Изучение структуры и стабильности белка оболочки Х-вируса картофеля в свободном состоянии и в составе вирионов
Диссертация
Все это в полной мере относится к типовому представителю данной группы и объекту наших исследований — Х-вирусу картофеля (ХВК). Кроме всех этих групповых особенностей, ХВК (и его белок оболочки (БО)) обладают и немалым числом собственных аномалий (или аномалий про которые неизвестно насколько широко они распространены в этой группе). Среди них можно назвать аномальные гидродинамические… Читать ещё >
Список литературы
- Арутюнян A.M., Рафикова Э. Р., Драчев В. А., Добров E.H. 2001. Появление ß--подобного спектра кругового дихроизма при агрегации белка, не сопровождающейся переходом в ß--структуру. Биохимия. 66, 1702−1705.
- Атабеков И.Г. 2002. Практикум по общей вирусологии. Издательство МГУ, Москва.
- Бобкова А.Ф., Гольдштейн М. И., Кафтанова A.C. 1989. Сравнение антигенных свойств Х-вируса картофеля и его белка оболочки. Влияние протеолитического расщепления на антигенные характеристики. Молек. Генет. Микробиол. Вирусол. 2,35−41.
- Богачева E.H., Шишков A.B. 2000. Тритиевая планиграфия как инструмент исследования пространственной структуры белков и их комплексов. Молекулярная биология. 34, 839−853.
- Гольдштейн М.И., Куст C.B., Добров E.H. 1987. Различия в механизмах сборки in vitro ВТМ и Х-вируса картофеля. Молек. Генет. Микробиол. Вирусол. 12, 45−49.
- Добров E.H., Ефимов A.B., Баратова JI.A. 2004. Исследование структуры рибонуклеопротеидов спиральных вирусов растений методами тритиевой плапиграфии и теоретического моделирования. Молекулярная биология. 38, 945 958.
- Донсон Р., Эллиот Д., Эллиот У., Джонс К. 1991. Справочник биохимика. Издательство «Мир», Москва.
- Козловский C.B., Карпова О. В., Архипенко М. В., Заякина О. В., Родионова Н. П., Атабеков И. Г. 2003. Влияние N-концевой области белка оболочки Х-вируса картофеля на структуру вирусных частиц. Докл. Акад. Наук. 391, 117−119.
- Ксенофонтов A. JL, Козловский B.C., Кордюкова JI.B., Радюхин В. А., Тимофеева A.B., Добров E.H. 2006. Определение концентрации и размера агрегатов в препаратах вируса гриппа про спектрам истинного поглощения в УФ-свете. Молекулярная биология. 40,172−179.
- Морозов С.Ю., Захарьев В. М., Чернов В. К., Прасолов B.C., Козлов Ю. В., Атабеков И. Г., Скрябин К. Г. 1983. Первичная структура и локализация гена белка оболочки в геномной РНК Х-вируса картофеля. Докл. Акад. Наук СССР. 271, 211−215.
- Новиков В.К., Кимаев В. З., Атабеков И. Г. 1972. Реконструкция нуклеопротеида вируса X картофеля. Докл. Акад. Наук СССР. 204, 1259−1262.
- Орлов В.Н., Арутюнян A.M., Куст С. В., Литманович Е. А., Драчев В. А., Добров Е. Н. 2001. Макроскопическая агрегация белка оболочки вируса табачной мозаики. Биохимия. 66, 154−162.
- Привалов П.Л. 1987. Стабильность белка и гидрофобные взаимодействия. Биофизика. 32, 742−759.
- Рафикова Э.Р., Панюков Ю. В., Арутюнян A.M., Ягужинский Л. С., Драчёв В. А., Добров Е. Н. 2004. Низкие концентрации Ds-Na ингибируют аморфную агрегацию белка оболочки вируса табачной мозаики и влияют на стабильность белка. Биохимия. 69, 1683−1690.
- Сердюк И.Н. 2007. Структурированные белки и белки с внутренней неупорядоченностью. Молекулярная биология. 41, 297−313.
