TESTING OF SEMIO-CHEMICAL PRODUCTS IN MONITORING AND CONTROL OF Rhagoletis cerasi L.
AGROLIFE SCIENTIFIC JOURNAL
Authors: Florian, Teodora; Macavei, Laura Ioana; Hulujan, Ionut Bogdan; Vasian, Iuliana; Totos, Stefania; Gorgan, Monica; Oltean, Ion; Florian, Vasile
Abstract
This paper aims to monitor the cherry fruit fly, as well as for possible actions to combat it by non-chemical methods. The Entomology Department of the USAMV Cluj-Napoca in collaboration with the UBB Cluj-Napoca researchers, started a study regarding the functionality of some Semi-chemical products to attract adults of Rhagoletis cerasi L. The chemistry research laboratories synthesized them and then, under natural conditions, screening studies of their attraction power were performed. The experiment was conducted over two experimental years, 2016 and 2017. Six variants of semiochemical formulations were tested: 2-hexanone, 3-heptanone, nonanal, beta-felandren, geranil acetate and (+) -limonen. The V6 variant that blends the acetylation made most capture. Therefore, the mixture of volatile substances in this variant may present a higher level of attractiveness.
Review: Unchained maladie - a reassessment of the role of Ubb(+1)-capped polyubiquitin chains in Alzheimer's disease
NEUROPATHOLOGY AND APPLIED NEUROBIOLOGY
Authors: Chadwick, L.; Gentle, L.; Strachan, J.; Layfield, R.
Abstract
Molecular misreading allows the formation of mutant proteins in the absence of gene mutations. A mechanism has been proposed by which a frameshift mutant of the ubiquitin protein, Ubb(+1), which accumulates in an age-dependent manner as a result of molecular misreading, contributes to neuropathology in Alzheimer's disease (Lam et al. 2000). Specifically, in the Ubb(+1)-mediated proteasome inhibition hypothesis Ubb(+1) 'caps' unanchored (that is, nonsubstrate linked) polyubiquitin chains, which then act as dominant inhibitors of the 26S proteasome. A review of subsequent literature indicates that this original hypothesis is broadly supported, and offers new insights into the mechanisms accounting for the age-dependent accumulation of Ubb(+1), and how Ubb(+1-)mediated proteasome inhibition may contribute to Alzheimer's disease. Further, recent studies have highlighted a physiological role for free endogenous unanchored polyubiquitin chains in the direct activation of certain protein kinases. This raises the possibility that Ubb(+1)-capped unanchored polyubiquitin chains could also exert harmful effects through the aberrant activation of tau or other ubiquitin-dependent kinases, neuronal NF-kappa B activity or NF-kappa B-mediated neuroinflammatory processes.