci 2007, 1108:481-488.
    • (2007) Ann N Y Acad Sci , vol.1108 , pp. 481-488
    • Krause, I.1    Blank, M.2    Cervera, R.3    Font, J.4    Matthias, T.5    Pfeiffer, S.6
  • 24
    • 33344458573 scopus 로고    scopus 로고
    • International consensus statement on an update of the classification criteria for definite antiphospholipid syndrome (APS)
    • Miyakis S., Lockshin M.D., Atsumi T., Branch D.W., Brey R.L., Cervera R., et al. International consensus statement on an update of the classification criteria for definite antiphospholipid syndrome (APS). J Thromb Haemost 2006, 4:295-306.
    • (2006) J Thromb Haemost , vol.4 , pp. 295-306
    • Miyakis, S.1    Lockshin, M.D.2    Atsumi, T.3    Branch, D.W.4    Brey, R.L.5    Cervera, R.6
  • 25
    • 0026322836 scopus 로고
    • Induction of anti-phospholipid syndrome in naive mice with mouse lupus monoclonal and human polyclonal anti-cardiolipin antibodies
    • Blank M., Cohen J., Toder V., Shoenfeld Y. Induction of anti-phospholipid syndrome in naive mice with mouse lupus monoclonal and human polyclonal anti-cardiolipin antibodies. Proc Natl Acad Sci U S A 1991, 88:3069-3073.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 3069-3073
    • Blank, M.1    Cohen, J.2    Toder, V.3    Shoenfeld, Y.4
  • 27
    • 0037634222 scopus 로고    scopus 로고
    • Differential activity of the gelatinases (matrix metalloproteinases 2 and 9) in the fetal membranes and decidua, associated with labour
    • Goldman S., Weiss A., Eyali V., Shalev E. Differential activity of the gelatinases (matrix metalloproteinases 2 and 9) in the fetal membranes and decidua, associated with labour. Mol Hum Reprod 2003, 9:367-373.
    • (2003) Mol Hum Reprod , vol.9 , pp. 367-373
    • Goldman, S.1    Weiss, A.2    Eyali, V.3    Shalev, E.4
  • 29
    • 0028158771 scopus 로고
    • Anticardiolipin antibodies recognize beta 2-glycoprotein I structure altered by interacting with an oxygen modified solid phase surface
    • Matsuura E., Igarashi Y., Yasuda T., Triplett D.A., Koike T. Anticardiolipin antibodies recognize beta 2-glycoprotein I structure altered by interacting with an oxygen modified solid phase surface. J Exp Med 1994, 179:457-462.
    • (1994) J Exp Med , vol.179 , pp. 457-462
    • Matsuura, E.1    Igarashi, Y.2    Yasuda, T.3    Triplett, D.A.4    Koike, T.5
  • 30
    • 33344456904 scopus 로고    scopus 로고
    • Pathogenic anti-beta2-glycoprotein I antibodies recognize domain I of beta2-glycoprotein I only after a conformational change
    • de Laat B., Derksen R.H., van Lummel M., Pennings M.T., de Groot P.G. Pathogenic anti-beta2-glycoprotein I antibodies recognize domain I of beta2-glycoprotein I only after a conformational change. Blood 2006, 107:1916-1924.
    • (2006) Blood , vol.107 , pp. 1916-1924
    • de Laat, B.1    Derksen, R.H.2    van Lummel, M.3    Pennings, M.T.4    de Groot, P.G.5
  • 31
    • 0036351974 scopus 로고    scopus 로고
    • Solution structure of human and bovine beta(2)-glycoprotein I revealed by small-angle X-ray scattering
    • Hammel M., Kriechbaum M., Gries A., Kostner G.M., Laggner P., Prassl R. Solution structure of human and bovine beta(2)-glycoprotein I revealed by small-angle X-ray scattering. J Mol Biol 2002, 321:85-97.
    • (2002) J Mol Biol , vol.321 , pp. 85-97
    • Hammel, M.1    Kriechbaum, M.2    Gries, A.3    Kostner, G.M.4    Laggner, P.5    Prassl, R.6
  • 32
    • 70349995796 scopus 로고    scopus 로고
    • Glycopeptide profiling of beta-2-glycoprotein I by mass spectrometry reveals attenuated sialylation in patients with antiphospholipid syndrome
    • Kondo A., Miyamoto T., Yonekawa O., Giessing A.M., Osterlund E.C., Jensen O.N. Glycopeptide profiling of beta-2-glycoprotein I by mass spectrometry reveals attenuated sialylation in patients with antiphospholipid syndrome. J Proteomics 2009, 73:123-133.
