About: The docking domain of histone H2A is required for H1 binding and RSC-mediated nucleosome remodeling

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About: The docking domain of histone H2A is required for H1 binding and RSC-mediated nucleosome remodeling Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
rdfs:seeAlso	http://dx.doi.org/10.1093/nar/gkq1174
Description	Using biochemical methods in combination with Atomic Force Microscopy and Electron Cryo-Microscopy, we show that the H2A-docking domain is a key structural feature within the nucleosome. Using biochemical methods in combination with Atomic Force Microscopy and Electron Cryo-Microscopy, we show that the H2A-docking domain is a key structural feature within the nucleosome. (en)
Title	The docking domain of histone H2A is required for H1 binding and RSC-mediated nucleosome remodeling The docking domain of histone H2A is required for H1 binding and RSC-mediated nucleosome remodeling (en)
skos:prefLabel	The docking domain of histone H2A is required for H1 binding and RSC-mediated nucleosome remodeling The docking domain of histone H2A is required for H1 binding and RSC-mediated nucleosome remodeling (en)
skos:notation	RIV/00216208:11110/11:10469!RIV12-GA0-11110___
http://linked.open...avai/predkladatel	1. lékařská fakulta
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(GA304/05/2168), P(LC535), Z(MSM0021620806)
http://linked.open...iv/cisloPeriodika	7
http://linked.open...vai/riv/dodaniDat	2012
http://linked.open...aciTvurceVysledku	Bednár, Ján
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Univerzita Karlova v Praze / 1. lékařská fakulta
http://linked.open...dnocenehoVysledku	195174
http://linked.open...ai/riv/idVysledku	RIV/00216208:11110/11:10469
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	chromatin; nucleosome; transcription factor; core particle; DNA (en)
http://linked.open.../riv/klicoveSlovo	DNA chromatin nucleosome core particle transcription factor
http://linked.open...odStatuVydavatele	GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV	[1DB36BC8156C]
http://linked.open...i/riv/nazevZdroje	Nucleic Acids Research
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	1 (xsd:int)
http://linked.open...cetTvurcuVysledku	12 (xsd:int)
http://linked.open...vavai/riv/projekt	Chromosome dynamics and organization during the cell cycle in normal and pathologic conditions Determination of the histone H5 globular domain position within the native nucleosome using cryo-electron microscopy and single particle reconstruction.
http://linked.open...UplatneniVysledku	2011
http://linked.open...v/svazekPeriodika	39
http://linked.open...iv/tvurceVysledku	Bednár, Ján Faivre-Moskalenko, C. Goutte-Gattat, Damien Hamiche, Ali Montel, Fabien Richard, John L. C. Shukla, Manu S. Syed, Sajad H. Travers, Andrew
http://linked.open...ain/vavai/riv/wos	000289628400015
http://linked.open...n/vavai/riv/zamer	Molekulární biologie a patologie buňky za normy a u vybraných klinicky závažných patologických procesů
issn	0305-1048
number of pages	12 (xsd:int)
http://localhost/t...ganizacniJednotka	11110
is http://linked.open...avai/riv/vysledek of	The docking domain of histone H2A is required for H1 binding and RSC-mediated nucleosome remodeling The docking domain of histone H2A is required for H1 binding and RSC-mediated nucleosome remodeling

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