References
- Stirpe A, Pantusa M, Rizzuti B, et al. Resveratrol induces thermal stabilization of human serum albumin and modulates the early aggregation stage. Int J Biol Macromol. 2016;92:1049-1056. doi:10.1016/j.ijbiomac.2016.08.014
- Słonina D, Gasińska A, Biesaga B, Janecka A, Kabat D. An association between low-dose hyper-radiosensitivity and the early G2-phase checkpoint in normal fibroblasts of cancer patients. DNA Repair (Amst). 2016;39:41-45. doi:10.1016/j.dnarep.2015.12.001
- Mishyna M, Volokh O, Danilova Y, Gerasimova N, Pechnikova E, Sokolova OS. Effects of radiation damage in studies of protein-DNA complexes by cryo-EM. Micron. 2017;96:57-64. doi:10.1016/j.micron.2017.02.004
- Gramatyka M, Skorupa A, Sokół M. Nuclear magnetic resonance spectroscopy reveals metabolic changes in living cardiomyocytes after low doses of ionizing radiation. Acta Biochim Pol. 2018;65(2):309-318. doi:10.18388/abp.2018_2568
- Radman M. Protein damage, radiation sensitivity and aging. DNA Repair (Amst). 2016;44:186-192. doi:10.1016/j.dnarep.2016.05.025
- Baccaro S, Bal O, Cemmi A, Di Sarcina I. The effect of gamma irradiation on rice protein aqueous solution. Radiation Physics and Chemistry. 2018;146:1-4. doi:10.1016/j.radphyschem.2018.01.011
- Cieśla K, Eliasson AC. DSC studies of retrogradation and amylose-lipid complex transition taking place in gamma irradiated wheat starch. Nucl Instrum Methods Phys Res B. 2007;265(1):399-405. doi:10.1016/j.nimb.2007.09.010
- Cieśla K, Vansant EF. Physico-chemical changes taking place in gamma irradiated bovine globulins studied by thermal analysis. In: Journal of Thermal Analysis and Calorimetry. Vol 99.; 2010:315-324. doi:10.1007/s10973-009-0155-8
- Garbett NC, Brock GN. Differential scanning calorimetry as a complementary diagnostic tool for the evaluation of biological samples. Biochim Biophys Acta Gen Subj. 2016;1860(5):981-989. doi:10.1016/j.bbagen.2015.10.004
- Garbett NC, Mekmaysy CS, DeLeeuw L, Chaires JB. Clinical application of plasma thermograms. Utility, practical approaches and considerations. Methods. 2015;76:41-50. doi:10.1016/j.ymeth.2014.10.030
- Garbett NC, Miller JJ, Jenson AB, Chaires JB. Calorimetry outside the box: A new window into the plasma proteome. Biophys J. 2008;94(4):1377-1383. doi:10.1529/biophysj.107.119453
- Michnik A, Drzazga Z. Thermal denaturation of mixtures of human serum proteins: DSC study. In: Journal of Thermal Analysis and Calorimetry. Vol 101.; 2010:513-518. doi:10.1007/s10973-010-0826-5
- Michnik A, Drzazga Z, Sadowska-Krępa E, Kłapcińska B. Calorimetric monitoring of the effect of endurance training and testosterone treatment on rat serum denaturation transition. J Therm Anal Calorim. 2014;115(3):2231-2237. doi:10.1007/s10973-013-3611-4
- Michnik A, Sadowska-Krępa E, Kiełboń A, Duch K, Bańkowski S. Blood serum denaturation profile examined by differential scanning calorimetry reflects the effort put into ultramarathon by amateur long-distance runners. J Therm Biol. 2021;99. doi:10.1016/j.jtherbio.2021.103013
- Kędra-Królik K, Chmielewska I, Michnik A, Zarzycki P. Blood Serum Calorimetry Indicates the Chemotherapeutic Efficacy in Lung Cancer Treatment. Sci Rep. 2017;7(1). doi:10.1038/s41598-017-17004-x
- Fish DJ, Brewood GP, Kim JS, Garbett NC, Chaires JB, Benight AS. Statistical analysis of plasma thermograms measured by differential scanning calorimetry. Biophys Chem. 2010;152(1-3):184-190. doi:10.1016/j.bpc.2010.09.007
