Hytest Articles

Go to:

• Troponin
• B-type natriuretic peptide
• IGFBP-4 and PAPP-A
• Transferrin receptor
• Adiponectin
• D-dimer
• Cystatin C
• SARS-CoV-2

Troponin

• Bogomolova AP, Katrukha IA, et al. (2025) Development of Immunochemical Systems for Detection of Human Skeletal Troponin I Isoforms. Biochemistry (Mosc). 2025;90(3):349-363. doi: 10.1134/S0006297924601928.
• Li L et al. (2025) Design and Analytical Evaluation of Novel Cardiac Troponin Assays Targeting Multiple Forms of the Cardiac Troponin I-Cardiac Troponin T-Troponin C Complex and Fragmentation Forms. Clin Chem. 2025;71(3):387-395. doi: 10.1093/clinchem/hvae182.
• Bogomolova AP, Katrukha IA. (2024) Troponins and Skeletal Muscle Pathologies. Biochemistry (Mosc). 2024;89(12):2083-2106. doi: 10.1134/S0006297924120010.
• Riabkova NS, Kogan AE, Katrukha IA, et al. (2024) Influence of Anticoagulants on the Dissociation of Cardiac Troponin Complex in Blood Samples. Int J Mol Sci. 2024;25(16):8919. doi: 10.3390/ijms25168919.
• Riabkova NS, et al. (2024) Interaction of heparin with human cardiac troponin complex and its influence on the immunodetection of troponins in human blood samples. Clin Chem Lab Med. 2024;62(11):2316-2325. doi: 10.1515/cclm-2024-0066.
• Katrukha IA, et al. (2023) Fragmentation of human cardiac troponin T after acute myocardial infarction. Clin Chim Acta. 2023;542:117281. doi: 10.1016/j.cca.2023.117281.
• Katrukha IA, et al. (2021) Myocardial Injury and the Release of Troponins I and T in the Blood of Patients. Clin Chem. 2021;67(1):124-130. doi: 10.1093/clinchem/hvaa281.
• Kharitonov AV, et al. (2020) Switching of cardiac troponin I between nuclear and cytoplasmic localization during muscle differentiation. Biochim Biophys Acta Mol Cell Res. 2020;1867(2):118601. doi: 10.1016/j.bbamcr.2019.118601.
• Vylegzhanina AV, et al. (2019) Full-Size and Partially Truncated Cardiac Troponin Complexes in the Blood of Patients with Acute Myocardial Infarction. Clin Chem. 2019;65(7):882-892. doi: 10.1373/clinchem.2018.301127.
• Katrukha IA, et al. (2018) Full-Size Cardiac Troponin I and Its Proteolytic Fragments in Blood of Patients with Acute Myocardial Infarction: Antibody Selection for Assay Development. Clin Chem. 2018;64(7):1104-1112. doi: 10.1373/clinchem.2017.286211.
• Katrukha IA; Kogan AE, et al. (2017) Thrombin Activation via Serum Preparation Is Not the Root Cause for Cardiac Troponin T Degradation. Clin Chem. 2017;63(11):1768-1769. doi: 10.1373/clinchem.2017.279182.
• Katrukha IA, et al. (2017) Thrombin-Mediated Degradation of Human Cardiac Troponin T. Clin Chem. 2017;63(6):1094-1100. doi: 10.1373/clinchem.2016.266635.
