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Randall T. Moon

Researcher at University of Washington

Publications -  305
Citations -  54792

Randall T. Moon is an academic researcher from University of Washington. The author has contributed to research in topics: Wnt signaling pathway & Signal transduction. The author has an hindex of 119, co-authored 305 publications receiving 51964 citations. Previous affiliations of Randall T. Moon include Marine Biological Laboratory & Howard Hughes Medical Institute.

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Inhibition of β-catenin signaling respecifies anterior-like endothelium into beating human cardiomyocytes

TL;DR: The manipulation of signals that control embryonic patterning allows human pluripotent stem cells to be differentiated into endothelial subpopulations with distinct haematopoietic, angiogenic and cardiogenic potential.
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Canonical Wnt3a Modulates Intracellular Calcium and Enhances Excitatory Neurotransmission in Hippocampal Neurons

TL;DR: The results identify the Wnt3a protein and a member of its complex receptor at the membrane, the low density lipoprotein receptor-related protein 6 (LRP6) coreceptor, as key molecules in neurotransmission modulation and suggest cross-talk between canonical and Wnt/Ca2+ signaling in central neurons.
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The armadillo homologs β-catenin and plakoglobin are differentially expressed during early development of Xenopus laevis

TL;DR: The presence of multiple homologs of armadillo in Xenopus embryos and the differences in their patterns of expression suggest distinct roles for these proteins in processes affected by cell adhesion.
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Inhibition of protein kinase A phenocopies ectopic expression of hedgehog in the CNS of wild-type and cyclops mutant embryos.

TL;DR: The zebrafish hedgehog family members tiggy-winkle hedgehog and sonic hedgehog are involved in patterning the ventral CNS and proximal eye and it is shown that these hh activities are mediated by protein kinase A.
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Biogenesis of the avian erythroid membrane skeleton: receptor-mediated assembly and stabilization of ankyrin (goblin) and spectrin.

TL;DR: The existence in the detergent-soluble compartment of newly synthesized ankyrin and alpha- and beta-spectrin that are catabolized, rather than assembled, suggests that ankyr in and spectrin are synthesized in excess of available respective membrane binding sites, and that the assembly of these polypeptides, while rapid, is not tightly coupled to their synthesis.