@article {BirzCsaba08,
	title = {{Alternative splicing and protein structure evolution}},
	journal = {Nucleic Acids Res.},
	volume = {36},
	year = {2008},
	month = {Feb},
	pages = {550{\textendash}558},
	abstract = {Alternative splicing is thought to be one of the major sources for
functional diversity in higher eukaryotes. Interestingly, when mapping splicing
events onto protein structures, about half of the events affect structured and
even highly conserved regions i.e. are non-trivial on the structure level. This
has led to the controversial hypothesis that such splice variants result in
nonsense-mediated mRNA decay or non-functional, unstructured proteins, which do
not contribute to the functional diversity of an organism. Here we show in a
comprehensive study on alternative splicing that proteins appear to be much more
tolerant to structural deletions, insertions and replacements than previously
thought. We find literature evidence that such non-trivial splicing isoforms
exhibit different functional properties compared to their native counterparts and
allow for interesting regulatory patterns on the protein network level. We
provide examples that splicing events may represent transitions between different
folds in the protein sequence-structure space and explain these links by a common
genetic mechanism. Taken together, those findings hint to a more prominent role
of splicing in protein structure evolution and to a different view of phenotypic
plasticity of protein structures.},
	keywords = {alternativ_splicing_gallery, birzele-csaba-zimmer-08, the-prosas-database},
	doi = {10.1093/nar/gkm1054},
	author = {Fabian Birzele and Gergely Csaba and Ralf Zimmer}
}