@article {363,
	title = {Diapause hormone in the corn earworm, Helicoverpa zea: optimum temperature for activity, structure-activity relationships, and efficacy in accelerating flesh fly pupariation},
	volume = {29},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalDepartment of Entomology, Ohio State University, 318 West 12th Avenue, Columbus, OH 43210, USA.enghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=18206265},
	pages = {196 - 205},
	abstract = {Diapause hormone (DH) effectively terminated pupal diapause in Helicoverpa zea. This effect was temperature-dependent, with an optimum of 21 degrees C. The dose-response curve indicated an ED50 of DH for diapause termination of approximately 100 pmol. The core sequence and essential amino acids were determined by bioassays using modified and truncated DH analogs. A C-terminal hepta-peptide, LWFGPRLa, was the core sequence required for diapause termination. Activity was lost when Alanine was substituted for any of the amino acids in the hepta-peptide, with the exception of Glycine. A fragment series of analogs suggested that the amide and Arginine were the most important components needed for terminating diapause. Leucine, Tryptophan, and Phenylalanine at the N-terminus of the hepta-peptide were also critical for activity. The C-terminal Leucine was less important: deletion resulted in decreased activity, although it could not be substituted by Alanine. The fact that a portion of the DH sequence is similar to the pyrokinin that accelerates fly pupariation prompted us to also evaluate the capability of DH to accelerate development in the flesh fly, Sarcophaga bullata. The threshold dose of DH essential to accelerate fly pupariation was 5 pmol for immobilization/retraction and longitudinal contraction and 10 pmol for tanning, approximately one or two orders of magnitude lower than the effective dose required for diapause termination in H. zea. Tensiometric measurements revealed that DH affected neuromuscular patterns of pupariation behavior and associated cuticular changes in a manner similar to that of the fly pyrokinins and their analogs.},
	keywords = {*Temperature, Amino Acid Substitution, Animals, development, Diptera/*growth \&amp, Dose-Response Relationship, Drug, Larva/drug effects/growth \&amp, Lepidoptera/*growth \&amp, Muscle Contraction/drug effects, Neuropeptides/chemistry/*pharmacology, Peptide Fragments/pharmacology, Pupa/drug effects/growth \&amp, Structure-Activity Relationship},
	author = {Zhang, Q. and Zd{\textquoteright}arek, J. and Nachman, R. J. and Denlinger, D. L.}
}
@article {279,
	title = {Extended FMRFamides in dipteran insects: conservative expression in the neuroendocrine system is accompanied by rapid sequence evolution},
	volume = {162},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalDepartment of General Zoology and Animal Physiology, Friedrich-Schiller-University, Erbertstr. 1, 07743 Jena, Germany.enghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=18789334},
	pages = {52 - 58},
	abstract = {Extended FMRFamides are found throughout the central nervous system (CNS) of insects and exhibit diverse physiological effects on different target organs, such as muscles, intestine, and the nervous system. The genes encoding for extended FMRFamides are known from a number of flies, including Drosophila species, and the pest insects Lucilia cuprina, Calliphora vomitoria, and Musca domestica. No data, however, exist about the expression of the numerous paralogs of the latter three species, and studies on Drosophila melanogaster resulted in controversial findings. We could unambiguously verify, that all predictable products of the extended FMRFamide precursor are expressed in neurohemal tissues of the thoracic neuromers of these flies and can easily be identified and also sequenced by using single specimens. In addition to the confirmation of extended FMRFamides in species with known precursor sequences, the current knowledge about homologous peptides of Sarcophaga (=Neobellieria) bullata could be extended by de novo sequencing using tandem mass spectrometry. The most intriguing finding in this study was the detection of an internal gene duplication, followed by an amino acid substitution, in an insecticide-resistant strain of L. cuprina. To our knowledge, this is the first detection of such an intraspecific event and confirms the low conservation of the extended FMRFamide gene sequences. In insects, no other neuropeptide family is known that shows such sequence variability between related species.},
	keywords = {*Evolution, Molecular, *Genetic Variation, Amino Acid Sequence, Amino Acid Substitution, Animals, Diptera/*genetics/metabolism, FMRFamide/chemistry/genetics/*metabolism, Gene Duplication, Houseflies/genetics/metabolism, Phylogeny, Protein Precursors/chemistry/metabolism, Sequence Analysis, Protein, Species Specificity, Tandem Mass Spectrometry},
	author = {Rahman, M. M. and Fromm, B. and Neupert, S. and Kreusch, S. and Predel, R.}
}
