SwePub
Sök i SwePub databas

  Extended search

Träfflista för sökning "WFRF:(Ayoub Nabieh) "

Search: WFRF:(Ayoub Nabieh)

  • Result 1-1 of 1
Sort/group result
   
EnumerationReferenceCoverFind
1.
  • Zoabi, Muhammad, et al. (author)
  • RNA-dependent chromatin localization of KDM4D lysine demethylase promotes H3K9me3 demethylation
  • 2014
  • In: Nucleic Acids Research. - : Oxford University Press (OUP). - 0305-1048 .- 1362-4962. ; 42:21, s. 13026-13038
  • Journal article (peer-reviewed)abstract
    • The JmjC-containing lysine demethylase, KDM4D, demethylates di-and tri-methylation of histone H3 on lysine 9 (H3K9me3). How KDM4D is recruited to chromatin and recognizes its histone substrates remains unknown. Here, we show that KDM4D binds RNA independently of its demethylase activity. We mapped two non-canonical RNA binding domains: the first is within the N-terminal spanning amino acids 115 to 236, and the second is within the C-terminal spanning amino acids 348 to 523 of KDM4D. We also demonstrate that RNA interactions with KDM4D N-terminal region are critical for its association with chromatin and subsequently for demethylating H3K9me3 in cells. This study implicates, for the first time, RNA molecules in regulating the levels of H3K9 methylation by affecting KDM4D association with chromatin.
  •  
Skapa referenser, mejla, bekava och länka
  • Result 1-1 of 1
Type of publication
journal article (1)
Type of content
peer-reviewed (1)
Author/Editor
Henn, Arnon (1)
Ušaj, Marko (1)
Zoabi, Muhammad (1)
Nadar-Ponniah, Prath ... (1)
Khoury-Haddad, Hanan (1)
Budowski-Tal, Inbal (1)
show more...
Haran, Tali (1)
Mandel-Gutfreund, Ya ... (1)
Ayoub, Nabieh (1)
show less...
University
Linnaeus University (1)
Language
English (1)
Research subject (UKÄ/SCB)
Natural sciences (1)
Year
2014 (1)

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Close

Copy and save the link in order to return to this view