- Серебрякова М. В, Лукашина Е. В., Федорова Н. В., Грачев С. А., Добров Е. Н., БаратоваЛ.А. 2004. Масс-спектрометрическое определение положения углеводных остатков в молекуле белка оболочки X вируса картофеля. Масс-спектрометрия. 1, 191−198.
- Abou-Haidar М., Bancroft J.B. 1978. The initiation of papaya mosaic virus assembly. Virology. 90, 54−59.
- Abou-Haidar M., Erickson J.W., Bancroft J.B. 1979. The inhibition of papaya mosaic virus assembly related to the effect of cations on its RNA. Virology. 98, 116−120.
- Abou-Haidar M.G., Bancroft J.B. 1980. The polarity of assembly of papaya mosaic virus and tobacco mosaic virus RNAs with PMV-protein under conditions of nonspecificity Virology. 107, 202−207.
- Abou-Haidar M.G. 1988. Nucleotide sequence of the capsid protein gene and 3' non-coding region of papaya mosaic virus RNA. J. Gen. Virol. 69, 219−226.
- Angell S.M., Davies C., Baulcombe D.C. 1996. Cell-to-cell movement of potato virus X is associated with a change in the size-exclusion limit of plasmodesmata in trichome cells ofNicotiana clevelandii. Virology. 216, 197−201.
- Atabekov J.G., Rodionova N.P., Karpova O.V., Kozlovsky S.V., Poljakov V.Yu. 2000. The movement protein-triggered in situ conversion of potato virus X virion RNA from a nontranslatable into a translatable form. Virology. 271, 259−263.
- Atabekov J.G., Rodionova N.P., Karpova O.V., Kozlovsky S.V., Novikov V.K., Arkhipenko M.V. 2001. Translational activation of encapsidated potato virus X RNA by coat protein phosphorylation. Virology. 286, 466−474.
- Bancroft J.B., Abou-Haidar M., Erickson J.W. 1979. The assembly of clover yellow mosaic virus and its protein. Virology. 98, 121−130.
- Bancroft B., Hills G.J., Richardson J.F. 1980. A re-evaluation of the structure of narcissus mosaic virus and polymers made from its protein. J. Gen. Virol. 50, 451−454.
- Bancroft J.B., Rouleau M., Johnston R., Prins L., Mackie G.A. 1991. The entire nucleotide sequence of foxtail mosaic virus RNA. J. Gen. Virol. 72, 2173−2181.
- Beck D.L., Guilford P.J., Voot D.M., Andersen M.T., Forster R.L. 1991. Triple gene block proteins of white clover mosaic potexvirus are required for transport. Virology. 183, 695−702.
- Bernal J.D., Fankuchen I. 1941. X-ray and crystallographic studies of plant virus preparations. I. Introduction and preparation of specimens. II. Modes of aggregation of the virus particles. J. Gen. Physiol. 25, 111−146.
- Bhyravbhatla B., Watowich S.J., Caspar D.L. 1998. Refined atomic model of the four-layer aggregate of the tobacco mosaic virus coat protein at 2.4 A resolution. Biophys. J. 74, 604−615.
- Chapman S., Hills G., Watts J., Baulcombe D. 1992. Mutational analysis of the coat protein gene of potato virus X: effects on virion morphology and viral pathogenicity Virology. 191,223−230.
- Chen Y.H., Yang J.T., Martinez H.M. 1972. Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry. 11, 41 204 131.
- Colowick S.P., Kaplan N.O. 1968. Nucleic Acids. In: Methods in enzymology. Eds. Crossman, L., Moldave, K. Academic Press, New York and London. Vol. 12, part B, pp. 129−104,728−732.
- Dawson R.M., Elliot D.C., Elliot W.II., Jones K.M. 1986. Data for biochemical research.
- Clarendon Press, Oxford. Dobrov E. N, Atabekov J.G. 1989. Reconstitution of plant viruses. In: Plant Viruses. Ed.
