@article {128,
	title = {Autoproteolysis in hedgehog protein biogenesis.},
	journal = {Science (New York, N.Y.)},
	volume = {266},
	year = {1994},
	month = {1994 Dec 2},
	pages = {1528-37},
	abstract = {Extracellular signaling proteins encoded by the hedgehog (hh) multigene family are responsible for the patterning of a variety of embryonic structures in vertebrates and invertebrates. The Drosophila hh gene has now been shown to generate two predominant protein species that are derived by an internal autoproteolytic cleavage of a larger precursor. Mutations that reduced the efficiency of autoproteolysis in vitro diminished precursor cleavage in vivo and also impaired the signaling and patterning activities of the HH protein. The two HH protein species exhibited distinctive biochemical properties and tissue distribution, and these differences suggest a mechanism that could account for the long- and short-range signaling activities of HH in vivo.},
	keywords = {Amino Acid Sequence, Animals, Cell Line, Drosophila, Drosophila Proteins, Embryo, Nonmammalian, Embryonic Induction, Gene Expression Regulation, Developmental, Genes, Insect, Hedgehog Proteins, Models, Biological, Molecular Sequence Data, Mutation, Protein Precursors, Protein Processing, Post-Translational, Proteins, Serine Endopeptidases, Signal Transduction},
	issn = {0036-8075},
	author = {Lee, J J and Ekker, S C and von Kessler, D P and Porter, J A and Sun, B I and Beachy, P A}
}
