The Effect of Oncomutations and Posttranslational Modifications of Histone H1 on Chromatosome Structure and Stability

Abstract— The stability of chromatosome when introducing posttranslational modifications and mutations observed in the case of oncological diseases into the structure of the linker histone was studied using bioinformatics analysis. The chromatosome is formed under the interaction of the nucleosome w...
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Gespeichert in:

Autor*in:	Bass, M. V. [verfasserIn] Armeev, G. A. [verfasserIn] Shaitan, K. V. [verfasserIn] Shaytan, A. K. [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2019

Übergeordnetes Werk:	Enthalten in: Moscow University biological sciences bulletin - New York, NY : Allerton Press, 2007, 74(2019), 3 vom: Juli, Seite 121-126
Übergeordnetes Werk:	volume:74 ; year:2019 ; number:3 ; month:07 ; pages:121-126

Links:	Volltext

DOI / URN:	10.3103/S0096392519030015

Katalog-ID:	SPR023274514

Internformat


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520			\|a Abstract— The stability of chromatosome when introducing posttranslational modifications and mutations observed in the case of oncological diseases into the structure of the linker histone was studied using bioinformatics analysis. The chromatosome is formed under the interaction of the nucleosome with the linker histone. This interaction can be characterized by the binding free energy. We hypothesized that oncomutations and posttranslational modifications of the linker histone are associated with a change in its free energy of binding to the nucleosome, and it probably leads to a change in chromatin compaction, thus affecting gene expression. Calculations of the binding free energy were performed using algorithms of the FoldX program. Screening of positions of posttranslational modifications in the linker histone for the presence of steric constraints was also performed. The analysis of the obtained data allowed for the identification of oncomutations and posttranslational modifications that significantly change the binding free energy of the linker histone with the nucleosome, thereby probably affecting the structure of the entire chromatin.
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700	1		\|a Shaytan, A. K. \|e verfasserin \|4 aut
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912			\|a GBV_ILN_62
912			\|a GBV_ILN_63
912			\|a GBV_ILN_65
912			\|a GBV_ILN_69
912			\|a GBV_ILN_70
912			\|a GBV_ILN_73
912			\|a GBV_ILN_74
912			\|a GBV_ILN_90
912			\|a GBV_ILN_95
912			\|a GBV_ILN_100
912			\|a GBV_ILN_101
912			\|a GBV_ILN_105
912			\|a GBV_ILN_110
912			\|a GBV_ILN_120
