Polyansky AA - Search Results

1

Atomistic mechanism of the constitutive activation of PDGFRA via its transmembrane domain.

Polyansky AA, Bocharov EV, Velghe AI, Kuznetsov AS, Bocharova OV, Urban AS, Arseniev AS, Zagrovic B, Demoulin JB, Efremov RG. Polyansky AA, et al. Biochim Biophys Acta Gen Subj. 2019 Jan;1863(1):82-95. doi: 10.1016/j.bbagen.2018.09.011. Epub 2018 Sep 22. Biochim Biophys Acta Gen Subj. 2019. PMID: 30253204

2

Effect of lipid composition on the "membrane response" induced by a fusion peptide.

Volynsky PE, Polyansky AA, Simakov NA, Arseniev AS, Efremov RG. Volynsky PE, et al. Among authors: polyansky aa. Biochemistry. 2005 Nov 8;44(44):14626-37. doi: 10.1021/bi0514562. Biochemistry. 2005. PMID: 16262262

3

Role of lipid charge in organization of water/lipid bilayer interface: insights via computer simulations.

Polyansky AA, Volynsky PE, Nolde DE, Arseniev AS, Efremov RG. Polyansky AA, et al. J Phys Chem B. 2005 Aug 11;109(31):15052-9. doi: 10.1021/jp0510185. J Phys Chem B. 2005. PMID: 16852905

4

Spatial structure and activity mechanism of a novel spider antimicrobial peptide.

Dubovskii PV, Volynsky PE, Polyansky AA, Chupin VV, Efremov RG, Arseniev AS. Dubovskii PV, et al. Among authors: polyansky aa. Biochemistry. 2006 Sep 5;45(35):10759-67. doi: 10.1021/bi060635w. Biochemistry. 2006. PMID: 16939228

5

Computer simulations of membrane-lytic peptides: perspectives in drug design.

Polyansky AA, Volynsky PE, Efremov RG. Polyansky AA, et al. J Bioinform Comput Biol. 2007 Apr;5(2B):611-26. doi: 10.1142/s0219720007002783. J Bioinform Comput Biol. 2007. PMID: 17636865

6

Three-dimensional structure/hydrophobicity of latarcins specifies their mode of membrane activity.

Dubovskii PV, Volynsky PE, Polyansky AA, Karpunin DV, Chupin VV, Efremov RG, Arseniev AS. Dubovskii PV, et al. Among authors: polyansky aa. Biochemistry. 2008 Mar 18;47(11):3525-33. doi: 10.1021/bi702203w. Epub 2008 Feb 23. Biochemistry. 2008. PMID: 18293934

7

Adaptation of a membrane-active peptide to heterogeneous environment. II. The role of mosaic nature of the membrane surface.

Polyansky AA, Volynsky PE, Arseniev AS, Efremov RG. Polyansky AA, et al. J Phys Chem B. 2009 Jan 29;113(4):1120-6. doi: 10.1021/jp803641x. J Phys Chem B. 2009. PMID: 19125636

8

Adaptation of a membrane-active peptide to heterogeneous environment. I. Structural plasticity of the peptide.

Polyansky AA, Volynsky PE, Arseniev AS, Efremov RG. Polyansky AA, et al. J Phys Chem B. 2009 Jan 29;113(4):1107-19. doi: 10.1021/jp803640e. J Phys Chem B. 2009. PMID: 19125640

9

N-terminal amphipathic helix as a trigger of hemolytic activity in antimicrobial peptides: a case study in latarcins.

Polyansky AA, Vassilevski AA, Volynsky PE, Vorontsova OV, Samsonova OV, Egorova NS, Krylov NA, Feofanov AV, Arseniev AS, Grishin EV, Efremov RG. Polyansky AA, et al. FEBS Lett. 2009 Jul 21;583(14):2425-8. doi: 10.1016/j.febslet.2009.06.044. Epub 2009 Jun 27. FEBS Lett. 2009. PMID: 19563807 Free article.

10

Linker and/or transmembrane regions of influenza A/Group-1, A/Group-2, and type B virus hemagglutinins are packed differently within trimers.

Kordyukova LV, Serebryakova MV, Polyansky AA, Kropotkina EA, Alexeevski AV, Veit M, Efremov RG, Filippova IY, Baratova LA. Kordyukova LV, et al. Among authors: polyansky aa. Biochim Biophys Acta. 2011 Jul;1808(7):1843-54. doi: 10.1016/j.bbamem.2011.03.005. Epub 2011 Mar 21. Biochim Biophys Acta. 2011. PMID: 21420932 Free article.

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