@article {1569,
	title = {Identification of elements of the peptide binding site of DnaK by peptide cross-linking},
	volume = {271},
	year = {Submitted},
	note = {29-12-201106-02-2012Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.enghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=8702669},
	pages = {19668 - 19674},
	abstract = {We used photocross-linking of peptides to DnaK to identify elements of the peptide binding site of DnaK. We attached a photoactivatable group (N-hydroxysuccinimidyl-4-azido-salicylic acid (NHS-ASA) or N-iodoacetamidobutyl-4-azido-salicylic acid (I-ABASA)) to different positions on peptide C of the vesicular stomatitis virus glycoprotein, 125I-radiolabeled the cross-linker, cross-linked the peptide to DnaK by UV irradiation, and then determined the amino acid residues of DnaK that were cross-linked to the peptide. Limited trypsin digestion of the DnaK-peptide complex revealed that the derivatives modified with photoactivatable cross-linker peptide C cross-linked to a C-terminal fragment of DnaK and that the N-terminal 45-kDa fragment of DnaK was not cross-linked by these modified peptides. The attachment points of the three peptide C derivatives carrying photoactivatable cross-linkers at different locations on the peptide, PepC-ASA, PepC-S7C-ABASA, and PepC-S8C-ABASA, have been identified as Arg-536, Arg-527, and His-541 of DnaK, respectively. Thus all three peptides cross-linked to amino acids located close together in a sequence that includes one end of the long alpha-helix in the NMR-based secondary structure model of the peptide binding domain of Hsp70 family (Morshauser, R., Wang, H., Flynn, G., and Zuiderweg, E. (1995) Biochemistry 34, 6261-6266).},
	keywords = {*Escherichia coli Proteins, *Heat-Shock Proteins, *Membrane Glycoproteins, Amino Acid Sequence, Animals, Binding Sites, Carrier Proteins/chemistry, Cross-Linking Reagents, HSC70 Heat-Shock Proteins, HSP70 Heat-Shock Proteins/*chemistry, Molecular Chaperones/chemistry, Molecular Sequence Data, Peptide Fragments/chemistry, Rats, Sequence Alignment, Trypsin/chemistry, Ultraviolet Rays, Vesicular stomatitis Indiana virus/chemistry, Viral Envelope Proteins/chemistry},
	author = {Zhang, J. and Walker, G. C.}
}
@article {766,
	title = {Isolation and characterization of a C-type lectin cDNA specifically expressed in the tip of mouthparts of the flesh fly Sarcophaga peregrina},
	volume = {13},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalPhysiology and Genetic Regulation Department, National Institute of Agrobiological Sciences, Tsukuba, Ibaraki, Japan. mamiy3@nias.affrc.go.jpenghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=15056360},
	pages = {133 - 140},
	abstract = {We have isolated a novel gene, CLEM 36, of the flesh fly Sarcophaga peregrina, which shows significant homology to the C-type lectin family. CLEM 36 mRNA was transcribed excessively from the second day after eclosion only in the tip of mouthparts. Whole mount in situ hybridization showed that CLEM 36 mRNA was expressed in the C-type lectin-producing tissue (CLPT) located at the entrance of the food canal and between the labellum and haustellum. Immunoblot analysis showed that the mature form of CLEM 36 protein was synthesized in the CLPT, then secreted into saliva. Our results indicate that CLEM 36 protein may play an important role in biological defence against pathogens during the food intake of this insect.},
	keywords = {*Gene Expression Profiling, Amino Acid Sequence, Animals, Base Sequence, Diptera/*genetics/immunology, DNA, Complementary/genetics, Immunoblotting, In Situ Hybridization, Lectins, C-Type/*genetics/isolation \&amp, Molecular Sequence Data, Mouth/*metabolism, purification, Reverse Transcriptase Polymerase Chain Reaction, Saliva/chemistry, Sequence Alignment, Sequence Analysis, DNA},
	author = {Yamamoto-Kihara, M. and Kotani, E.}
}
@article {649,
	title = {A virus essential for insect host-parasite interactions encodes cystatins},
	volume = {79},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalInstitut de Recherche sur la Biologie de l{\textquoteright}Insecte, UMR CNRS 6035, Faculte des Sciences et Techniques, Parc de Grandmont, Tours.eng SI  - GENBANK/AJ632321http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=16014938},
