The regulation of AMP-activated protein kinase by phosphorylation.

By S. Stein, A. Woods, N. A. Jones, M. Davison, David Carling. Biochemical Journal, 2000

623 citations recorded by the source corpus.

Subfields: Molecular Biology, Surgery

View Paper: https://www.semanticscholar.org/paper/9b18d819e0c61cdb627a9b03a56721e56652b5ed

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. D. Hardie
2. R. Shaw
3. David M. Sabatini
4. Michael Pollak
5. S. Hawley
6. David Carling
7. B. Manning
8. J. Scott

In Surgery

1. D. Hardie
2. R. Shaw
3. Michael Pollak
4. S. Hawley
5. David Carling
6. K. Green
7. J. Scott
8. B. Kahn

Citations in the corpus

• Metformin inhibits mammalian target of rapamycin-dependent translation initiation in breast cancer cells. (2007, background): “AMPK requires an allosteric change induced by AMP, as well as phosphorylation on Thr(172) within the catalytic domain of the a subunit (21, 22).”
• Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase (2002, background): “Phosphorylation of this residue is essential for activation of AMP”
• CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations. (2004, methodology): “(32); in c, the cells were harvested by rapid or slow lysis and the assays were conducted at 200 μM AMP.”
• The AMP-activated protein kinase AAK-2 links energy levels and insulin-like signals to lifespan in C. elegans. (2004, background): “To determine whether AAK-2 possesses AMPK activity, we asked whether it can phosphorylate a classical AMPK substrate, the SAMS peptide, and whether it is regulated by AMP and phosphorylation (Davies et al. 1989; Stein et al. 2000).”
• TSC2 mediates cellular energy response to control cell growth and survival. (2003, neutral): “These data further support the (Scott et al., 2002; Stein et al., 2000).”
• Phosphorylation and activation of heart PFK-2 by AMPK has a role in the stimulation of glycolysis during ischaemia. (2000, neutral): “The constructs encoding wild-type and mutant His6–PFK-2 [17], and α1, α2, β1 and γ1 AMPK subunits [34] have been described.”
• The LKB1 tumor suppressor negatively regulates mTOR signaling. (2004, background): “As seen in Figure 1B, loop of AMPK, a modification that is absolutely required for AMPK catalytic activity (Stein et al., 2000).”
• AMP‐activated protein kinase: the energy charge hypothesis revisited (2001, background): “which phosphorylates a threonine residue (Thr-172) within the ``activation loop'' of the kinase domain.((18,19)) AMP promotes this phosphorylation both by binding to dephospho-AMPK and making it a better substrate, and by activating AMPKK itself.”
• Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase (2002, background): “The phosphorylation of Thr 172 in αAMPK is associated with activation of both the α1 and α2 subunits of AMPK (ref”
• AMP-activated protein kinase: an energy sensor that regulates all aspects of cell function. (2011, background): “…serine/threonine kinase domain at the N terminus; as for many protein kinases, these only have significant activity when phosphorylated by upstream kinases (described below) at a conserved threonine residue within the activation loop (Thr 172 in human a1) (Hawley et al. 1996; Stein et al. 2000).”