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Getting Access to Low-Complexity Domain Modifications.
- Source :
-
Trends in biochemical sciences [Trends Biochem Sci] 2016 Nov; Vol. 41 (11), pp. 894-897. Date of Electronic Publication: 2016 Jun 06. - Publication Year :
- 2016
-
Abstract
- 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).<br /> (Copyright © 2016 Elsevier Ltd. All rights reserved.)
- Subjects :
- Amino Acid Sequence
Animals
Calmodulin-Binding Proteins genetics
Chickens
Gene Expression
Humans
Mice
Mutation
Protein Domains
RNA Polymerase II genetics
RNA-Binding Protein EWS
RNA-Binding Protein FUS genetics
RNA-Binding Proteins genetics
Sequence Alignment
Sequence Homology, Amino Acid
TATA-Binding Protein Associated Factors genetics
Transcription, Genetic
Amino Acid Substitution
Calmodulin-Binding Proteins chemistry
RNA Polymerase II chemistry
RNA-Binding Protein FUS chemistry
RNA-Binding Proteins chemistry
TATA-Binding Protein Associated Factors chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0968-0004
- Volume :
- 41
- Issue :
- 11
- Database :
- MEDLINE
- Journal :
- Trends in biochemical sciences
- Publication Type :
- Academic Journal
- Accession number :
- 27283512
- Full Text :
- https://doi.org/10.1016/j.tibs.2016.05.010