English
Русский
English
Open access Molecular systems

Analysis of the level of oxidative stress by assessing the damage to the plasma protein serum albumin under the influence of an oxidizing agent

Irina Vlasova1,2
Irina Vlasova
Irina Vlasova
Сorrespondence:[email protected]
1
Center For Theoretical Problems of Physico-Chemical Pharmacology RAS, 109029, Srednyaya Kalitnikovskaya 30, Moscow, Russia
2
Lomonosov Moscow State University, Physics Faculty 119991, Leninskiye Gory 1-2, Moscow, Russia
Find this author on Google Scholar
,
Alexander Vlasov2
Alexander Vlasov
Alexander Vlasov
2
Lomonosov Moscow State University, Physics Faculty 119991, Leninskiye Gory 1-2, Moscow, Russia
Find this author on Google Scholar
1.
Center For Theoretical Problems of Physico-Chemical Pharmacology RAS, 109029, Srednyaya Kalitnikovskaya 30, Moscow, Russia
2.
Lomonosov Moscow State University, Physics Faculty 119991, Leninskiye Gory 1-2, Moscow, Russia

References of this article:

  1. Mitochondrial Reactive Oxygen Species (ROS) and ROS-Induced ROS Release

    D. Zorov, M. Juhaszova, S. Sollott

    Physiological Reviews. 2014, 94, 909-950

    https://doi.org/10.1152/physrev.00026.2013

    Article|Google Scholar

  2. Reactive Oxygen Species (ROS)-Responsive Prodrugs, Probes, and Theranostic Prodrugs: Applications in the ROS-Related Diseases

    P. Wang, Q. Gong, J. Hu, X. Li, X. Zhang

    Journal of Medicinal Chemistry. 2021, 64, 298-325

    https://doi.org/10.1021/acs.jmedchem.0c01704

    Article|Google Scholar

  3. Superoxide dismutases: Dual roles in controlling ROS damage and regulating ROS signaling

    Y. Wang, R. Branicky, A. Noë, S. Hekimi

    Journal of Cell Biology. 2018, 217, 1915-1928

    https://doi.org/10.1083/jcb.201708007

    Article|Google Scholar

  4. Reactive oxygen species are physiological mediators of the noradrenergic signaling pathway in the mouse supraoptic nucleus

    R. St-Louis, C. Parmentier, V. Grange-Messent, S. Mhaouty-Kodja, H. Hardin-Pouzet

    Free Radical Biology and Medicine. 2014, 71, 231-239

    https://doi.org/10.1016/j.freeradbiomed.2014.03.024

    Article|Google Scholar

  5. UVB Radiation Induces Apoptosis in Keratinocytes by Activating a Pathway Linked to “BLT2-Reactive Oxygen Species”

    H. Ryu, C. Kim, J. Kim, J. Chung, J. Kim

    Journal of Investigative Dermatology. 2010, 130, 1095-1106

    https://doi.org/10.1038/jid.2009.436

    Article|Google Scholar

  6. Reactive oxygen species mediate A??(25-35)-induced activation of BV-2 microglia

    J. Kang, E. Park, I. Jou, J. Kim, E. Joe

    Neuroreport. 2001, 12, 1449-1452

    https://doi.org/10.1097/00001756-200105250-00030

    Article|Google Scholar

  7. Mitochondria and reactive oxygen species in renal cancer

    E. HERVOUET, H. SIMONNET, C. GODINOT

    Biochimie. 2007, 89, 1080-1088

    https://doi.org/10.1016/j.biochi.2007.03.010

    Article|Google Scholar

  8. Increased Stress-Induced Generation of Reactive Oxygen Species and Apoptosis in Human Keratoconus Fibroblasts

    M. Chwa, S. Atilano, V. Reddy, N. Jordan, D. Kim, M. Kenney

    Investigative Opthalmology & Visual Science. 2006, 47, 1902

    https://doi.org/10.1167/iovs.05-0828

    Article|Google Scholar

  9. Elevated Cytosolic Na <sup>+</sup> Increases Mitochondrial Formation of Reactive Oxygen Species in Failing Cardiac Myocytes

