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Description
  • Chromatin appears to be ramarkably resistant to physical perturbation and inhospitable to molecular machines that use it as a substrate for transcription, replication, recombination, DNA repair and chromosome segregation. All of these processes are associated with chromatin remodeling increasing DNA accessibility to DNA-binding proteins. Several mechanisms have been identified that modelate chromatine structure: ATP-dependent chromatin remodeling complexes which work as machines to physically dissociate the DNA from histones and complex enzyme machinery chemically modifying histones. Histone post-translation modofications include acetylation, phosphorylation, methylation and ubiquitination, which usually take place on the tail domains of histones. Hisone modifications may alter chromatine structure by affecting histone-DNA interactions or may represent specific histone language - a %22histone code%22 - encoded on the histone tail domains and read by other proteins or protein complexes. Chromatin remodeli (en)
  • Chromatin je substrátem pro buněčné systémy zajišťující transkripci, replikaci, rekombinaci, reparaci DNA a segregaci chromozómů. Průběh těchto procesů závisí na přestavbách chromatinu, při kterých se zvyšuje přístupnost DNA pro určité proteiny. Přestavby chromatinu probíhají různými mechanismy, jejichž podstata je předmětem tohoto souborného článku.
Title
  • Mechanisms of chromatin remodeling (en)
  • Mechanismy přestavby chromatinu
  • Mechanismy přestavby chromatinu (cs)
skos:prefLabel
  • Mechanisms of chromatin remodeling (en)
  • Mechanismy přestavby chromatinu
  • Mechanismy přestavby chromatinu (cs)
skos:notation
  • RIV/00216224:14310/01:00005617!RIV/2002/MSM/143102/N
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  • 283
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  • Z(MSM 143100008), Z(MZ00020980501)
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  • 686357
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  • RIV/00216224:14310/01:00005617
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  • Mechanisms of chromatin remodeling (en)
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  • CZ - Česká republika
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  • [E408B7109B3B]
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  • 66
http://linked.open...iv/tvurceVysledku
  • Šmarda, Jan
  • Šmardová, Jana
http://linked.open...n/vavai/riv/zamer
issn
  • 0366-0486
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  • 14310
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