Albert Einstein College of Medicine

Publications

2014 

118. Stepanenko Olesya V., Stepanenko Olga V., Kuznetsova I.M., Verkhusha V.V. and Turoverov K.K.  Sensitivity of superfolder GFP to ionic agents. PLoS ONE 2014, 9: e110750. doi:10.1371/journal.pone.0110750
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117. Piatkevich K.D., English B.P., Malashkevich V.N., Xiao H., Almo S.C., Singer R.H. and Verkhusha V.V.  Photoswitchable red fluorescent protein with a large Stokes shift. Chemistry & Biology. 2014, 21: 1402-1414.
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116. Yao J., Shcherbakova D.M., Li C., Krumholz A., Lorca R.A., Reinl E., England S.K., Verkhusha V.V. and Wang L.V.  Reversibly switchable fluorescence microscopy with enhanced resolution and image contrast. J. Biomed. Opt. 2014, 19: 086018.
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115. Pletnev S., Shcherbakova D.M., Subach O.M., Pletneva N.V., Malashkevich V.N., Almo S.C., Dauter Z. and Verkhusha V.V.  Orange fluorescent proteins: structural studies of LSSmOrange, PSmOrange and PSmOrange2. PLoS ONE 2014, 9: e99136. doi:10.1371/journal.pone.0099136
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114. Nedosekin D.A., Verkhusha V.V. Melerzanov A.V., Zharov V.P. and Galanzha E.I.  In vivo photoswitchable flow cytometry for direct tracking of single circulating tumor cells. Chemistry & Biology. 2014, 21: 792-801.
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113. Denisova O.V., Söderholm S., Virtanen S., … Verkhusha V.V. and and Kainov D.E.  Akt inhibitor MK2206 prevents influenza pH1N1 virus infection in vitro. Antimicrob. Agents Chemother. 2014, 58: 3689-3696
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112. Shcherbakova D.M., Sengupta P., Lippincott-Schwartz J. and Verkhusha V.V. Photocontrollable fluorescent proteins for superresolution imaging. Annu. Rev. Biophys. 2014, 43: 303-329.
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111. Shcherbakova D.M. and Verkhusha V.V. Chromophore chemistry of fluorescent proteins controlled by light. Curr. Opin. Chem. Biol. 2014, 20: 60-68.
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110. Stepanenko Olesya V., Bublikov G.S., Stepanenko Olga V., Shcherbakova D.M., Verkhusha V.V., Turoverov K.K. and Kuznetsova I.M. A knot in the protein structure – probing the near-infrared fluorescent protein iRFP designed from a bacterial phytochrome. FEBS Journal. 2014, 281:2284-2298.
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109. Krumholz A., Shcherbakova D.M., Xia, J., Wang L.V. and Verkhusha V.V. Multicontrast photoacoustic in vivo imaging using near-infrared fluorescent proteins. Scientific Reports 2014, 4: 3939. doi:10.1038/srep03939
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108. Pletnev S., Subach F.V., Verkhusha V.V. and Dauter Z. The rotational order-disorder structure of the reversibly photoswitchable red fluorescent protein rsTagRFP. Acta Crystallogr. D 2014, 70: 31-39.
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107. Galanzha E.I., Nedosekin D.A., Sarimollaoglu M., Orza A.I., Biris A.S., Verkhusha V.V. and Zharov V.P. Photoacoustic and photothermal cytometry using photoswitchable proteins and nanoparticles with ultrasharp resonances. J. Biophotonics 2014, 7: in press. doi: 10.1002/jbio.201300140.
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2013 

