Matches in Nanopublications for { ?s ?p "This observation, together with the very rapid kinetics of GSK3-beta phosphorylation in response to aortic coarctaction, supports the hypothesis that melusin selectively senses the biomechanical stimuli. In contrast to other kinases, GSK3-beta is highly active in unstimulated cells and becomes inactivated by phosphorylation of serine 9 in response to several stimuli28. Recent studies have shown that this inactivation is required for cardiac hypertrophy. In cardiomyocytes, active GSK3-beta phosphorylates the transcription factors NF-AT and GATA4, inducing their translocation from the nucleus to the cytoplasm and thus inhibiting their transcriptional activity25-27. In addition, active GSK3-beta also induces inhibition of elF2B, a principal initiation factor regulating protein synthesis." ?g. }
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- _4 value "This observation, together with the very rapid kinetics of GSK3-beta phosphorylation in response to aortic coarctaction, supports the hypothesis that melusin selectively senses the biomechanical stimuli. In contrast to other kinases, GSK3-beta is highly active in unstimulated cells and becomes inactivated by phosphorylation of serine 9 in response to several stimuli28. Recent studies have shown that this inactivation is required for cardiac hypertrophy. In cardiomyocytes, active GSK3-beta phosphorylates the transcription factors NF-AT and GATA4, inducing their translocation from the nucleus to the cytoplasm and thus inhibiting their transcriptional activity25-27. In addition, active GSK3-beta also induces inhibition of elF2B, a principal initiation factor regulating protein synthesis." provenance.
- _5 value "This observation, together with the very rapid kinetics of GSK3-beta phosphorylation in response to aortic coarctaction, supports the hypothesis that melusin selectively senses the biomechanical stimuli. In contrast to other kinases, GSK3-beta is highly active in unstimulated cells and becomes inactivated by phosphorylation of serine 9 in response to several stimuli28. Recent studies have shown that this inactivation is required for cardiac hypertrophy. In cardiomyocytes, active GSK3-beta phosphorylates the transcription factors NF-AT and GATA4, inducing their translocation from the nucleus to the cytoplasm and thus inhibiting their transcriptional activity25-27. In addition, active GSK3-beta also induces inhibition of elF2B, a principal initiation factor regulating protein synthesis." provenance.