    • (2009) J Proteomics , vol.73 , pp. 123-133
    • Kondo, A.1    Miyamoto, T.2    Yonekawa, O.3    Giessing, A.M.4    Osterlund, E.C.5    Jensen, O.N.6
  • 33
    • 20444420860 scopus 로고    scopus 로고
    • Oxidation and biotinylation of beta 2 glycoprotein I glycan chains induce an increase in its affinity for anionic phospholipids similar to that obtained by the addition of anti-beta 2 glycoprotein I or anti-cardiolipin antibodies
    • d'Angeac A.D., Stefas I., Duperray C, Rucheton M., Graafland H., Montero J.L., et al. Oxidation and biotinylation of beta 2 glycoprotein I glycan chains induce an increase in its affinity for anionic phospholipids similar to that obtained by the addition of anti-beta 2 glycoprotein I or anti-cardiolipin antibodies. J Immunol Methods 2005, 300:160-178.
    • (2005) J Immunol Methods , vol.300 , pp. 160-178
    • d'Angeac, A.D.1    Stefas, I.2    Duperray, C.3    Rucheton, M.4    Graafland, H.5    Montero, J.L.6
  • 34
    • 30044451650 scopus 로고    scopus 로고
    • Biotinylation of glycan chains in beta2 glycoprotein I induces dimerization of the molecule and its detection by the human autoimmune anti-cardiolipin antibody EY2C9
    • Dupuy D'Angeac A., Stefas I., Graafland H., De Lamotte F., Rucheton M., Palais C., et al. Biotinylation of glycan chains in beta2 glycoprotein I induces dimerization of the molecule and its detection by the human autoimmune anti-cardiolipin antibody EY2C9. Biochem J 2006, 393:117-127.
    • (2006) Biochem J , vol.393 , pp. 117-127
    • Dupuy D'Angeac, A.1    Stefas, I.2    Graafland, H.3    De Lamotte, F.4    Rucheton, M.5    Palais, C.6
  • 35
    • 80054091683 scopus 로고    scopus 로고
    • In vivo distribution of beta2 glycoprotein I under various pathophysiologic conditions
    • Agostinis C., Biffi S., Garrovo C., Durigutto P., Lorenzon A., Bek A., et al. In vivo distribution of beta2 glycoprotein I under various pathophysiologic conditions. Blood 2011, 118:4231-4238.
    • (2011) Blood , vol.118 , pp. 4231-4238
    • Agostinis, C.1    Biffi, S.2    Garrovo, C.3    Durigutto, P.4    Lorenzon, A.5    Bek, A.6
  • 36
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Nagase H., Woessner J.F. Matrix metalloproteinases. J Biol Chem 1999, 274:21491-21494.
    • (1999) J Biol Chem , vol.274 , pp. 21491-21494
    • Nagase, H.1    Woessner, J.F.2
  • 37
    • 0031151126 scopus 로고    scopus 로고
    • Trophoblast differentiation and invasion: its significance for human embryo implantation
    • Bischof P., Campana A. Trophoblast differentiation and invasion: its significance for human embryo implantation. Early Pregnancy 1997, 3:81-95.
    • (1997) Early Pregnancy , vol.3 , pp. 81-95
    • Bischof, P.1    Campana, A.2
  • 38
    • 1342287025 scopus 로고    scopus 로고
    • Matrix metalloproteinases in reproductive endocrinology
    • Shah B.H., Catt K.J. Matrix metalloproteinases in reproductive endocrinology. Trends Endocrinol Metab 2004, 15:47-49.
    • (2004) Trends Endocrinol Metab , vol.15 , pp. 47-49
    • Shah, B.H.1    Catt, K.J.2
  • 39
    • 0036962123 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinase (MMP)-2 and MMP-9 in human placenta and fetal membranes in relation to preterm and term labor
    • Xu P., Alfaidy N., Challis J.R. Expression of matrix metalloproteinase (MMP)-2 and MMP-9 in human placenta and fetal membranes in relation to preterm and term labor. J Clin Endocrinol Metab 2002, 87:1353-1361.