	pages = {9765 - 9776},
	abstract = {Cotesia congregata is a parasitoid wasp that injects its eggs in the host caterpillar Manduca sexta. In this host-parasite interaction, successful parasitism is ensured by a third partner: a bracovirus. The relationship between parasitic wasps and bracoviruses constitutes one of the few known mutualisms between viruses and eukaryotes. The C. congregata bracovirus (CcBV) is injected at the same time as the wasp eggs in the host hemolymph. Expression of viral genes alters the caterpillar{\textquoteright}s immune defense responses and developmental program, resulting in the creation of a favorable environment for the survival and emergence of adult parasitoid wasps. Here, we describe the characterization of a CcBV multigene family which is highly expressed during parasitism and which encodes three proteins with homology to members of the cystatin superfamily. Cystatins are tightly binding, reversible inhibitors of cysteine proteases. Other cysteine protease inhibitors have been described for lepidopteran viruses; however, this is the first description of the presence of cystatins in a viral genome. The expression and purification of a recombinant form of one of the CcBV cystatins, cystatin 1, revealed that this viral cystatin is functional having potent inhibitory activity towards the cysteine proteases papain, human cathepsins L and B and Sarcophaga cathepsin B in assays in vitro. CcBV cystatins are, therefore, likely to play a role in host caterpillar physiological deregulation by inhibiting host target proteases in the course of the host-parasite interaction.},
	keywords = {Amino Acid Sequence, Animals, Base Sequence, Cathepsins/antagonists \&amp, Cystatins/genetics/isolation \&amp, Diptera/enzymology, Genes, Viral, Host-Parasite Interactions, Humans, inhibitors, Manduca/*parasitology, Molecular Sequence Data, Multigene Family/physiology, OID - NLM: PMC1181612, Ovum/virology, Papain/antagonists \&amp, PMC - PMC1181612, Polydnaviridae/*metabolism, purification/*metabolism/pharmacology, Sequence Alignment, Wasps/*metabolism/*physiology/virology},
	author = {Espagne, E. and Douris, V. and Lalmanach, G. and Provost, B. and Cattolico, L. and Lesobre, J. and Kurata, S. and Iatrou, K. and Drezen, J. M. and Huguet, E.}
}
@article {468,
	title = {Purification of a cysteine protease inhibitor from larval hemolymph of the tobacco hornworm (Manduca sexta) and functional expression of the recombinant protein},
	volume = {37},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalLaboratory of Food Molecular Functionality, College of Agriculture, Ibaraki University, 3-21-1 Chuo, Ami-machi, Inashiki-gun, Ibaraki 300-0393, Japan.enghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=17681235},
	pages = {960 - 968},
	abstract = {A cysteine protease inhibitor (CPI) with an apparent molecular mass of 11.5kDa was purified from larval hemolymph of the tobacco hornworm (Manduca sexta) by gel filtration on Sephadex G-50 followed by hydrophobic and ion-exchange column chromatographies. The purified cysteine proteinase inhibitor, denoted as MsCPI, strongly inhibited the plant cysteine protease, papain, with a K(i) value of 5.5 x 10(-9)M. Nucleotide sequence analysis of a partial cDNA encoding MsCPI indicated that MsCPI consists of 105 amino acid residues in a sequence that is similar to sarcocystatin A from Sarcophaga peregrina. However, northern blotting and PCR analyses using the specific primers of MsCPI suggested that the mRNA encoding MsCPI had a size of more than 12 kilobases, which included at least six tandemly repeated MsCPI segments. MsCPI was expressed in Escherichia coli and the recombinant protein effectively inhibited cysteine proteases from plants as well as from animals such as cathepsins B (K(i), 6.8 nM), H (3.0 nM), and L (0.87 nM). There was no inhibition exhibited toward trypsin, chymotrypsin, subtilisin, pepsin or themolysin.},
