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Science 29 July 1994: Vol. 265. no. 5172, pp. 615 - 621 DOI: 10.1126/science.8036511
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Articles
Science, Vol 265, Issue 5172, 615-621
Copyright © 1994 by American Association for the Advancement of Science
Conserved structures and diversity of functions of RNA-binding proteins
CG Burd
and
G Dreyfuss
Howard Hughes Medical Institute, University of Pennsylvania School of Medicine, Philadelphia 19104-6148.
In eukaryotic cells, a multitude of RNA-binding proteins play key roles in the posttranscriptional regulation of gene expression. Characterization of these proteins has led to the identification of several RNA-binding motifs, and recent experiments have begun to illustrate how several of them bind RNA. The significance of these interactions is reflected in the recent discoveries that several human and other vertebrate genetic disorders are caused by aberrant expression of RNA-binding proteins. The major RNA-binding motifs are described and examples of how they may function are given.
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- Crystal structure of the phosphorolytic exoribonuclease RNase PH from Bacillus subtilis and implications for its quaternary structure and tRNA binding.
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Protein Sci.
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- ETR-3 and CELF4 protein domains required for RNA binding and splicing activity in vivo.
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- XSEB4R, a novel RNA-binding protein involved in retinal cell differentiation downstream of bHLH proneural genes.
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Development
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- The Yeast RNA-binding Protein Rbp1p Modifies the Stability of Mitochondrial Porin mRNA.
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- A Novel Set of Nuclear Localization Signals Determine Distributions of the {alpha}CP RNA-Binding Proteins.
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