By 24 hours p.i. the amount of ERC1 was 
observably diminished in DENV-2 infected cells and by 48 hours p.i. was barely detectable. PRAF2 accumulated most strongly in the cytoplasm of the mock infected cells, showing a punctate distribution, supporting the previous observation that the protein was localized to the ER and transGolgi network. By contrast, in DENV-2 infected cells, PRAF2 appeared to co-localize with the viral E protein at 24 hours p.i. and in the majority of infected cells was severely decreased in amount by 48 hours p.i.. In a similar fashion, the levels of CSTL1, MFN1, KPNA2 and UBE2S in DENV-2 infected were examined by IFA. However for CSTL1, MFN1 and UBE2S, the specific antibodies available could either not detect the proteins of interest or reacted non-specifically with other proteins. For KPNA2, there appeared to be no difference in the amount or localization during DENV-2 infection compared to mock infected cells at 24 and 48 hours p.i.. This may have been due to an interaction of the anti-KPNA2 antisera with the smaller product detected in the Western blot analysis of KPNA2, masking any overall decrease in KPNA2 amounts. The analysis supported the Western blot analysis in that proteins that were observed to be significantly decreased during infection by Western blot analysis were also observed to decrease in virus infected cells when examined by IFA. Proteins that showed a smaller decrease were found to be more difficult to visualize by IFA although this was also dependent on the availability of highly specific antibodies. The biological validation identified two proteins that were severely decreased in DENV-2 infected cells, ERC1 and PRAF2. The decrease in the amounts of these proteins may be a direct or indirect effect of virus replication. ERC1 has previously been identified to interact with the DENV NS5 protein in a yeast two hybrid screen which we have also observed using a highthroughput co-immunoprecipitation analysis. siRNA knockdown of ERC1 inhibited the replication of a DENV replicon suggesting that ERC1 is required for efficient DENV replication which appears to contradict this study showing that ERC1 is decreased during DENV infection. However it may be that ERC1 plays different roles at various stages of the DENV lifecycle which illustrates how the use of different high-throughput approaches can complement one another to increase our understanding of the role of cellular proteins in the DENV lifecycle. Medicinal use of water in chronic kidney disease has gained research interest lately, as established efforts to retard CKD progression remain far from 20(S)-Notoginsenoside-R2 satisfactory. Epidemiological data associating fluid intake or urine volume with GFR decline in humans have not been fully conclusive. Nonetheless, there is increasing evidence linking fluid intake, vasopressin suppression and osmotic control with CKD and ADPKD progression. Kidney excretion is adjusted according to water and dietary solute intake, as well as water and solute losses by lungs, skin, and the gastrointestinal tract. The required urine volume can be determined by dividing the daily osmolar excretion, to maintain the body��s solute content at 9-methoxycamptothecine steady state, by the maximal urine osmolality, with failing kidneys losing capacity to concentrate urine maximally.