2002
DOI: 10.1016/s0041-0101(02)00240-4
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Plant toxic proteins with insecticidal properties. A review on their potentialities as bioinsecticides

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Cited by 451 publications
(312 citation statements)
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References 244 publications
(261 reference statements)
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“…However, data in the literature associating larvicidal or insecticidal action with proteolytic activity are scarce. Most of the available data deal with insecticidal plant proteins such as lectins, ribosome-inactivating proteins, enzyme inhibitors, arcelins, chitinases, ureases and modified storage proteins (Carlini & Grossi-de-Sá 2002). On the other hand, Pechan et al (2002) have described a correlation between the impaired growth of caterpillars and a cysteine proteinase present in some Maize (Zea mays L.) lines that are resistant to feeding by a number of lepidopteran species.…”
Section: Discussionmentioning
confidence: 99%
“…However, data in the literature associating larvicidal or insecticidal action with proteolytic activity are scarce. Most of the available data deal with insecticidal plant proteins such as lectins, ribosome-inactivating proteins, enzyme inhibitors, arcelins, chitinases, ureases and modified storage proteins (Carlini & Grossi-de-Sá 2002). On the other hand, Pechan et al (2002) have described a correlation between the impaired growth of caterpillars and a cysteine proteinase present in some Maize (Zea mays L.) lines that are resistant to feeding by a number of lepidopteran species.…”
Section: Discussionmentioning
confidence: 99%
“…Screening of plant extracts for deleterious effect on insects is one of the approaches in the search of novel biological insecticides [1]. Insecticidal activity of many plants against several insects has been demonstrated [2,3]. Seed as well as foliar extracts of several plants have been reported to have toxic and potent growth reducing activity to insects [4].…”
Section: Introductionmentioning
confidence: 99%
“…Technically, the protein bands present in the range of 5-25 kDa suggest the presence of inhibitors of serine peptidases type Kunitz, Bowman-Birk and 2S albumin which has been reported in the scientific literature (Carlini & Grossi-de-Sá, 2002;Ruan et al, 2011). The band near the molecular weight of 11 kDas was more abundant in both phases, this being apparently very similar to the protein that shows 40% activity against trypsin, purified from Pequi seed, called 2S albumin (Costa, 2012).…”
Section: Electrophoresis Of Isolated Fractions Of Pequi Seedsmentioning
confidence: 72%