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Filatov VL, et al. (1998) Epitope mapping of anti-troponin I monoclonal antibodies. Biochem. Mol. Biol. Int. 45(6), 1179- 1187.

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Katrukha A, et al. (1999) Biochemical factors in uencing measurement of cardiac troponin I in serum. Clin. Chem. Lab. Med. 37(11-12), 1091-1095.

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Katrukha AG. (2003) Antibody selection strategies in cardiac troponin assays. Cardiac Markers, 2nd edition, Edited by Alan HB. Wu. 173-185.

Kogan A, et al. (2005) Immunological study of complex formation between soluble transferrin receptor and transferrin. Am. J. Hematol. 79(4), 281-287.

Kogan AE, et al. (2007) Comparison of soluble and placental transferrin receptors as standards for the determination of soluble transferrin receptor in humans. Int. J. Lab. Hematol. 29(5), 335-340.

Kogan AE, et al. (2013) Oligomeric adiponectin forms and their complexes in the blood of healthy donors and patients with type 2 diabetes mellitus. J. Immunoassay Immunochem. 34(2), 180-196.

Kogan AE, et al. (2016) Monoclonal antibodies with equal speci city to D-dimer and high-molecular-weight brin degradation products. Blood Coagul. Fibrinolysis, 27(5), 542-550.

Konev AA, et al. (2015) Characterization of endogenously circulating IGFBP-4 fragments—Novel biomarkers for cardiac risk assessment. Clin. Biochem. 48(12), 774-780.

Postnikov AB, et al. (2012) N-terminal and C-terminal fragments of IGFBP-4 as novel biomarkers for short-term risk assessment of major adverse cardiac events in patients presenting with ischemia. Clin. Chem. 45, 519-524.

Røsjø H, et al. (2012) Diagnostic utility of a single-epitope sandwich B-type natriuretic peptide assay in stable coronary artery disease: data from the Akershus Cardiac Examination (ACE) 1 Study. Clin. Biochem. 45(16-17), 1269- 1275.

Schulz O, et al. (2014) Clinical di erences between total PAPP-A and measurements speci c for the products of free PAPP-A activity in patients with stable cardiovascular disease. Clin. Biochem. 47(3), 177-183

Seferian KR, et al. (2007) The brain natriuretic peptide (BNP) precursor is the major immunoreactive form of BNP in patients with heart failure. Clin. Chem. 53, 866-873.

Seferian KR, et al. (2008) Immunodetection of glycosylated NT-proBNP circulating in human blood. Clin. Chem. 54(5), 866-873.

Semenov AG and Katrukha AG. (2016) Di erent Susceptibility of B-Type Natriuretic Peptide (BNP) and BNP Precursor (proBNP) to Cleavage by Neprilysin: The N-Terminal Part Does Matter. Clin. Chem. 62(4), 617-622.

Semenov AG and Seferian KR. (2011) Biochemistry of the human B-type natriuretic peptide precursor and molecular aspects of its processing. Clin. Chim. Acta 412(11-12), 850- 860.

Semenov AG, et al. (2009) Processing of pro-brain natriuretic peptide is suppressed by O-glycosylation in the region close to the cleavage site. Clin. Chem. 55(3), 489- 498.

Semenov AG, et al. (2010) Processing of Pro-B-Type Natriuretic Peptide: Furin and Corin as Candidate Convertases. Clin. Chem. 56(7), 1166-1176.

Semenov AG, et al. (2011) Human Pro-B-Type Natriuretic Peptide Is Processed in the Circulation in a Rat Model. Clin. Chem. 57(6), 883-890.

Semenov AG, et al. (2016) Searching for a BNP standard: Glycosylated proBNP as a common calibrator enables improved comparability of commercial BNP immunoassays. Clin Biochem. doi: 10.1016/j.clinbiochem.2016.11.003.

Tamm NN, et al. (2008) Novel immunoassay for quanti cation of brain natriuretic peptide and its precursor in human blood. Clin. Chem. 54(9), 1511-1518.

Tamm NN, et al. (2011) Measurement of B-type natriuretic peptide by two assays utilizing antibodies with di erent epitope speci city. Clin. Biochem. 44(2-3), 257-259.

Vylegzhanina AV, et al. (2013) Epitope Speci city of Anti– Cardiac Troponin I Monoclonal Antibody 8I-7. Clin. Chem. 59(12), 1814-1816.

Vylegzhanina AV, et al. (2017) Anti-Cardiac Troponin Autoantibodies Are Speci c to the Conformational Epitopes Formed by Cardiac Troponin I and Troponin T in the Ternary Troponin Complex. Clin Chem. doi: 10.1373/ clinchem.2016.261602.

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