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  1. 1
    Academic Journal

    المصدر: Vestnik Moskovskogo universiteta. Seriya 16. Biologiya; Том 72, № 3 (2017); 169-173 ; Вестник Московского университета. Серия 16. Биология; Том 72, № 3 (2017); 169-173 ; 0137-0952

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    Relation: https://vestnik-bio-msu.elpub.ru/jour/article/view/474/398; Ngo T.T., Zhang Q., Zhou R., Yodh J.G., Ha T. Asymmetric unwrapping of nucleosomes under tension directed by DNA local flexibility // Cell. 2015. Vol. 160 N 6. P. 1135–1144.; Li G., Levitus M., Bustamante C., Widom J. Rapid spontaneous accessibility of nucleosomal DNA // Nat. Struct. Mol. Biol. 2005. Vol. 12. N 1. P. 46–53.; Gansen A., Toth K., Schwarz N.,Langowski J. Structural variability of nucleosomes detected by single-pair Forster resonance energy transfer: histone acetylation, sequence variation, and salt effects // J. Phys. Chem. B. 2009. Vol. 113. N 9. P. 2604–2613.; Gansen A., Valeri A., Hauger F., Felekyan S., Kalinin S., Toth K., Langowski J., Seidel C.A. Nucleosome disassembly intermediates characterized by single-molecule FRET // Proc. Natl. Acad. Sci. U.S.A. 2009. Vol. 106. N 36. P. 15308–15313.; Zinchenko A.A., Yoshikawa K. Na+ shows a markedly higher potential than K+ in DNA compaction in a crowded environment // Biophys. J. 2005. Vol. 88. N 6. P. 4118–4123.; Savelyev A., Papoian G.A. Electrostatic, steric, and hydration interactions favor Na(+) condensation around DNA compared with K(+) // J. Am. Chem. Soc. 2006. Vol. 128. N 45. P. 14506–14518.; Materese C.K., Savelyev A., Papoian G.A. Counterion atmosphere and hydration patterns near a nucleosome core particle // J. Am. Chem. Soc. 2009. Vol. 131. N 41. P. 15005– 15013.; Gaykalova D.A., Kulaeva O.I., Bondarenko V.A., Studitsky V.M. Preparation and analysis of uniquely positioned mononucleosomes // Chromatin Protocols. Methods Mol. Biol. Vol. 523 / Ed. S.P. Chellappan. Humana Press, 2009. P. 109–123.; Kudryashova K.S., Chertkov O.V., Nikitin D.V., Pestov N.A., Kulaeva O.I., Efremenko A.V., Solonin A.S., Kirpichnikov M.P., Studitsky V.M., Feofanov A.V. Preparation of mononucleosomal templates for analysis of transcription with RNA polymerase using spFRET // Chromatin Protocols. Methods Mol. Biol. Vol. 1288 / Ed. S.P. Chellappan. N.Y.: Springer, 2015. P. 395–412.; Lyubitelev A.V., Kudryashova K.S., Mikhaylova M.S., Malyuchenko N.V., Chertkov O.V., Studitsky V.M., Feofanov A.V., Kirpichnikov M.P. Change in conformation of linker DNA upon binding of histone H1.5 to nucleosome: fluorescent microscopy of single complexes // Moscow Univ. Biol. Sci. Bull. 2016. Vol. 71. N 2. P. 108–113.; Manning G.S. The persistence length of DNA is reached from the persistence length of its null isomer through an internal electrostatic stretching force // Biophys. J. 2006. Vol. 91. N 10. P. 3607–3616.; Valieva M.E., Armeev G.A., Kudryashova K.S., Gerasimova N.S., Shaytan A.K., Kulaeva O.I., McCullough L.L., Formosa T., Georgiev P.G., Kirpichnikov M.P., Studitsky V.M., Feofanov A.V. Large-scale ATP-independent nucleosome unfolding by a histone chaperone // Nat. Struct. Mol. Biol. 2016. Vol. 23. N 12. P. 1111–1116.; Sultanov D., Gerasimova N., Kudryashova K., Maluchenko N., Kotova E., Langelier M.F., Pascal J., Kirpichnikov M., Feofanov A., Studitsky V. Unfolding of core nucleosomes by PARP- 1 revealed by spFRET microscopy // AIMS Genetics. 2017. Vol. 4. N 1. P. 21–31.; Choy J.S., Lee T.H. Structural dynamics of nucleosomes at single-molecule resolution // Trends Biochem. Sci. 2012. Vol. 37. N 10. P. 425–435.; Wei S., Falk S.J., Black B.E., Lee T.H. A novel hybrid single molecule approach reveals spontaneous DNA motion in the nucleosome // Nucleic Acids Res. 2015. Vol. 43. N 17. e111.; Koopmans W.J., Brehm A., Logie C., Schmidt T., van Noort J. Single-pair FRET microscopy reveals mononucleosome dynamics // J. Fluoresc. 2007. Vol. 17. N 6. P. 785–795.; Kenzaki H., Takada S. Partial unwrapping and histone tail dynamics in nucleosome revealed by coarse-grained molecular simulations // PLoS Comput. Biol. 2015. Vol. 11. N 8. e1004443.; Li Z., Kono H. Distinct roles of histone H3 and H2A tails in nucleosome stability // Sci. Rep. 2016. Vol. 6. 31437.; Forties R.A., North J.A., Javaid S., Tabbaa O.P., Fishel R., Poirier M.G., Bundschuh R. A quantitative model of nucleosome dynamics // Nucleic Acids Res. 2011. Vol. 39. N 19. P. 8306–8313.; https://vestnik-bio-msu.elpub.ru/jour/article/view/474

