| Year |
Citation |
Score |
| 2024 |
Sulatskaya AI, Stepanenko OV, Sulatsky MI, Mikhailova EV, Kuznetsova IM, Turoverov KK, Stepanenko OV. Structural determinants of odorant-binding proteins affecting their ability to form amyloid fibrils. International Journal of Biological Macromolecules. 264: 130699. PMID 38460650 DOI: 10.1016/j.ijbiomac.2024.130699 |
0.356 |
|
| 2024 |
Sulatsky MI, Stepanenko OV, Stepanenko OV, Kuznetsova IM, Turoverov KK, Sulatskaya AI. Prediction of the Feasibility of Using the ≪Gold Standard≫ Thioflavin T to Detect Amyloid Fibril in Acidic Media. Analytical Chemistry. 96: 2158-2164. PMID 38269442 DOI: 10.1021/acs.analchem.3c05118 |
0.371 |
|
| 2023 |
Stepanenko OV, Sulatskaya AI, Sulatsky MI, Mikhailova EV, Kuznetsova IM, Turoverov KK, Stepanenko OV. Mammalian odorant-binding proteins are prone to form amorphous aggregates and amyloid fibrils. International Journal of Biological Macromolecules. 253: 126872. PMID 37722633 DOI: 10.1016/j.ijbiomac.2023.126872 |
0.383 |
|
| 2022 |
Stepanenko OV, Kuznetsova IM, Turoverov KK, Stepanenko OV. Impact of Double Covalent Binding of BV in NIR FPs on Their Spectral and Physicochemical Properties. International Journal of Molecular Sciences. 23. PMID 35806351 DOI: 10.3390/ijms23137347 |
0.405 |
|
| 2021 |
Stepanenko OV, Sulatsky MI, Mikhailova EV, Kuznetsova IM, Turoverov KK, Stepanenko OV, Sulatskaya AI. New findings on GFP-like protein application as fluorescent tags: Fibrillogenesis, oligomerization, and amorphous aggregation. International Journal of Biological Macromolecules. 192: 1304-1310. PMID 34687761 DOI: 10.1016/j.ijbiomac.2021.10.107 |
0.451 |
|
| 2021 |
Fonin AV, Silonov SA, Antifeeva IA, Stepanenko OV, Stepanenko OV, Fefilova AS, Povarova OI, Gavrilova AA, Kuznetsova IM, Turoverov KK. Photophysical Properties of BADAN Revealed in the Study of GGBP Structural Transitions. International Journal of Molecular Sciences. 22. PMID 34681772 DOI: 10.3390/ijms222011113 |
0.364 |
|
| 2021 |
Fonin AV, Antifeeva IA, Shpironok OG, Stepanenko OV, Silonov SA, Stepanenko OV, Antifeev IE, Romanovich AE, Kuznetsova IM, Kim JI, Uversky VN, Turoverov KK. Photo-dependent membrane-less organelles formed from plant phyB and PIF6 proteins in mammalian cells. International Journal of Biological Macromolecules. 176: 325-331. PMID 33582218 DOI: 10.1016/j.ijbiomac.2021.02.075 |
0.325 |
|
| 2020 |
Stepanenko OV, Stepanenko OV, Turoverov KK, Kuznetsova IM. Probing the allostery in dimeric near-infrared biomarkers derived from the bacterial phytochromes: The impact of the T204A substitution on the inter-monomer interaction. International Journal of Biological Macromolecules. 162: 894-902. PMID 32569685 DOI: 10.1016/J.Ijbiomac.2020.06.162 |
0.452 |
|
| 2020 |
Sulatsky MI, Sulatskaya AI, Stepanenko OV, Povarova OI, Kuznetsova IM, Turoverov KK. Denaturant effect on amyloid fibrils: Declasterization, depolymerization, denaturation and reassembly. International Journal of Biological Macromolecules. 150: 681-694. PMID 32057863 DOI: 10.1016/J.Ijbiomac.2020.01.290 |
0.369 |
|
| 2019 |
Stepanenko OV, Stepanenko OV, Shpironok OG, Fonin AV, Kuznetsova IM, Turoverov KK. Near-Infrared Markers based on Bacterial Phytochromes with Phycocyanobilin as a Chromophore. International Journal of Molecular Sciences. 20. PMID 31810174 DOI: 10.3390/Ijms20236067 |
