The SCX fractions in which most Meth-R peptides were detected (not shown). This likely contributed to the analyte complexity, limiting the number of Meth-R peptides identified. However, these data brought to our attention key physico-chemical properties of Meth-R tryptic peptides. Arginines prone to be methylated are likely to be fully exposed to solvent and therefore most often embedded within se
Channels at glutamatergic synapses (Maximov Bezprozvanny 2002). In the postsynaptic compartment, NL1 may bind through cytoplasmic PDZ-domain interactions to PSD95 and thereby recruit NMDA-Rs to glutamatergic synapses (Irie et al. 1997). Although the relevance of PSD95 or other scaffolding molecules for the NL1-mediated synaptic recruitment of NMDA-Rs remains to be tested, a conceptually similar
Level. Additionally, the translational start sites of 52 proteins were confirmed, and 22 proteins were validated through extension of the translational start sites based on N-terminus-derived peptides. There are 103 secreted proteins that have not been reported in previous studies on the mycobacterial secretome and are unique to our study. The physicochemical characteristics of the secreted protei
F the nematode Caenorhabditis elegans. Philos. Trans. R. Soc. Lond. B Biol. Sci. 1986; 314:1?40. Wilson SI, Shafer B, Lee KJ, Dodd J. A molecular program for contralateral trajectory: Rig-1 control by LIM homeodomain transcription factors. Neuron. 2008; 59:413?4. [PubMed: 18701067] Winberg ML, Mitchell KJ, Goodman CS. Genetic analysis of the mechanisms controlling target selection: complementary a
Obtain a more comprehensive view on the molecular networks underlying neurite outgrowth. Although it cannot be formally ruled out, several lines of evidence exist to assure that our overexpression approach did not yield unspecific results. First, proteins with an established role in neuronal differentiation and function but not involved in neurite initiation or elongation showed no apparent effect
N animal model of pneumonia. We hypothesized that during P. aeruginosa infection adenoviral CaM gene transfer would counteract actions of the E3 ligase FBXL2, thereby preserving CCT and surfactant levels. In mice, the PA103 pathogen decreased CCT levels (Fig. 7A and B), thereby reducing surfactant phosphatidylcholine (Fig. 7C) needed to stabilize lung function (39). Mice infected with PA103 also e