• Vylegzhanina AV, et al. (2017) Anti-Cardiac Troponin Autoantibodies Are Specific to the Conformational Epitopes Formed by Cardiac Troponin I and Troponin T in the Ternary Troponin Complex. Clin Chem. 2017;63(1):343-350. doi: 10.1373/clinchem.2016.261602.
• Tate JR, et al. (2015) Evaluation of standardization capability of current cardiac troponin I assays by a correlation study: results of an IFCC pilot project. Clin Chem Lab Med. 2015;53(5):677-690. doi: 10.1515/cclm-2014-1197.
• Barth JH, et al. (2014) Recommendation to harmonize the units for reporting cardiac troponin results. Clin Chim Acta. 2014;432:166. doi: 10.1016/j.cca.2013.10.023.
• Vylegzhanina AV, et al. (2013) Epitope specificity of anti-cardiac troponin I monoclonal antibody 8I-7. Clin Chem. 2013;59(12):1814-1816. doi: 10.1373/clinchem.2013.209528.
• Tate JR, et al. (2010) Standardisation of cardiac troponin I measurement: past and present. Pathology. 2010;42(5):402-408. doi: 10.3109/00313025.2010.495246.
• Noble JE, et al. (2010) Development of a candidate secondary reference procedure (immunoassay based measurement procedure of higher metrological order) for cardiac troponin I: I. Antibody characterization and preliminary validation. Clin Chem Lab Med. 2010;48(11):1603-1610. doi: 10.1515/CCLM.2010.316.
• Panteghini M, et al. (2008) Standardization of troponin I measurements: an update. Clin Chem Lab Med. 2008;46(11):1501-1506. doi: 10.1515/CCLM.2008.291.
• Katrukha AG. (2003) Antibody Selection Strategies in Cardiac Troponin Assays. In: Wu AHB, editor. Cardiac Markers. 2nd ed. Totowa (NJ): Humana Press; 2003. p. 173-185. doi: 10.1007/978-1-59259-385-9_10.
• Katrukha A, et al. (1999) Biochemical factors influencing measurement of cardiac troponin I in serum. Clin Chem Lab Med. 1999;37(11-12):1091-1095. doi: 10.1515/CCLM.1999.159.
• Katrukha A, et al. (1999) New approach to standardisation of human cardiac troponin I (cTnI). Scand J Clin Lab Invest Suppl. 1999;230:124-127.
• Filatov VL, et al. (1999) Troponin: structure, properties, and mechanism of functioning. Biochemistry (Mosc). 1999;64(9):969-985.
• Filatov VL, et al. (1998) Epitope mapping of anti-troponin I monoclonal antibodies. Biochem Mol Biol Int. 1998;45(6):1179-1187. doi: 10.1080/15216549800203412.
• Katrukha AG, et al. (1998) Degradation of cardiac troponin I: implication for reliable immunodetection. Clin Chem. 1998;44(12):2433-2440.
• Katrukha AG, et al. (1997) Troponin I is released in bloodstream of patients with acute myocardial infarction not in free form but as complex. Clin Chem. 1997;43(8 Pt 1):1379-1385.
• Katrukha AG, et al. (1995) A new method of human cardiac troponin I and troponin T purification. Biochem Mol Biol Int. 1995;36(1):195-202.

