Using this approach, we have identified three major determinants of the effect of GAGs on the kinetics of amyloid formation: the sulfation state of the GAG, the molar concentration of all compounds present in the buffer, and the protein/GAG molar ratio. It is highly significant that the two strategies have identified the same parameters, reinforcing the conclusions. The results do not rule out the importance of additional factors, particularly those arising from the chemical nature and structure of the protein undergoing aggregation. However, our statistical approach could not identify any of such determinants, most probably because of the limited size of our database. The recognition of IL-17 producing T cells has opened novel pathways to explain several features of SSc. Our experiments have Fulvestrant demonstrated that the role retinal astrocytes play in retinal vascularization is mediated only in a small part by VEGF. The most likely explanation for the minor effects of astrocyte VEGF deletion on retinal angiogenesis is compensation of VEGF production by other cells, such as neurons. In comparison to retinal astrocytes, RGCs and cells in the inner nuclear layer display a much weaker in situ hybridization signal for Vegf mRNA, but because these low expressing cells are more abundant, VEGF is likely to be produced in sufficient quantities to allow for almost normal vascularization. It is likely that there are other aspects of retinal astrocytes that involve these cells critically in retinal vascularization. For instance, it has been suggested that retinal astrocytes mediate extracellular assembly of fibronectin matrices required for vessel growth. It is also possible that they provide not yet identified factors that are required for retinal angiogenesis. In general, T cell priming by professional antigen presenting cells is tuned by inflammatory mediators, including TGFb, IL-6 and IL-12. The combination of these cytokines determines the ultimate fate of naive T cells. We have also demonstrated that the last 212 amino acids of nucleolin are sufficient for the activation of ErbB1 receptor. These amino acids are comprised of two distinct regions, RBD and GAR. Neither RBD nor GAR effectively interacted with either ErbB4 or ErbB1, ergo the entire sequence is important for the stable interaction with ErbB receptors. A specific interaction of with the MoMuLV Gag precursor was previously demonstrated. All three structural domains contain interactive sequences for recognition, selection and solubilization of unfolding protein and for subunitsubunit interactions in the self assembly of the polydisperse complexes. The specific surface exposed sequences used for interactions with unfolding proteins overlap with sequences used for interactions between aB crystallin subunits, suggesting that the accessibility of the interactive sequences has functional significance.