106. Filonov G. S. and Verkhusha V.V. A near-infrared BiFC reporter for in vivo imaging of protein-protein interactions. Chemistry & Biology 2013, 20: 1078-1086.
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105. Hartwich T.M., Subach F.V., Cooley L., Verkhusha V.V. and Bewersdorf J. Determination of two-photon photoactivation rates of fluorescent proteins. Phys. Chem. Chem. Phys. 2013, 15: 14868-14872.
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104. Piatkevich, K.D., Subach F.V. and Verkhusha V.V. Far-red light photoactivatable near-infrared fluorescent proteins engineered from a bacterial phytochrome. Nature Communications 2013, 4: 2153 doi:10.1038/ncomms3153.
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103. Shcherbakova D.M. and Verkhusha V.V. Near-infrared fluorescent proteins for multicolor in vivo imaging. Nature Methods 2013, 10: 751-754.
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102. Piatkevich K.D., Malashkevich V.N., Morozova K.S., Nemkovich N.A., Almo S.C. and Verkhusha V.V. Extended Stokes shift in fluorescent proteins: chromophore - protein interactions in a near-infrared TagRFP675 variant. Scientific Reports 2013, 3: 1847. doi:10.1038/srep01847.
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101. Piatkevich K.D., Subach F.V. and Verkhusha V.V. Engineering of bacterial phytochromes for near-infrared imaging, sensing, and light-control in mammals. Chem. Soc. Rev. 2013, 42:3441-3452.
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100. Stepanenko Olesya V., Stepanenko Olga V., Kuznetsova I.M., Verkhusha V.V. and Turoverov K.K. Beta-barrel scaffold of fluorescent proteins: folding, stability and role in chromophore formation. Int. Rev. Cell Mol. Biol. 2013, 302: 221-278.
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99. Costantini L.M., Subach O.M., Jaureguiberry-bravo M., Verkhusha V.V. and Snapp E.L. Cysteineless non-glycosylated monomeric blue fluorescent protein, secBFP2, for studies in the eukaryotic secretory pathway. Biochem. Biophys. Res. Commun. 2013, 430: 1114–1119.
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2012 

98. Telford W.G., Hawley T.,Subach F., Verkhusha V.V. and Hawley R.G. Flow cytometry of fluorescent proteins. Methods 2012, 56: 318-330.
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97. Stepanenko Olesya V. Stepanenko Olga V., Kuznetsova I.M., Shcherbakova D.M.,Verkhusha V.V. and Turoverov K.K. Distinct effects of guanidine thiocyanate on the structure of superfolder GFP. PLoS ONE 2012, 7: e48809. doi: 10.1371/journal.pone.0048809.
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96 . Miyawaki A., Shcherbakova D.M. and Verkhusha V.V..Red fluorescent proteins: chromophore formation and cellular applications. Curr. Opin. Struct. Biol. 2012, 22: 679-688.
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95. Salomonnson E., Mihalko L.A.,Verkhusha V.V. , Luker K.E. and Luker G.D. Cell-based and in vivo spectral analysis of fluorescent proteins for multiphoton microscopy. J. Biomed. Opt. 2012, 17: 96001.
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94. Nedosekin D.A., Sarimollaoglu M., Galanzha E.I., Sawant R., Torchilin V.P.,Verkhusha V.V. , Ma J., Frank M.H., Biris A.S. and Zharov V.P. Synergy of photoacoustic and fluorescence flow cytometry of circulating cells with negative and positive contrasts. J. Biophotonics, 2013, 6: 425-434.
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93. Subach O.M., Entenberg D., Condeelis J.S. and Verkhusha V.V. A FRET-facilitated photoswitching using an orange fluorescent protein with the fast photoconversion kinetics. J. Am. Chem. Soc. 2012, 134: 14789-14799.
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92. Shcherbakova D.M., Subach O.M. and Verkhusha V.V. Red fluorescent proteins: advanced imaging applications and future design. Angew. Chem. Int. Ed. 2012, 51: 10724-10738.
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91. Subach F.M. and Verkhusha V.V. Chromophore transformations in red fluorescent proteins. Chemical Reviews 2012, 112: 4308-4327.
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90. Shcherbakova D.M., Hink M.A., Joosen L., Gadella T.W.J. and Verkhusha V.V. An orange fluorescent protein with a large Stokes shift for single-excitation multicolor FCCS and FRET imaging. J. Am. Chem. Soc., 2012, 134: 7913-7923.
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89. Pletnev S., Subach F.V., Dauter Z., Wlodawer A. and Verkhusha V.V. A structural basis for reversible photoswitching of absorbance spectra in red fluorescent protein rsTagRFP. J. Mol. Biol., 2012, 417: 144-151.
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88. Bravaya K.B., Subach O.M., Verkhusha V.V. and Krylov A.I. Insight into the common mechanism of the chromophore formation in the red fluorescent proteins: the elusive blue intermediate revealed. J. Am. Chem. Soc. 2012, 134: 2807-2814.
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87. Filonov G.S., Krumholz A., Xia J., Yao J., Wang L.V. and Verkhusha V.V. Deep-tissue photoacoustic tomography of a genetically encoded near-infrared fluorescent probe. Angew. Chem. Int. Ed. 2012, 51: 1448-1451.
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2011 

