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Самый цитируемый биологический институт РФ *

Муронец Владимир Израилевич

профессор, доктор биологических наук
Контакт
Телефон: 8 (495) 939-14-56
Адрес: корп. А, к. 435 или корп. Б, к. 417
Факс: 8 (495) 939-31-81
E-mail: Этот адрес e-mail защищен от спам-ботов, Вам необходимо включить JavaScript, что бы его увидеть.
Возглавляет отдел: Отдел биохимии животной клетки
Подразделение: Отдел биохимии животной клетки
Статьи
  1. Evdokimov V.V., Barinova K.V., Turovetskii V.B., Muronetz V.I., Schmalhausen E.V. (2015) Low concentrations of hydrogen peroxide activate the antioxidant defense system in human sperm cells. Biochem.-Moscow, 80 (9): 1178-1185. >>

  2. Kuravsky M.L., Barinova K.V., Asryants R.A., Schmalhausen E.V., Muronetz V.I. (2015) Structural basis for the NAD binding cooperativity and catalytic characteristics of sperm-specific glyceraldehyde-3-phosphate dehydrogenase. Biochimie, 115: 28-34. >>

  3. Semenyuk P., Orlov V., Muronetz V., Izumrudov V. (2015) Two-stage binding of a protein to the polyanion: Non-denaturing interaction followed by denaturation. Polymer, 65: 210-214. >>

  4. Makshakova O.N., Semenyuk P.I., Kuravsky M.L., Ermakova E.A., Zuev Y.F., Muronetz V.I. (2015) Structural basis for regulation of stability and activity in glyceraldehyde-3-phosphate dehydrogenases. Differential scanning calorimetry and molecular dynamics. J. Struct. Biol., 190 (2): 224-235. >>

  5. Lazarev V.F., Benken K.A., Semenyuk P.I., Sarantseva S.V., Bolshakova O.I., Mikhaylova E.R., Muronetz V.I., Guzhova I.V., Margulis B.A. (2015) GAPDH binders as potential drugs for the therapy of polyglutamine diseases: Design of a new screening assay. FEBS Lett., 589 (5): 581-587. >>

  6. Semenyuk P.I., Moiseeva E.V., Stroylova Y.Y., Lotti M., Izumrudov V.A., Muronetz V.I. (2015) Sulfated and sulfonated polymers are able to solubilize efficiently the protein aggregates of different nature. Arch. Biochem. Biophys., 567: 22-29. >>

  7. Kuravsky M., Barinova K., Marakhovskaya A., Eldarov M., Semenyuk P., Muronetz V., Schmalhausen E. (2014) Sperm-specific glyceraldehyde-3-phosphate dehydrogenase is stabilized by additional proline residues and an interdomain salt bridge. BBA-Proteins Proteomics, 1844 (10): 1820-1826. >>

  8. Stroylova Y.Y., Semenyuk P.I., Asriyantz R.A., Gaillard C., Haertle T., Muronetz V.I. (2014) Creation of Catalytically Active Particles From Enzymes Crosslinked with a Natural Bifunctional Agent-Homocysteine Thiolactone. Biopolymers, 101 (9): 975-984. >>

  9. Stroylova Y.Y., Kiselev G.G., Schmalhausen E.V., Muronetz V.I. (2014) Prions and chaperones: Friends or foes?. Biochem.-Moscow, 79 (8): 761-775. >>

  10. Arutyunov D., Schmalhausen E., Orlov V., Rahuel-Clermont S., Nagradova N., Branlant G., Muronetz V. (2013) An unusual effect of NADP(+) on the thermostability of the nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans. Biochem. Cell Biol., 91 (5): 295-302. >>

  11. Semenyuk P.I., Muronetz V.I., Haertle T., Izumrudov V.A. (2013) Effect of poly(phosphate) anions on glyceraldehyde-3-phosphate dehydrogenase structure and thermal aggregation: comparison with influence of poly(sulfoanions). Biochim. Biophys. Acta-Gen. Subj., 1830 (10): 4800-4805. >>

  12. Pyrkov T.V., Sevostyanova I.A., Schmalhausen E.V., Shkoporov A.N., Vinnik A.A., Muronetz V.I., Severin F.F., Fedichev P.O. (2013) Structure-Based Design of Small-Molecule Ligands of Phosphofructokinase-2 Activating or Inhibiting Glycolysis. ChemMedChem, 8 (8): 1322-1329. >>

  13. Stroylova Y.Y., Konnova T., Zuev Y.F., Chobert J.M., Choiset Y., Haertle T., Muronetz V.I. (2013) Selective Introduction of Sulfhydryl Groups into Recombinant Proteins for Study of Protein-Protein Interactions. Chromatographia, 76 (11): 621-628. >>

  14. Arutyunova E.I., Domnina L.V., Chudinova A.A., Makshakova O.N., Arutyunov D.Y., Muronetz V.I. (2013) Localization of non-native D-glyceraldehyde-3-phosphate dehydrogenase in growing and apoptotic HeLa cells. Biochem.-Moscow, 78 (1): 91-95. >>

