Unless "header.h" is declared in `srcs`, target won't be rebuilt on change (with no warning) #473

This change also involves reformatting code that is confusing, but only turns off this feature according to Constants.HARD_DISABLE_CC_INCLUDE_SCANNING so invert this bit to make Bazel the same as before there is.

I can imagine that sandbox eventually replaces traditional scanner, but I do not think there will be Bazel (at least in C ++ code); sandboxing is still on all platforms It is not supported.

If you change baz library, just rebuild baz and reinstall baz in omega handler subproject. Throwing an observer in the process (eg npm script like 'watch' npm run build 'src - wait = 5) will make your build process richer and improve local development experience. One thing I really like about this is that it only works when they need it. It does not even need an incremental compiler to implement it. If the source file has not been updated, you do not need to regenerate the target file. To understand this, compare the last modification time of the source file with the comparison time of the target file. You can see simple integration into existing tools like tsc or npm. You do not have to wait (or create your own wrapper) until you create a wrapper in the codebase build tool.

The SRC protein is a tyrosine kinase. Kinases are enzymes that transfer phosphate groups to target molecules. An important aspect of this process is that removal / addition of phosphate alters biomolecules and is an important way to regulate cell viability. The phosphate addition / removal process acts as an on / off switch to control the activity of the target molecule. The src protein changes several target molecules, transfers signals to the nucleus, and helps regulate cells.

First of all, Sprycel is not a "competitor" of Gleevec. For some reason, Sprycel is suitable for patients who did not respond to Gleevec. Sprycel targets BCR-ABL and other molecules (there may be more than 200 dasatinib targets, but here Src kinase is the major player). Therefore, Sprycel is more toxic than Gleevec only for BCR-ABL (and the other two proteins). Unfortunately, when Sprycel is to be used, the inhibition of BCR-ABL is not sufficient and that other molecules (mainly Src kinase) also need to be targeted. This means that CML can not be selected because it proceeds in much the same way as other cancers in terms of diversity of acquired mutations and other "errors" in the cell.

Src kinases are linked to each other by a flexible linker region and recognize their target proteins through the SH2 and SH3 domains linked to the catalytic domain (FIG. 3-24b). In the absence of an activation signal, these domains bind to the kinase domain leaving it in the inactive conformation (FIGS. 3 to 26): the SH2 domain binds to inhibitory phosphate on tyrosine. Figure 3-24 Conserved protein kinase catalytic domain (a) Signal expressed in cells of the immune system The catalytic domain of Lck, a tyrosine kinase, is typical of highly conserved catalytic domains of all protein kinases. It is structurally divided into two leaves. Although the amino-terminal (upper) leaf (light gray) is almost completely formed by the β-chain, a single α helix (C-helix, red) and a carboxy terminal (lower) leaf (dark gray) alpha Almost completely formed by helix