One of the common methods for detecting LRRK2 phosphorylation is immunoblotting, typically after immunoprecipation. The complexities of this methodology make it highly impractical for the processing and analysis of large sample Vorinostat numbers typically associated with screening experiments. The TR-FRET cellular assay reported here is in a fully homogenous format without washing, lysate transfer, or separation procedures. Cells transduced with BacMam LRRK2-GFP can be plated onto a 384-well assay plate, treated as desired and then incubated with 6 X lysis buffer containing Tb-labeled detection antibody added directly to the wells. To further simplify the procedure, we demonstrated that cells can be transduced, cryopreserved, later thawed and used directly to run the assay without the need for culturing. This indicates that one can perform a large batch transduction and cryopreserve the cells for screening applications at a later time, which will reduce the time, labor and day-to-day variables. We profiled 1120 compounds of the TocriscreenTM Mini library to gain insight into the biology of Ser935 phosphorylation and demonstrate the utility of the TR-FRET cellular assay in screening. Using a maximal inhibition threshold of 50%, we observed the previously identified inhibitors of LRRK2 SP600125, indirubin-39-monoxime and ROCK inhibitor Y-27632 induced dephosphorylation of Ser935, which increased confidence in our assays. In addition to compounds with known LRRK2 inhibitory activity, we identified several novel LRRK2 kinase inhibitors from this screen. GW441756 is a known TrkA inhibitor and has some degree of structure similarity to GW5074. Here we show GW441756 can inhibit the phosphorylation of LRRK2 on Ser935 in cells by both TR-FRET assays and IP-Western. We further confirmed that GW441756 is a LRRK2 kinase inhibitor in the TR-FRET LRRK2 in vitro kinase assay with an IC50 of 320 nM. Interestingly, we did not observe in vivo dephosphorylation of Ser935 with the PKC inhibitors GF109203X and Ro31-8220, which were present in the ARRY-142886 MEK inhibitor Tocriscreen library and identified previously to inhibit LRRK2 autophosphorylation in vitro. Interestingly, we observed that 5 out of the top 16 compounds Bay 11-7085, Bay 11-7821, IKK16, Ro106-9920 and TPCA-1 intersect with the NFkB pathway. HCMV gene expression in endogenously infected glioblastoma does not fit the classic definition of latency since most GBM samples described to date exhibit expression of IE1, a lytic gene. A more suitable definition of HCMV infection in glioblastoma has been postulated as a chronic infection with viral gene expression but no cytopathic effect. Our study aimed to assess patterns of long-term HCMV infection in glioblastoma cell lines and primary GSC cultures, which could serve as a model for studying the effects of HCMV endogenous infection in GBM pathogenesis.