@article {651,
	title = {A peptide from insects protects transgenic tobacco from a parasitic weed},
	volume = {14},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalVirginia Tech, Department of Plant Pathology, Phlysiology, and Weed Science, Blacksburg VA 24061, USA.enghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=16145831},
	pages = {227 - 236},
	abstract = {Parasitic plants present some of the most intractable weed problems for agriculture in much of the world. Species of root parasites such as Orobanche can cause enormous yield losses, yet few control measures are effective and affordable. An ideal solution to this problem is the development of parasite-resistant crops, but this goal has been elusive for most susceptible crops. Here we report a mechanism for resistance to the parasitic angiosperm Orobanche based on expression of sarcotoxin IA in transgenic tobacco. Sarcotoxin IA is a 40-residue peptide with antibiotic activity, originally isolated from the fly, Sarcophaga peregrina. The sarcotoxin IA gene was fused to an Orobanche-inducible promoter, HMG2, which is induced locally in the host root at the point of contact with the parasite, and used to transform tobacco. The resulting transgenic plants accumulated more biomass than non-transformed plants in the presence of parasites. Furthermore, plants expressing sarcotoxin IA showed enhanced resistance to O. aegyptiaca as evidenced by abnormal parasite development and higher parasite mortality after attachment as compared to non-transformed plants. The transgenic plants were similar in appearance to non-transformed plants suggesting that sarcotoxin IA is not detrimental to the host.},
	keywords = {*Plant Diseases, Animals, Diptera/genetics, HMGB2 Protein/genetics, Insect Proteins/*genetics/metabolism, Orobanche/*physiology, Plants, Genetically Modified, Promoter Regions, Genetic, Tobacco/*genetics/metabolism, Transfection},
	author = {Hamamouch, N. and Westwood, J. H. and Banner, I. and Cramer, C. L. and Gepstein, S. and Aly, R.}
}
@article {282,
	title = {Neuropeptide-like precursor 4 is uniquely expressed during pupal diapause in the flesh fly},
	volume = {30},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalDepartment of Entomology, Ohio State University, Columbus, OH 43210, USA.enghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=19007830},
	pages = {518 - 521},
	abstract = {Suppression subtractive hybridization comparing brains from diapausing and nondiapausing pupae of the flesh fly, Sarcophaga crassipalpis, suggested that the gene encoding neuropeptide-like precursor 4 (Nplp4) was uniquely expressed during diapause. We have sequenced the full-length cDNA encoding Nplp4 and used Northern blots to further evaluate linkage to diapause. The open reading frame of this cDNA encodes a 61-amino acid residue precursor protein containing a predicted 18 residue signal peptide, one 22-amino acid and one 2-amino acid propeptides, and a 19-amino acid neuropeptide. The amino acid sequence of the precursor protein shows 64\% identity to Drosophila melanogaster Nplp4; homologues of this precursor protein are not known from species other than these two flies. Nplp4 mRNA levels were quite low in nondiapausing (long day) pupae, but in contrast the gene was highly upregulated in diapausing (short day) pupae. Expression increased at the onset of diapause, remained high throughout diapause, and then decreased 2 days after diapause was terminated. Although the function of this precursor protein and the neuropeptide it yields remain unknown, this close association with diapause suggests a potential role for Nplp4 in initiating and maintaining diapause in the flesh fly.},
	keywords = {Amino Acid Sequence, Animals, Diptera/genetics, Gene Expression Regulation, Developmental, Molecular Sequence Data, Neuropeptides/*genetics, Protein Precursors/*genetics, Pupa/metabolism, Sequence Alignment},
	author = {Li, A. and Rinehart, J. P. and Denlinger, D. L.}
}
