Relevant bibliographies by topics / Insect, protease, peptides

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'Insect, protease, peptides'

Author: Grafiati
Published: 6 September 2023
Last updated: 31 July 2025

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Journal articles on the topic "Insect, protease, peptides"

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COPLEY, S. Kathrin, M. Sheri ALM, A. David SCHOOLEY, and E. William COURCHESNE. "Expression, processing and secretion of a proteolytically-sensitive insect diuretic hormone by Saccharomyces cerevisiae requires the use of a yeast strain lacking genes encoding the Yap3 and Mkc7 endoproteases found in the secretory pathway." Biochemical Journal 330, no. 3 (1998): 1333–40. http://dx.doi.org/10.1042/bj3301333.

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A system is described for the heterologous expression of peptides in Saccharomyces cerevisiae. A synthetic gene encoding a precursor of the 41 amino acid Manduca sexta diuretic hormone (Mas-DH) was expressed at 0.8 mg/l purified peptide. A precursor of a mutant peptide of Mas-DH, Mas-DH[K22Q] was also expressed. The peptides were purified, then treated with peptidylglycine α-amidating enzyme to generate the α-amidated, mature, form of Mas-DH or Mas-DH[K22Q], which were biologically active. Successful expression of full-length Mas-DH+Gly depended upon the use of a protease-deficient yeast strai
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Deng, Yuping, James Gibbs, Igor Bačík, et al. "Assembly of MHC Class I Molecules with Biosynthesized Endoplasmic Reticulum-Targeted Peptides Is Inefficient in Insect Cells and Can Be Enhanced by Protease Inhibitors." Journal of Immunology 161, no. 4 (1998): 1677–85. http://dx.doi.org/10.4049/jimmunol.161.4.1677.

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Abstract To study the requirements for assembly of MHC class I molecules with antigenic peptides in the endoplasmic reticulum (ER), we studied Ag processing in insect cells. Insects lack a class I recognition system, and their cells therefore provide a “blank slate” for identifying the proteins that have evolved to facilitate assembly of class I molecules in vertebrate cells. H-2Kb heavy chain, mouse β2-microglobulin, and an ER-targeted version of a peptide corresponding to Ova257–264 were expressed in insect cells using recombinant vaccinia viruses. Cell surface expression of Kb-OVA257–264 co
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Liu, Huawei, Jiahui Xu, Luoling Wang, et al. "Serpin-1a and serpin-6 regulate the Toll pathway immune homeostasis by synergistically inhibiting the Spätzle-processing enzyme CLIP2 in silkworm, Bombyx mori." PLOS Pathogens 19, no. 10 (2023): e1011740. http://dx.doi.org/10.1371/journal.ppat.1011740.

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The Toll receptor signaling pathway is an important innate immune response of insects to pathogen infection; its extracellular signal transduction involves serine protease cascade activation. However, excessive or constitutive activation of the Toll pathway can be detrimental. Hence, the balance between activation and inhibition of the extracellular protease cascade must be tightly regulated to achieve favorable outcomes. Previous studies have shown that serpins—serine protease inhibitors—negatively regulate insect innate immunity by inhibiting extracellular protease cascade signaling. Althoug
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Caldas, C., A. Cherqui, A. Pereira, and N. Simões. "Purification and Characterization of an Extracellular Protease from Xenorhabdus nematophila Involved in Insect Immunosuppression." Applied and Environmental Microbiology 68, no. 3 (2002): 1297–304. http://dx.doi.org/10.1128/aem.68.3.1297-1304.2002.