912			\|a GBV_ILN_138
912			\|a GBV_ILN_150
912			\|a GBV_ILN_151
912			\|a GBV_ILN_161
912			\|a GBV_ILN_170
912			\|a GBV_ILN_171
912			\|a GBV_ILN_187
912			\|a GBV_ILN_213
912			\|a GBV_ILN_224
912			\|a GBV_ILN_230
912			\|a GBV_ILN_250
912			\|a GBV_ILN_281
912			\|a GBV_ILN_285
912			\|a GBV_ILN_293
912			\|a GBV_ILN_370
912			\|a GBV_ILN_602
912			\|a GBV_ILN_636
912			\|a GBV_ILN_702
912			\|a GBV_ILN_2001
912			\|a GBV_ILN_2003
912			\|a GBV_ILN_2004
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912			\|a GBV_ILN_2006
912			\|a GBV_ILN_2007
912			\|a GBV_ILN_2008
912			\|a GBV_ILN_2009
912			\|a GBV_ILN_2010
912			\|a GBV_ILN_2011
912			\|a GBV_ILN_2014
912			\|a GBV_ILN_2015
912			\|a GBV_ILN_2020
912			\|a GBV_ILN_2021
912			\|a GBV_ILN_2025
912			\|a GBV_ILN_2026
912			\|a GBV_ILN_2027
912			\|a GBV_ILN_2031
912			\|a GBV_ILN_2034
912			\|a GBV_ILN_2037
912			\|a GBV_ILN_2038
912			\|a GBV_ILN_2039
912			\|a GBV_ILN_2044
912			\|a GBV_ILN_2048
912			\|a GBV_ILN_2049
912			\|a GBV_ILN_2050
912			\|a GBV_ILN_2055
912			\|a GBV_ILN_2057
912			\|a GBV_ILN_2059
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2064
912			\|a GBV_ILN_2065
912			\|a GBV_ILN_2068
912			\|a GBV_ILN_2070
912			\|a GBV_ILN_2086
912			\|a GBV_ILN_2088
912			\|a GBV_ILN_2093
912			\|a GBV_ILN_2106
912			\|a GBV_ILN_2107
912			\|a GBV_ILN_2108
912			\|a GBV_ILN_2110
912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2112
912			\|a GBV_ILN_2113
912			\|a GBV_ILN_2116
912			\|a GBV_ILN_2118
912			\|a GBV_ILN_2119
912			\|a GBV_ILN_2122
912			\|a GBV_ILN_2129
912			\|a GBV_ILN_2143
912			\|a GBV_ILN_2144
912			\|a GBV_ILN_2147
912			\|a GBV_ILN_2148
912			\|a GBV_ILN_2152
912			\|a GBV_ILN_2153
912			\|a GBV_ILN_2188
912			\|a GBV_ILN_2190
912			\|a GBV_ILN_2232
912			\|a GBV_ILN_2336
912			\|a GBV_ILN_2446
912			\|a GBV_ILN_2470
912			\|a GBV_ILN_2472
912			\|a GBV_ILN_2507
912			\|a GBV_ILN_2522
912			\|a GBV_ILN_2548
912			\|a GBV_ILN_4035
912			\|a GBV_ILN_4037
912			\|a GBV_ILN_4046
912			\|a GBV_ILN_4112
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4242
912			\|a GBV_ILN_4246
912			\|a GBV_ILN_4249
912			\|a GBV_ILN_4251
912			\|a GBV_ILN_4305
912			\|a GBV_ILN_4306
912			\|a GBV_ILN_4307
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912			\|a GBV_ILN_4322
912			\|a GBV_ILN_4323
912			\|a GBV_ILN_4324
912			\|a GBV_ILN_4325
912			\|a GBV_ILN_4326
912			\|a GBV_ILN_4333
912			\|a GBV_ILN_4334
912			\|a GBV_ILN_4335
912			\|a GBV_ILN_4336
912			\|a GBV_ILN_4338
912			\|a GBV_ILN_4393
912			\|a GBV_ILN_4700
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952			\|d 74 \|j 2019 \|e 3 \|c 07 \|h 121-126