86. Subach O.M, Cranfill P.J., Davidson W.M. and Verkhusha V.V. An enhanced monomeric blue fluorescent protein with the high chemical stability of the chromophore. PLoS ONE 2011, 6: e28674. doi:10.1371/journal.pone.0028674
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85. Subach F.V., Piatkevich K.D. and Verkhusha V.V. Directed molecular evolution to design advanced red fluorescent proteins. Nature Methods 2011, 8: 1019-1026.
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84. Stepanenko Olesya V., Stepanenko Olga V., Shcherbakova D.M., Kuznetsova I.M., Turoverov K.K., and Verkhusha V.V. Modern fluorescent proteins: from chromophore formation to novel intracellular applications. BioTechniques. 2011, 51: 313-327.
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83. Gunewardene M.S., Subach F.V., Gould T.J., Penoncello G.P., Gudheti M.V., Verkhusha V.V. and Hess S.T. Superresolution imaging of multiple fluorescent proteins with highly overlapping emission spectra in living cells. Biophys. J. 2011, 101: 1522-1528.
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82. Entenberg D., Wyckoff J., Gligorijevic B., Roussos E., Verkhusha V.V. Pollard J.W. and Condeelis J. Setup and use of a two-laser multiphoton microscope for multichannel intravital fluorescence imaging. Nature Protocols. 2011, 6: 1500-1520.
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81. Subach O.M., Patterson G.H., Ting L.-M., Wang Y., Condeelis J.S. and Verkhusha V.V. A photoswitchable orange-to-far-red fluorescent protein, PSmOrange. Nature Methods. 2011, 8: 771-777.
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80. Filonov G.S., Piatkevich K.D., Ting L.-M., Zhang J., Kim K. and Verkhusha V.V. Bright and stable near infra-red fluorescent protein for in vivo imaging. Nature Biotechnology. 2011, 29: 757-761.
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79. Stepanenko O.V., Fonin A.V., Stepanenko O.V., Morozova K.M., Verkhusha V.V., Kuznetsova I.M., Turoverov K.K., Staiano M. and 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. J. Phys. Chem. B. 2011, 115: 9022-9032.
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78. Koga H., Martinez-Vicente M., Macian F., Verkhusha V.V. and Cuervo A.M. A photoconvertible fluorescent reporter to track chaperone-mediated autophagy. Nature Communications. 2011, 2: 386 doi: 10.1038/ncomms1393.
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77. Gudkov D.A., Lyagin I.V., Verkhusha V.V. and Efremenko E.N. Hybrid proteins with organophosphorous hydrolase activity and fluorescence of deGFP4 protein. Moscow Univ. Chem. Bull., 2011, 66: 92–98.
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76. Piatkevich K.D. and Verkhusha V.V. Guide to red fluorescent proteins and biosensors for flow cytometry.Methods Cell Biol., 2011, 104: 431-461.
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75. Wu B., Piatkevich K.D., Lionnet T., Singer R.H., and Verkhusha V.V. Modern fluorescent proteins and imaging technologies to study gene expression, nuclear localization, and dynamics. Curr. Opin. Cell Biol., 2011, 23: 310-317.
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2010 

