Alternative pre-mRNA splicing is an important element in eukaryotic gene expression, as most of the protein-coding genes use this process to generate multiple protein isoforms from a single gene. An increasing number of human diseases are now recognized to be caused by the selection of ‘wrong’ alternative exons. Research during the last few years identified a number of low–molecular-mass chemical substances that can change alternative exon usage. Most of these substances act by either blocking histone deacetylases or by interfering with the phosphorylation of splicing factors. How the remaining large number of these substances affect splicing is not yet fully understood. The emergence of these low-molecular-mass substances provides not only probes for studying alternative pre-mRNA splicing, but also opens the door to the possible harnessing of these compounds as drugs to control diseases caused by the selection of ‘wrong’ splice sites.
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June 2008
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Conference Article|
May 21 2008
Substances that can change alternative splice-site selection
Chiranthani Sumanasekera;
Chiranthani Sumanasekera
1Department of Molecular and Cellular Biochemistry, University of Kentucky, College of Medicine, B283, Biomedical Biological Sciences Research Building, 741 South Limestone, Lexington, KY 40536, U.S.A.
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David S. Watt;
David S. Watt
1Department of Molecular and Cellular Biochemistry, University of Kentucky, College of Medicine, B283, Biomedical Biological Sciences Research Building, 741 South Limestone, Lexington, KY 40536, U.S.A.
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Stefan Stamm
Stefan Stamm
1
1Department of Molecular and Cellular Biochemistry, University of Kentucky, College of Medicine, B283, Biomedical Biological Sciences Research Building, 741 South Limestone, Lexington, KY 40536, U.S.A.
1To whom correspondence should be addressed (email stefan@stamms-lab.net).
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Biochem Soc Trans (2008) 36 (3): 483–490.
Article history
Received:
January 08 2008
Citation
Chiranthani Sumanasekera, David S. Watt, Stefan Stamm; Substances that can change alternative splice-site selection. Biochem Soc Trans 1 June 2008; 36 (3): 483–490. doi: https://doi.org/10.1042/BST0360483
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