0.382 |
|
| 2019 |
Stepanenko OV, Stepanenko OV, Kuznetsova IM, Turoverov KK. The unfolding of iRFP713 in a crowded milieu. Peerj. 7: e6707. PMID 30993043 DOI: 10.7717/Peerj.6707 |
0.484 |
|
| 2018 |
Fonin AV, Stepanenko OV, Sitdikova AK, Antifeeva IA, Kostyleva EI, Polyanichko AM, Karasev MM, Silonov SA, Povarova OI, Kuznetsova IM, Uversky VN, Turoverov KК. Folding of poly-amino acids and intrinsically disordered proteins in overcrowded milieu induced by pH change. International Journal of Biological Macromolecules. PMID 30529354 DOI: 10.1016/J.Ijbiomac.2018.12.038 |
0.493 |
|
| 2018 |
Stepanenko OV, Stepanenko OV, Kuznetsova IM, Turoverov KK. The Pathways of the iRFP713 Unfolding Induced by Different Denaturants. International Journal of Molecular Sciences. 19. PMID 30223568 DOI: 10.3390/Ijms19092776 |
0.509 |
|
| 2017 |
Stepanenko OV, Stepanenko OV, Kuznetsova IM, Shcherbakova DM, Verkhusha VV, Turoverov KK. Interaction of Biliverdin Chromophore with Near-Infrared Fluorescent Protein BphP1-FP Engineered from Bacterial Phytochrome. International Journal of Molecular Sciences. 18. PMID 28481303 DOI: 10.3390/Ijms18051009 |
0.454 |
|
| 2017 |
Stepanenko OV, Stepanenko OV, Bublikov GS, Kuznetsova IM, Verkhusha V, Turoverov KK. Stabilization of structure in near-infrared fluorescent proteins by binding of biliverdin chromophore Journal of Molecular Structure. 1140: 22-31. DOI: 10.1016/J.Molstruc.2016.10.095 |
0.571 |
|
| 2016 |
Stepanenko OV, Stepanenko OV, Kuznetsova IM, Uversky VN, Turoverov KK. Peculiarities of the Super-Folder GFP Folding in a Crowded Milieu. International Journal of Molecular Sciences. 17. PMID 27801849 DOI: 10.3390/Ijms17111805 |
0.596 |
|
| 2016 |
Stepanenko OV, Roginskii DO, Stepanenko OV, Kuznetsova IM, Uversky VN, Turoverov KK. Structure and stability of recombinant bovine odorant-binding protein: I. Design and analysis of monomeric mutants. Peerj. 4: e1933. PMID 27114880 DOI: 10.7717/peerj.1933 |
0.543 |
|
| 2016 |
Stepanenko OV, Roginskii DO, Stepanenko OV, Kuznetsova IM, Uversky VN, Turoverov KK. Structure and stability of recombinant bovine odorant-binding protein: III. Peculiarities of the wild type bOBP unfolding in crowded milieu. Peerj. 4: e1642. PMID 27114858 DOI: 10.7717/peerj.1642 |
0.496 |
|
| 2016 |
Stepanenko OV, Roginskii DO, Stepanenko OV, Kuznetsova IM, Uversky VN, Turoverov KK. Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms. Peerj. 4: e1574. PMID 27114857 DOI: 10.7717/Peerj.1574 |
0.58 |
|
| 2016 |
Ferreira LA, Povarova OI, Stepanenko OV, Sulatskaya AI, Madeira PP, Kuznetsova IM, Turoverov KK, Uversky VN, Zaslavsky BY. Effects of low urea concentrations on protein-water interactions. Journal of Biomolecular Structure & Dynamics. 1-33. PMID 26726130 DOI: 10.1080/07391102.2015.1135823 |
0.531 |
|
| 2016 |
Stepanenko OV, Baloban M, Bublikov GS, Shcherbakova DM, Stepanenko OV, Turoverov KK, Kuznetsova IM, Verkhusha VV. Allosteric effects of chromophore interaction with dimeric near-infrared fluorescent proteins engineered from bacterial phytochromes. Scientific Reports. 6: 18750. PMID 26725513 DOI: 10.1038/Srep18750 |
0.504 |
|
| 2015 |