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ABSTRACT Xenorhabdus nematophila, a bacterium pathogenic for insects associated with the nematode Steinernema carpocapsae, releases high quantities of proteases, which may participate in the virulence against insects. Zymogram assays and cross-reactions of antibodies suggested that two distinct proteases were present. The major one, protease II, was purified and shown to have a molecular mass of 60 kDa and an estimated isoelectric point of 8.5. Protease II digested the chromogenic substrate N-tosyl-Gly-Pro-Arg-paranitroanilide (pNA) with V max and Km values of 0.0551 μM/min and 234 μM, respect
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Pfrepper, Klaus-Ingmar, Hans-Richard Rackwitz, Martina Schnölzer, Hans Heid, Martin Löchelt, and Rolf M. Flügel. "Molecular Characterization of Proteolytic Processing of the Pol Proteins of Human Foamy Virus Reveals Novel Features of the Viral Protease." Journal of Virology 72, no. 9 (1998): 7648–52. http://dx.doi.org/10.1128/jvi.72.9.7648-7652.1998.

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ABSTRACT Spumaviruses, or foamy viruses, express a pol-specific transcript that codes for a Pol polyprotein that consists of the protease, reverse transcriptase, ribonuclease H, and the integrase domains. To delineate the proteolytic cleavage sites between the Pol subdomains, recombinant human foamy virus (HFV) Pol proteins were expressed, purified by affinity chromatography, and subjected to either HFV protease assays or autocatalytic processing. In control experiments, HFV protease-deficient mutant proteins in which the active site Asp was replaced by an Ala residue were used to rule out uns
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Lin, Ying-Chuan, Zachary Beck, Taekyu Lee, et al. "Alteration of Substrate and Inhibitor Specificity of Feline Immunodeficiency Virus Protease." Journal of Virology 74, no. 10 (2000): 4710–20. http://dx.doi.org/10.1128/jvi.74.10.4710-4720.2000.

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ABSTRACT Feline immunodeficiency virus (FIV) protease is structurally very similar to human immunodeficiency virus (HIV) protease but exhibits distinct substrate and inhibitor specificities. We performed mutagenesis of subsite residues of FIV protease in order to define interactions that dictate this specificity. The I37V, N55M, M56I, V59I, and Q99V mutants yielded full activity. The I37V, N55M, V59I, and Q99V mutants showed a significant increase in activity against the HIV-1 reverse transcriptase/integrase and P2/nucleocapsid junction peptides compared with wild-type (wt) FIV protease. The I
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Pfrepper, Klaus-Ingmar, Martin Löchelt, Hans-Richard Rackwitz, Martina Schnölzer, Hans Heid, and Rolf M. Flügel. "Molecular Characterization of Proteolytic Processing of the Gag Proteins of Human Spumavirus." Journal of Virology 73, no. 9 (1999): 7907–11. http://dx.doi.org/10.1128/jvi.73.9.7907-7911.1999.

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ABSTRACT Spumaviruses, or foamy viruses, express Gag proteins that are incompletely processed by the viral protease in cell cultures. To delineate the proteolytic cleavage sites between potential Gag subdomains, recombinant human spumaretrovirus (HSRV) Gag proteins of different lengths were expressed, purified by affinity chromatography, and subjected to HSRV protease assays. HSRV-specific proteolytic cleavage products were isolated and characterized by Western blotting. Peptides spanning potential cleavage sites, as deduced from the sizes of the proteolytic cleavage products, were chemically
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SIMONET, Gert, Bert BREUGELMANS, Paul PROOST, et al. "Characterization of two novel pacifastin-like peptide precursor isoforms in the desert locust (Schistocerca gregaria): cDNA cloning, functional analysis and real-time RT-PCR gene expression studies." Biochemical Journal 388, no. 1 (2005): 281–89. http://dx.doi.org/10.1042/bj20041414.

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In the last decade, a new serine protease inhibitor family has been described in arthropods. Eight members of the family were purified from locusts and share a conserved cysteine array (Cys-Xaa9–12-Cys-Asn-Xaa-Cys-Xaa-Cys-Xaa2–3-Gly-Xaa3–6-Cys-Thr-Xaa3-Cys) with nine inhibitory domains of the light chain of the crayfish protease inhibitor, pacifastin (PLDs; pacifastin light chain domains). Using cDNA cloning, several pacifastin-related precursors have been identified, encoding additional PLD-related peptides in different insect species. In the present study, two isoforms of a novel pacifastin-
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Beck, Zachary Q., Ying-Chuan Lin, and John H. Elder. "Molecular Basis for the Relative Substrate Specificity of Human Immunodeficiency Virus Type 1 and Feline Immunodeficiency Virus Proteases." Journal of Virology 75, no. 19 (2001): 9458–69. http://dx.doi.org/10.1128/jvi.75.19.9458-9469.2001.