  15. Sevostyanova I.A., Kulikova K.V., Kuravsky M.L., Schmalhausen E.V., Muronetz V.I. (2012) Sperm-specific glyceraldehyde-3-phosphate dehydrogenase is expressed in melanoma cells. Biochem. Biophys. Res. Commun., 427 (3): 649-653. >>

  16. Stroylova Y.Y., Chobert J.M., Muronetz V.I., Jakubowski H., Haertle T. (2012) N-homocysteinylation of ovine prion protein induces amyloid-like transformation. Arch. Biochem. Biophys., 526 (1): 29-37. >>

  17. Kuravsky M.L., Schmalhausen E.V., Pozdnyakova N.V., Muronetz V.I. (2012) Isolation of antibodies against different protein conformations using immunoaffinity chromatography. Anal. Biochem., 426 (1): 47-53. >>

  18. Naletova I.N., Popova K.M., Eldarov M.A., Kuravsky M.L., Schmalhausen E.V., Sevostyanova I.A., Muronetz V.I. (2011) Chaperonin TRiC assists the refolding of sperm-specific glyceraldehyde-3-phosphate dehydrogenase. Archives of Biochemistry and Biophysics, 516 (1): 75–83. >>

  19. Kiselev G.G., Naletova I.N., Sheval E.V., Stroylova Y.Y., Schmalhausen E.V., Haertlé T., Muronetz V.I. (2011) Chaperonins induce an amyloid-like transformation of ovine prion protein: The fundamental difference in action between eukaryotic TRiC and bacterial GroEL. Biochimica et Biophysica Acta, 1814 (12): 1730–1738. >>

  20. Guzhova I.V., Lazarev V.F., Kaznacheeva A.V., Ippolitova M.V., Muronetz V.I., Kinev A.V., Margulis B.A. (2011) Novel mechanism of Hsp70 chaperone-mediated prevention of polyglutamine aggregates in a cellular model of huntington disease. Human Molecular Genetics, 20 (20): 3953-3963.

  21. Stroylova Y.Y., Zimny J., Yousefi R., Chobert J.M., Jakubowski H., Muronetz V.I., Haertle T. (2011) Aggregation and structural changes of alpha(S1)-, beta- and kappa-caseins induced by homocysteinylation. Biochimica et Biophysica Acta-Proteins and Proteomics, 1814 (10): 1234-1245.

  22. Kuravsky M.L., Aleshin V.V., Frishman D., Muronetz V.I. (2011) Testis-specific glyceraldehyde-3-phosphate dehydrogenase: origin and evolution. BMC Evolutionary Biology, 11: 160.

  23. Elkina Y.L., Atroshchenko M.M., Bragina E.E., Muronetz V.I., Schmalhausen E.V. (2011) Oxidation of Glyceraldehyde-3-Phosphate Dehydrogenase Decreases Sperm Motility. Biochemistry-Moscow, 76 (2): 268-272.

  24. Chernorizov K.A., Elkina J.L., Semenyuk P.I., Svedas V.K., Muronetz V.I. (2010) Novel Inhibitors of Glyceraldehyde-3-phosphate Dehydrogenase: Covalent Modification of NAD-Binding Site by Aromatic Thiols. Biochemistry-Moscow, 75 (12): 1444-1449.

  25. Elkina Y.L., Kuravsky M.L., el'darov M.A., Stogov S.V., Muronetz V.I., Schmalhausen E.V. (2010) Recombinant human sperm-specific glyceraldehyde-3-phosphate dehydrogenase: Structural basis for enhanced stability. Biochimica et Biophysica Acta-Proteins and Proteomics, 1804 (12): 2207-2212.

  26. Eronina T.B., Chebotareva N.A., Bazhina S.G., Kleymenov S.Y., Naletova I.N., Muronetz V.I., Kurganov B.I. (2010) Effect of GroEL on Thermal Aggregation of Glycogen Phosphorylase b from Rabbit Skeletal Muscle. Macromolecular Bioscience, 10 (7): 768-774.

  27. Stogov S.V., Izumrudov V.A., Muronetz V.I. (2010) Structural changes of a protein bound to a polyelectrolyte depend on the hydrophobicity and polymerization degree of the polyelectrolyte. Biochemistry-Moscow, 75 (4): 437-442.

  28. Markossian K.A., Golub N.V., Chebotareva N.A., Asryants R.A., Naletova I.N., Muronetz V.I., Muranov K.O., Kurganov B.I. (2010) Comparative Analysis of the Effects of alpha-Crystallin and GroEL on the Kinetics of Thermal Aggregation of Rabbit Muscle Glyceraldehyde-3-Phosphate Dehydrogenase. Protein Journal, 29 (1): 11-25.

  29. Gaudin J.C., le Parc A., Castrec B., Ropers M.H., Choiset Y., Shchutskaya J., Yousefi R., Muronetz V.I., Zuev Y., Chobert J.M., Haertle T. (2009) Engineering of caseins and modulation of their structures and interactions. Biotechnology Advances, 27 (6): 1124-1131.

  30. Stogov S.V., Muronetz V.I., Izumrudov V.A. (2009) Short synthetic polyelectrolytes destabilize proteins most efficiently. Doklady Biochemistry and Biophysics, 427 (1): 187-190.

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