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Molekuliarnaia Biologiia|April 29, 2015
[The ability of cells to adjust to the low oxigen content associated with Na,K-ATPase glutationilation]I Iu Petrushanko, O V Simonenko, K M Burnysheva, et al.
Biomeditsinskaia Khimiia|May 16, 2015
[Physico-chemical methods for studing β-amyloid aggregation]S P Radko, S A Khmeleva, E V Suprun, et al.
Acta Crystallographica. Section D, Biological Crystallography|May 23, 2013
Structure and functional studies of the ribonuclease binase Glu43Ala/Phe81Ala mutantV A Mitkevich, A A Schulga, A A Trofimov, et al.
Molekuliarnaia Biologiia|December 8, 2023
[Low-Molecular Thiols as a Factor Improving the Sensitivity of Escherichia coli Mutants with Impaired ADP-Heptose Synthesis to Antibiotics]T A Seregina, I Yu Petrushanko, P I Zaripov, et al.
Biomeditsinskaia Khimiia|November 8, 2008
[Determination of "amino acids conflicts" and amino acids substitutions in primary structures of 41 human proteins by use the proteomic technologies]M A Kovaleva, L I Kovalev, L S Eremina, et al.
Molekuliarnaia Biologiia|December 4, 2020
[Direct Molecular Fishing of Zinc-Dependent Protein Partners of Amyloid-beta 1-16 with the Taiwan (D7H) Mutation and Phosphorylated Ser8 Residue]P V Ershov, Yu V Mezentsev, E O Yablokov, et al.
Biochimie|February 26, 2014
Ribonuclease binase decreases destructive changes of the liver and restores its regeneration potential in mouse lung carcinoma modelA V Sen'kova, N L Mironova, O A Patutina, et al.
Molekuliarnaia Biologiia|August 17, 2018
[Enalaprilat Inhibits Zinc-Dependent Oligomerization of Metal-Binding Domain of Amyloid-beta Isoforms and Protects Human Neuroblastoma Cells from Toxic Action of these Isoforms]S A Kozin, V I Polshakov, Y V Mezentsev, et al.
Molekuliarnaia Biologiia|June 25, 2015
[Effect of mutations and modifications of amino acid residues on zinc-induced interaction of the metal-binding domain of β-amyloid with DNA]S A Khmeleva, Y V Mezentsev, S A Kozin, et al.
Bioorganicheskaia Khimiia|December 14, 2004
[I87E mutation prevents barstar dimerization]D S Korchuganov, A A Shul'ga, Ia S Ermoliuk, et al.
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