- Dobrov E.N., Kust S.V., Yakovleva O.A., Tikchonenko T.I. 1977. Structure of single-stranded virus RNA in situ. II. Optical activity of five tobacco mosaic-like viruses and their components. Biochim. Biophys. Acta. 475, 623−637.
- Edsall J.T., McKenzie H.A. 1978. Water and proteins. I. The significance and structure of water: its interaction with electrolytes and non-electrolytes. Adv. Biophys. 10, 137−207.
- Efimov A.V. 1984. A novel super-secondary structure of proteins and the relation between the structure and the amino acid sequence. FEBSLett. 166, 33−38.
- Efimov A.V. 1993. Standard structures in proteins. Prog. Biophys. Mol. Biol. 60, 201−239.
- Efimov A.V. 1995. Structural similarity between two-layer a/p and P-proteins. J. Mol. Biol. 245,402−415.
- Efimov A.V. 1999. Complementary packing of a -helices in proteins. FEBS Lett. 463, 3−6.
- Erhardt M., Stussi-Garaud C., Guilley H., Richards K.E., Jonard G., Bouzoubaa S. 1999. The first triple gene block protein of peanut clump virus localizes to the plasmodesmata during virus infection. Virology. 264, 220−229.
- Erickson J.W., Bancroft J.B., Home R.W. 1976. The assembly of papaya mosaic virus protein. Virology. 72, 514−517.
- Erickson J.W., Abou-Haidar M., Bancroft J.B. 1978. The specificity of papaya mosaic virus assembly. Virology. 90, 60−66.
- Erickson J.W., Bancroft J.B. 1978. The self-assembly of papaya mosaic virus. Virology. 90, 36−46.
- Erickson J.W., Bancroft J.B. 1981. Melting of viral RNA by coat protein: Assembly strategies for elongated plant viruses. Virology. 108, 235−240.
- Erickson J.W., Bancroft J.B., Stillman M.J. 1981. Circular dichroism studies of papaya mosaic virus coat protein and its polymers. J. Mol. Biol. 47, 337−439.
- Erickson J.W., Hallett F.R., Bancroft J.B. 1983. Subassembly aggregates of papaya mosaic virus protein. Virology. 129,207−211.
- Finney J.L., Gellatly B.J., Golton I.C., Goodfellow J. 1980. Solvent effects and polar interactions in the structural stability and dynamics of globular proteins. Biophys J. 32, 17−33.
- Fraenkel-Conrat H. 1957. Degradation of tobacco mosaic virus with acetic acid. Virology, 4, 1−4.
- Francki R.I. 1985. Plant virus satellites. Annu. Rev. Microbiol. 39, 151−174.
- Franklin R.E., Klug A. 1956. The nature of the helical groove on the tobacco mosiac virus particle- x-ray diffraction studies. Biochim. Biophys. Acta. 19, 403−416.
- Francki R.I., McLean G.D. 1968. Purification of potato virus X and preparation of infectious ribonucleic acid by degradation with lithium chloride. Aust. J. Biol. Sci. 21, 1311−1318.
- Ghosh S., Banerjee A. 2002. A multitechnique approach in protein/surfactant interaction study: Physicochemical aspects of sodium dodecyl sulfate in the presence of trypsin in aqueous medium. Biomacromolecules. 3, 9−16.
- Gilmer D., Bouzoubaa S., Hehn A., Guilley H., Richards K., Jonard G. 1992. Efficient cell-to-cell movement of beet necrotic yellow vein virus requires 31 proximal genes located on RNA 2. Virology. 189,40−47.
- Goodman R.M. 1975. Reconstitution of potato virus X in vitro. I. Properties of the dissociated protein structural subunits. Virology. 68, 287−298.
- Goodman R.M., Home R.W., Hobart J.M. 1975. Reconstruction of potato virus X in vitro. II. Characterization of the reconstituted product. Virology. 68, 299−308.
