R. Saldova, et al., Levels of specific serum N-glycans identify breast cancer patients with higher circulating tumor cell counts, Ann. Oncol. 22 (2011) 1113–1119.
 U.M. Abd Hamid, et al., A strategy to reveal potential glycan markers from serum glycoproteins associated with breast cancer progression, Glycobiology 18 (2008) 1105
 Z. Kyselova, et al., Breast cancer diagnosis and prognosis through quantitative measurements of serum glycan profiles, Clin. Chem. 54 (2008) 1166–1175.
 A. Pierce, et al., Levels of specific glycans significantly distinguish lymph node–
 de Leoz, M. L., et al., (2011) High-mannose glycans are elevated during breast cancer progression. Mol. Cell. Proteomics 10, M110.00271
 Alley, W. R., Jr., et al., (2010) Chip-based reversed-phase liquid chromatography-mass spectrometry of permethylated N-linked glycans: a potential methodology for cancerbiomarker discovery. Anal. Chem. 82, 5095–5106
 J. Bones, et al., Ultra performance liquid chromatographic profiling of serum N-glycans for fast and efficient identification of cancer associated alterations in glycosylation, Anal. Chem. 82 (2010) 10208–10215.
 J. Bones, et al., Glycomic and glycoproteomic analysis of serum from patients with stomach cancer reveals potential markers arising from host defence response mechanisms, J. Proteome Res. 10 (2011) 1246–1265.
 Goldman, R., et al., (2009) Detection of hepatocellular carcinoma using glycomic analysis. Clin. Cancer Res. 15, 1808–1813
 Liu, X. E., et al., (2007) N-glycomic changes in hepatocellular carcinoma patients with liver cirrhosis induced by hepatitis B virus. Hepatology 46, 1426–1435
 K. Noda, et al, Gene expressionof α1-6 fucosyltransferase in human hepatoma tissues: a possible implicationfor increased fucosylation of α-fetoprotein, Hepatology 28 (1998), 944–952.
 Y. Sato, et al.,Early recognition of hepatocellular carcinoma based on altered profiles of alphafetoprotein,N. Engl. J. Med. 328 (1993) 1802–1806.
 J.N. Arnold, R. Saldova, M.C. Galligan, T.B. Murphy, Y. Mimura-Kimura, J.E. Telford, A.K. Godwin, P.M. Rudd, Novel glycan biomarkers for the detection of lung cancer, J. Proteome Res. 10 (2011) 1755–1764.
 Kim, Y. G., et al., (2009) Rapid and high-throughput analysis of N-glycans from ovarian cancer serum using a 96-well plate platform. Anal. Biochem. 391, 151–153.
 R. Saldova, et al., Ovarian cancer is associated with changes in glycosylation in both acute-phase proteins and IgG, Glycobiology 17 (2007) 1344.
 Alley, W. R., Jr., et al., (2012) N-linked glycan structures and their expressions change in the blood sera of ovarian cancer patients. J. Proteome Res. 11, 2282–2300
 Kronewitter, S. R., et al., (2012) The glycolyzer: automated glycan annotation software for high performance mass spectrometry and its application to ovarian cancer glycan biomarker discovery. Proteomics 12, 2523–2538
 Storr SJ, et al., The O-linked glycosylation of secretory/shed MUC1 from an advanced breast cancer patient’s serum. Glycobiology 2008, 18(6):456-462.
 R. Saldova, et al., Core fucosylation and alpha2-3 sialylation in serum N-glycome is significantly increased in prostate cancer comparing to benign prostate hyperplasia, Glycobiology 21 (2011) 195–205.
 A. Sarrats, et al., Glycan characterization of PSA 2-DE subforms from serum and seminal plasma, OMICS: A J. of Integr. Biol. 14 (2010) 465–474.
 A. Sarrats, et al., Differential percentage of serum prostate-specific antigen subforms suggests a new way to improve prostate cancer diagnosis, Prostate 70 (2010) 1–9.
 Hua, S., et al., (2011) Comprehensive native glycan profiling with isomer separation and quantitation for the discovery of cancer biomarkers. Analyst 136, 3663–3671.
 N. Okuyama, et al., 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 118 (2006) 2803–2808.
 E. Miyoshi, M. Nakano, Fucosylated haptoglobin is a novel marker for pancreatic cancer: detailed analyses of oligosaccharide structures, Proteomics 8 (2008) 3257–3262.
 Nakano M, et al., 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: 2301–9.
 Kukowska-Latallo JF, et al., A cloned human cDNA determines expression of a mouse stagespecific embryonic antigen and the Lewis blood group a(1,3/1,4)fucosyltransferase. Genes Dev 1990;4:1288–303.
 Hanski C, et al., Fucosyltransferase III and sialyl-Le(x) expression correlate in cultured colon carcinoma cells but not in colon carcinoma tissue. Glycoconj J 1996;13:727–33.
 Majuri ML, et al., Expression and function of a2,3-sialyl- and a,3/l,4- fucosyltransferases in colon adenocarcinoma cell lines: role in synthesis of E-selectin counter-receptors. Int J Cancer 1995;63:551–9.
 Ercan et al. Hypogalactosylation of serum N-glycans fails to predict clinical response to methotrexate and TNF inhibition in rheumatoid arthritis.Arthritis Research & Therapy 2012, 14:R43
 James N. Arnold et al., Mannan binding lectin and its interaction with immunoglobulins inhealth and in disease, Immunology Letters 106 (2006) 103–110
 Pauline M. Rudd et al. Glycosylation and the Immune System. Science 291, 2370 (2001)
 Arnold, J. N:, et al., The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu. Rev. Immunol. 25, 21-50 (2007)
 Gaya Thanabalasingham, G. Lauc, et al., “Mutations in HNF1A Result in Marked Alterations of Plasma Glycan Profile“, Diabetes 2013, 62, 1329.
 Zihao Wang, et al., “Site-Specific GlcNAcylation of Human Erythrocyte Proteins“, Diabetes 2009, 59, 309 .