Search Results - "Artemova, N V"

Acceleration of protein aggregation by amphiphilic peptides: Transformation of supramolecular structure of the aggregates by Artemova, N. V., Stein-Margolina, V. A., Bumagina, Z. M., Gurvits, B. Ya

“…Protein self‐assembly and aggregation represent a special tool in biomedicine and biotechnology to produce biological materials for a wide range of…”
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Opioid peptides derived from food proteins suppress aggregation and promote reactivation of partly unfolded stressed proteins by Artemova, N.V., Bumagina, Z.M., Kasakov, A.S., Shubin, V.V., Gurvits, B.Ya

“…A new view of the opioid peptides is presented. The potential of small peptides derived from precursor food proteins, to bind to partly unfolded stressed…”
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Stabilization of the Central Part of Tropomyosin Molecule Alters the Ca2+-sensitivity of Actin-Myosin Interaction by Shchepkin, D V, Matyushenko, A M, Kopylova, G V, Artemova, N V, Bershitsky, S Y, Tsaturyan, A K, Levitsky, D I

“…We show that the mutations D137L and G126R, which stabilize the central part of the tropomyosin (Tm) molecule, increase both the maximal sliding velocity of…”
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RHEUMAORTOPEDICAL AID TO THE POPULATION OF RUSSIAN FEDERATION by Zhadenov, L L, Mitrofanov, V A, Artemova, N V

“…Analysis of the work of the Republican arthrologic center of Saratov Research Institute of Traumatology and Orthopedics was done. The reasons of the absence of…”
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Stabilization of the Central Part of Tropomyosin Molecule Alters the Ca 2+-sensitivity of Actin-Myosin Interaction by Shchepkin, D. V., Matyushenko, A. M., Kopylova, G. V., Artemova, N. V., Bershitsky, S. Y., Tsaturyan, A. K., Levitsky, D. I.

“…We show that the mutations D137L and G126R, which stabilize the central part of the tropomyosin (Tm) molecule, increase both the maximal sliding velocity of…”
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Opioid peptides derived from food proteins suppress aggregation and promote reactivation of partly unfolded stressed proteins by ARTEMOVA, N. V, BUMAGINA, Z. M, KASAKOV, A. S, SHUBIN, V. V, GURVITS, B. Ya

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The effects of stabilizing mutations in the central part of the α-chain of tropomyosin on the structural and functional properties of αβ-tropomyosin heterodimers by Matyushenko, A. M., Artemova, N. V., Shchepkin, D. V., Kopylova, G. V., Levitsky, D. I.

“…The effects of the D137L/G126R double mutation in the central part of the tropomyosin α-chain via the simultaneous replacement of two highly conserved…”
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The effects of stabilizing mutations in the central part of the [alpha]-chain of tropomyosin on the structural and functional properties of [alpha][beta]-tropomyosin heterodimers by Matyushenko, A M, Artemova, N V, Shchepkin, D V, Kopylova, G V, Levitsky, D I

“…The effects of the D137L/G126R double mutation in the central part of the tropomyosin [alpha]-chain via the simultaneous replacement of two highly conserved…”
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The effects of stabilizing mutations in the central part of the alpha -chain of tropomyosin on the structural and functional properties of alpha beta -tropomyosin heterodimers by Matyushenko, A M, Artemova, N V, Shchepkin, D V, Kopylova, G V, Levitsky, DI

“…The effects of the D137L/G126R double mutation in the central part of the tropomyosin alpha -chain via the simultaneous replacement of two highly conserved…”
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Efficient method for the synthesis of diphosphine ligands with a heteroaryl–aryl bridge by Artemova, Nataliya V., Chevykalova, Marina N., Luzikov, Yuri N., Nifant'ev, Ilya E., Nifant'ev, Eduard E.

“…A new efficient method for the synthesis of heteroaryl–aryl diphosphine ligands by direct double metallation of heteroaryl–aryls followed by phosphorylation of…”
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Studies of the possibility of indicating bacteria in water by a spectroultramicroscopic method by Artemova, V N

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