Stepanenko OV, Povarova OI, Sulatskaya AI, Ferreira LA, Zaslavsky BY, Kuznetsova IM, Turioverov KK, Uversky VN. Protein unfolding in crowded milieu: What crowding can do to a protein undergoing unfolding? Journal of Biomolecular Structure & Dynamics. 1-0. PMID 26474212 DOI: 10.1080/07391102.2015.1109554 |
0.607 |
|
| 2015 |
Stepanenko OV, Bublikov GS, Stepanenko OV, Rychkov GN, Povarova OI, Verkhusha VV, Turoverov KK, Kuznetsova IM. [Knotted proteins]. Tsitologiia. 57: 177-83. PMID 26021166 |
0.412 |
|
| 2015 |
Stepanenko OV, Fonin AV, Stepanenko OV, Staiano M, D'Auria S, Kuznetsova IM, Turoverov KK. Tryptophan residue of the D-galactose/D-glucose-binding protein from E. Coli localized in its active center does not contribute to the change in intrinsic fluorescence upon glucose binding. Journal of Fluorescence. 25: 87-94. PMID 25501855 DOI: 10.1007/S10895-014-1483-Z |
0.475 |
|
| 2014 |
Stepanenko OV, Stepanenko OV, Kuznetsova IM, Verkhusha VV, Turoverov KK. Sensitivity of superfolder GFP to ionic agents. Plos One. 9: e110750. PMID 25347822 DOI: 10.1371/Journal.Pone.0110750 |
0.569 |
|
| 2014 |
Fonin AV, Stepanenko OV, Povarova OI, Volova CA, Philippova EM, Bublikov GS, Kuznetsova IM, Demchenko AP, Turoverov KK. Spectral characteristics of the mutant form GGBP/H152C of D-glucose/D-galactose-binding protein labeled with fluorescent dye BADAN: influence of external factors. Peerj. 2: e275. PMID 24711960 DOI: 10.7717/Peerj.275 |
0.439 |
|
| 2014 |
Stepanenko OV, Bublikov GS, Stepanenko OV, Shcherbakova DM, Verkhusha VV, Turoverov KK, Kuznetsova IM. A knot in the protein structure - probing the near-infrared fluorescent protein iRFP designed from a bacterial phytochrome. The Febs Journal. 281: 2284-98. PMID 24628916 DOI: 10.1111/Febs.12781 |
0.572 |
|
| 2014 |
Stepanenko OV, Stepanenko OV, Staiano M, Kuznetsova IM, Turoverov KK, D'Auria S. The quaternary structure of the recombinant bovine odorant-binding protein is modulated by chemical denaturants. Plos One. 9: e85169. PMID 24409322 DOI: 10.1371/Journal.Pone.0085169 |
0.535 |
|
| 2014 |
Ostroumova OS, Chulkov EG, Stepanenko OV, Schagina LV. Effect of flavonoids on the phase separation in giant unilamellar vesicles formed from binary lipid mixtures. Chemistry and Physics of Lipids. 178: 77-83. PMID 24361549 DOI: 10.1016/J.Chemphyslip.2013.12.005 |
0.341 |
|
| 2013 |
Stepanenko OV, Stepanenko OV, Kuznetsova IM, Verkhusha VV, Turoverov KK. Beta-barrel scaffold of fluorescent proteins: folding, stability and role in chromophore formation. International Review of Cell and Molecular Biology. 302: 221-78. PMID 23351712 DOI: 10.1016/B978-0-12-407699-0.00004-2 |
0.55 |
|
| 2012 |
Stepanenko OV, Stepanenko OV, Kuznetsova IM, Shcherbakova DM, Verkhusha VV, Turoverov KK. Distinct effects of guanidine thiocyanate on the structure of superfolder GFP. Plos One. 7: e48809. PMID 23144981 DOI: 10.1371/Journal.Pone.0048809 |
0.512 |
|
| 2012 |
Stepanenko OV, Stepanenko OV, Kuznetsova IM, Verkhusha VV, Turoverov KK. Structural Perturbation of Superfolder GFP in the Presence of Guanidine Thiocyanate Spectroscopy. 27: 381-386. DOI: 10.1155/2012/868154 |
0.493 |
|
| 2012 |