    M. Kohlhaas, T. Liu, A. Knopp, T. Zeller, M. Ong, M. Böhm, B. O'Rourke, C. Maack

    Circulation. 2010, 121, 1606-1613

    https://doi.org/10.1161/CIRCULATIONAHA.109.914911

    Article|Google Scholar

  10. Reactive Oxygen Species, Cancer and Anti-Cancer Therapies

    G. Manda, M. Nechifor, T. Neagu

    Current Chemical Biology. 2009, 3, 342-366

    https://doi.org/10.2174/187231309787158271

    Article|Google Scholar

  11. Role of reactive oxygen and nitrogen species in the vascular responses to inflammation

    P. R. Kvietys and D. N. Granger

    Free Radical Biology and Medicine. 2012, 52(3), 556-592

    https://doi.org/10.1016/j.freeradbiomed. 2011.11.002

    Article|Google Scholar

  12. Окислительный стресс. Биохимический и патофизиологический аспекты

    Н. К. Зенков, В. З. Ланкин, Е. Б. Меньщикова

    М: МАИК Наука / Интерпериодика. 2001, ,

    Google Scholar

  13. Альбумин сыворотки крови в клинической медицине

    Ю. А. Грызунов, Г. Е. Добрецов

    М.: ИРИУС. 1994, ,

    Google Scholar

  14. Физическая химия. Принципы и применение в биологических науках

    И. Тиноко, К. Зауэр, Дж. Вэнг, Дж. Паглиси

    М.: Техносфера. 2005, ,

    Google Scholar

  15. Оптическая спектроскопия для химиков и биологов

    В. Шмидт

    М.: Техносфера. 2007, ,

    Google Scholar

  16. Interaction of ionic detergent cethyltrimethylammonium bromide with human serum albumin at various values of pH: Spectroscopic study

    I. Vlasova, A. Vlasov, A. Saletsky

    Journal of Molecular Structure. 2010, 984, 332-338

    https://doi.org/10.1016/j.molstruc.2010.09.051

    Article|Google Scholar

  17. Interaction of cationic surfactant cethyltrimethylammonium bromide with bovine serum albumin in dependence on pH: A study of tryptophan fluorescence

    I. Vlasova, V. Zhuravleva, A. Vlasov, A. Saletsky

    Journal of Molecular Structure. 2013, 1034, 89-94

    https://doi.org/10.1016/j.molstruc.2012.08.053

    Article|Google Scholar

  18. Denaturation of bovine serum albumin initiated by sodium dodecyl sulfate as monitored via the intrinsic fluorescence of the protein

    I. Vlasova, V. Zhuravleva, A. Saletsky

    Russian Journal of Physical Chemistry B. 2014, 8, 385-390

    https://doi.org/10.1134/S1990793114030154

    Article|Google Scholar

  19. Association Constants in the Bovine Serum Albumin/Human Serum Albumin–Tween 20 System in Aqueous Solutions

    I. Vlasova, A. Vlasov, G. Grapendaal, A. Saletskii

    Russian Journal of Physical Chemistry A. 2018, 92, 714-718

    https://doi.org/10.1134/S0036024418040325

    Article|Google Scholar

  20. Protein oxidation in aging and the removal of oxidized proteins

    A. Höhn, J. König, T. Grune

    Journal of Proteomics. 2013, 92, 132-159

    https://doi.org/10.1016/j.jprot.2013.01.004

    Article|Google Scholar

  21. Protein S-nitrosylation and oxidation contribute to protein misfolding in neurodegeneration

    T. Nakamura, C. Oh, X. Zhang, S. Lipton

    Free Radical Biology and Medicine. 2021, 172, 562-577

    https://doi.org/10.1016/j.freeradbiomed.2021.07.002

    Article|Google Scholar

  22. Ozone-induced damage of fibrinogen molecules: identification of oxidation sites by high-resolution mass spectrometry

    L. Yurina, A. Vasilyeva, M. Indeykina, A. Bugrova, M. Biryukova, A. Kononikhin, E. Nikolaev, M. Rosenfeld

    Free Radical Research. 2019, 53, 430-455

    https://doi.org/10.1080/10715762.2019.1600686

    Article|Google Scholar