- Todinova S, Krumova S, Kurtev P, et al. Calorimetry-based profiling of blood plasma from colorectal cancer patients. Biochim Biophys Acta Gen Subj. 2012;1820(12):1879-1885. doi:10.1016/j.bbagen.2012.08.001
- Krumova S, Rukova B, Todinova S, et al. Calorimetric monitoring of the serum proteome in schizophrenia patients. Thermochim Acta. 2013;572:59-64. doi:10.1016/j.tca.2013.09.015
- Ferencz A, Lőrinczy D. DSC measurements of blood plasma on patients with chronic pancreatitis and operable and inoperable pancreatic adenocarcinoma. J Therm Anal Calorim. 2017;127(2):1187-1192. doi:10.1007/s10973-016-5371-4
- Barceló F, Cerdà JJ, Gutiérrez A, et al. Characterization of monoclonal gammopathy of undetermined significance by calorimetric analysis of blood serum proteome. PLoS One. 2015;10(3). doi:10.1371/journal.pone.0120316
- Farkas P, Könczöl F, Lőrinczy D. Monitoring the side effects with DSC caused by cyclophosphamide treatment. J Therm Anal Calorim. 2020;142(2):765-770. doi:10.1007/s10973-019-09064-0
- Garbett NC, Mekmaysy CS, Helm CW, Jenson AB, Chaires JB. Differential scanning calorimetry of blood plasma for clinical diagnosis and monitoring. Exp Mol Pathol. 2009;86(3):186-191. doi:10.1016/j.yexmp.2008.12.001
- Peters T. All About Albumin: Biochemistry, Genetics, and Medical Applications. Academic Press,; 1995.
- Bohlooli M, Moosavi-Movahedi AA, Taghavi F, et al. Investigation of thermal reversibility and stability of glycated human serum albumin. Int J Biol Macromol. 2013;62:358-364. doi:10.1016/j.ijbiomac.2013.09.015
- Bohlooli M, Moosavi-Movahedi AA, Taghavi F, et al. Inhibition of fluorescent advanced glycation end products (AGEs) of human serum albumin upon incubation with 3-β-hydroxybutyrate. Mol Biol Rep. 2014;41(6):3705-3713. doi:10.1007/s11033-014-3235-1
- Ajmal MR, Chandel TI, Alam P, et al. Fibrillogenesis of human serum albumin in the presence of levodopa – spectroscopic, calorimetric and microscopic studies. Int J Biol Macromol. 2017;94:301-308. doi:10.1016/j.ijbiomac.2016.10.025
- Guglielmelli A, Rizzuti B, Guzzi R. Stereoselective and domain-specific effects of ibuprofen on the thermal stability of human serum albumin. European Journal of Pharmaceutical Sciences. 2018;112:122-131. doi:10.1016/j.ejps.2017.11.013
- Gorobets MG, Wasserman LA, Bychkova A V., Rosenfeld MA. Thermodynamic features of bovine and human serum albumins under ozone and hydrogen peroxide induced oxidation. DSC study. Chem Phys. 2019;523:34-41. doi:10.1016/j.chemphys.2019.03.018
- Gan N, Sun Q, Suo Z, et al. How hydrophilic group affects drug–protein binding modes: Differences in interaction between sirtuins inhibitors Tenovin-1/Tenovin-6 and human serum albumin. J Pharm Biomed Anal. 2021;201. doi:10.1016/j.jpba.2021.114121
- Gorobets MG, Wasserman LA, Vasilyeva AD, et al. Modification of human serum albumin under induced oxidation. Dokl Biochem Biophys. 2017;474(1):231-235. doi:10.1134/S1607672917030218
- Bruschi M, Candiano G, Santucci L, Ghiggeri GM. Oxidized albumin. the long way of a protein of uncertain function. Biochim Biophys Acta Gen Subj. 2013;1830(12):5473-5479. doi:10.1016/j.bbagen.2013.04.017
- Palumbo E, Piotto C, Calura E, et al. Individual Radiosensitivity in Oncological Patients: Linking Adverse Normal Tissue Reactions and Genetic Features. Front Oncol. 2019;9. doi:10.3389/fonc.2019.00987
- Matyjanka A, Fornalski KW. Individual radiosensitivity – is it possible to precisely determine it? Postępy Techniki Jądrowej. 2024;67(2):2-17.