74. Stepanenko O.V., Kuznetsova I.M., Kuznetsova I.M., Verkhusha V.V., Staiano M.,D’Auria S., and Turoverov K.K. Denaturation of proteins with beta-barrel topology induced by guanidine hydrochloride. Spectrosc. Int. J. , 2010, 24: 367-373.
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73. Piatkevich K.D., Malashkevich V.N., Almo S.C., and Verkhusha V.V. Engineering ESPT pathways based on structural analysis of LSSmKate red fluorescent proteins with large Stokes shift. J. Am. Chem. Soc. 2010, 132: 10762–10770.
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72. Subach F.V., Zhang L., Gadella T.W.J., Gurskaya N.G., Lukyanov K.A., and Verkhusha V.V. Red fluorescent protein with reversibly photoswitchable absorbance for photochromic FRET. Chemistry & Biology (Cell press). 2010, 17: 745-755.
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71. Morozova K.S., Piatkevich K.D., Gould T.G., Zhang J., Bewersdorf J., and Verkhusha V.V. Far-Red fluorescent protein excitable with red lasers for flow cytometry and super-resolution STED nanoscopy. Biophys. J. 2010, 99: L13-L15.
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70. Piatkevich K.D., Efremenko E.N., Verkhusha V.V., and Varfolomeev S.D. Red fluorescent proteins and their properties. Russ. Chem. Rev. 2010, 79: 243-258.
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69. Subach F.M., Patterson G.H., Renz M., Lippincott-Schwartz J., and Verkhusha V.V. Bright monomeric photoactivatable red fluorescent protein for two-color super-resolution sptPALM of live cells. J. Am. Chem. Soc. 2010, 132: 6481-6491.
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68. Subach O.M., Malashkevich V.N., Zencheck W.D., Morozova K.S., Piatkevich K.D., Almo S.C., and Verkhusha V.V. Structural characterization of acylimine-containing blue and red chromophores in mTagBFP and TagRFP fluorescent proteins. Chemistry & Biology (Cell press). 2010, 17: 333-341.
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67. Piatkevich K.D., Hulit J., Subach O.M., Wu B., Abdulla A., Segall J.E., and Verkhusha V.V. Monomeric red fluorescent proteins with a large Stokes shift. Proc. Natl. Acad. Sci. USA 2010, 107: 5369-5374.
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66. Pletnev S., Subach F.V., Dauter Z., Wlodawer A., and Verkhusha V.V. Understanding blue-to-red conversion in monomeric fluorescent timers and hydrolytic degradation of their chromophores. J. Am. Chem. Soc. 2010, 132: 2243-2253.
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65. Piatkevich K.D. and Verkhusha V.V. Advances in engineering of fluorescent proteins and photoactivatable proteins with red emission. Curr. Opin. Chem. Biol. 2010, 14: 23-29.
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2009 

64. Subach F.V., Malashkevich V.N., Zencheck W.D., Xiao H., Filonov G.S., Almo S.C., and Verkhusha V.V. Photoactivation mechanism of PAmCherry based on crystal structures of the protein in the dark and fluorescent states. Proc. Natl. Acad. Sci. USA 2009, 106: 21097-21102.
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63. Pletnev S., Morozova K.S., Verkhusha V.V., and Dauter Z. Rotational order-disorder structure of fluorescent protein FP480. Acta Crystallogr. D 2009, 65: 906-912.
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62. He J., Vora M., Haney R.M., Filonov G.S., Musselman C.A., Burd C.G., Kutateladze A.G., Verkhusha V.V., Stahelin R.V., and Kutateladze T.G. Membrane insertion of the FYVE domain is modulated by pH. Proteins. 2009, 76: 852-860.
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61. Bogdanov A.M., Mishin A.S., Yampolsky I.V., Belousov V.V., Chudakov D.M., Subach F.V., Verkhusha V.V., Lukyanov S., and Lukyanov K.A. Green fluorescent proteins are light-induced electron donors. Nature Chemical Biology. 2009, 5: 459-461.
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60. Shcherbo D., Murphy C.S., Ermakova G.V., Solovieva E.A., Chepurnykh T.V., Shcheglov A.S., Verkhusha V.V., Pletnev V.Z., Hazelwood K.L., Roche P.M., Lukyanov S., Zaraisky A.G., Davidson M.W., and Chudakov D.M. Far-red fluorescent tags for protein imaging in living tissues. Biochem. J. 2009, 418: 567-574.
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59. Gould T.J., Verkhusha V.V., and Hess S.T. Imaging biological structures with fluorescence photoactivation localization microscopy. Nature Protocols. 2009, 4: 291-308.
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58. Subach F.V., Patterson G.H., Manley S., Gillette J.M., Lippincott-Schwartz J., and Verkhusha V.V. Photoactivatable mCherry for high-resolution two-color fluorescence microscopy. Nature Methods. 2009, 6: 153-159.
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57. Telford W.G., Subach F.V., and Verkhusha V.V. Supercontinuum white light lasers for flow cytometry. Cytometry. 2009, 75A: 450-459.
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56. Subach F.V., Subach O.M., Gundorov I.S., Morozova K.S., Piatkevich K.D., Cuervo A.M., and Verkhusha V.V. Monomeric fluorescent timers that change color from blue to red report on cellular trafficking. Nature Chemical Biology. 2009, 5: 118-126.
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2008 

