High-throughput mass spectrometry approaches along with improved techniques such as SILAC for quantitative proteomics have provided the building blocks of the current knowledge base for this new grammar of drug discovery. About 60% of Drosophila proteins have human homologues with well-conserved canonical signaling cascades. Because Drosophila is a less complex model system than a vertebrate, it gives an opportunity to analyze complex signaling networks and Pyriproxyfen translate the findings to identify novel drug targets for human diseases. Datasets from model systems with conserved canonical signaling pathways play an important part in rapidly generating a knowledge base. By forcing stable, homogeneous expression of individual E2F family members in non-transformed parental cells, our approach provides a model of dysregulated E2F expression, and allows an unprecedented systematic comparison of the oncogenic capacity of six different E2F family members. Thus both limiting and luminal membranes are composed of diverse lipid domains. It is now well-accepted that the sorting of down regulated signaling receptors into intralumenal membranes mediates their lysosomal targeting and degradation. Consistent with our findings, the rate-limiting nucleation process of polyQ aggregation is thought to involve folding within mutant monomers. These data suggest that the protein surface structure detected by 1C2 in soluble mutant monomers acts as an amyloid-precursor epitope, leading to nucleation, a key process of protein aggregation, and thereby determining HD onset. Moreover, 1C2 has been shown to inhibit the in vitro aggregation of the protein implicated in HD. Our results indicate that the gain-of-function of polyQ pathogenesis involves two steps. A gain-of-toxic-function mechanism for polyQ expansion mutation has been suggested by results from cell transfection and transgenic and knock-out 2,6-Diaminopurine animal experiments,. Our findings suggest, however, that the genetic gain-of-function conferred by polyQ expansion is a gain of amyloid-precursor structure rather than a toxic effect on the cells.