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Open Access Green as soon as Postprint is submitted to ZB.
Getting access to low-complexity domain modifications.
Trends Biochem. Sci. 41, 894-897 (2016)
Low-complexity (LC) domains regulate the aggregation and phase transition of proteins in a modification-dependent manner. The study of LC domain modifications has now become feasible, as shown by genetic variants of the carboxy-terminal domain (CTD) of RNA Polymerase II (Pol II) that provide access to the type and position of modifications of a LC domain by mass spectrometry (MS).
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2.923
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Rna-polymerase-ii; C-terminal Domain; Ctd; Fus; Phosphorylation; Protein
Language
english
Publication Year
2016
HGF-reported in Year
2016
ISSN (print) / ISBN
0376-5067
e-ISSN
0968-0004
Quellenangaben
Volume: 41,
Issue: 11,
Pages: 894-897
Publisher
Elsevier
Publishing Place
Cambridge
Reviewing status
Peer reviewed
Institute(s)
Institute of Functional Epigenetics (IFE)
POF-Topic(s)
30203 - Molecular Targets and Therapies
Research field(s)
Helmholtz Diabetes Center
PSP Element(s)
G-502890-001
PubMed ID
27283512
WOS ID
WOS:000387196300002
Scopus ID
84973140798
Erfassungsdatum
2016-06-13