Skip CCR Main Navigation National Cancer Institute National Cancer Institute U.S. National Institutes of Health
CCR - For Our Staff| Home |

Our Science – Pletnev Website

Sergei Pletnev, Ph.D.

Selected Publications

1)  Pletnev S, Subach FV, Verkhusha VV, Dauter Z.
The rotational order-disorder structure of the reversibly photoswitchable red fluorescent protein rsTagRFP.
Acta Crystallogr. D Biol. Crystallogr. 70: 31-9, 2014.
2)  Pletnev VZ, Pletneva NV, Lukyanov KA, Souslova EA, Fradkov AF, Chudakov DM, Chepurnykh T, Yampolsky IV, Wlodawer A, Dauter Z, Pletnev S.
Structure of the red fluorescent protein from a lancelet (Branchiostoma lanceolatum): a novel GYG chromophore covalently bound to a nearby tyrosine.
Acta Crystallogr. D Biol. Crystallogr. 69: 1850-60, 2013.
3)  Pletneva NV, Pletnev VZ, Souslova E, Chudakov DM, Lukyanov S, Martynov VI, Arhipova S, Artemyev I, Wlodawer A, Dauter Z, Pletnev S.
Yellow fluorescent protein phiYFPv (Phialidium): structure and structure-based mutagenesis.
Acta Crystallogr. D Biol. Crystallogr. 69: 1005-12, 2013.
4)  Pletnev S, Subach FV, Dauter Z, Wlodawer A, Verkhusha VV.
A structural basis for reversible photoswitching of absorbance spectra in red fluorescent protein rsTagRFP.
J. Mol. Biol. 417: 144-51, 2012.
5)  Pletnev S, Pletneva NV, Souslova EA, Chudakov DM, Lukyanov S, Wlodawer A, Dauter Z, Pletnev V.
Structural basis for bathochromic shift of fluorescence in far-red fluorescent proteins eqFP650 and eqFP670.
Acta Crystallogr. D Biol. Crystallogr. 68: 1088-97, 2012.
6)  Pletneva NV, Pletnev VZ, Shemiakina II, Chudakov DM, Artemyev I, Wlodawer A, Dauter Z, Pletnev S.
Crystallographic study of red fluorescent protein eqFP578 and its far-red variant Katushka reveals opposite pH-induced isomerization of chromophore.
Protein Sci. 20: 1265-74, 2011.
7)  Magracheva E, Pletnev S, Kotenko S, Li W, Wlodawer A, Zdanov A.
Purification, crystallization and preliminary crystallographic studies of the complex of interferon-lambda1 with its receptor.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66: 61-3, 2010.
8)  Pletneva NV, Pletnev VZ, Lukyanov KA, Gurskaya NG, Goryacheva EA, Martynov VI, Wlodawer A, Dauter Z, Pletnev S.
Structural evidence for a dehydrated intermediate in green fluorescent protein chromophore biosynthesis.
J. Biol. Chem. 285: 15978-84, 2010.
9)  Pletnev S, Subach FV, Dauter Z, Wlodawer A, Verkhusha VV.
Understanding blue-to-red conversion in monomeric fluorescent timers and hydrolytic degradation of their chromophores.
J. Am. Chem. Soc. 132: 2243-53, 2010.
10)  Pletnev S, Morozova KS, Verkhusha VV, Dauter Z.
Rotational order-disorder structure of fluorescent protein FP480.
Acta Crystallogr. D Biol. Crystallogr. 65: 906-12, 2009.
11)  Pletnev S, Gurskaya NG, Pletneva NV, Lukyanov KA, Chudakov DM, Martynov VI, Popov VO, Kovalchuk MV, Wlodawer A, Dauter Z, Pletnev V.
Structural basis for phototoxicity of the genetically encoded photosensitizer KillerRed.
J. Biol. Chem. 284: 32028-39, 2009.
12)  Pletnev S, Shcherbo D, Chudakov DM, Pletneva N, Merzlyak EM, Wlodawer A, Dauter Z, Pletnev V.
A crystallographic study of bright far-red fluorescent protein mKate reveals pH-induced cis-trans isomerization of the chromophore.
J. Biol. Chem. 283: 28980-7, 2008.
13)  Pletneva NV, Pletnev SV, Chudakov DM, Tikhonova TV, Popov VO, Martynov VI, Wlodawer A, Dauter Z, Pletnev VZ.
[Three-dimensional structure of yellow fluorescent protein zYFP538 from Zoanthus sp. at the resolution 1.8 angstrom].
Bioorg. Khim. 33: 421-30, 2007.
14)  Pletneva N, Pletnev V, Tikhonova T, Pakhomov AA, Popov V, Martynov VI, Wlodawer A, Dauter Z, Pletnev S.
Refined crystal structures of red and green fluorescent proteins from the button polyp Zoanthus.
