[Ajiro K., Borun T.W., Solter D. (1981). Quantitative changes in the expression of histone H1 and H2Bsubtypes and their relationship to the differentiation of mouse embryonal carcinoma cells. Dev. Biol., 86: 206-211.]Search in Google Scholar
[Bhan S., May W., Warren S.L., Sittman D.B. (2008). Global gene expression analysis reveals specific and redundant roles for H1 variants, H1c and H10, in gene expression regulation. Gene, 414: 10-18.]Search in Google Scholar
[Catez F., Ueda T., Bustin M. (2006). Determinants of histone H1 mobility and chromatin binding in living cells. Nat. Struct. Mol. Biol., 13: 305-310.]Search in Google Scholar
[Clausell J., Happel N., Hale T.K., Doenecke D., Beato M. (2009). Histone H1 subtypes differently modulate chromatin condensation without preventing ATP-dependent remodeling by SWI/SNFor NURF. PLo S One, 4: e0007243. doi: 10.1371/journal.pone.0007243.]Search in Google Scholar
[Daujat S., Zeissler U., Waldmann T., Happel N., Schneider R. (2005). HP1 binds specifically to Lys26-methylated histone H1.4, whereas simultaneous Ser27 phosphorylation blocks HP1 binding. J. Biol. Chem., 280: 38090-38095.]Search in Google Scholar
[Fan Y., Sirotkin A.M., Russel R.G., Ayala J., Skoultchi A.I. (2001). Individual somatic H1 subtypes are dispensable for mouse development even in mice lacking the H1(0) replacement subtype. Mol. Cell. Biol., 21: 7933-7943.]Search in Google Scholar
[Fan Y., Nikitina T., Zhao J., Fleury T.J., Bhattacharyya R., Bouhassira E.E., Stein A., Woodcock C.L., Skoultchi A.I. (2005). Histone H1 depletion in mammals alter global chromatin structure but causes specific changes in gene regulation. Cell, 123: 1199-1212.]Search in Google Scholar
[Garg M., Perumalsamy L.R., Shivashankar G.V., Sarin A. (2014). The linker histone H1.2 is an intermediate in the aptoptotic response to cytokine deprivation in T-effectors. Int. J. Cell Biol., 2014: 674753. doi: 10.1155/2014/674753.]Search in Google Scholar
[Hansen J.C. (2002). Conformational dynamics of the chromatin fiber in solution: determinants, mechanisms, and functions. Ann. Rev. Biophys. Biomol. Struct., 31: 361-392.]Search in Google Scholar
[Happel N., Doenecke D. (2009). Histone H1 and its isoforms: contribution to chromatin structure and function. Gene, 431: 1-12.]Search in Google Scholar
[Happel N., Warneboldt J., Hänecke K., Haller F., Doenecke D. (2009). H1 subtype expression during cell proliferation and growth arrest. Cell Cycle, 8: 2226-2232.]Search in Google Scholar
[Hashimoto H., Takami Y., Sonoda E., Iwasaki T., Iwano H., Tachibana M., Takeda S., Nakayama T., Kimura H., Shinkai Y. (2010). Histone H1 null vertebrate cells exhibit altered nucleosome architecture. Nucleic Acids Res., 38: 3533-3545.]Search in Google Scholar
[Hergeth S.P., Schneider R. (2015). The H1 linker histones: multifunctional proteins beyond the nucleosomal core particle. EMBO Rep., 16: 1439-1453.]Search in Google Scholar
[Izzo A., Schneider R. (2016). The role of linker histone H1 modifications in the regulation of gene expression and chromatin dynamics. Biochim. Biophys. Acta, 1859: 486-495.]Search in Google Scholar
[Izzo A., Kamieniarz K., Schneider R. (2008). The histone H1 family: specific members, specific functions? Biol. Chem., 389: 333-343.]Search in Google Scholar
[Izzo A., Kamieniarz - Gdula K., Ramirez F., Noureen N., Kind J., Manke T.,van Steensel B., Schneider R. (2013). The genomic landscape of the somatic linker histone subtypes H1.1 to H1.5 in human cells. Cell Rep., 3: 2142-2154.]Search in Google Scholar
