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Getting access to low-complexity domain modifications.

Trends Biochem. Sci. 41, 894-897 (2016)
Open Access Green as soon as Postprint is submitted to ZB.
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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Publication type Article: Journal article
Document type Scientific Article
Keywords Rna-polymerase-ii; C-terminal Domain; Ctd; Fus; Phosphorylation; Protein
ISSN (print) / ISBN 0376-5067
e-ISSN 0968-0004
Quellenangaben Volume: 41, Issue: 11, Pages: 894-897 Article Number: , Supplement: ,
Publisher Elsevier
Publishing Place Cambridge
Reviewing status Peer reviewed