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allfields	10.3103/S0096392519030015 doi (DE-627)SPR023274514 (SPR)S0096392519030015-e DE-627 ger DE-627 rakwb eng 570 370 ASE Bass, M. V. verfasserin aut The Effect of Oncomutations and Posttranslational Modifications of Histone H1 on Chromatosome Structure and Stability 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract— The stability of chromatosome when introducing posttranslational modifications and mutations observed in the case of oncological diseases into the structure of the linker histone was studied using bioinformatics analysis. The chromatosome is formed under the interaction of the nucleosome with the linker histone. This interaction can be characterized by the binding free energy. We hypothesized that oncomutations and posttranslational modifications of the linker histone are associated with a change in its free energy of binding to the nucleosome, and it probably leads to a change in chromatin compaction, thus affecting gene expression. Calculations of the binding free energy were performed using algorithms of the FoldX program. Screening of positions of posttranslational modifications in the linker histone for the presence of steric constraints was also performed. The analysis of the obtained data allowed for the identification of oncomutations and posttranslational modifications that significantly change the binding free energy of the linker histone with the nucleosome, thereby probably affecting the structure of the entire chromatin. Armeev, G. A. verfasserin aut Shaitan, K. V. verfasserin aut Shaytan, A. K. verfasserin aut Enthalten in Moscow University biological sciences bulletin New York, NY : Allerton Press, 2007 74(2019), 3 vom: Juli, Seite 121-126 (DE-627)532695607 (DE-600)2325902-4 1934-791X nnns volume:74 year:2019 number:3 month:07 pages:121-126 https://dx.doi.org/10.3103/S0096392519030015 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 74 2019 3 07 121-126
spelling	10.3103/S0096392519030015 doi (DE-627)SPR023274514 (SPR)S0096392519030015-e DE-627 ger DE-627 rakwb eng 570 370 ASE Bass, M. V. verfasserin aut The Effect of Oncomutations and Posttranslational Modifications of Histone H1 on Chromatosome Structure and Stability 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract— The stability of chromatosome when introducing posttranslational modifications and mutations observed in the case of oncological diseases into the structure of the linker histone was studied using bioinformatics analysis. The chromatosome is formed under the interaction of the nucleosome with the linker histone. This interaction can be characterized by the binding free energy. We hypothesized that oncomutations and posttranslational modifications of the linker histone are associated with a change in its free energy of binding to the nucleosome, and it probably leads to a change in chromatin compaction, thus affecting gene expression. Calculations of the binding free energy were performed using algorithms of the FoldX program. Screening of positions of posttranslational modifications in the linker histone for the presence of steric constraints was also performed. The analysis of the obtained data allowed for the identification of oncomutations and posttranslational modifications that significantly change the binding free energy of the linker histone with the nucleosome, thereby probably affecting the structure of the entire chromatin. Armeev, G. A. verfasserin aut Shaitan, K. V. verfasserin aut Shaytan, A. K. verfasserin aut Enthalten in Moscow University biological sciences bulletin New York, NY : Allerton Press, 2007 74(2019), 3 vom: Juli, Seite 121-126 (DE-627)532695607 (DE-600)2325902-4 1934-791X nnns volume:74 year:2019 number:3 month:07 pages:121-126 https://dx.doi.org/10.3103/S0096392519030015 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 74 2019 3 07 121-126
allfields_unstemmed	10.3103/S0096392519030015 doi (DE-627)SPR023274514 (SPR)S0096392519030015-e DE-627 ger DE-627 rakwb eng 570 370 ASE Bass, M. V. verfasserin aut The Effect of Oncomutations and Posttranslational Modifications of Histone H1 on Chromatosome Structure and Stability 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract— The stability of chromatosome when introducing posttranslational modifications and mutations observed in the case of oncological diseases into the structure of the linker histone was studied using bioinformatics analysis. The chromatosome is formed under the interaction of the nucleosome with the linker histone. This interaction can be characterized by the binding free energy. We hypothesized that oncomutations and posttranslational modifications of the linker histone are associated with a change in its free energy of binding to the nucleosome, and it probably leads to a change in chromatin compaction, thus affecting gene expression. Calculations of the binding free energy were performed using algorithms of the FoldX program. Screening of positions of posttranslational modifications in the linker histone for the presence of steric constraints was also performed. The analysis of the obtained data allowed for the identification of oncomutations and posttranslational modifications that significantly change the binding free energy of the linker histone with the nucleosome, thereby probably affecting the structure of the entire chromatin. Armeev, G. A. verfasserin aut Shaitan, K. V. verfasserin aut Shaytan, A. K. verfasserin aut Enthalten in Moscow University biological sciences bulletin New York, NY : Allerton Press, 2007 74(2019), 3 vom: Juli, Seite 121-126 (DE-627)532695607 (DE-600)2325902-4 1934-791X nnns volume:74 year:2019 number:3 month:07 pages:121-126 https://dx.doi.org/10.3103/S0096392519030015 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 74 2019 3 07 121-126
