TY - JOUR
T1 - Two introns define functional domains of a neuropeptide precursor in aplysia1
AU - Taussig, Ronald
AU - Picciotto, Marina R.
AU - Scheller, Richard H.
N1 - Funding Information:
This work is supported by grants t o Richard H. Scheller from the NIH, The March of Dimes, The McKnight Foundation and The Sloan Foundation.
PY - 1984
Y1 - 1984
N2 - Biologically active peptides are synthesized as parts of precursor proteins which are proteolytically processed to generate active molecules. The structure of the gene encoding peptides expressed in Aplysia neurons R3-14 suggests that two intervening sequences split the transcript into functional domains. The first exon encodes the 5' untranslated region, the second exon the signal sequence and the bulk of the negative charge of the precursor protein while the third exon encodes the remainder of the precursor and the 3' untranslated region.
AB - Biologically active peptides are synthesized as parts of precursor proteins which are proteolytically processed to generate active molecules. The structure of the gene encoding peptides expressed in Aplysia neurons R3-14 suggests that two intervening sequences split the transcript into functional domains. The first exon encodes the 5' untranslated region, the second exon the signal sequence and the bulk of the negative charge of the precursor protein while the third exon encodes the remainder of the precursor and the 3' untranslated region.
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U2 - 10.3109/10641968409046142
DO - 10.3109/10641968409046142
M3 - Article
C2 - 6532597
AN - SCOPUS:0021670073
SN - 1064-1963
VL - 6
SP - 2133
EP - 2140
JO - Clinical and Experimental Hypertension
JF - Clinical and Experimental Hypertension
IS - 10-11
ER -