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.
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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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