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1

Effect of recombinant Aea-TMOF on Heliothis virescens

100%
Borovsky D., Iannotti D. A., Shatters R.G.,Jr., Powell C. A.
Pestycydy
|
2005
|
nr 3
79-85
2

Antinociceptive effect of insect hexapeptide, insect trypsin modulating oostatic factor [Neb-TMOF] in rats

100%
Plech A., Kuczer M., Szewczyk A., Konopinska D.
Pestycydy
|
2005
|
nr 1-2
5-13
3

Synthesis and biological activity of new analogues Neobellieria bullata trypsin modulating oostatic factor Neb-TMOF

100%
Konopinska D., Bartosz-Bechowski H., Kuczer M., Szeszel-Fedorowicz W., Janssen I., De Loof A.
Pestycydy
|
2000
|
nr 1-2
4

The effect of Aea-TMOF on egg maturation in Heliothis virescens: a preliminary study

84%
Pszczolkowski M. A., Rhine C., Ramaswamy S. B., Borovsky D.
Pestycydy
|
2007
|
nr 3-4
33-38
Trypsin Modulating Oostatic Factor from the mosquito, Aedes aegypti, (Aea-TMOF) inhibits juvenile hormone (JH) - stimulated egg chorionation and patency in the follicular epithelium cells of Heliothis virescens. Aea-TMOF exhibits highest inhibitory effect on oocytes or follicular epithelium cells when it is administered together with JH I rather than with JH III. These results indicate that Aea-TMOF specifically inhibits JH I-dependent events during egg maturation in Heliothis virescens. Preliminary pharmacological analysis of the Aea-TMOF effect on patency suggests that the decapeptide hormone acts upstream of the protein kinase-dependent step during the JH activated cellular signaling pathway.
5

Central opioid receptors mediate antinociceptive effect in rats of insect hexapeptide - trypsin modulating oostatic factor [Neb-TMOF] and of its synthetic analogs

84%
Rykaczewska-Czerwinska M., Wrobel M., Kuczer M., Konopinska D., Plech A.
Pestycydy
|
2006
|
nr 1-2
21-27
6

Control of mosquito larval trypsin with Aea-trypsin modulating oostatic factor [TMOF] and its analogues

67%
Borovsky D.
Pestycydy
|
2005
|
nr 3
71-77
7
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Control of mosquito larvae with TMOF and 60 kDa Cry4Aa expressed in Pichia pastoris

67%
Borovsky D., Nauwelaers S., Van Mileghem A., Meyvis Y., Laeremans A., Theunis C., Bertier L., Boons E.
Pestycydy
|
2011
|
nr 1-4
Cry4Aa 678 amino acids fragment (60 kDa) was cloned into Escherichia coli. After induction with IPTG the 60 kDa Cry4Aa fragment was purified by Ni chromatography, separated by SDS PAGE and identified by mass spectrometry (MS/MS). The 60 kDa Cry4Aa fragment exhibited high toxicity towards Ae. aegypti larvae. The earlier results [1] show that Pichia pastoris yeast cells expressing tmfA (synthetic gene coding for the Trypsin Modulating Oostatic Factor of Ae. aegypti) together with E. coli cells expressing Bti toxin genes (cry4Aa, cry11Aa, cyt1Aa and p20) are synergistic. Therefore, P. pastoris, which synthesizes high amounts of heterologous proteins was genetically engineered to produce TMOF and Cry4Aa. Codon-optimized synthetic genes, cry4Aa-tmfA, gst-cry4Aa-tmfA, tmfA and gfptmfA that were expressed by P. pastoris and fed to Ae. aegypti larvae caused 90% mortality. GST (glutathione-S-transferase) enhanced the activity of Cry4Aa-TMOF and protected it from heat denaturation and GFP (Green Fluorescent Protein)- TMOF allowed us to follow yeast cells consumption by individual larva using fluorescent microscopy. This report shows for the first time that 60 kDa Cry4Aa and TMOF expressed together in P. pastoris are highly toxic to Ae. aegypti larvae.
8
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Binding of Aedes aegypti trypsin modulating oostatic factor [Aea-TMOF] to its receptor stimulates phosphorylation and protease processing of gut-membrane proteins