- Goodman R.M., McDonald J.G., Home R.W., Bancroft J.B. 1976. Assembly of flexuous plant viruses and their proteins. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 276, 173−179.
- Goodman R.M. 1977. Reconstitution of potato virus X in vitro. III. Evidence for a role for hydrophobic interactions. Virology. 76, 72−78.
- Greenfield N., Fasman G.D. 1969. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry. 8, 4108−4116.
- Greenwood N.N., Earnshaw A. 1997. Chemistry of the elements. Butterworth-Heinemann, Oxford.
- Guttenplan J.B., Calvin M. 1973. Tertiary and quaternary structure of tobacco mosaic virus and protein. I. Effect of pH on fluorescence and 2-p-toluidinylnaphthalene-6-sulfonate binding. Biochim. Biophys. Acta. 322, 294−300.
- Harrison B.D., Finch J.T., Gibbs A.J., Hollings M., Shepherd R.J., Valenta V., Wetter C. 1971. Sixteen groups of plant viruses. Gen. Virol. 12, 175−178.
- Hiscox J. A, Ball L.A. 1997. Cotranslational disassembly of flock house virus in a cell-free system. J. Virol. 71, 7974−7977.
- Homer R.B., Goodman R.M. 1975. Circular dichroism and fluorescence studies on potato virus X and its structural components. Biochim. Biophys. Acta. 378, 296−304.
- Homer R.B., Dalton D.I. 1976. A pH-dependent conformational change in the coat protein subunits from potato virus X. Biochim. Biophys. Acta. 44, 542−546.
- Horwitz J., Strickland E.H., Billups C. 1969. Analysis of vibrational structure in the near-ultraviolet circular dichroism and absorption spectra of phenylalanine and its derivatives. J. Am. Chem. Soc. 91, 184−190.
- Horwitz J., Strickland E.H., Billups C. 1970. Analysis of the vibrational structure in the near-ultraviolet circular dichroism and absorption spectra of tyrosine derivatives and ribonuclease-A at 77.deg. K. J. Am. Chem. Soc. 92, 2119−2129.
- Huang Y.L., Han Y.T., Chang Y.T., Hsu Y.H., Meng M. 2004. Critical residues for GTP methylation and formation of the covalent m7GMP-enzyme intermediate in the capping enzyme domain of bamboo mosaic virus. J. Virol. 78, 1271−1280.
- Huisman M.J., Linthorst H.J., Bol J.F., Cornelissen J.C. 1988. The complete nucleotide sequence of potato virus X and its homologies at the amino acid level with various plus-stranded RNA viruses. J. Gen. Virol. 69, 1789−1798.
- Jagadish M.N., Huang D., Ward C.W. 1993. Site-directed mutagenesis of a potyvirus coat protein and its assembly in Escherichia coli. J. Gen. Virol. 74, 893−896.
- Kaftanova A.S., Kiselev N.A., Novikov V.K., Atabekov J.G. 1975. Structure of products of protein reassembly and reconstruction of potato virus X. Virology. 67, 283−287. ¦
- Kalinina N.O., Fedorkin O.N., Samuilova O.V., Maiss E., Korpela T., Morozov S.Yu., Atabekov J.G. 1996. Expression and biochemical analyses of the recombinant potato virus X 25K movement protein. FEBSLett. 397, 75−78.
- Kalinina N.O., Rakitina D.A., Solovyev A.G., Schiemann J., Morozov S.Yu. 2002. RNA helicase activity of the plant virus movement proteins encoded by the first gene of the triple gene block. Virology. 296,321−329.
- Karpova O.V., Ivanov K.I., Rodionova N.P., Dorokhov Yu.L., Atabekov J.G. 1997. Nontranslatability and dissimilar behavior in plants and protoplasts of viral RNA and movement protein complexes formed in vitro. Virology. 230, 11−21.
- Kelloniemi J., Makinen K., Valkonen J.P. 2006. A potyvirus-based gene vector allows producing active human S-COMT and animal GFP, but not human sorcin, in vector-infected plants. Biochimie. 88, 505−513.