  2. 2
    Academic Journal

    المصدر: Vestnik Moskovskogo universiteta. Seriya 16. Biologiya; № 2 (2016); 49-54 ; Вестник Московского университета. Серия 16. Биология; № 2 (2016); 49-54 ; 0137-0952

    وصف الملف: application/pdf

    Relation: https://vestnik-bio-msu.elpub.ru/jour/article/view/327/312; Shrestha D., Jenei A., Nagy P., Vereb G., Szöllősi J. Understanding FRET as a research tool for cellular studies // Int. J. Mol. Sci. 2015. Vol.16. N 4. P. 6718–6756.; Sustarsic M.K. Taking the ruler to the jungle: singlemolecule FRET for understanding biomolecular structure and dynamics in live cells // Curr. Opin. Struct. Biol. 2015 Vol. 18. P. 52–59.; Arai Y.N. Extensive use of FRET in biological imaging // Microscopy (Oxf). 2013. Vol. 62. P. 419–428.; Sugawa M.A., Iwane A.H., Ishii Y., Yanagida T. Single molecule FRET for the study on structural dynamics of biomolecules // Biosystems. 2007. Vol. 88. N 3. P. 243–250.; Lee W., Obubuafo A., Lee Y.I., Davis L.M., Soper S.A. Single-pair fluorescence resonance energy transfer (spFRET) for the high sensitivity analysis of low-abundance proteins using aptamers as molecular recognition elements // J. Fluoresc. 2010. Vol. 20. N 1. 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P. 12711–12716.; Syed S.H., Goutte-Gattat D., Becker N., Meyer S., Shukla M.S., Hayes J.J., Everaers R., Angelov D., Bednar J., Dimitrov S. Single-base resolution mapping of H1-nucleosome interactions and 3D organization of the nucleosome // Proc. Natl. Acad. Sci. USA. 2010. Vol. 107. N 21. P. 9620–9625.; Meyer S. B., Syed S.H., Goutte-Gattat D., Shukla M.S., Hayes J.J., Angelov D., Bednar J., Dimitrov S., Everaers R. From crystal and NMR structures, footprints and cryo-electron- micrographs to large and soft structures: nanoscale modeling of the nucleosomal stem // Nucleic Acids Res. 2011. Vol. 39. P. 9139–9154.; Zhou B.R., Feng H., Kato H., Dai L., Yang Y., Zhou Y., Bai Y. Structural insights into the histone H1-nucleosome complex // Proc. Natl. Acad. Sci. USA. 2013. Vol. 110. N 48. P. 19390–19395.; Gaykalova D.A., Kulaeva O.I., Bondarenko V.A., Studitsky V.M. Preparation and analysis of uniquely positioned mononucleosomes // Methods Mol. Biol. 2009. Vol. 523. P. 109–123.; Meyer S., Becker N.B., Syed S.H., Goutte-Gattat D., Shukla M.S., Hayes J.J., Angelov D, Bednar J., Dimitrov S., Everaers R. From crystal and NMR structures, footprints and cryo-electron-micrographs to large and soft structures: nanoscale modeling of the nucleosomal stem // Nucleic Acids Res. 2011. Vol. 39. N 21. P. 9139–9154.; Song F., Chen P., Sun D., Wang M., Dong L., Liang D., Xu R.M., Zhu P., Li G. Cryo-EM study of the chromatin fiber reveals a double helix twisted by tetranucleosomal units // Science. 2014. Vol. 344. N 6182. P. 376–380.; Fan L., Roberts V.A. Complex of linker histone H5 with the nucleosome and its implications for chromatin packing // Proc. Natl. Acad. Sci. USA. 2006. Vol. 103. N 22. P. 8384–8289.; Cui F., Zhurkin V.B. Distinctive sequence patterns in metazoan and yeast nucleosomes: implications for linker histone binding to AT-rich and methylated DNA // Nucleic Acids Res. 2009. Vol. 37. N 9. P. 2818–2829.; Zhou B.R., Jiang J., Feng H., Ghirlando R., Xiao T.S., Bai Y. Structural mechanisms of nucleosome recognition by linker histones // Mol. Cell. 2015. Vol. 59. N 4. P. 628–638.; Bernier M., Luo Y., Nwokelo K.C., Goodwin M., Dreher S.J., Zhang P., Parthun M.R., Fondufe-Mittendorf Y., Ottesen J.J., Poirier M.G. Linker histone H1 and H3K56 acetylation are antagonistic regulators of nucleosome dynamics // Nat. Commun. 2015. Vol. 6. P. 10152.; https://vestnik-bio-msu.elpub.ru/jour/article/view/327