allfieldsGer	10.3103/S0096392519030015 doi (DE-627)SPR023274514 (SPR)S0096392519030015-e DE-627 ger DE-627 rakwb eng 570 370 ASE Bass, M. V. verfasserin aut The Effect of Oncomutations and Posttranslational Modifications of Histone H1 on Chromatosome Structure and Stability 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract— The stability of chromatosome when introducing posttranslational modifications and mutations observed in the case of oncological diseases into the structure of the linker histone was studied using bioinformatics analysis. The chromatosome is formed under the interaction of the nucleosome with the linker histone. This interaction can be characterized by the binding free energy. We hypothesized that oncomutations and posttranslational modifications of the linker histone are associated with a change in its free energy of binding to the nucleosome, and it probably leads to a change in chromatin compaction, thus affecting gene expression. Calculations of the binding free energy were performed using algorithms of the FoldX program. Screening of positions of posttranslational modifications in the linker histone for the presence of steric constraints was also performed. The analysis of the obtained data allowed for the identification of oncomutations and posttranslational modifications that significantly change the binding free energy of the linker histone with the nucleosome, thereby probably affecting the structure of the entire chromatin. Armeev, G. A. verfasserin aut Shaitan, K. V. verfasserin aut Shaytan, A. K. verfasserin aut Enthalten in Moscow University biological sciences bulletin New York, NY : Allerton Press, 2007 74(2019), 3 vom: Juli, Seite 121-126 (DE-627)532695607 (DE-600)2325902-4 1934-791X nnns volume:74 year:2019 number:3 month:07 pages:121-126 https://dx.doi.org/10.3103/S0096392519030015 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 74 2019 3 07 121-126
allfieldsSound	10.3103/S0096392519030015 doi (DE-627)SPR023274514 (SPR)S0096392519030015-e DE-627 ger DE-627 rakwb eng 570 370 ASE Bass, M. V. verfasserin aut The Effect of Oncomutations and Posttranslational Modifications of Histone H1 on Chromatosome Structure and Stability 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract— The stability of chromatosome when introducing posttranslational modifications and mutations observed in the case of oncological diseases into the structure of the linker histone was studied using bioinformatics analysis. The chromatosome is formed under the interaction of the nucleosome with the linker histone. This interaction can be characterized by the binding free energy. We hypothesized that oncomutations and posttranslational modifications of the linker histone are associated with a change in its free energy of binding to the nucleosome, and it probably leads to a change in chromatin compaction, thus affecting gene expression. Calculations of the binding free energy were performed using algorithms of the FoldX program. Screening of positions of posttranslational modifications in the linker histone for the presence of steric constraints was also performed. The analysis of the obtained data allowed for the identification of oncomutations and posttranslational modifications that significantly change the binding free energy of the linker histone with the nucleosome, thereby probably affecting the structure of the entire chromatin. Armeev, G. A. verfasserin aut Shaitan, K. V. verfasserin aut Shaytan, A. K. verfasserin aut Enthalten in Moscow University biological sciences bulletin New York, NY : Allerton Press, 2007 74(2019), 3 vom: Juli, Seite 121-126 (DE-627)532695607 (DE-600)2325902-4 1934-791X nnns volume:74 year:2019 number:3 month:07 pages:121-126 https://dx.doi.org/10.3103/S0096392519030015 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 74 2019 3 07 121-126
language	English
source	Enthalten in Moscow University biological sciences bulletin 74(2019), 3 vom: Juli, Seite 121-126 volume:74 year:2019 number:3 month:07 pages:121-126
sourceStr	Enthalten in Moscow University biological sciences bulletin 74(2019), 3 vom: Juli, Seite 121-126 volume:74 year:2019 number:3 month:07 pages:121-126
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container_title	Moscow University biological sciences bulletin
authorswithroles_txt_mv	Bass, M. V. @@aut@@ Armeev, G. A. @@aut@@ Shaitan, K. V. @@aut@@ Shaytan, A. K. @@aut@@
publishDateDaySort_date	2019-07-01T00:00:00Z
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author	Bass, M. V.
spellingShingle	Bass, M. V. ddc 570 The Effect of Oncomutations and Posttranslational Modifications of Histone H1 on Chromatosome Structure and Stability
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topic_title	570 370 ASE The Effect of Oncomutations and Posttranslational Modifications of Histone H1 on Chromatosome Structure and Stability
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title	The Effect of Oncomutations and Posttranslational Modifications of Histone H1 on Chromatosome Structure and Stability