- Kendall A., Bian W., Junn J., McCullough I., Gore D., Stubbs G. 2007. Radial density distribution and symmetry of a Potexvirus, narcissus mosaic virus. Virology. 357, 158−164.
- Kim K.H., Hemenway C. 1996. The 5' nontranslated region of potato virus X RNA affects both genomic and subgenomic RNA synthesis. J. Virol. 70, 5533−5540.
- Kiselyova O.I., Yaminsky I.V., Karpova O.V., Rodionova N.P., Kozlovsky S.V., Arkhipenko M.V., Atabekov J.G. 2003. AFM study of potato virus X disassembly induced by movement protein. J. Mol. Biol. 332, 321−325.
- Koenig R., Stegemann H., Francksen H., Paul H.L. 1970. Protein subunits in the potato virus X group. Determination of the molecular weights by polyacrylamide electrophoresis. Biochim. Biophys. Acta. 207, 184−189.
- Koenig R. 1972. Anomalous behavior of the coat proteins of potato virus X and cactus virus X during electrophoresis in dodecyl sulfate-containing polyacrylamide gels. Virology. 50, 263−266.
- Koenig R., Tremaine J.H., Shepard J.F. 1978. In situ degradation of the protein chain of potato virus X at the N- and C-termini J. Gen. Virol. 38, 329−337.
- Koenig R. Torrance L. 1986. Antigenic analysis of potato virus X by means of monoclonal antibodies J. Gen. Virol. 67,2145−2151.
- Koonin E.V., Dolja V.V. 1993. Evolution and taxonomy of positive-strand RNA viruses: implications of comparative analysis of amino acid sequences. Crit. Rev. Biochem. Mol. Biol. 28, 375−430.
- Mandahar C.L. 1989. Monopartite elongated viruses. In: Plant Viruses. Ed. Mandahar C.L. Boca Raton, Florida: Inc.: CRCPress, 12−15.
- Mattice W.L., Riser J.M., Clark D.S. 1976. Conformational properties of the complexes formed by proteins and sodium dodecyl sulfate. Biochemistry. 15, 4264−4272.
- Morozov S. Yu, Lukasheva L.I., Chernov B.K., Skriabin K.G., Atabekov I.G. 1987. Primary structure of the potato virus X genome: the region preceding the capsid protein cistron. Mol. Gen. Mikrobiol. Virusol. 3, 32−38.
- Morozov S.Yu., Dolja V.V., Atabekov J.G. 1989. Probable reassortment of genomic elements among elongated RNA-containing plant viruses. J. Mol. Evol. 29, 52−62.
- Morozov S.Y., Miroshnichenko N.A., Zelenina D.A., Fedorkin O.N., Solovijev A.G., Lukasheva L.I., Atabekov J.C. 1990. Expression of RNA transcripts of potato virus X full-length and subgenomic cDNAs. Biochimie. 72, 677−684.
- Morozov S.Yu., Miroshnichenko N.A., Solovyev A.G., Fedorkin O.N., Zelenina D.A., Lukasheva L.I., Karasev A.V., Dolja V.V., Atabekov J.G. 1991. Expression strategy of the potato virus X triple gene block. J. Gen. Virol. 72, 2039−2042.
- Morozov S.Y., Solovyev A.G., Kalinina N.O., Fedorkin O.N., Samuilova O.V., Schiemann J., Atabekov J.G. 1999. Evidence for two nonoverlapping functional domains in the potato virus X 25K movement protein. Virology. 260, 55−63.
- Morozov S.Y., Solovyev A.G. 2003. Triple gene block: modular design of a multifunctional machine for plant virus movement. J. Gen. Virol. 84, 1351−1366.
- Namba K., Pattanayek R., Stubbs G. 1989. Visualization of intact tobacco mosaic virus at 2.9 A resolution by X-ray fiber diffraction. J. Mol. Biol. 208, 307−325.