67%
Borovsky D., Hamdaoui A.
Pestycydy
|
2008
|
nr 1-2
13-25
The binding of TMOF to its gut receptor was followed by incubating guts removed from male and female Aedes aegypti. TMOF at physiological concentrations, in the presence of [γ32P]ATP, causes phosphorylation and release of gut-membrane protein (45 kDa) that is further processed by proteolysis. In the presence of protease inhibitors only the 45 kDa protein was released. The phosphorylation and processing of the 45 kDa protein does not happen in the absence of TMOF. Both larvae and adult guts release the protein in the presence of TMOF. Male Ae. aegypti do not synthesize trypsin in their gut and do not release the 45 kDa protein in the presence of TMOF because a TMOF receptor is probably absent. Homogenized guts do not release the 45 kDa protein, indicating that the protease processing or the ecto-protein kinase activity is probably reduced after breaking the tissue. The 45 kDa phosphorylated protein can be dephosphorylated by alkaline phosphatase and protein phosphatase, indicating that the phosphate group is covalently linked to either a serine or a tyrosine moiety. This is the first report that shows that in insects, binding of a peptide hormone activates its receptor by proteolysis.
9

Biological and biochemical effects of organo-synthetic analogues of trypsin modulating oostatic factor [TMOF] on Aedes aegypti, Heliothis virescens and Plutella xylostella

67%
Borovsky D., Nauen R.
Pestycydy
|
2007
|
nr 3-4
17-26
The three-dimensional conformation of Aea-TMOF (Aedes aegypti Trypsin Modulating Oostatic Factor), a decapeptide (YDPAPPPPPP) isolated from mosquito ovaries that inhibits the translation of many trypsin-like serine proteases, e.g. in mosquitoes, flies and lepidopterans, was used as a model for the synthesis of 10 aromatic and aliphatic organic acid and ester analogues. The organic TMOF analogues were tested against herbivorous pest lepidopterans and larval Ae. aegypti. The compounds administered to microtiter plates or to leaf disks caused mortality to mosquito larvae and the diamondback moth, Plutella xylostella, larvae 3-6 days after treatment. The surviving diamondback moth larvae were sluggish, immobile and stopped feeding. A biochemical analysis showed that in larval P. xylostella the trypsin activity was low and correlated with the observed mortality. No activity was found against Heliothis virescens when four of the synthetic compounds that affected P. xylostella and Ae. aegypti were tested, although the decapeptide, TMOF, does affect trypsin biosynthesis in H. virescens.
10
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Control of Aedes aegypti larvae with Aea-TMOF mimics: aromatic derivatives of enoic acid

67%
Borovsky D.
Pestycydy
|
2008
|
nr 1-2
27-34
Based on the 3D conformation of the N-terminus of TMOF in solution, six aromatic derivatives of enoic acid: 7-biphenyl-4-yl-hept-4-enoic acid (BPHE), 7-(4-butyl-phenyl)-hept-4-enoic acid (BuPHE), 7-cyclohexyl-hept-4-enoic acid (CyHE), 10-phenyl-dec-7-enoic acid (PDE), 7-p-tolyl-hept-2-enoic acid ethyl ester (THEEE) and 7-(4-methoxy-phenyl)-hept-2-enoic acid ethyl ester (MPEEE) were computer-modeled and synthesized. Treating first instar Aedes aegypti larvae with different concentrations of the TMOF mimics showed that addition of butyl to the benzyl ring, use of p-tolyl or converting the benzyl ring into cyclohexane increased the biological activity of the mimics by 5.2, 5.0 and 3.8-fold, respectively. Esterifying the carboxyl terminus into ethyl ester and addition of a methoxy group to the benzyl ring also increased, by 2-fold, the biological activity of the derivative. The position of the double bond in the aliphatic chain is important for enhanced biological activity. Aea-TMOF and CyHE fed to mosquito larvae equally inhibited trypsin biosynthesis in larvae for the first 24 h. The biological activity of CyHE, however, rapidly declined 2-3 days later, whereas TMOF activity stayed stable. These results indicate that TMOF organic mimics, although potent, need to be formulated in order to be more stable for future field applications.
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