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title_full	The Effect of Oncomutations and Posttranslational Modifications of Histone H1 on Chromatosome Structure and Stability
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author_browse	Bass, M. V. Armeev, G. A. Shaitan, K. V. Shaytan, A. K.
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title_sort	effect of oncomutations and posttranslational modifications of histone h1 on chromatosome structure and stability
title_auth	The Effect of Oncomutations and Posttranslational Modifications of Histone H1 on Chromatosome Structure and Stability
abstract	Abstract— The stability of chromatosome when introducing posttranslational modifications and mutations observed in the case of oncological diseases into the structure of the linker histone was studied using bioinformatics analysis. The chromatosome is formed under the interaction of the nucleosome with the linker histone. This interaction can be characterized by the binding free energy. We hypothesized that oncomutations and posttranslational modifications of the linker histone are associated with a change in its free energy of binding to the nucleosome, and it probably leads to a change in chromatin compaction, thus affecting gene expression. Calculations of the binding free energy were performed using algorithms of the FoldX program. Screening of positions of posttranslational modifications in the linker histone for the presence of steric constraints was also performed. The analysis of the obtained data allowed for the identification of oncomutations and posttranslational modifications that significantly change the binding free energy of the linker histone with the nucleosome, thereby probably affecting the structure of the entire chromatin.
abstractGer	Abstract— The stability of chromatosome when introducing posttranslational modifications and mutations observed in the case of oncological diseases into the structure of the linker histone was studied using bioinformatics analysis. The chromatosome is formed under the interaction of the nucleosome with the linker histone. This interaction can be characterized by the binding free energy. We hypothesized that oncomutations and posttranslational modifications of the linker histone are associated with a change in its free energy of binding to the nucleosome, and it probably leads to a change in chromatin compaction, thus affecting gene expression. Calculations of the binding free energy were performed using algorithms of the FoldX program. Screening of positions of posttranslational modifications in the linker histone for the presence of steric constraints was also performed. The analysis of the obtained data allowed for the identification of oncomutations and posttranslational modifications that significantly change the binding free energy of the linker histone with the nucleosome, thereby probably affecting the structure of the entire chromatin.
abstract_unstemmed	Abstract— The stability of chromatosome when introducing posttranslational modifications and mutations observed in the case of oncological diseases into the structure of the linker histone was studied using bioinformatics analysis. The chromatosome is formed under the interaction of the nucleosome with the linker histone. This interaction can be characterized by the binding free energy. We hypothesized that oncomutations and posttranslational modifications of the linker histone are associated with a change in its free energy of binding to the nucleosome, and it probably leads to a change in chromatin compaction, thus affecting gene expression. Calculations of the binding free energy were performed using algorithms of the FoldX program. Screening of positions of posttranslational modifications in the linker histone for the presence of steric constraints was also performed. The analysis of the obtained data allowed for the identification of oncomutations and posttranslational modifications that significantly change the binding free energy of the linker histone with the nucleosome, thereby probably affecting the structure of the entire chromatin.
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title_short	The Effect of Oncomutations and Posttranslational Modifications of Histone H1 on Chromatosome Structure and Stability
url	https://dx.doi.org/10.3103/S0096392519030015
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author2	Armeev, G. A. Shaitan, K. V. Shaytan, A. K.
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up_date	2024-07-03T17:56:48.182Z
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V.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="4"><subfield code="a">The Effect of Oncomutations and Posttranslational Modifications of Histone H1 on Chromatosome Structure and Stability</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2019</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract— The stability of chromatosome when introducing posttranslational modifications and mutations observed in the case of oncological diseases into the structure of the linker histone was studied using bioinformatics analysis. 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The Effect of Oncomutations and Posttranslational Modifications of Histone H1 on Chromatosome Structure and Stability

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