- Michnik A, Polaczek-Grelik K, Staś M, Sadowska-Krępa E, Gibińska J, Drzazga Z. Delayed effects of neutron radiation on human serum: In vitro DSC study. J Therm Anal Calorim. 2016;126(1):37-45. doi:10.1007/s10973-016-5255-7
- Berlett BS, Stadtman ER. Protein Oxidation in Aging, Disease, and Oxidative Stress*. http://www.jbc.org
- Levine RL, Stadtman ER. Oxidative Modi®cation of Proteins during Aging. www.elsevier.com/locate/expgero
- Requena JR, Levine RL, Stadtman ER. Recent advances in the analysis of oxidized proteins. Amino Acids. 2003;25(3-4):221-226. doi:10.1007/s00726-003-0012-1
- Richardson AG, Schadt EE. The role of macromolecular damage in aging and age-related disease. Journals of Gerontology - Series A Biological Sciences and Medical Sciences. 2014;69:S28-S32. doi:10.1093/gerona/glu056
- Frolov A, Hoffmann R. Identification and relative quantification of specific glycation sites in human serum albumin. Anal Bioanal Chem. 2010;397(6):2349-2356. doi:10.1007/s00216-010-3810-9
- Bodiga VL, Eda SR, Veduruvalasa VD, et al. Attenuation of non-enzymatic thermal glycation of bovine serum albumin (BSA) using β-carotene. Int J Biol Macromol. 2013;56:41-48. doi:10.1016/j.ijbiomac.2013.01.030
- Bohlooli M, Moosavi-Movahedi AA, Ghaffari-Moghaddam M, et al. Comparative study of thermal domains analyzing of glycated and non-glycated human serum albumin. Thermochim Acta. 2014;594:e1-e10. doi:10.1016/j.tca.2014.08.034
- Thornalley PJ, Rabbani N. Detection of oxidized and glycated proteins in clinical samples using mass spectrometry - A user’s perspective. Biochim Biophys Acta Gen Subj. 2014;1840(2):818-829. doi:10.1016/j.bbagen.2013.03.025
- Musante L, Bruschi M, Candiano G, et al. Characterization of oxidation end product of plasma albumin “in vivo.” Biochem Biophys Res Commun. 2006;349(2):668-673. doi:10.1016/j.bbrc.2006.08.079
- Michnik A, Michalik K, Kluczewska A, Drzazga Z. Introduction COMPARATIVE DSC STUDY OF HUMAN AND BOVINE SERUM ALBUMIN. Vol 84.; 2006.
- Pîrnău A, Mic M, Neamţu S, Floare CG, Bogdan M. Calorimetric and spectroscopic studies of the interaction between zidovudine and human serum albumin. Spectrochim Acta A Mol Biomol Spectrosc. 2018;191:226-232. doi:10.1016/j.saa.2017.10.032
- Maciążek-Jurczyk M, Szkudlarek A, Chudzik M, Pożycka J, Sułkowska A. Alteration of human serum albumin binding properties induced by modifications: A review. Spectrochim Acta A Mol Biomol Spectrosc. 2018;188:675-683. doi:10.1016/j.saa.2017.05.023
- Szkudlarek A, Wilk M, Maciazek-Jurczyk M. In vitro investigations of acetohexamide binding to glycated serum albumin in the presence of fatty acid. Molecules. 2020;25(10). doi:10.3390/molecules25102340
- Maciążek-Jurczyk M, Janas K, Pożycka J, et al. Human serum albumin aggregation/fibrillation and its abilities to drugs binding. Molecules. 2020;25(3). doi:10.3390/molecules25030618
- Koslen MM, Eskew MW, Pinkert V, et al. Capture Reagent and Strategy for Retrieving Albumin-Bound Ligands from Plasma. Adv Biol Chem. 2019;09(03):110-134. doi:10.4236/abc.2019.93009