- Ohtsubo K., Marth J.D. 2006. Glycosylation in cellular mechanisms of health and disease. Cell. 126, 855−867.
- Orlov V. N, Kust S. V, Kalmykov P. V, Krivosheev V. P, Dobrov E. N, Drachev V.A. 1998. A comparative differential scanning calorimetric study of tobacco mosaic virus and of its coat protein ts mutant. FEBS Lett. 433, 307−311.
- Panyukov Y., Yudin I., Drachev V., Dobrov E., Kurganov B. 2007. The study of amorphous aggregation of tobacco mosaic virus coat protein by dynamic light scattering. Biophys. Chem. 127,9−18.
- Parker L., Kendall A., Stubbs G. 2002. Surface features of potato virus X from fiber diffraction. Virology. 300, 291−295.
- Parker L., Kendall A., Berger P.H., Shiel P.J., Stubbs G. 2005. Wheat streak mosaic virus -structural parameters for a Potyvirus. Virology. 340, 64−69.
- Pivovarova A.V., Mikhailova V.V., Chernik I.S., Chebotareva N.A., Levitsky D.I., Gusev N.B. 2005. Effects of small heat shock proteins on the thermal denaturation and aggregation of F-actin. Biochem. Biophys. Res. Commun. 331, 1548−1553.
- Privalov P.L., Gill S.J. 1988. Stability of protein structure and hydrophobic interaction. Adv. Protein. Chem. 39, 191−234.
- Qu C., Liljas L., Opalka N., Brugidou C., Yeager M., Beachy R., Fauquet C., Johnson J., Lin T. 2000. 3D domain swapping modulates the stability of members of an icosahedral virus group. Structure. 8, 1095−1103.
- Rafikova E.R., Kurganov B.I., Arutyunyan A.M., Kust S.V., Drachev V.A., Dobrov E.N. 2003. A mechanism of macroscopic (amorphous) aggregation of the tobacco mosaic virus coat protein. Int. J. Biochem. Cell Biol. 35, 1452−1460.
- Receveur-Brechot V., Bourhis J.M., Uversky V.N., Canard B., Longhi S. 2006. Assessing protein disorder and induced folding. Proteins. 62, 24−45.
- Richardson J.F., Tollin P., Bancroft J.B. 1981. The architecture of the potexviruses. Virology. 112, 34−39.
- Rodionova N.P., Karpova O.V., Kozlovsky S.V., Zayakina O.V., Arkhipenko M.V., Atabekov J.G. 2003. Linear remodeling of helical virus by movement protein binding. J. Mol. Biol. 333, 565−572.
- Santa Cruz S., Roberts A.G., Prior D.A.M., Chapman S., Oparka, K.J. 1998. Cell-to-cell and phloem-mediated transport of potato virus X: the role of virions. Plant Cell. 10, 495−510.
- Sawyer L., Tollin P., Wilson H.R. 1987. A comparison between the predicted secondary structures of potato virus X and papaya mosaic virus coat protein. J. Gen. Virol. 68, 1229−1232.
- Schuck P. 2000. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys. J. 78, 1606−1619.
- Shalla T.A., Shepard J.F. 1970. An antigenic analysis of potato virus X and of its degraded protein. II. Evidence for a conformational change associated with the depolymerization of structural protein. Virology. 42, 835−847.
- Shanmugam G., Polavarapu P.L., Kendall A., Stubbs G. 2005. Structures of plant viruses from vibrational circular dichroism. J. Gen. Virol. 86, 2371−2377.
- Shapiro A.L., Vinuela E., Maizel J.V.Jr. 1967. Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochem. Biophys. Res. Commun. 28, 815−820.
- Shepard J.F., Secor G.A. 1972. The effects of enzymatic digestion on the moleculat weight and antigenic specificity of potato virus X protein. Phytopathology. 62, 1154−1160.
- Short M.N., Davies J.W. 1983. Narcissus mosaic virus: a potexvirus with an encapsidated subgenomic messenger RNA for coat protein. Biosci. Rep. 3, 837−846.