Stepanenko OV, Stepanenko OV, Fonin AV, Verkhusha VV, Kuznetsova IM, Turoverov KK. Protein-Ligand Interactions of the D-Galactose/D-Glucose-Binding Protein as a Potential Sensing Probe of Glucose Biosensors Spectroscopy. 27: 373-379. DOI: 10.1155/2012/169579 |
0.47 |
|
| 2012 |
Nashchekin AV, Nevedomskiy VN, Obraztsov PA, Stepanenko OV, Sidorov AI, Usov OA, Turoverov KK, Konnikov SG. Waveguide-type localized plasmon resonance biosensor for noninvasive glucose concentration detection Proceedings of Spie. 8427: 842739. DOI: 10.1117/12.922454 |
0.32 |
|
| 2011 |
Stepanenko OV, Stepanenko OV, Shcherbakova DM, Kuznetsova IM, Turoverov KK, Verkhusha VV. Modern fluorescent proteins: from chromophore formation to novel intracellular applications. Biotechniques. 51: 313-4, 316, 318 pass. PMID 22054544 DOI: 10.2144/000113765 |
0.473 |
|
| 2011 |
Stepanenko OV, Fonin AV, Stepanenko OV, Morozova KS, Verkhusha VV, Kuznetsova IM, Turoverov KK, Staiano M, D'Auria S. New insight in protein-ligand interactions. 2. Stability and properties of two mutant forms of the D-galactose/D-glucose-binding protein from E. coli. The Journal of Physical Chemistry. B. 115: 9022-32. PMID 21671572 DOI: 10.1021/Jp204555H |
0.455 |
|
| 2011 |
Stepanenko OV, Stepanenko OV, Povarova OI, Fonin AV, Kuznetsova IM, Turoverov KK, Staiano M, Varriale A, D'Auria S. New insight into protein-ligand interactions. The case of the D-galactose/D-glucose-binding protein from Escherichia coli. The Journal of Physical Chemistry. B. 115: 2765-73. PMID 21332109 DOI: 10.1021/Jp1095486 |
0.516 |
|
| 2011 |
Stepanenko OV, Povarova OI, Fonin AV, Stepanenko OV. [Stability of sugar-binding proteins: D-galactose/D-glucose-binding protein from Escherichia coli and trehalose/maltose-binding protein from Thermococcus litoralis]. Tsitologiia. 52: 950-4. PMID 21268855 |
0.38 |
|
| 2011 |
Fonin AV, Stepanenko OV, Turoverov KK, Vorobyev VI. Interaction between non-histone chromatin protein HMGB1 and linker histone H1 Cell and Tissue Biology. 5: 120-122. DOI: 10.1134/S1990519X11020076 |
0.403 |
|
| 2010 |
Povarova OI, Stepanenko OV, Sulatskaya AI, Kuznetsova IM, Turoverov KK, Staiano M, Vitale A, D'Auria S. High stability of trehalose/maltose binding protein from Thermococcus litoralis makes it a good candidate as a sensitive element in biosensor systems for sugar control Spectroscopy. 24: 349-353. DOI: 10.3233/Spe-2010-0469 |
0.476 |
|
| 2010 |
Stepanenko OV, Povarova OI, Stepanenko OV, Fonin AV, Kuznetsova IM, Turoverov KK, Staiano M, D'Auria S. Structure and stability of D-galactose/D-glucose-binding protein. The role of D-glucose binding and Ca ion depletion Spectroscopy. 24: 355-359. DOI: 10.3233/Spe-2010-0441 |
0.432 |
|
| 2010 |
Fonin AV, Stepanenko OV, Kuznetsova IM, Turoverov KK, Kostyleva EI, Vorobyev VI. Interaction between linker histone H1 and non-histone chromatin protein HMGB1 Spectroscopy. 24: 165-168. DOI: 10.3233/Spe-2010-0417 |
0.39 |
|
| 2008 |
Stepanenko OV, Verkhusha VV, Kuznetsova IM, Uversky VN, Turoverov KK. Fluorescent proteins as biomarkers and biosensors: throwing color lights on molecular and cellular processes. Current Protein & Peptide Science. 9: 338-69. PMID 18691124 DOI: 10.2174/138920308785132668 |
0.585 |
|
| 2008 |
Stepanenko OV, Verkhusha VV, Shavlovsky MM, Kuznetsova IM, Uversky VN, Turoverov KK. Understanding the role of Arg96 in structure and stability of green fluorescent protein. Proteins. 73: 539-51. PMID 18470931 DOI: 10.1002/Prot.22089 |
