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Engineering Hydrology By Jayarami Reddy.pdf [2022-Latest]







Category:Hydrology Category:Erosion Category:Water Category:Water management in engineeringQ: Is it possible to override or extend a grid cell? I know that in Extjs a grid is a container. But in Extjs 3.4.1 I can only extend it, not override it (at least that is what I have read so far). Is it possible to override a grid cell? If so, could anyone point me to the right documentation (in particular an example of a working override)? If not, what is the alternative? A: You can override a cell renderer by providing a custom render function. var cellRenderer = function(value, metaData, record, rowIndex, colIndex, store, view) { ... } MyApplication.grid.getView().getCellRenderer('Name').setRenderer(cellRenderer); In the documentation they point to the setRenderer method that indicates how to supply a renderer function. ) / 8 ) . L e t k = 1 2 4 - q . I s k a c o m p o s i t e n u m b e r ? T r u e L e t d = 3 0 5 - - 5 8 . I s d a c o m p o s i t e n u m b e r ? F a l s e L e t k ( d ) = - 3 * d * * 3 - 3 * d * * 2 + 2 * d . L e t 01e38acffe Category:Hydrologists Category:21st-century Indian physicists Category:Living people Category:Year of birth missing (living people) Category:Savitribai Phule Pune University alumniPost-translational modifications and chaperones are involved in cytosolic misfolding of the human sulfated glycoprotein hormone alpha-subunit. The human α-subunit of human chorionic gonadotropin (α-hCG) and human placental lactogen (α-hPL) have been structurally characterized by proteomic analysis and the folding of the hormone-subunit complexes at low pH was characterized by FTIR spectroscopy. The post-translational modifications and chaperones required for the folding of these hormones in the cytosol are still not fully understood. The disulfide bonds of α-hCG and α-hPL are exclusively formed in the endoplasmic reticulum. The α-hCG and α-hPL structures show a high degree of similarity to the homologous hormone-subunit complexes from the rabbit and mouse. The α-hCG and α-hPL structures display differences in the secondary structures due to differences in glycosylation, the presence of two disulfide bonds in the α-hCG structure, and the presence of different numbers of terminal sialic acids in the α-hPL structure. The human cytosolic isoform of glucose-regulated protein 78 (hGRP78) was identified as a chaperone that facilitates the folding of the hormone-subunit complexes. The α-hCG and α-hPL homologous complexes showed similar abilities to interact with hGRP78. In contrast, the folding of the α-hPL complex was more sensitive to the loss of the disulfide bonds and terminal sialic acids than the α-hCG complex. This finding suggests that hGRP78 might promote the folding of the α-hCG complex in the cytosol by unfolding the precursor, and to a lesser extent, by interacting with the preformed complex. The folding of the α-hPL and α-hCG complexes was partially inhibited by the addition of mild heat shock protein 90 (hsp90) inhibitors, compound 1 and N-Methyl-3-(1-adamantyl)-acrylamide (AMAA). In conclusion, the α-hCG and α-hPL complexes are


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