- Short M.N., Turner D.S., March J.F., Pappin D.J.C., Parente A., Davies J.W. 1986. The primary structure of papaya mosaic virus coat protein. Virology. 152, 280−283.
- Shukla D.D., Ward C.M. 1989. Structure of potyvirus coat proteins and its application in the taxonomy of the potyvirus group. Adv. Virus Res. 36, 273−314.
- Simpson A.A., Chipman P.R., Baker T.S., Tijssen P., Rossmann M.G. 1998. The structure of an insect parvovirus (Galleria mellonella densovirus) at 3.7 A resolution. Structure. 6, 1355−1367.
- Sit T.L., Abouhaidar M.G., Holy S. 1989. Nucleotide sequence of papaya mosaic virus RNA. J. Gen. Virol. 70, 2325−2331.
- Skryabin K.G., Kraev A.S., Morozov S.Yu., Rozanov M.N., Chernov B.K., Lukasheva L.I., Atabekov J.G. 1988. The nucleotide sequence of potato virus X RNA. Nucleic Acids Res. 16, 10 929−10 930.
- Schepetilnikov M.V., Manske U., Solovyev A.G., Zamyatnin A.A. Schiemann J., Morozov S.Y. 2005. The hydrophobic segment of Potato virus X TGBp3 is a major determinant of the protein intracellular trafficking. J. Gen. Virol. 86,2379−2391.
- Strickland E. H., Horwitz J., Billups C. 1969. Fine structure in the near-ultraviolet circular dichroism and absorption spectra of tryptophan derivatives and chymotrypsinogen A at 77 °K. Biochemistry. 8, 3205−3213.
- Stubbs G., Warren S., Holmes K. 1977. Structure of RNA and RNA binding site in tobacco mosaic virus from 4 A map calculated from X-ray fiber diagrams. Nature. 267,216−221.
- Stubbs G. Developments in fiber diffraction. 1999. Curr. Opin. Struct. Biol. 9, 615−619.
- Tate J., Liljas, L., Scotti P., Christian P., Lin T., Johnson J.E. 1999. The crystal structure of cricket paralysis virus: the first view of a new virus family. Nat. Struct. Biol. 6, 765−774.
- Tollin P., Wilson H.R., Young D.W., Cathro J., Mowat W.P. 1967. X-ray diffraction and electron microscope studies of narcissus mosaic virus, and comparison with potato virus X. J. Mol. Biol. 26, 353−355.
- Tollin P., Bancroft J.B., Richardson J.F., Payne N.C., Beveridge T.J. 1979. Diffraction studies of papaya mosaic virus. Virology. 98, 108−115.
- Tollin, P & Wilson, H. R. 1988. Particle structure. In: The Plant Viruses: The Filamentous Plant Viruses. Ed. Milne R.C. N.Y.: Plenum Press. 4, 51−83.
- Tomashevskaya O.L., Solovyev A.G., Karpova O.V., Fedorkin O.N., Rodionova N.P., Morozov S.Yu., Atabekov J.G. 1993. Effects of sequence elements in the potato virus
- X RNA 5' non-translated alpha beta-leader on its translation enhancing activity. J. Gen. Virol. 74, 2717−2724. Tozzini A.C., Ek B., Palva E.T., Hopp H.E. 1994. Potato virus X coat protein: a glycoprotein. Virology. 202, 651−658.
- Zamyatnin A.A., Solovyev A.G., Bozhkov P.V., Valkonen J.P., Morozov S.Y., Savenkov E.I. 2006. Assessment of the integral membrane protein topology in living cells. Plant J. 46, 145−154.
- Zhang H., Todderud E., Stubbs G. 1993. Crystallization and preliminary X-ray analysis of papaya mosaic virus coat protein. J. Mol. Biol. 234, 885−887.
- Zhu D.M., Evans R.K. 2006. Molecular mechanism and thermodynamics study of plasmid