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Protein-protein interaction is one of the key regulatory mechanisms for controlling protein function in various cellular processes.
Much attention has been lavished on these molecular marvels with the hope of understanding and harnessing their chemistry for novel biochemical transformations including coupling peptides from synthetic or biological origins and controlling protein function.
The characterization of this unique LQT2 mutant Kv11.1 channel may provide structural information about the Kv11.1 C-terminus, and provide insight related to the process of proteasomal degradation of LQT2 mutants, and the importance of this mechanism in controlling protein function [30], [31].
In order to realize these applications through controlling protein function by optochemically triggered translocation into the nucleus, a tight photoactivatable nuclear entry mechanism is needed.
Accumulating evidence indicates that the reduction and rearrangement of disulfide bonds constitutes a mechanism controlling protein function on the cell surface (Hogg, 2003).
Consequently, protein kinases, which are responsible for the phosphorylations, play an important role in controlling protein function, cellular machine regulation and information transfer through cell signaling pathways.
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Discoveries based on these methods have shed light on the importance of many PTMs in controlling protein functions, signaling networks and cell fates in hPSCs.
We went on to show that these binders recognize the respective fluorescent protein in cultured cells, as well as in cells of Drosophila and zebrafish embryos, and that the binders can be functionalized in order to modify and control protein function.
Three sirtuins (SIRT3, SIRT4, and SIRT5) primarily localized in mitochondria remove distinct acyl-groups from lysine side chains, which control protein function.
Optogenetics, the use of genetically encoded tools to control protein function with light, can generate localized changes in signaling within living cells and animals.
Specific patterns of mono- or poly-ubiquitylation are used by the cell to control protein function or stability.
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