0.575 |
|
| 2008 |
Stepanenko OV, Marabotti A, Kuznetsova IM, Turoverov KK, Fini C, Varriale A, Staiano M, Rossi M, D'Auria S. Hydrophobic interactions and ionic networks play an important role in thermal stability and denaturation mechanism of the porcine odorant-binding protein. Proteins. 71: 35-44. PMID 17918730 DOI: 10.1002/prot.21658 |
0.465 |
|
| 2007 |
Staiano M, D'Auria S, Varriale A, Rossi M, Marabotti A, Fini C, Stepanenko OV, Kuznetsova IM, Turoverov KK. Stability and dynamics of the porcine odorant-binding protein. Biochemistry. 46: 11120-7. PMID 17845011 DOI: 10.1021/bi7008129 |
0.449 |
|
| 2006 |
Kuznetsova IM, Stepanenko OV, Turoverov KK, Huang C, Wang C-. [Conformational changes of disulfide isomerase C induced by guanidine hydrochloride]. Tsitologiia. 47: 1007-16. PMID 16706202 |
0.427 |
|
| 2006 |
Stepanenko OV, Kuznetsova IM, Turoverov KK, Scognamiglio V, Staiano M, D'Auria S. [The structure and stability of the glutamine-binding protein from Escherichia coli and its complex with glutamine]. Tsitologiia. 47: 988-1006. PMID 16706201 |
0.461 |
|
| 2005 |
Staiano M, Scognamiglio V, Rossi M, D'Auria S, Stepanenko OV, Kuznetsova IM, Turoverov KK. Unfolding and refolding of the glutamine-binding protein from Escherichia coli and its complex with glutamine induced by guanidine hydrochloride. Biochemistry. 44: 5625-33. PMID 15823021 DOI: 10.1021/Bi0478300 |
0.554 |
|
| 2005 |
Kuznetsova IM, Stepanenko OV, Turoverov KK, Staiano M, Scognamiglio V, Rossi M, D'Auria S. Fluorescence properties of glutamine-binding protein from Escherichia coli and its complex with glutamine. Journal of Proteome Research. 4: 417-23. PMID 15822918 DOI: 10.1021/Pr0498077 |
0.532 |
|
| 2004 |
Giordano A, Russo C, Raia CA, Kuznetsova IM, Stepanenko OV, Turoverov KK. Highly UV-absorbing complex in selenomethionine-substituted alcohol dehydrogenase from Sulfolobus solfataricus. Journal of Proteome Research. 3: 613-20. PMID 15253444 DOI: 10.1021/Pr034132D |
0.464 |
|
| 2004 |
Stepanenko OV, Kuznetsova IM, Turoverov KK, Huang C, Wang CC. Conformational change of the dimeric DsbC molecule induced by GdnHCl. A study by intrinsic fluorescence. Biochemistry. 43: 5296-303. PMID 15122895 DOI: 10.1021/Bi0359325 |
0.481 |
|
| 2003 |
Verkhusha VV, Shavlovsky MM, Nevzglyadova OV, Gaivoronsky AA, Artemov AV, Stepanenko OV, Kuznetsova IM, Turoverov KK. Expression of recombinant GFP-actin fusion protein in the methylotrophic yeast Pichia pastoris. Fems Yeast Research. 3: 105-11. PMID 12702253 DOI: 10.1111/J.1567-1364.2003.Tb00145.X |
0.412 |
|
| 2002 |
Kuznetsova IM, Stepanenko OV, Stepanenko OV, Povarova OI, Biktashev AG, Verkhusha VV, Shavlovsky MM, Turoverov KK. The place of inactivated actin and its kinetic predecessor in actin folding-unfolding. Biochemistry. 41: 13127-32. PMID 12403613 DOI: 10.1021/Bi026412X |
0.408 |
|
| 2002 |
Kuznetsova IM, Stepanenko OV, Turoverov KK, Zhu L, Zhou JM, Fink AL, Uversky VN. Unraveling multistate unfolding of rabbit muscle creatine kinase. Biochimica Et Biophysica Acta. 1596: 138-55. PMID 11983429 DOI: 10.1016/S0167-4838(02)00212-1 |
0.548 |
|
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