The general importance of caveolae to cell signalling can be partially explained by the cav-1 scaffolding domain interacting with and regulating proteins which interact with and transduce G-coupled receptor effects, including, α-subunits of trimeric G proteins, PLC, the G protein RhoA and its downstream effector Rho kinase, and Ca2+-sensitive PKC isoforms.
In this time lapse, preferential direction of growth of the protofibril can be explained by the fact that it was interacting with another fibrillar structure that could influence the way it was elongating.
Its involvement in HCV replication may be explained by the fact that it also interacts with the 3′-UTR of HCV RNA and prevents its degradation, in addition to promoting the linkage between the 5′-UTR and 3′-UTR (Kumar et al., 2013).
The above findings might be partly explained by the fact that PB1 physically interacts with PB2 and PA for the formation of viral polymerase complex [60].
These findings might be explained by the effect of two different, but interacting mechanisms: First, a general N1 reduction takes place which is directly caused by the brain damage and which is larger in those patients with larger brain lesions and more severe impairments, i.e. the severe aphasia group.
Furthermore, the sex-bias we observed in the activity of PARP-1 may be partially explained by the ability of PARP-1 to interact with estradiol and estrogen receptor α (ER α).
The absence of a direct role of Hat1p in the efficiency and timing of these origins could be explained by the possibility that Hat1p/Hat2p does not interact with ORC at these origins and that the S-phase recruitment of Hat1p is solely mediated by Hat1p/Hat2p-Hif1p.
This can be explained by the fact that the SUMO does not interact with cellulose, what was confirmed by the negative controls (results not shown).
The lack of complementation could be explained by the inability of HsCdc7 and HsDbf4 to interact with their yeast counterparts.
This could be explained by the fact that when irradiated, l-Trp could interact with RB resulting in products, which absorb at 410 nm (Fig. 2 6b)).