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ABSTRACT We have used a random hexamer phage library to delineate similarities and differences between the substrate specificities of human immunodeficiency virus type 1 (HIV-1) and feline immunodeficiency virus (FIV) proteases (PRs). Peptide sequences were identified that were specifically cleaved by each protease, as well as sequences cleaved equally well by both enzymes. Based on amino acid distinctions within the P3-P3′ region of substrates that appeared to correlate with these cleavage specificities, we prepared a series of synthetic peptides within the framework of a peptide sequence cle
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Zhang, T. T., G. C. Zhang, F. F. Zeng, C. Y. Liu, and J. J. Mao. "Insulin-like peptides regulate vitellogenesis and oviposition in the green lacewing, Chrysopa septempunctata." Bulletin of Entomological Research 107, no. 2 (2016): 148–54. http://dx.doi.org/10.1017/s0007485316000742.

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AbstractInsulin-like peptides (ILPs) act through a conserved insulin signaling pathway and play crucial roles in insect metabolism, growth, reproduction, and aging. Application of bovine insulin is able to increase vitellogenin (Vg) mRNA and protein levels in female insects. Here, we first show that injection of bovine insulin into previtellogenic Chrysopa septempunctata female adults promoted ovarian growth, increased Vg protein abundance, elevated reproductive performance, and enhanced protease activity. These data suggested that ILPs play crucial roles in reproductive regulation of the gree
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Dissertations / Theses on the topic "Insect, protease, peptides"

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Saikhedkar, N. "Peptides for inhibition of insect proteases." Thesis(Ph.D.), CSIR-National Chemical Laboratory, Pune, 2019. http://dspace.ncl.res.in:8080/xmlui/handle/20.500.12252/4594.

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Jamriska, Lubomira. "Characterisation of dipeptidyl peptidase I of the Asian blood fluke, Schistosoma japonicum." Thesis, Queensland University of Technology, 2000.

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Book chapters on the topic "Insect, protease, peptides"

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Law, John H., Peter E. Dunn, and Karl J. Kramer. "Insect Proteases and Peptidases." In Advances in Enzymology - and Related Areas of Molecular Biology. John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470122907.ch5.

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Beatriz Meriño-Cabrera, Yaremis, and Maria Goreti de Almeida Oliveira. "Trypsins: Structural Characterization and Inhibition Focus in Insects." In Hydrolases [Working Title]. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.102632.

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Serine proteases are considered the main class of protein digestive enzymes present in the midgut of many lepidopteran species and are the focus of the review in this chapter. Among them, trypsin and chymotrypsin are the most studied and participate in a great diversity of physiological processes that include, in addition to digestion, activation of specific proteins, such as in the coagulation cascades, in the immune system of insects and plants, in the development and production of biologically active peptides, in signal transduction, hormone activation, and development. In this chapter, a r
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Conference papers on the topic "Insect, protease, peptides"

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Lopez, J. A., D. W. Chung, K. Fujikawa, F. S. Hagen, T. Papavannopoulou, and G. J. Roth. "MOLECULAR CLONING OF HUMAN PLATELET GLYCOPROTEIN Ib." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642927.

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Glycoprotein Ib (GPIb) mediates von Willebrand factor-dependent platelet adhesion and participates in the resulting platelet activation process. In the present investigation, the primary structure of human platelet GPIb was studied. GPIb and its proteolytic fragment glycocalicin were purified to near homogeneity from human platelets by affinity chromatography using wheat germ agglutinin and anti-GPIb monoclonal antibody (D. Nugent, University of Washington) coupled to Sepharose. GPIba chain, β chain, and glycocalicin were isolated, reduced and carboxymethylated, and then fragmented by trypsin
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Journal articles
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