The regulatory α and β subunits of phosphorylase kinase directly interact with its substrate, glycogen phosphorylase.

Kinetic and catalytic mechanisms of protein kinases. Chem Rev (2001) 3.80

The isolation and crystallization of rabbit skeletal muscle phosphorylase b. J Biol Chem (1958) 3.40

The regulation of skeletal muscle phosphorylase kinase by Ca2+. J Biol Chem (1971) 2.07

Docking interactions in protein kinase and phosphatase networks. Curr Opin Struct Biol (2006) 2.00

Glycogen phosphorylase: control by phosphorylation and allosteric effectors. FASEB J (1992) 1.95

Cyclin-dependent kinases. Chem Rev (2001) 1.82

Reversible stimulation of muscle phosphorylase b kinase by low concentrations of calcium ions. J Biochem (1967) 1.79

The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition. EMBO J (1997) 1.68

Substrate and docking interactions in serine/threonine protein kinases. Chem Rev (2007) 1.55

The muscle phosphorylase b kinase reaction. J Biol Chem (1958) 1.52

Phosphorylase kinase: the complexity of its regulation is reflected in the complexity of its structure. Front Biosci (1999) 1.50

Spatially separate docking sites on ERK2 regulate distinct signaling events in vivo. Curr Biol (2005) 1.46

An epitope proximal to the carboxyl terminus of the alpha-subunit is located near the lobe tips of the phosphorylase kinase hexadecamer. J Mol Biol (1994) 1.09

Role of T-loop phosphorylation in PDK1 activation, stability, and substrate binding. J Biol Chem (2005) 1.09

Synergistic activation by Ca2+ and Mg2+ as the primary cause for hysteresis in the phosphorylase kinase reactions. J Biol Chem (1981) 1.08

Proximal regions of the catalytic gamma and regulatory beta subunits on the interior lobe face of phosphorylase kinase are structurally coupled to each other and with enzyme activation. J Mol Biol (1997) 1.06

The role of calcium ions, calmodulin and troponin in the regulation of phosphorylase kinase from rabbit skeletal muscle. Eur J Biochem (1980) 1.05

A Ca(2+)-dependent global conformational change in the 3D structure of phosphorylase kinase obtained from electron microscopy. Structure (2002) 1.03

Isolation and physicochemical properties of active complexes of rabbit muscle phosphorylase kinase. J Biol Chem (1982) 1.03

Kinetic mechanism and specificity of the phosphorylase kinase reaction. J Biol Chem (1978) 0.97

Catalytic mechanism of phosphorylase kinase probed by mutational studies. Biochemistry (1999) 0.95

The structure of phosphorylase kinase holoenzyme at 9.9 angstroms resolution and location of the catalytic subunit and the substrate glycogen phosphorylase. Structure (2009) 0.91

The regulatory alpha subunit of phosphorylase kinase may directly participate in the binding of glycogen phosphorylase. Biochemistry (Mosc) (2002) 0.87

Allosteric nucleotide specificity of phosphorylase kinase: correlation of binding, conformational transitions, and activation. Utilization of lin-benzo-ADP to measure the binding of other nucleoside diphosphates, including the phosphorothioates of ADP. J Biol Chem (1988) 0.87

Activation of muscle phosphorylase b kinase by Mg++. Biochem Biophys Res Commun (1968) 0.85

Analysis of the surface topography of glycogen phosphorylase a: implications for metabolic interconversion and regulatory mechanisms. Can J Biochem (1979) 0.83

A kinetic re-interpretation of the regulation of rabbit skeletal-muscle phosphorylase kinase activity by Ca2+ and phosphorylation. Biochem J (1992) 0.82

Divalent cations but not other activators enhance phosphorylase kinase's affinity for glycogen phosphorylase. Biochemistry (1996) 0.81

Revisiting protein kinase-substrate interactions: Toward therapeutic development. Sci Signal (2016) 0.81

Enzyme kinetics of muscle glycogen phosphorylase b. Biochemistry (2007) 0.80

Affinity labeling of rabbit skeletal muscle phosphorylase kinase by 5'-(p-fluorosulfonylbenzoyl) adenosine. FEBS Lett (1982) 0.80

The role of mangesium in muscle phosphorylase kinase activity. Biochim Biophys Acta (1972) 0.80

[Inhibition of the phosphorylase kinase activity by ATP analogs and their binding to the enzyme subunits]. Biokhimiia (1978) 0.79

Mutational analyses of the metal ion and substrate binding sites of phosphorylase kinase gamma subunit. Biochemistry (1994) 0.78

Structural features contributing to complex formation between glycogen phosphorylase and phosphorylase kinase. Biochemistry (1999) 0.77

A recombinant form of the catalytic subunit of phosphorylase kinase that is soluble, monomeric, and includes key C-terminal residues. Arch Biochem Biophys (1999) 0.77

Site-directed mutants of glycogen phosphorylase are altered in their interaction with phosphorylase kinase. Biochemistry (2000) 0.77

Physicochemical changes in phosphorylase kinase induced by its cationic activator Mg(2+). Protein Sci (2013) 0.77

Kinetic characterization of the double mutant R148A/E182S of glycogen phosphorylase kinase catalytic subunit: the role of the activation loop. J Protein Chem (2000) 0.76

Solution conformations of the N-terminal CNBr fragment of glycogen phosphorylase and its interaction with calmodulin. Biochim Biophys Acta (1991) 0.76