	keywords = {Amino Acid Sequence, Animals, Cathepsins/drug effects/isolation \&amp, Cloning, Molecular, Conserved Sequence, Cysteine Proteinase Inhibitors/genetics/*isolation \&amp, development, DNA Primers, Escherichia coli/genetics, Hemolymph/*chemistry, Humans, inhibitors, Larva, Manduca/*growth \&amp, Molecular Sequence Data, Papain/antagonists \&amp, Polymerase Chain Reaction, purification/metabolism, purification/pharmacology, Recombinant Proteins/isolation \&amp, Sequence Alignment, Sequence Homology, Amino Acid},
	author = {Miyaji, T. and Kouzuma, Y. and Yaguchi, J. and Matsumoto, R. and Kanost, M. R. and Kramer, K. J. and Yonekura, M.}
}
@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.}
}
@article {286,
	title = {Length variation in a specific region of the period gene correlates with differences in pupal diapause incidence in the flesh fly, Sarcophaga bullata},
	volume = {55},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalDepartment of Entomology, The Ohio State University, 318W 12th Ave., Columbus, OH 43210, USA.enghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=19186187},
	pages = {415 - 418},
	abstract = {We report differences in the length of a specific region of the circadian clock gene period (per) that correlate with different capacities for pupal diapause in the flesh fly, Sarcophaga bullata. The conspicuous difference is located in a region we refer to as the putative C-terminal photoperiodic (CP) region. The length of the CP region correlates inversely with the incidence of diapause. A deletion of 33 amino acids in this region correlates with a significant increase in the incidence of diapause, from 78.1\% to 93.0\%, and an insertion of 9 amino acids in the same area correlates with a drop in the diapause incidence to 4.0\%. This correlation suggests a possible functional role for this region of per in photoperiodism.},
	keywords = {*Genetic Variation, Amino Acid Sequence, Animals, development/metabolism, Diptera/chemistry/*genetics/*growth \&amp, Insect Proteins/chemistry/*genetics/metabolism, Molecular Sequence Data, Pupa/chemistry/genetics/growth \&amp, Sequence Alignment},
	author = {Han, B. and Denlinger, D. L.}
}
@article {288,
	title = {Two hsp23 genes in the Mediterranean fruit fly, Ceratitis capitata: structural characterization, heat shock regulation and developmental expression},
	volume = {18},
	year = {Submitted},
	note = {08-10-200906-02-2012NormalDepartment of Biology, University of Patras, Greece.enghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=19320758},
	pages = {171 - 181},
	abstract = {In the present study, we characterized a 3320-bp genomic DNA fragment encoding two medfly (Ceratitis capitata) homologues of the Drosophila melanogaster heat shock protein 23 (hsp23) gene, named Cchsp23-alphaand -beta. The two medfly hsp23 genes are transcribed in opposite directions and encode two almost identical proteins. Furthermore, the two genes exhibit a very high degree of similarity in their 5{\textquoteright} untranslated and proximal promoter regions. Phylogenetic analysis indicated that the CcHsp23 proteins are orthologous to Drosophila Hsp23 and Sarcophaga crassipalpis Hsp23. Structural analysis of the 5{\textquoteright} flanking regions of the Cchsp23 genes revealed the presence of several putative heat shock elements. Both CcHsp23 genes are induced by heat in a similar manner. In addition to heat-induction, the Cchsp23 genes are expressed at several stages of normal development as well as in ovaries and testes. In general, the developmental expression patterns of the medfly genes are similar, suggesting that they are under similar regulatory mechanisms. However, the expression of the Cchsp23 genes differs significantly from the expression of the Drosophila hsp23 gene in certain embryonic and larval stages, suggesting differential regulation of the hsp23 genes in the two dipteran species. The expression of both Cchsp23 genes in adult flies is increased with age, especially in males.},
	keywords = {*Gene Expression Regulation, Developmental, *Genes, Insect, Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Ceratitis capitata/*genetics, Drosophila, Heat-Shock Proteins/chemistry/*genetics/metabolism, Heat-Shock Response/*genetics, Molecular Sequence Data, Phylogeny, Restriction Mapping, Sequence Alignment},
	author = {Kokolakis, G. and Kritsidima, M. and Tkachenko, T. and Mintzas, A. C.}
}