Back to top

B-type natriuretic peptide

• Selezneva EM, Feygina EE, Ageeva LV et al. (2025) Neprilysin 2 catalyses the degradation of natriuretic peptides despite sacubitrilat inhibition. Sci Rep. 2025;15(1):27401. doi: 10.1038/s41598-025-10166-z.
• Li L, et al. (2023) Diagnostic utility of total NT-proBNP testing by immunoassay based on antibodies targeting glycosylation-free regions of NT-proBNP. Clin Chem Lab Med. 2023;61(3):485-493. doi: 10.1515/cclm-2022-1194.
• Semenov AG (2020) In-Depth Analysis of Molecular Heterogeneity of Circulating N-Terminal pro-BNP: Does Detailed Characterization of Analyte Structure Really Matter for Its Diagnostic Use? Clin Chem. 2020;66(9):1131-1133. doi: 10.1093/clinchem/hvaa162.
• Feygina EE, et al. (2019) Neutral Endopeptidase (Neprilysin) in Therapy and Diagnostics: Yin and Yang. Biochemistry (Mosc). 2019;84(11):1346-1358. doi: 10.1134/S0006297919110105.
• Feygina EE, et al. (2019) Detection of Neprilysin-Derived BNP Fragments in the Circulation: Possible Insights for Targeted Neprilysin Inhibition Therapy for Heart Failure. Clin Chem. 2019;65(10):1239-1247. doi: 10.1373/clinchem.2019.303438.
• Semenov AG and Katrukha AG (2019) A View on the Interrelationship between Obesity and Natriuretic Peptide Measurements: Can Dysregulation in pro-B-type Natriuretic Peptide Glycosylation Explain Decreased B-type Natriuretic Peptide Concentrations in Obese Heart Failure Patients? Clin Chem. 2019;65(9):1070-1072. doi: 10.1373/clinchem.2019.306175.
• Semenov AG and Feygina EE (2018) Standardization of BNP and NT-proBNP Immunoassays in Light of the Diverse and Complex Nature of Circulating BNP-Related Peptides. Adv Clin Chem. 2018;85:1-30. doi: 10.1016/bs.acc.2018.02.001.
• Semenov AG, et al. (2017) Searching for a BNP standard: Glycosylated proBNP as a common calibrator enables improved comparability of commercial BNP immunoassays. Clin Biochem. 2017;50(4-5):181-185. doi: 10.1016/j.clinbiochem.2016.11.003.
• Semenov AG and Katrukha AG (2016) Analytical Issues with Natriuretic Peptides - has this been Overly Simplified? EJIFCC. 2016;27(3):189-207.
• Semenov AG and Katrukha AG (2016) Different Susceptibility of B-Type Natriuretic Peptide (BNP) and BNP Precursor (proBNP) to Cleavage by Neprilysin: The N-Terminal Part Does Matter. Clin Chem. 2016;62(4):617-622. doi: 10.1373/clinchem.2016.254524.
• 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. 2012;45(16-17):1269-1275. doi: 10.1016/j.clinbiochem.2012.05.010.
• Semenov AG and Seferian KR (2011) Biochemistry of the human B-type natriuretic peptide precursor and molecular aspects of its processing. Clin Chim Acta. 2011;412(11-12):850-860. doi: 10.1016/j.cca.2011.03.006.
• Semenov AG, et al. (2011) Human pro-B-type natriuretic peptide is processed in the circulation in a rat model. Clin Chem. 2011;57(6):883-890. doi: 10.1373/clinchem.2010.161125.
• Tamm NN, et al. (2011) Measurement of B-type natriuretic peptide by two assays utilizing antibodies with different epitope specificity. Clin Biochem. 2011;44(2-3):257-259. doi: 10.1016/j.clinbiochem.2010.09.030.
• Semenov AG, et al. (2010) Processing of pro-B-type natriuretic peptide: furin and corin as candidate convertases. Clin Chem. 2010;56(7):1166-1176. doi: 10.1373/clinchem.2010.143883.
• 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. 2009;55(3):489-498. doi: 10.1373/clinchem.2008.113373.
• Tamm NN, et al. (2008) Novel immunoassay for quantification of brain natriuretic peptide and its precursor in human blood. Clin Chem. 2008;54(9):1511-1518. doi: 10.1373/clinchem.2007.100545.
• Seferian KR, et al. (2008) Immunodetection of glycosylated NT-proBNP circulating in human blood. Clin Chem. 2008;54(5):866-873. doi: 10.1373/clinchem.2007.100040.
• 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. 2007;53(5):866-873. doi: 10.1373/clinchem.2006.076141.