[Kalashnikova A.A., Rogge R.A., Hansen J.C. (2016). Linker histone H1 and protein-protein interactions. Biochim. Biophys. Acta, 1859: 455-461.]Search in Google Scholar
[Kavi H., Lu X., Xu N., Bartholdy B.A., Vershilova E., Skoultchi A.I., Fyodorov D.V. (2015). Agenetic screen and transcript profiling revealedashared regulatory program for Drosophila linker histone H1 and chromatin remodeler CHD1. G3, 5: 677-687.]Search in Google Scholar
[Kowalski A. (2015). Abundance of intrinsic structural disorder in the histone H1 subtypes. Comput. Biol. Chem., 59: 16-27.]Search in Google Scholar
[Kowalski A., Pałyga J. (2011). Chromatin compaction in terminally differentiated avian blood cells: the role of linker histone H5 and non-histone protein MENT. Chromosome Res., 19: 579-590.]Search in Google Scholar
[Kowalski A., Pałyga J. (2012 a). Linker histone subtypes and their allelic variants. Cell Biol. Int., 36: 981-996.10.1042/CBI2012013323075301]Search in Google Scholar
[Kowalski A., Pałyga J. (2012 b). High-resolution two-dimensional polyacrylamide gel electrophoresis: Atool for identification of polymorphic and modified linker histone components. In: Gel Electrophoresis - Principles and Basics, Magdeldin S. (ed.). In Tech (Croatia), pp. 117-136.10.5772/38235]Search in Google Scholar
[Kowalski A., Pałyga J. (2016). Modulation of chromatin function through linker histone H1 variants. Biol. Cell, 108: 1-18.]Search in Google Scholar
[Koutzamani E., Loborg H., Sarg B., Lindner H.H., Rundquist I. (2002). Linker histone subtype composition and affinity for chromatin in situ in nucleated mature erythrocytes. J. Biol. Chem., 227: 44688-44694.]Search in Google Scholar
[Lennox R.W., Cohen L.H. (1984). The alterations in histone H1 complement during mouse spermatogenesis and their significance for H1 subtype function. Dev. Biol., 103: 80-84.]Search in Google Scholar
[Lu H., Hamkalo B., Parseghian M.H., Hansen J.C. (2009). Chromatin condensing functions of the linker histone C-terminal domain are mediated by specific amino acid composition and intrinsic protein disorder. Biochemistry, 48: 164-172.]Search in Google Scholar
[Medrzycki M., Zhang Y., Cao K., Fan Y. (2012). Expression analysis of mammalian linkerhistone subtypes. J. Vis. Exp., (61). doi: 10.3791/3577.]Search in Google Scholar
[Meergans T., Albig W., Doenecke D. (1997). Varied expression patterns of human histone H1 genes in different cell lines. DNA Cell Biol., 16: 1041-1049.]Search in Google Scholar
[Millãn- Ariño L., Izquierdo-Bouldstridge A., Jordan A. (2016). Specificities and genomic distribution of somatic mammalian histone H1 subtypes. Biochim. Biophys. Acta, 1859: 510-519.]Search in Google Scholar
[Montes de Oca R., Lee K.K., Wilson K.L. (2005). Binding of barrier to autointegration factor (BAF) to histone H3 and selected linker histones including H1.1. J. Biol. Chem., 280: 42252-42262.]Search in Google Scholar
[Neelin J.M., Neelin E.M., Lindsay D.W., Pałyga J., Nichols C.R., Cheng K.M. (1995). The occurrence ofamutant dimerizable histone H5 in Japanese quail erythrocytes. Genome, 38: 982-990.]Search in Google Scholar
[Ni J.Q., Liu L.P., Hess D., Rietdorf J., Sun F.L. (2006). Drosophila ribosomal proteins are associated with linker histones H1 and suppress gene transcription. Gene. Dev., 20: 1959-1973.]Search in Google Scholar