55. Lyagin I., Gudkov D., Verkhusha V., and Efremenko E. Genetic construct encoding the biosynthesis of N-His6-e-pHluorins-OPH in E.coli cells. In book: Chemical and Biochemical Physics, Kinetics and Thermodynamics: New Perspectives. (Scott P.E., Zaikov G.E., and Kablov V.F., Eds.), 2008, 83-90. Nova Science Publishers, NY, ISBN 1-60456-024-X.

54. Gould T.J., Gunewardene M.S., Gudheti M.V., Verkhusha V.V., Yin S.R., Gosse J.A., and Hess S.T. Nanoscale imaging of molecular positions and anisotropies. Nature Methods. 2008, 5: 1027-1030.
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53. Kedrin D., Gligorijevic B., Wyckoff J., Verkhusha V.V., Condeelis J., Segall J.E., and van Rheenen J. Intravital imaging of metastatic behavior through a mammary imaging window. Nature Methods. 2008, 5: 1019-1021.
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52. Stepanenko O.V., Verkhusha V.V., Kuznetsova I.M., Uversky V.N., and Turoverov К.К. Fluorescent proteins as biomarkers and biosensors: throwing color lights on molecular and cellular processes. Curr. Protein Pept. Sci. 2008, 9: 338-369.
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51. Subach O.M., Gundorov I.S., Yoshimura M., Subach F.V., Zhang J., Grüenwald G., Souslova E.A., Chudakov D.M., and Verkhusha V.V. Conversion of red fluorescent protein into a bright blue probe. Chemistry & Biology (Cell press). 2008, 15: 1116-1124.
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50. Stepanenko O.V., Verkhusha V.V., Shavlovsky M.M., Kuznetsova I.M., Uversky V.N., and Turoverov K.K. Understanding the role of Arg96 in structure and stability of green fluorescent protein. Proteins. 2008, 73: 539-551.
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49. He J., Haney R.M., Vora M., Verkhusha V.V., Stahelin R.V., and Kutateladze T.G. Molecular mechanism of membrane targeting by the GRP1 PH domain. J. Lipid Res. 2008, 49, 1807-1815.
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48. Pena P.V., Hom R.A., Hung T., Lin H., Kuo A.J., Wong R.P.C., Subach O.M., Champagne K.S., Zhao R., Verkhusha V.V., Li G., Gozani O., and Kutateladze T.G. Histone H3K4me3 binding is required for the DNA repair and apoptotic activities of ING1 tumor suppressor. J. Mol. Biol. 2008, 380: 303-312.
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47. Kapoor V., Karpov V., Linton C., Subach F.V., Verkhusha V.V., and Telford W.G. Solid state yellow and orange lasers for flow cytometry. Cytometry. 2008, 73A: 570-577.
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46. Mishin A.S., Subach F.V., Yampolsky I.V., King W., Lukyanov K.A., and Verkhusha V.V.* The first mutant of the Aequorea victoria green fluorescent protein that forms a red chromophore. Biochemsitry. 2008, 47: 4666-4673. *Corresponding author
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2007 

