References
- Denton CP. Advances in pathogenesis and treatment of systemic sclerosis. Clin Med (Lond). 2016;16(1):55–60.
- Mulherin D, Bresnihan B. Systemic lupus erythematosus. Baillieres Clin Rheumatol. 1993;7(1):31–57.
- Axford JS. Glycosylation and rheumatic disease. Biochim Biophys Acta. 1999;1455(2-3):219–229.
- Gruszewska E, Chludzinska A, Chrostek L, et al. Carbohydrate-deficient transferrin depends on disease activity in rheumatoid arthritis and systemic sclerosis. Scand J Rheumatol. 2013;42(3):203–206.
- Routier FH, Hounsell EF, Rudd PM, et al. Quantitation of the oligosaccharides of human serum IgG from patients with rheumatoid arthritis: a critical evaluation of different methods. J Immunol Methods. 1998;213(2):113–130.
- Gindzienska-Sieskiewicz E, Klimiuk PA, Kisiel DG, et al. The changes in monosaccharide composition of immunoglobulin G in the course of rheumatoid arthritis. Clin Rheumatol. 2007;26(5):685–690.
- Domysławska I, Kita K, Sulik A, et al. Concentration and microheterogeneity of acute-phase glycoproteins in patients with systemic lupus erythematosus. Rocz Akad Med Bialym. 2005;50(suppl 1):259–262.
- Kamboh MI, Ferrell RE. Human transferrin polymorphism. Hum Hered. 1987;37(2):65–81.
- Petri M, Orbai AM, Alarcon GS, et al. Derivation and validation of systemic lupus international collaborating clinics classification criteria for systemic lupus erythematosus. Arthritis Rheum. 2012;64(8):2677–2686.
- Pope JE, Johnson SR. New classification criteria for systemic sclerosis (scleroderma). Rheum Dis Clin North Am. 2015;41(3):383–398.
- Schellenberg F, Wielders JP. Evaluation of capillary electrophoresis assay for CDT on SEBIA's Capillarys System: intra and inter laboratory precision, reference interval and cut-off. Clin Chim Acta. 2010;411(23-24):1888–1893.
- Dube S, Fischer JW, Powell JS. Glycosylation at specific sites of erythropoietin is essential for biosynthesis, secretion and biological function. J Biol Chem. 1988;263:17516–17521.
- Pos O, Oostendorp RA, van der Stelt ME, et al. Con A-nonreactive human alpha 1-acid glycoprotein (AGP) is more effective in modulation of lymphocyte proliferation than Con A-reactive AGP serum variants. Inflammation. 1990;14(2):133–141.
- de Jong G, Van Dijk JP, Van Eijk HG. The biology of transferrin. Clin Chim Acta. 1990;190(1-2):1–46.
- de Jong G, Van Eijk HG. Functional properties of the carbohydrate moiety of human transferrin. Int J Biochem. 1989;21(3):253–263.
- Chrostek L, Cylwik B, Gindzienska-Sieskiewicz E, et al. Sialic acid level reflects the disturbances of glycosylation and acute-phase reaction in rheumatic diseases. Rheumatol Int. 2014;34(3):393–399.
- Gruszewska E, Sienkiewicz M, Abramowicz P, et al. Serum profile of transferrin isoforms in JIA: a preliminary study. Rheumatol Int. 2018;38(7):1235–1240.
- Gornik O, Lauc G. Glycosylation of serum proteins in inflammatory diseases. Dis Markers. 2008;25(4-5):267–278.
- Mackiewicz A, Mackiewicz K. Glycoforms of serum alpha 1-acid glycoprotein as markers of inflammation and cancer. Glycoconj J. 1995;12(3):241–247.