Marchenkov V - Search Results

1

Back to GroEL-Assisted Protein Folding: GroES Binding-Induced Displacement of Denatured Proteins from GroEL to Bulk Solution.

Marchenkov V, Gorokhovatsky A, Marchenko N, Ivashina T, Semisotnov G. Marchenkov V, et al. Biomolecules. 2020 Jan 20;10(1):162. doi: 10.3390/biom10010162. Biomolecules. 2020. PMID: 31968530 Free PMC article.

2

Ligands regulate GroEL thermostability.

Surin AK, Kotova NV, Kashparov IA, Marchenkov VV, Marchenkova SYu, Semisotnov GV. Surin AK, et al. Among authors: marchenkov vv. FEBS Lett. 1997 Apr 1;405(3):260-2. doi: 10.1016/s0014-5793(97)00199-3. FEBS Lett. 1997. PMID: 9108300 Free article.

3

[Monomeric form of the molecular chaperone GroEL: structure, stability, and oligomerization].

Surin AK, Kotova NV, Marchenkova SIu, Marchenkov VV, Semisotnov GV. Surin AK, et al. Among authors: marchenkov vv. Bioorg Khim. 1999 May;25(5):358-64. Bioorg Khim. 1999. PMID: 10495893 Russian.

4

Homogeneous assay for biotin based on Aequorea victoria bioluminescence resonance energy transfer system.

Gorokhovatsky AY, Rudenko NV, Marchenkov VV, Skosyrev VS, Arzhanov MA, Burkhardt N, Zakharov MV, Semisotnov GV, Vinokurov LM, Alakhov YB. Gorokhovatsky AY, et al. Among authors: marchenkov vv. Anal Biochem. 2003 Feb 1;313(1):68-75. doi: 10.1016/s0003-2697(02)00514-6. Anal Biochem. 2003. PMID: 12576060

5

[Effect of ADP and GroES on interaction of molecular chaperonin GroEL with non-native lysozyme].

Marchenko NIu, Marchenkov VV, Kotova NV, Semisotnov GV, Bulankina NI, Kaliman PA. Marchenko NIu, et al. Among authors: marchenkov vv. Ukr Biokhim Zh (1999). 2003 May-Jun;75(3):88-94. Ukr Biokhim Zh (1999). 2003. PMID: 14577157 Russian.

6

Fusion of Aequorea victoria GFP and aequorin provides their Ca(2+)-induced interaction that results in red shift of GFP absorption and efficient bioluminescence energy transfer.

Gorokhovatsky AY, Marchenkov VV, Rudenko NV, Ivashina TV, Ksenzenko VN, Burkhardt N, Semisotnov GV, Vinokurov LM, Alakhov YB. Gorokhovatsky AY, et al. Among authors: marchenkov vv. Biochem Biophys Res Commun. 2004 Jul 30;320(3):703-11. doi: 10.1016/j.bbrc.2004.06.014. Biochem Biophys Res Commun. 2004. PMID: 15240105

7

[The interaction of the GroEL chaperone with early kinetic intermediates of renaturing proteins inhibits the formation of their native structure].

Marchenkov VV, Sokolovskiĭ IV, Kotova NV, Galzitskaya OV, Bochkareva ES, Girshovich AS, Semisotnov GV. Marchenkov VV, et al. Biofizika. 2004 Nov-Dec;49(6):987-94. Biofizika. 2004. PMID: 15612537 Russian.

8

Affinity chromatography of GroEL chaperonin based on denatured proteins: role of electrostatic interactions in regulation of GroEL affinity for protein substrates.

Marchenko NIu, Marchenkov VV, Kaĭsheva AL, Kashparov IA, Kotova NV, Kaliman PA, Semisotnov GV. Marchenko NIu, et al. Among authors: marchenkov vv. Biochemistry (Mosc). 2006 Dec;71(12):1357-64. doi: 10.1134/s000629790612011x. Biochemistry (Mosc). 2006. PMID: 17223789

9

Importance of a single disulfide bond for the PsbO protein of photosystem II: protein structure stability and soluble overexpression in Escherichia coli.

Nikitina J, Shutova T, Melnik B, Chernyshov S, Marchenkov V, Semisotnov G, Klimov V, Samuelsson G. Nikitina J, et al. Among authors: marchenkov v. Photosynth Res. 2008 Oct-Dec;98(1-3):391-403. doi: 10.1007/s11120-008-9327-9. Epub 2008 Aug 16. Photosynth Res. 2008. PMID: 18709441

10

GroEL-assisted protein folding: does it occur within the chaperonin inner cavity?

Marchenkov VV, Semisotnov GV. Marchenkov VV, et al. Int J Mol Sci. 2009 May 12;10(5):2066-2083. doi: 10.3390/ijms10052066. Int J Mol Sci. 2009. PMID: 19564940 Free PMC article. Review.

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