45. Stepanenko O.V., Verkhusha V.V., Kuznetsova I.M., and Turoverov K.K. Fluorescent proteins: physical-chemical properties and application in cell biology. Cytology. 2007, 49, 395-420.
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44. Hom R.A, Vora M., Regner M., Subach O.M., Cho W., Verkhusha V.V., Stahelin R.V., and Kutateladze T.G. pH-dependent binding of the epsin ENTH domain and the AP180 ANTH domain to PI(4,5)P2-containing bilayers. J. Mol. Biol. 2007, 373, 412-423.
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43. Kapoor V., Subach F.V., Kozlov V.G., Grudinin A., Verkhusha V.V., and Telford W.G. New lasers for flow cytometry: filling the gaps. Nature Methods. 2007, 4, 678-679.
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42. Nevzglyadova O.V., Artemov A.V., Zenin V.V., Verkhusha V.V., Shavlovsky M.M., Povarova O.I., Stepanenko O.V., Kuznetsova I.M., and Turoverov K.K. Expression of recombinant actin 5C from Drosophila in the methylotrophic yeast Pichia pastoris. Cell Tissue Biol. 2007, 1, 248-258.
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2006 

41. Pena P.V., Davrazou F., Shi X., Walter K., Verkhusha V.V., Gozani O., Zhao R., and Kutateladze T.G. Molecular mechanism of histone H3K4Me3 recognition by plant homeodomain of ING2. Nature. 2006, 442, 100-103.
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40. Gurskaya N.G., Verkhusha V.V., Shcheglov A.S., Staroverov D.B., Chepurnykh T.V., Fradkov A.F., Lukyanov S., and Lukyanov K.A. Engineering of a monomeric green-to-red photoactivatable fluorescent protein induced by blue light. Nature Biotechnol. 2006, 24: 461-465.
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2005 

39. Lukyanov K.A., Chudakov D.M., Lukyanov S., and Verkhusha V.V.* Photoactivatable fluorescent proteins. Nature Rev. Mol. Cell Biol. 2005, 6: 885-891. *Corresponding author
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38. Lee S.A., Eyeson R., Cheever M.L., Geng J., Verkhusha V.V., Burd C., Overduin M., and Kutateladze T.G. Targeting of the FYVE domain to endosomal membranes is regulated by a histidine switch. Proc. Natl. Acad. Sci. USA. 2005, 102, 13052-13057.
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37. Stepanenko O.V., Verkhusha V.V., Shavlovsky M.M., Aleinikova T.D., Uversky V.N., Kuznetsova I.M., and Turoverov K.K. The role of quaternary structure in fluorescent protein stability. Cytology. 2005, 47, 1017-1027.
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36. Verkhusha V.V.,* and Sorkin A. Conversion of the monomeric red fluorescent protein into a photoactivatable probe. Chemistry & Biology (Cell press). 2005, 12, 279-285.*Corresponding author
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2004 

35. Stepanenko O.V., Verkhusha V.V., Kazakov V.I., Shavlovsky M.M., Kuznetsova I.M., Uversky V.N., and Turoverov K.K. Comparative studies on the structure and stability of fluorescent proteins EGFP, zFP506, mRFP1, dimer2 and DsRed. Biochemistry. 2004, 43, 14913-14923.
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34. Galperin E.#, Verkhusha V.V.,# and Sorkin A. Three-chromophore FRET microscopy to analyze multiprotein interactions in living cells. Nature Methods. 2004, 1, 209-217. #Co-first author
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33. Chudakov D.M.#, Verkhusha V.V.#, Staroverov D.B., Lukyanov S., and Lukyanov K.A. Photo-switchable fluorescent label for protein tracking. Nature Biotechnol. 2004, 22, 1435-1439. #Co-first author
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32. Verkhusha V.V., Chudakov D.M., Gurskaya N.G., Lukyanov S., and Lukyanov K.A. Common pathway for the red chromophore formation in the fluorescent proteins and chromoproteins. Chemistry & Biology (Cell press).2004, 11, 845-854.
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31. Verkhusha V.V.*, and Lukyanov K.A. The molecular properties and applications of Anthozoa fluorescent proteins and chromoproteins. Nature Biotechnol. 2004, 22, 289-296. *Corresponding author
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2003 