[Over R.S., Michaels S.D. (2014). Open and closed: the roles of linker histones in plants and animals. Mol. Plant, 7: 481-491.]Search in Google Scholar
[Pałyga J. (1991). Acomparison of the histone H1 complements of avian erythrocytes. Int. J. Biochem., 23: 845-849.]Search in Google Scholar
[Parseghian M.H. (2015). What is the role of histone H1 heterogeneity? AIMS Biophys., 2: 724-772.]Search in Google Scholar
[Parseghian M.H., Newcomb R.L., Winokur S.T., Hamkalo B.A. (2000). The distribution of somatic H1 subtypes is non-random on active vs. inactive chromatin: distribution in human fetal fibroblasts. Chromosome Res., 8: 405-424.]Search in Google Scholar
[Peng Z., Mizianty M.J., Xue B., Kurgan L., Uversky V.N. (2012). More than just tails: intrinsic disorder in histone proteins. Mol. Biosyst., 8: 1886-1901.]Search in Google Scholar
[Routh A., Sandin S., Rhodes D. (2008). Nucleosome repeat length and linker histone stoichiometry determine chromatin fiber structure. Proc. Natl. Acad. Sci. USA, 105: 8872-8877.]Search in Google Scholar
[Sarg B., Lopez B., Lindner H., Ponte I., Suau P., Roque A. (2014). Sequence conservation of linker histones between chicken and mammalian species. Data Brief, 1: 60-64.]Search in Google Scholar
[Sarg B., Lopez R., Lindner H., Ponte I., Suau P., Roque A. (2015). Identification of novel post-translational modifications in linker histones from chicken erythrocytes. J. Proteomics, 113: 162-177.]Search in Google Scholar
[Shannon M.F., Wells J.R.E. (1987). Characterization of the six chicken histone H1 proteins and alignment with their respective genes. J. Biol. Chem., 262: 9664-9668.]Search in Google Scholar
[She W., Grimanelli D., Rutowicz K., Whitehead M.W.J., Puzio M., Kotliński M., Jerzmanowski A., Baroux C. (2013). Chromatin reprogramming during the somatic-toreproductive cell fate transition in plants. Development, 140: 4008-4019.]Search in Google Scholar
[Soria G., Polo S.E., Almouzni G. (2012). Prime, repair, restore: the active role of chromatin in the DNAdamage response. Mol. Cell, 46: 722-734.]Search in Google Scholar
[Talbert P.B., Ahmad K., Almouzni G., Ausio J., Berger F., Bhalla P.L., Bonner W.M., Cande W.Z., Chadwick B., Chan S.W.L., Cross G.A.M,, Cui L., Dimitrov S.I., Doenceke D., Eirin-Lopez J.M., Gorovsky M.A., Hake S.B., Hamkalo B.A., Holec S., Jacobsen S.E., Kamieniarz K., Kchohbin S., Ladurner A.G., Landsman D., Latham J.A., Loppin B., Malik H.S., Marzluff W.F., Pehrson J.R., Postberg J., Schneider R., Singh M.B., Smith M.M., Thompson E., Torres - Padilla M-E., Tremethick D.J., Turner B.M., Waterborg J.H., Wollmann H., Yelagandula R., Zhu B., Henikoff S. (2012). Aunified phylogeny-based nomenclature for histone variants. Epigenet. Chromatin, 5: 7. doi: 10.1186/1756-8935-5-7.]Search in Google Scholar
[Th’ng J.P., Sung R., Ye M., Hendzel M.J. (2005). H1 family histone in the nucleus. Control of binding and localization by the C-terminal domain. J. Biol. Chem., 280: 27809-27814.]Search in Google Scholar
[Yang S-M., Kim B.J., Norwood Toro L., Skoultchi A.I. (2013). H1 linker histone promotes epigenetic silencing by regulating both DNAmethylation and histone H3 methylation. Proc. Natl. Acad. Sci. USA, 110: 1708-1713.]Search in Google Scholar
[Zhang Y., Liu Z., Medrzycki M., Cao K., Fan Y. (2012). Reduction of Hox gene expression by histone H1 depletion. PLo S One, 7:e38829. doi: 10.1371/journal.pone.0038829. ]Search in Google Scholar