Back to top

IGFBP-4 and PAPP-A

• Artemieva MM, et al. (2026) Left Ventricular and Right Ventricular Hypertrophy Modelling to Study PAPP-A-Mediated IGFBP-4 Cleavage-a Mechanism That Regulates IGF Bioavailability in Adult Rats. Int J Mol Sci. 2026;27(6):2761. doi: 10.3390/ijms27062761.
• Dya GA, Lebedeva OS, et al. (2024) Specific cleavage of IGFBP-4 by PAPP-A in nervous tissue. Biochem Biophys Res Commun. 2024;733:150655. doi: 10.1016/j.bbrc.2024.150655.
• Adasheva DA, et al. (2023) PAPP-A-Specific IGFBP-4 Proteolysis in Human Induced Pluripotent Stem Cell-Derived Cardiomyocytes. Int J Mol Sci. 2023;24(9):8420. doi: 10.3390/ijms24098420.
• Serebryanaya DV, et al. (2021) IGFBP-4 Proteolysis by PAPP-A in a Primary Culture of Rat Neonatal Cardiomyocytes under Normal and Hypertrophic Conditions. Biochemistry (Mosc). 2021;86(11):1395-1406. doi: 10.1134/S0006297921110043.
• Konev AA, et al. (2020) CT-IGFBP-4 as a novel prognostic biomarker in acute heart failure. ESC Heart Fail. 2020;7(2):434-444. doi: 10.1002/ehf2.12590.
• Konev AA, et al. (2018) Glycosylated and non-glycosylated NT-IGFBP-4 in circulation of acute coronary syndrome patients. Clin Biochem. 2018;55:56-62. doi: 10.1016/j.clinbiochem.2018.03.004.
• Konev AA, et al. (2015) Characterization of endogenously circulating IGFBP-4 fragments-novel biomarkers for cardiac risk assessment. Clin Biochem. 2015;48(12):774-780. doi: 10.1016/j.clinbiochem.2015.05.010.
• Schulz O, et al. (2014) Clinical differences between total PAPP-A and measurements specific for the products of free PAPP-A activity in patients with stable cardiovascular disease. Clin Biochem. 2014;47(3):177-183. doi: 10.1016/j.clinbiochem.2013.10.027.
• 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 Biochem. 2012;45(7-8):519-524. doi: 10.1016/j.clinbiochem.2011.12.030.
• Qin QP, et al. (2006) Immunoassays developed for pregnancy-associated plasma protein-A (PAPP-A) in pregnancy may not recognize PAPP-A in acute coronary syndromes. Clin Chem. 2006;52(3):398-404. doi: 10.1373/clinchem.2005.058396.
• Qin QP, et al. (2005) Molecular distinction of circulating pregnancy-associated plasma protein A in myocardial infarction and pregnancy. Clin Chem. 2005;51(1):75-83. doi: 10.1373/clinchem.2004.036467.

Back to top

Transferrin receptor

• 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. 2007;29(5):335-340. doi: 10.1111/j.1365-2257.2006.00874.x.
• Kogan A, et al. (2005) Immunological study of complex formation between soluble transferrin receptor and transferrin. Am J Hematol. 2005;79(4):281-287. doi: 10.1002/ajh.20429.

Back to top

Adiponectin

• 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. 2013;34(2):180-196. doi: 10.1080/15321819.2012.699494.

Back to top

D-dimer

• Kogan AE, et al. (2016) Monoclonal antibodies with equal specificity to D-dimer and high-molecular-weight fibrin degradation products. Blood Coagul Fibrinolysis. 2016;27(5):542-550. doi: 10.1097/MBC.0000000000000453.

Back to top

Cystatin C

• Östner G, et al. (2011) High throughput testing of drug library substances and monoclonal antibodies for capacity to reduce formation of cystatin C dimers to identify candidates for treatment of hereditary cystatin C amyloid angiopathy. Scand J Clin Lab Invest. 2011;71(8):676-682. doi: 10.3109/00365513.2011.621026.
• Ristiniemi N, et al. (2010) Dry-reagent double-monoclonal assay for cystatin C. Clin Chem. 2010;56(9):1424-1431. doi: 10.1373/clinchem.2009.141663.

Back to top

SARS-CoV-2

• Maryukhnich EV, et al. (2025) An Ex Vivo Lung Histoculture Model for Studying Pulmonary Infection and Immune Response With SARS-CoV-2 as an Example of RNA Virus. Bio Protoc. 2025;15(24):e5552. doi: 10.21769/BioProtoc.5552.
• Vorobyeva DA, Potashnikova DM, et al. (2024) Cytokine production in an ex vivo model of SARS-CoV-2 lung infection. Front Immunol. 2024;15:1448515. doi: 10.3389/fimmu.2024.1448515.

Back to top