30. Verkhusha V.V.*, Pozhitkov A.E., Smirnov S.A., Borst J.W., van Hoek A., Klyachko N.L., Levashov A.V., and Visser A.J. Effect of high pressure and reversed micelles on the fluorescent proteins. Biochim. Biophys. Acta. 2003, 1622, 192-195. *Corresponding author
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29. Verkhusha V.V.*, Kuznetsova I.M., Stepanenko O.V., Zaraisky A.G., Shavlovsky M.M., Turoverov K.K., and Uversky V.N. High stability of Discosoma DsRed as compared to Aequorea EGFP. Biochemistry. 2003, 42, 7879-7884. *Corresponding author
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28. Bulina M.E.#, Verkhusha V.V.#, Staroverov D.B., Chudakov D.M., and Lukyanov K.A. Heterooligomeric tagging diminishes non-specific aggregation of target proteins fused with Anthozoa fluorescent proteins. Biochem. J. 2003, 371, 109-114. #Co-first author
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27. Verkhusha V.V., Shavlovsky M.M., Nevzglyadova O.V., Gaivoronsky A.A., Artemov A.V., Stepanenko O.V., Kuznetsova I.M., and Turoverov K.K. Expression of recombinant GFP-actin fusion protein in the methylotrophic yeast P.pastoris. FEMS Yeast Res. 2003, 3, 105-111.
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26. Verkhusha V.V.*, Matz M.V., Sakurai T., and Lukyanov K.A. GFP-like fluorescent proteins and chromoproteins of class Anthozoa. In book: Protein Structures: Kaleidoscope of Structural Properties and Functions. (Uversky V.N, Ed.). 2003, 405-439. Research Signpost Publishers. ISBN 81-7736-1775. *Corresponding author
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2002 

25. Kuznetsova I.M., Stepanenko O.V., Stepanenko O.V., Povarova O.I., Biktashev A.G, Verkhusha V.V., Shavlovsky M.M., and Turoverov K.K. The place of inactivated actin and its kinetic predecessor in actin folding-unfolding. Biochemistry. 2002, 41, 13127-13132.
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24. Fradkov A.F., Verkhusha V.V., Staroverov D.B., Bulina M.E., Yanushevich Y.G., Martynov V.I., Lukyanov S., and Lukyanov K.A. Far-red fluorescent tag for protein labelling. Biochem. J. 2002, 368, 17-21.
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23. Turoverov K.K., Verkhusha V.V., Shavlovsky M.M., Biktashev A.G., Povarova O.I., and Kuznetsova I.M. Kinetics of actin unfolding induced by guanidine hydrochloride. Biochemistry. 2002, 41, 1014-1019.
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2001 

22. Verkhusha V.V.*, Akovbian N.A., Efremenko E.N., Varfolomeyev S.D., and Vrzheshch P.V. The kinetic analysis of maturation and denaturation of DsRed, a coral-derived red fluorescent protein. Biochemistry (Mosc). 2001, 66, 342-1351. *Corresponding author
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21. Verkhusha V.V.*, Otsuna H., Awasaki T., Oda H., Tsukita S., and Ito K. An enhanced mutant of red fluorescent protein DsRed for double labeling and developmental timer of neural fiber bundle formation. J. Biol. Chem. 2001, 276, 29621­29624. *Corresponding author
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1990 - 2000 

20. Vrzheshch P.V.#, Abovikyan N.A., Varfolomeyev S.D., and Verkhusha V.V. # Denaturation and partial renaturation of a tightly tetramerized DsRed protein under mildly acidic conditions. FEBS Letters. 2000, 487, 203-208. #Co-first author
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19. Varfolomeyev, S.D., Efremenko, A.I., Verkhusha, V.V., and Vrzheshch, P.V. Synthetic amino acid analogues in cells and proteins. Moscow Univ. Chem. Bull. 2000, 41, 352-354.
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18. Verkhusha V.V.*, Tsukita S., and Oda H. Analysis of cytoskeleton dynamics and cell migration in Drosophila ovaries using GFP-actin and E-cadherin-GFP fusion molecules. Proc. SPIE. 1999, 3604, 130-139. *Corresponding author  

