The Neurospora crassa CYT-18 protein C-terminal RNA-binding domain helps stabilize interdomain tertiary interactions in group I introns.
about
Evolution of RNA-protein interactions: non-specific binding led to RNA splicing activity of fungal mitochondrial tyrosyl-tRNA synthetasesToward predicting self-splicing and protein-facilitated splicing of group I introns.Structural Divergence of the Group I Intron Binding Surface in Fungal Mitochondrial Tyrosyl-tRNA Synthetases That Function in RNA Splicing.Protein-facilitated folding of group II intron ribozymes.NMR Structure of the C-terminal domain of a tyrosyl-tRNA synthetase that functions in group I intron splicingRNA chaperone activity and RNA-binding properties of the E. coli protein StpA.
P2860
The Neurospora crassa CYT-18 protein C-terminal RNA-binding domain helps stabilize interdomain tertiary interactions in group I introns.
description
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name
The Neurospora crassa CYT-18 p ...... teractions in group I introns.
@en
type
label
The Neurospora crassa CYT-18 p ...... teractions in group I introns.
@en
prefLabel
The Neurospora crassa CYT-18 p ...... teractions in group I introns.
@en
P2093
P2860
P356
P1433
P1476
The Neurospora crassa CYT-18 p ...... teractions in group I introns.
@en
P2093
Alan M Lambowitz
Georg Mohr
P2860
P304
P356
10.1261/RNA.5212604
P407
P577
2004-04-01T00:00:00Z