Structural insight into the autoinhibition mechanism of AMP-activated protein kinase

[1]  D. Hardie,et al.  Edinburgh Research Explorer The glycogen-binding domain on the AMPK beta subunit allows the kinase to act as a glycogen sensor , 2008 .

[2]  B. Kemp,et al.  Thienopyridone drugs are selective activators of AMP-activated protein kinase beta1-containing complexes. , 2008, Chemistry & biology.

[3]  M. Gu,et al.  Small Molecule Antagonizes Autoinhibition and Activates AMP-activated Protein Kinase in Cells* , 2008, Journal of Biological Chemistry.

[4]  B. Viollet,et al.  Mechanism of Action of A-769662, a Valuable Tool for Activation of AMP-activated Protein Kinase* , 2007, Journal of Biological Chemistry.

[5]  R. Heath,et al.  Defining the Mechanism of Activation of AMP-activated Protein Kinase by the Small Molecule A-769662, a Member of the Thienopyridone Family* , 2007, Journal of Biological Chemistry.

[6]  D. Hardie,et al.  AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy , 2007, Nature Reviews Molecular Cell Biology.

[7]  David Carling,et al.  Structural basis for AMP binding to mammalian AMP-activated protein kinase , 2007, Nature.

[8]  Liang Tong,et al.  Crystal structure of the heterotrimer core of Saccharomyces cerevisiae AMPK homologue SNF1 , 2007, Nature.

[9]  Randy J. Read,et al.  Phaser crystallographic software , 2007, Journal of applied crystallography.

[10]  John Kuriyan,et al.  Structural Basis for the Inhibition of Tyrosine Kinase Activity of ZAP-70 , 2007, Cell.

[11]  D. Carling,et al.  Investigating the mechanism for AMP activation of the AMP-activated protein kinase cascade. , 2007, The Biochemical journal.

[12]  Lawrence Shapiro,et al.  Crystal Structures of the Adenylate Sensor from Fission Yeast AMP-Activated Protein Kinase , 2007, Science.

[13]  F. Ross,et al.  Regulation of AMP‐activated protein kinase by a pseudosubstrate sequence on the γ subunit , 2007 .

[14]  D. Hardie,et al.  AMP-activated protein kinase as a drug target. , 2007, Annual review of pharmacology and toxicology.

[15]  Tao Pang,et al.  Conserved α-Helix Acts as Autoinhibitory Sequence in AMP-activated Protein Kinase α Subunits* , 2007, Journal of Biological Chemistry.

[16]  John Kuriyan,et al.  Protein-protein interactions in the allosteric regulation of protein kinases. , 2006, Current opinion in structural biology.

[17]  E. Mandelkow,et al.  Structural Variations in the Catalytic and Ubiquitin-associated Domains of Microtubule-associated Protein/Microtubule Affinity Regulating Kinase (MARK) 1 and MARK2* , 2006, Journal of Biological Chemistry.

[18]  L. Kifle,et al.  Identification and characterization of a small molecule AMPK activator that treats key components of type 2 diabetes and the metabolic syndrome. , 2006, Cell metabolism.

[19]  A. Prescott,et al.  The ubiquitin-associated domain of AMPK-related kinases regulates conformation and LKB1-mediated phosphorylation and activation. , 2006, The Biochemical journal.

[20]  S. Berger,et al.  Structure and dimerization of the kinase domain from yeast Snf1, a member of the Snf1/AMPK protein family. , 2006, Structure.

[21]  L. Tong,et al.  Crystal structure of the protein kinase domain of yeast AMP-activated protein kinase Snf1. , 2005, Biochemical and biophysical research communications.

[22]  A. Edelman,et al.  Calmodulin-dependent protein kinase kinase-beta is an alternative upstream kinase for AMP-activated protein kinase. , 2005, Cell metabolism.

[23]  B. Kemp,et al.  AMP-activated Protein Kinase β Subunit Tethers α and γ Subunits via Its C-terminal Sequence (186–270)* , 2005, Journal of Biological Chemistry.

[24]  D. Hardie,et al.  AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism. , 2005, Cell metabolism.

[25]  Kevin Cowtan,et al.  research papers Acta Crystallographica Section D Biological , 2005 .

[26]  Susan S. Taylor,et al.  Regulation of protein kinases; controlling activity through activation segment conformation. , 2004, Molecular cell.

[27]  D. Hardie,et al.  CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations. , 2004, The Journal of clinical investigation.

[28]  David Carling,et al.  The AMP-activated protein kinase cascade--a unifying system for energy control. , 2004, Trends in biochemical sciences.

[29]  D. Carling,et al.  Mammalian AMP-activated protein kinase: functional, heterotrimeric complexes by co-expression of subunits in Escherichia coli. , 2003, Protein expression and purification.

[30]  D. Vertommen,et al.  Identification of Phosphorylation Sites in AMP-activated Protein Kinase (AMPK) for Upstream AMPK Kinases and Study of Their Roles by Site-directed Mutagenesis* , 2003, Journal of Biological Chemistry.

[31]  Randy J Read,et al.  Electronic Reprint Biological Crystallography Phenix: Building New Software for Automated Crystallographic Structure Determination Biological Crystallography Phenix: Building New Software for Automated Crystallographic Structure Determination , 2022 .

[32]  J. Kuriyan,et al.  The Conformational Plasticity of Protein Kinases , 2002, Cell.

[33]  B. Kemp,et al.  Functional Domains of the α1 Catalytic Subunit of the AMP-activated Protein Kinase* , 1998, The Journal of Biological Chemistry.

[34]  Z. Otwinowski,et al.  Processing of X-ray diffraction data collected in oscillation mode. , 1997, Methods in enzymology.

[35]  S. Hawley,et al.  Characterization of the AMP-activated Protein Kinase Kinase from Rat Liver and Identification of Threonine 172 as the Major Site at Which It Phosphorylates AMP-activated Protein Kinase* , 1996, The Journal of Biological Chemistry.

[36]  D. Hardie,et al.  5′‐AMP inhibits dephosphorylation, as well as promoting phosphorylation, of the AMP‐activated protein kinase. Studies using bacterially expressed human protein phosphatase‐2Cα and native bovine protein phosphatase‐2Ac , 1995, FEBS letters.

[37]  L. Riechmann,et al.  An antibody VH domain with a lox‐Cre site integrated into its coding region: bacterial recombination within a single polypeptide chain , 1995, FEBS letters.

[38]  D. Carling,et al.  Tissue distribution of the AMP-activated protein kinase, and lack of activation by cyclic-AMP-dependent protein kinase, studied using a specific and sensitive peptide assay. , 1989, European journal of biochemistry.

[39]  K. A. Quayle.  Regulation of rat liver acetyl CoA carboxylase , 1986 .

[40]  R. Roskoski.  Assays of protein kinase. , 1983, Methods in enzymology.

[41]  K. Kim,et al.  Regulation of rat liver acetyl-CoA carboxylase. Regulation of phosphorylation and inactivation of acetyl-CoA carboxylase by the adenylate energy charge. , 1980, The Journal of biological chemistry.