17. Verkhusha V.V.*, Tsukita S., and Oda H. Actin dynamics in lamellipodia of migrating border cells in the Drosophila ovaries revealed by a GFP-actin fusion protein. FEBS Letters. 1999, 445, 395-401. *Corresponding author
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16. Potanin A.A., Verkhusha V.V., and Muller V.M. Disaggregation of particles with biospecific interactions in shear flow. J. Coll. Interface Sci. 1997, 188, 251-256.
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15. Potanin A.A., Verkhusha V.V., and Muller V.M. Aggregate breakage of particles with biospecific interaction in a shear flow. Colloid J. 1996, 58, 355-362.

14. Takikawa O., Oku T., lto N., Ushio Y., Yamamoto N., Yoneda Y., Tsuji J., Sanchez-Bueno A., Verkhusha V.V., and Yoshida R. Multiple expression of Ly-6C and accumulation of Ly-6C pre-mRNA in activated macrophages involved in rejection of an allografted tumor. Biochem. Biophys. Res. Commun. 1996, 226, 247-253.
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13. Sanchez-Bueno A., Verkhusha V.V., Takikawa O., Tanaka Y., and Yoshida R. Interferon-gamma dependent expression of inducible nitric oxide synthase, interleukin-12 and interferon-g-inducing factor in macrophages elicited by allografted tumor cells. Biochem. Biophys. Res. Commun. 1996, 224, 555-563.
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12. Verkhusha V.V.*, Staroverov V.M., and Vrzheshch P.V. Model of cell adhesive interaction in liquid flow. Membr. Cell. Biol. 1995, 8, 455-470. *Corresponding author  

11. Potanin A.A., Verkhusha V.V., Belokoneva O.S., and Wiegel F.W. Kinetics of ligand binding to a cluster of membrane-associated receptors. Eur. Biophys. J. 1994, 23, 197-205.
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10. Potanin A.A., Verkhusha V.V., Vrzheshch P.V., and Muller V.M. Theory of adhesion interaction of biological cells in liquid flow: influence of cell deformation on coagulation. Colloid J. 1994, 56, 365-369.

9. Potanin A.A., Verkhusha V.V., Vrzheshch P.V., and Muller V.M. Theory of adhesion interaction of biological cells in liquid flow: undeformed cells. Colloid J. 1994, 56, 356-364.

8. Verkhusha V.V.*, Lebedev E.S., Vrzheshch P.V., and Muller V.M. Experimental investigation of aggregation of platelets and latex immunoconjugates in shear flow. Colloid J. 1994, 56, 269-279. *Corresponding author  

7. Verkhusha V.V.*, Staroverov V.M., and Vrzheshch P.V. Model for cell adhesion in the flow of liquid. Biol. Membranes. 1994, 11, 437-450. *Corresponding author  

6. Verkhusha V.V.*, Smorodin V.E., and Vrzheshch P.V. Model of bioaerosol adhesion interactions in respiratory tracts. J. Aerosol Sci. 1993, 24, S433-S434. *Corresponding author  

5. Potanin A.A., Verkhusha V.V., Vrzheshch P.V. Coagulation of particles in shear flow: applications to biological cells. J. Coll. Interface Sci. 1993, 160, 405-418.
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4. Verkhusha V.V., Vrzheshch P.V., Staroverov V.M., and Varfolomeyev S.D. Cell-cell adhesion in shear flow. J. Chem. Biochem. Kinetics. 1992, 2, 135-153.

3. Verkhusha V.V., Vrzheshch P.V., and Varfolomeyev S.D. Mathematical approaches for kinetics of blood platelet aggregation. Proc. USSR Acad. Med. Sci. 1991, 10, 20-28.

2. Vrzheshch P.V., Verkhusha V.V., and Varfolomeyev S.D. Rate equation for platelets aggregation. Biophysics (Mosc). 1990, 35, 637-641.

1. Vrzheshch P.V., Verkhusha V.V., and Varfolomeyev S.D. Kinetic analysis of blood platelets aggregation. Proc. USSR Acad. Sci. 1990, 313, 726-729.

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