GSK3 takes centre stage more than 20 years after its discovery.

By S. Frame, P. Cohen. Biochemical Journal, 2001

1,516 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/19911bd33a6a7fe2fa5e7374a0fb99a012965ec5

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Citations in the corpus

AKT/PKB signaling: navigating downstream. (2007, positive): “Our discussion is specific to Akt, but the criteria are similar to that put forward for other protein kinases (Frame and Cohen, 2001).”
Ras, PI(3)K and mTOR signalling controls tumour cell growth (2006, background): “Glycogen synthase kinase-3 (GSK-3) is a highly conserved protein kinase that is inhibited by AKT phosphorylatio”
GSK-3: tricks of the trade for a multi-tasking kinase (2003, background): “We now know that, beyond its role in glycogen metabolism, GSK3 acts as a downstream regulatory switch that determines the output of numerous signalling pathways initiated by diverse stimuli (reviewed in Frame and Cohen, 2001; Grimes and Jope, 2001; Woodgett, 2001).”
LTP inhibits LTD in the hippocampus via regulation of GSK3beta. (2007, positive): “Numerous potential substrates for GSK3  have been identified, including several different transcription factors, metabolic enzymes, proteins that bind to microtubules, and components of the machinery involved in cell division and cell adhesion (Doble and Woodgett, 2003; Frame and Cohen, 2001).”
Capture of authentic embryonic stem cells from rat blastocysts. (2008, positive): “GSK3 is a central node for negative modulation of a range of anabolic processes and generally acts to suppress cellular biosynthetic capacity (Frame and Cohen, 2001).”
Generation of regionally specified neural progenitors and functional neurons from human embryonic stem cells under defined conditions. (2012, background): “Accordingly, chemical inhibition of GSK3 can activate canonical WNT signaling and induce expression of downstream WNT targets (Frame and Cohen, 2001).”
Glycogen synthase kinase-3 (GSK3): regulation, actions, and diseases (2014, background): “Phosphorylation on Tyr216-GSK3β and Tyr279-GSK3α is required for maximal activity (Hughes et al., 1993; Frame and Cohen, 2001).”
Mechanisms of activation of the transcription factor Nrf2 by redox stressors, nutrient cues, and energy status and the pathways through which it attenuates degenerative disease (2015, positive): “GSK-3 is a key regulator of glycogen metabolism that inhibits glycogen synthase, as well as being a regulator of insulin signaling, cell fate specification in embryo development, and cell cycle and apoptosis (reviewed in [293, 294]).”
Glycosylation and stabilization of programmed death ligand-1 suppresses T-cell activity (2016, neutral): “It was later shown to be a key component of the Wnt signalling pathway, which plays important roles in embryonic development and tumorigenesis 17,18 .”
Role that phosphorylation of GSK3 plays in insulin and Wnt signalling defined by knockin analysis (2005, background): “In order for GSK3 to phosphorylate many of its substrates, including glycogen synthase, the substrate is required to be phosphorylated at a priming site, lying four residues C-terminal to the Ser/Thr residue phosphorylated by GSK3 (Frame and Cohen, 2001; Roach, 2002).”
Functional redundancy of GSK-3α and GSK-3β in wnt/β-catenin signaling shown by using an allelic series of embryonic stem cell lines (2007, background): “Still, as Frame and Cohen outlined in their 7 criteria for establishing a protein as a bona fide physiological substrate of GSK-3 (Frame and Cohen, 2001), one of the burdens of proof required for substrate validation is to show that the substrate cannot be phosphorylated on putative target residues…”