Pacifastin-related peptides: Structural and functional characteristics of a family of serine peptidase inhibitors
- 31 March 2009
- Vol. 30 (3) , 622-632
- https://doi.org/10.1016/j.peptides.2008.07.026
Abstract
No abstract availableKeywords
This publication has 51 references indexed in Scilit:
- Quantitative RT‐PCR analysis of pacifastin‐related precursor transcripts during the reproductive cycle of solitarious and gregarious desert locustsInsect Molecular Biology, 2008
- Molecular markers of phase transition in locustsInsect Science, 2006
- The prophenoloxidase‐activating system in invertebratesImmunological Reviews, 2004
- Peptide differential display: a novel approach for phase transition in locustsComparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2002
- Peptidomics of the pars intercerebralis–corpus cardiacum complex of the migratory locust, Locusta migratoriaEuropean Journal of Biochemistry, 2001
- Low molecular weight serine protease inhibitors from insects are proteins with highly conserved sequencesInsect Biochemistry and Molecular Biology, 2000
- cDNA cloning of prophenoloxidase from the freshwater crayfish Pacifastacus leniusculus and its activation.Proceedings of the National Academy of Sciences, 1995
- Insect immunity: Two proteinase inhibitors from hemolymph of Locusta migratoriaBiochemical and Biophysical Research Communications, 1992
- Natural protein proteinase inhibitors and their interaction with proteinasesEuropean Journal of Biochemistry, 1992
- The effect of endogeneous proteinase inhibitors on the prophenoloxidase activating enzyme, a serine proteinase from crayfish haemocytesInsect Biochemistry, 1990