Acta Crystallogr. D Biol. Crystallogr. 63: 1082-93, 2007.
15)  Pletneva N, Pletnev S, Tikhonova T, Popov V, Martynov V, Pletnev V.
Structure of a red fluorescent protein from Zoanthus, zRFP574, reveals a novel chromophore.
Acta Crystallogr. D Biol. Crystallogr. 62: 527-32, 2006.
16)  Pletnev S, Magracheva E, Wlodawer A, Zdanov A.
A model of the ternary complex of interleukin-10 with its soluble receptors.
BMC Struct. Biol. 5: 10, 2005.
17)  Pletnev VZ, Goriacheva EA, Tsygannik IN, Nesmeianov VA, Pletnev SV, Pangborn W, Daux W.
[A new crystal form of the Fab fragment of a monoclonal antibody to human interleukin-2: the three-dimensional structure at 2.7 A resolution].
Bioorg. Khim. 30: 466-9, 2004.
18)  Pletnev S, Magracheva E, Kozlov S, Tobin G, Kotenko SV, Wlodawer A, Zdanov A.
Characterization of the recombinant extracellular domains of human interleukin-20 receptors and their complexes with interleukin-19 and interleukin-20.
Biochemistry. 42: 12617-24, 2003.
19)  Zhang Y, Corver J, Chipman PR, Zhang W, Pletnev SV, Sedlak D, Baker TS, Strauss JH, Kuhn RJ, Rossmann MG.
Structures of immature flavivirus particles.
EMBO J. 22: 2604-13, 2003.
20)  Zhang W, Mukhopadhyay S, Pletnev SV, Baker TS, Kuhn RJ, Rossmann MG.
Placement of the structural proteins in Sindbis virus.
J. Virol. 76: 11645-58, 2002.
21)  Kuhn RJ, Zhang W, Rossmann MG, Pletnev SV, Corver J, Lenches E, Jones CT, Mukhopadhyay S, Chipman PR, Strauss EG, Baker TS, Strauss JH.
Structure of dengue virus: implications for flavivirus organization, maturation, and fusion.
Cell. 108: 717-25, 2002.
22)  Afonin P, Fokin A, Shingarova L, Korobko V, Tsygannik I, Artemev I, Pletnev S, Pangborn W, Duax W, Pletnev V.
Three-Dimensional Structure of the Arg32His Mutant of the Human Necrosis Factor Determined at 2.5 Angstrom Resolution from X-Ray Data for a Twin Crystal.
Crystallography Reports. 47: 629-34, 2002.
23)  Rossmann MG, Bernal R, Pletnev SV.
Combining electron microscopic with x-ray crystallographic structures.
J. Struct. Biol. 136: 190-200, 2001.
24)  Pletnev SV, Zhang W, Mukhopadhyay S, Fisher BR, Hernandez R, Brown DT, Baker TS, Rossmann MG, Kuhn RJ.
Locations of carbohydrate sites on alphavirus glycoproteins show that E1 forms an icosahedral scaffold.
Cell. 105: 127-36, 2001.
25)  Dokland T, Bernal RA, Burch A, Pletnev S, Fane BA, Rossmann MG.
The role of scaffolding proteins in the assembly of the small, single-stranded DNA virus phiX174.
J. Mol. Biol. 288: 595-608, 1999.
26)  Pletnev S, Antson A, Sinitsina N, Dauter Z, Isupov M, Hurs H, Faleev N, Wilson K, Dodson G, Demidkina T, Harutyunyan E.
Crystallographic study of tyrosine phenol-lyase from Erwinia herbicola.
Crystallographiya (Russ). 42: 865-76, 1997.
27)  Pletnev VZ, Ruzeinikov SN, Tsigannik IN, Ivanov VT, Pletnev SV, Langs DA, Duax WL.
The crystal and molecular structure of a valinomycin analogue cyclo[(D-Val-L-Lac-L-Ala-D-Hyi)2(D-Val-L-Lac-L-Val-D-Hyi)]. H2O(C50H82N6 O18.H2O).
Biopolymers. 42: 651-8, 1997.
28)  Pletnev SV, Isupov MN, Dauter Z, Wilson KS, Faleev NG, Harutyunyan EG, Demidkina TV.
Purification and crystals of tyrosine phenol-lyase from Erwinia herbicola.
Biochem. Mol. Biol. Int. 38: 37-42, 1996.
29)  Pletnev VZ, Tsygannik IN, Ivanov VT, Pletnev SV, Langs DA, Duax WL.
Crystal and molecular structure of the centrosymmetric meso-valinomycin analogue--cyclo (D-Val-D-Hyi-D-Val-L-Hyi-L-Val-D-Hyi-L-Val-L-Hyi-L-Val-D-Hyi-D-Val-L-Hy i) (C60H102N6O18).
Biopolymers. 36: 615-21, 1995.
30)  Pletnev V, Tsygannik I, Fonarev Y, Pletnev S, Ivanov V.
Crystal and molecular structure of octadepsipeptide valinomycin analogue--Cyclo[-(D-Val-L-Lac-L-Val-D-Pro)2-].
Crystallographiya (Russ). 38: 98-107, 1993.
Click Here to View Collapsed Bibliography.

This page was last updated on 4/10/2014.