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Recent biophysical analysis of the PRH protein has shown that it forms homo-oligomeric complexes in vivo and in vitro and that the proline-rich region of PRH forms a novel dimerization interface.
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There were 547 family data sets available for analysis of children's PRH.
We confirmed that the nuclear localization of the PRH F32E was not altered compared with wild-type PRH, using immunostaining experiments and confocal microscopy.
Quantitative estimates were made of the extent of the PRh damage (Table 3).
(iii) Could the impact of the PRh damage be reversed by additional training?
However, PRH-binding sites have not been identified and it is not known whether PRH binds to the Prh promoter and activates expression of the Prh gene directly or regulates this promoter in a more indirect fashion by, for example, binding to the other homeodomain proteins [ 88, 100].
Since a defect in binding TLE blocks repression as effectively as a defect in DNA binding, we conclude that most of the PRH-dependent repression observed at the pTK PRH promoter is TLE-dependent; however, it is possible that mutation of the Eh-1 domain might also affect the conformation of the PRH protein and hence also decrease the interaction of PRH with other PRH-interacting proteins.
We have now shown that the specific expression of miR-132 within the PRh impairs short-term recognition memory, a process known to be dependent on the activity of the PRh.
We hypothesized that treatment of the PRh with ChABC might recover the profound OR memory deficit described above.
HNF3 and GATA-4 bind and further activate expression of the Prh gene in liver cells [ 85].
Consequently, the final, updated D2 scores of the PRh rats were far lower than those of the control rats (t20 = 10.65, P< 0.001), though the PRh group scores were above chance (one-sample t-test, t11 = 3.48, P< 0.005).
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