Тропонины
Bogomolova AP, Katrukha IA, et al. (2025) Development of Immunochemical Systems for Detection of Human Skeletal Troponin I Isoforms. BIOCHEMISTRY-MOSCOW Volume 90 Issue 3 Page 349-363 DOI10.1134/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.
Bogomolova AP, Katrukha IA. (2024) Troponins and Skeletal Muscle Pathologies. BIOCHEMISTRY-MOSCOW Volume 89 Issue 12-13 Page 2083-2106 DOI10.1134/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. Published 2024 Aug 16. 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. doi: 10.1515/cclm-2024-0066. Epub ahead of print.
Katrukha IA , et al. (2023) Fragmentation of human cardiac troponin T after acute myocardial infarction. Clin Chim Acta. 1;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 Jan 8;67(1):124-130. doi: 10.1093/clinchem/hvaa281.
Alexey V Kharitonov, et al. (2021)
Switching of cardiac troponin I between nuclear and cytoplasmic localization during muscle differentiation
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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 Jul;65(7):882-892. doi: 10.1373/clinchem.2018.301127. Epub 2019 Mar 11.
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 Jul;64(7):1104-1112. doi: 10.1373/clinchem.2017.286211. Epub 2018 Apr 9.
Katrukha IA; Kogan AE, et al. (2017) Thrombin Activation via Serum Preparation Is Not the Root Cause for Cardiac Troponin T Degradation. IN REPLY CLINICAL CHEMISTRY Volume 63 Issue 11 Page 1769-1770 DOI10.1373/clinchem.2017.280800
Katrukha IA, et al. (2017) Thrombin-Mediated Degradation of Human Cardiac Troponin T. Clin. Chem. 2017 Jun;63(6):1094-1100. doi: 10.1373/clinchem.2016.266635. Epub 2017 Apr 20.
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. 63(1), 343-350.
Tate JR, et al. (2015) IFCC Working Group on Standardization of Cardiac Troponin I. Evaluation of standardization capability of current cardiac troponin I assays by a correlation study: results of an IFCC pilot project. Clin. Chem. Lab. Med. 53(5): 677-690.
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Vylegzhanina AV, et al. (2013) Epitope Specificity of Anti-Cardiac Troponin I Monoclonal Antibody 8I-7. Clin. Chem. 59(12), 1814-1816.
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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.
Katrukha A, et al. (1999) Biochemical factors influencing measurement of cardiac troponin I in serum. Clin. Chem. Lab. Med. 37(11-12), 1091-1095.
Katrukha A, et al. (1999) New approach to standardisation of human cardiac troponin I (cTnI). Scand. J. Clin. Lab. Invest. Suppl. 230, 124-7.
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Katrukha AG, et al. (1998) Degradation of cardiac troponin I: implication for reliable immunodetection. Clin. Chem. 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. 43(8), 1379-1385.
Katrukha AG, et al. (1995) A new method of human cardiac troponin I and troponin T purification. Biochem. Mol. Biol. Int. 36, 195-202.
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Натрийуретический пептид типа B
Selezneva EM, Feygina E.E., Ageeva L.V. et al. (2025) Neprilysin 2 catalyses the degradation of natriuretic peptides despite sacubitrilat Inhibition. Sci Rep 15, 27401. doi: 10.1038/s41598-025-10166-z.
Li L , et al. (2022) Diagnostic utility of total NT-proBNP testing by immunoassay based on antibodies targeting glycosylation-free regions of NT-proBNP. Clin Chem Lab Med. 2;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 Sep 1;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 Nov;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 Jul 15. pii:clinchem.2019.303438. 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 Jun 24. pii:clinchem.2019.306175. 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. In Advances in Clinical Chemistry, pp 1–30, Elsevier.
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 Mar;50(4-5):181-185.
Semenov AG and Katrukha AG (2016) Analytical Issues with Natriuretic Peptides - has this been Overly Simplified? EJIFCC. 2016 Aug 1;27(3):189-207. eCollection 2016 Aug.
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 Apr;62(4):617-22. doi: 10.1373/clinchem.2016.254524. Epub 2016 Feb 10.
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. 2016 Nov 5. pii: S0009-9120(16)30503-3. doi: 10.1016/j.clinbiochem.2016.11.003.
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), 1269-75.
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. (2011) Human pro-B-type natriuretic peptide is processed in the circulation in a rat model. Clin. Chem. 57(6), 883-890.
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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. (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.
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Seferian KR, et al. (2008) Immunodetection of glycosylated NT-proBNP circulating in human blood. Clin. Chem. 54(5), 866-873.
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.
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IGFBP-4 и PAPP-A
Marina Artemieva, 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 Mar 18;27(6):2761. doi: 10.3390/ijms27062761.
Dya GA, Lebedeva OS, et al. (2025) Specific cleavage of IGFBP-4 by papp-a in nervous tissue. Biochem Biophys Res Commun. 2024 Nov 12:733:150655. doi: 10.1016/j.bbrc.2024.150655. Epub 2024 Sep 5.
Adasheva DA, et al.(2023) PAPP-A-Specific IGFBP-4 Proteolysis in Human Induced Pluripotent Stem Cell-Derived Cardiomyocytes , Biochemistry (Moscow) 8;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). 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 Apr;7(2):434-444.
Konev AA, et al. (2018) Glycosylated and non-glycosylated NT-IGFBP-4 in circulation of acute coronary syndrome patients. Clin Biochem. 2018.
Konev AA, et al. (2015) Characterization of endogenously circulating IGFBP-4 fragments—Novel biomarkers for cardiac risk assessment. Clin. Biochem. 48(12): 774-80.
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. 47(3):177-83.
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. 45:519-24.
Qiu-Ping Qin, 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 Mar;52(3):398-404. doi: 10.1373/clinchem.2005.058396. Epub 2006 Jan 19.
Qiu-Ping Qin , et al. (2005)
Molecular distinction of circulating pregnancy-associated plasma protein A in myocardial infarction and pregnancy
. Clin Chem. 2005 Jan;51(1):75-83. doi: 10.1373/clinchem.2004.036467.
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Рецептор трансферрина
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 A, et al. (2005) Immunological study of complex formation between soluble transferrin receptor and transferrin. Am. J. Hematol. 79(4), 281-287.
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Адипонектин
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. doi: 10.1080/15321819.2012.699494.
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Д-димер
Kogan AE, Mukharyamova KS, et al. (2016) Monoclonal antibodies with equal specificity to D-dimer and high-molecular-weight fibrin degradation products. Blood Coagul Fibrinolysis. 2016 Jul;27(5):542-550.
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SARS-Cov 2
Elena V Maryukhnich, 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 Dec 20;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 Oct 21:15:1448515. doi: 10.3389/fimmu.2024.1448515. eCollection 2024.
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Цистатин С
Gustav Östner 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 Dec;71(8):676-82. doi: 10.3109/00365513.2011.621026. Epub 2011 Oct 21.
Noora Ristiniemi, et al. (2010) Dry-reagent double-monoclonal assay for cystatin C. Clin Chem. 2010 Sep;56(9):1424-31. doi: 10.1373/clinchem.2009.141663. Epub 2010 Jul 12.
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