    • (2002) J Clin Endocrinol Metab , vol.87 , pp. 1353-1361
    • Xu, P.1    Alfaidy, N.2    Challis, J.R.3
  • 40
    • 77949840400 scopus 로고    scopus 로고
    • Interleukin-8 (CXCL8) stimulates trophoblast cell migration and invasion by increasing levels of matrix metalloproteinase (MMP)2 and MMP9 and integrins alpha5 and beta1
    • Jovanovic M., Stefanoska I., Radojcic L., Vicovac L. Interleukin-8 (CXCL8) stimulates trophoblast cell migration and invasion by increasing levels of matrix metalloproteinase (MMP)2 and MMP9 and integrins alpha5 and beta1. Reproduction 2011, 139:789-798.
    • (2011) Reproduction , vol.139 , pp. 789-798
    • Jovanovic, M.1    Stefanoska, I.2    Radojcic, L.3    Vicovac, L.4
  • 41
    • 70449624784 scopus 로고    scopus 로고
    • P53 Mediates epidermal growth factor (EGF) induction of MMP-2 transcription and trophoblast invasion
    • Staun-Ram E., Goldman S., Shalev E. p53 Mediates epidermal growth factor (EGF) induction of MMP-2 transcription and trophoblast invasion. Placenta 2009, 30:1029-1036.
    • (2009) Placenta , vol.30 , pp. 1029-1036
    • Staun-Ram, E.1    Goldman, S.2    Shalev, E.3
  • 42
    • 34547771658 scopus 로고    scopus 로고
    • The efficacy of specific IVIG anti-idiotypic antibodies in antiphospholipid syndrome (APS): trophoblast invasiveness and APS animal model
    • Blank M., Anafi L., Zandman-Goddard G., Krause I., Goldman S., Shalev E., et al. The efficacy of specific IVIG anti-idiotypic antibodies in antiphospholipid syndrome (APS): trophoblast invasiveness and APS animal model. Int Immunol 2007, 19:857-865.
    • (2007) Int Immunol , vol.19 , pp. 857-865
    • Blank, M.1    Anafi, L.2    Zandman-Goddard, G.3    Krause, I.4    Goldman, S.5    Shalev, E.6
  • 46
    • 70449637047 scopus 로고    scopus 로고
    • Inhibiton of RET and JAK2 signals and upregulation of VEGFR3 phosphorylation in vitro by galectin-1 in trophoblast tumor cells BeWo
    • Fischer I., Schulze S., Kuhn C., Friese K., Walzel H., Markert U.R., et al. Inhibiton of RET and JAK2 signals and upregulation of VEGFR3 phosphorylation in vitro by galectin-1 in trophoblast tumor cells BeWo. Placenta 2009, 30:1078-1082.
    • (2009) Placenta , vol.30 , pp. 1078-1082
    • Fischer, I.1    Schulze, S.2    Kuhn, C.3    Friese, K.4    Walzel, H.5    Markert, U.R.6
  • 47
    • 9744222923 scopus 로고    scopus 로고
    • Dimeric galectin-1 induces IL-10 production in T-lymphocytes: an important tool in the regulation of the immune response
    • van der Leij J., van den Berg A., Blokzijl T., Harms G., van Goor H., Zwiers P., et al. Dimeric galectin-1 induces IL-10 production in T-lymphocytes: an important tool in the regulation of the immune response. J Pathol 2004, 204:511-518.
    • (2004) J Pathol , vol.204 , pp. 511-518
    • van der Leij, J.1    van den Berg, A.2    Blokzijl, T.3    Harms, G.4    van Goor, H.5    Zwiers, P.6
  • 49
    • 0028233805 scopus 로고
    • Inverse expression of two laminin binding proteins, 67LR and galectin-3, correlates with the invasive phenotype of trophoblastic tissue
    • van den Brule F.A., Price J., Sobel M.E., Lambotte R., Castronovo V. Inverse expression of two laminin binding proteins, 67LR and galectin-3, correlates with the invasive phenotype of trophoblastic tissue. Biochem Biophys Res Commun 1994, 201:388-393.
    • (1994) Biochem Biophys Res Commun , vol.201 , pp. 388-393
    • van den Brule, F.A.1    Price, J.2    Sobel, M.E.3    Lambotte, R.4    Castronovo, V.5
  • 50


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