Digitale Medien
[s.l.]
:
Nature Publishing Group
Nature structural & molecular biology
14 (2007), S. 252-254
ISSN:
1545-9985
Quelle:
Nature Archives 1869 - 2009
Thema:
Biologie
,
Medizin
Notizen:
[Auszug] The N-terminal tails of histones are subject to a plethora of post-translational modifications, such as acetylation, phosphorylation, ubiquitination and methylation, by specific chromatin-modifying enzymes. Lysine residues in histone tails can be mono-, di- or trimethylated. The differentially ...
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1038/nsmb0407-252
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