Published in Structure on January 01, 2002
Evidence for the location of the allosteric activation switch in the multisubunit phosphorylase kinase complex from mass spectrometric identification of chemically crosslinked peptides. J Mol Biol (2006) 1.07
Ca2+-induced structural changes in phosphorylase kinase detected by small-angle X-ray scattering. Protein Sci (2005) 1.02
Cryoelectron microscopy reveals new features in the three-dimensional structure of phosphorylase kinase. Protein Sci (2005) 0.97
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
Electrostatic changes in phosphorylase kinase induced by its obligatory allosteric activator Ca2+. Protein Sci (2007) 0.88
Structural evidence for co-evolution of the regulation of contraction and energy production in skeletal muscle. J Mol Biol (2008) 0.86
Mass spectrometry reveals differences in stability and subunit interactions between activated and nonactivated conformers of the (αβγδ)4 phosphorylase kinase complex. Mol Cell Proteomics (2012) 0.82
Single molecule analyses of the conformational substates of calmodulin bound to the phosphorylase kinase complex. Protein Sci (2007) 0.80
Structure and location of the regulatory β subunits in the (αβγδ)4 phosphorylase kinase complex. J Biol Chem (2012) 0.80
Physicochemical changes in phosphorylase kinase associated with its activation. Protein Sci (2008) 0.79
Expressed phosphorylase b kinase and its alphagammadelta subcomplex as regulatory models for the rabbit skeletal muscle holoenzyme. Biochemistry (2009) 0.78
A review of methods used for identifying structural changes in a large protein complex. Methods Mol Biol (2012) 0.77
A model for activation of the hexadecameric phosphorylase kinase complex deduced from zero-length oxidative crosslinking. Protein Sci (2015) 0.77
Activation of Phosphorylase Kinase by Physiological Temperature. Biochemistry (2015) 0.75
The regulatory α and β subunits of phosphorylase kinase directly interact with its substrate, glycogen phosphorylase. Biochem Biophys Res Commun (2016) 0.75
Mass Spectrometric Analysis of Surface-Exposed Regions in the Hexadecameric Phosphorylase Kinase Complex. Biochemistry (2015) 0.75
Dynamic assembly of MinD on phospholipid vesicles regulated by ATP and MinE. Proc Natl Acad Sci U S A (2002) 3.06
GroEL as a molecular scaffold for structural analysis of the anthrax toxin pore. Nat Struct Mol Biol (2008) 1.91
The 13 angstroms structure of a chaperonin GroEL-protein substrate complex by cryo-electron microscopy. J Mol Biol (2005) 1.19
Nucleotide-induced switch in oligomerization of the AAA+ ATPase ClpB. Protein Sci (2004) 1.17
Evidence for the location of the allosteric activation switch in the multisubunit phosphorylase kinase complex from mass spectrometric identification of chemically crosslinked peptides. J Mol Biol (2006) 1.07
The calmodulin-binding domain of the catalytic gamma subunit of phosphorylase kinase interacts with its inhibitory alpha subunit: evidence for a Ca2+ sensitive network of quaternary interactions. J Biol Chem (2002) 1.04
Ca2+-induced structural changes in phosphorylase kinase detected by small-angle X-ray scattering. Protein Sci (2005) 1.02
Calmodulin-induced structural changes in endothelial nitric oxide synthase. FEBS Lett (2012) 0.98
Cryoelectron microscopy reveals new features in the three-dimensional structure of phosphorylase kinase. Protein Sci (2005) 0.97
CrossSearch, a user-friendly search engine for detecting chemically cross-linked peptides in conjugated proteins. Mol Cell Proteomics (2008) 0.96
Three-dimensional structure of phosphorylase kinase at 22 A resolution and its complex with glycogen phosphorylase b. Structure (2002) 0.96
Differential inhibition of cytosolic PEPCK by substrate analogues. Kinetic and structural characterization of inhibitor recognition. Biochemistry (2008) 0.94
Protein Interactions Captured by Chemical Cross-linking: One-Step Cross-linking with Formaldehyde. CSH Protoc (2007) 0.91
Caspase-3 dependent cleavage and activation of skeletal muscle phosphorylase b kinase. Mol Cell Biochem (2005) 0.88
Electrostatic changes in phosphorylase kinase induced by its obligatory allosteric activator Ca2+. Protein Sci (2007) 0.88
Structural evidence for co-evolution of the regulation of contraction and energy production in skeletal muscle. J Mol Biol (2008) 0.86
Mass spectrometry reveals differences in stability and subunit interactions between activated and nonactivated conformers of the (αβγδ)4 phosphorylase kinase complex. Mol Cell Proteomics (2012) 0.82
The regulatory beta subunit of phosphorylase kinase interacts with glyceraldehyde-3-phosphate dehydrogenase. Biochemistry (2008) 0.80
Following Natures Lead: On the Construction of Membrane-Inserted Toxins in Lipid Bilayer Nanodiscs. J Membr Biol (2015) 0.80
Single molecule analyses of the conformational substates of calmodulin bound to the phosphorylase kinase complex. Protein Sci (2007) 0.80
The effects of the flavonoid baicalein and osmolytes on the Mg 2+ accelerated aggregation/fibrillation of carboxymethylated bovine 1SS-alpha-lactalbumin. Arch Biochem Biophys (2006) 0.80
Structure and location of the regulatory β subunits in the (αβγδ)4 phosphorylase kinase complex. J Biol Chem (2012) 0.80
Protein Interactions Captured by Chemical Cross-linking: Simple Cross-linking Screen Using Sulfo-MBS. CSH Protoc (2007) 0.80
Physicochemical changes in phosphorylase kinase associated with its activation. Protein Sci (2008) 0.79
Strategies for folding of affinity tagged proteins using GroEL and osmolytes. J Struct Funct Genomics (2008) 0.78
The cytoskeletal organizing protein Cdc42-interacting protein 4 associates with phosphorylase kinase in skeletal muscle. Biochem Biophys Res Commun (2006) 0.78
Expressed phosphorylase b kinase and its alphagammadelta subcomplex as regulatory models for the rabbit skeletal muscle holoenzyme. Biochemistry (2009) 0.78
Physicochemical changes in phosphorylase kinase induced by its cationic activator Mg(2+). Protein Sci (2013) 0.77
Protein Interactions Captured by Chemical Cross-linking: Two-Step Cross-linking with ANB*NOS. CSH Protoc (2007) 0.77
A review of methods used for identifying structural changes in a large protein complex. Methods Mol Biol (2012) 0.77
The glucoamylase inhibitor acarbose is a direct activator of phosphorylase kinase. Biochemistry (2010) 0.77
Quenching of Protein Cross-linking. CSH Protoc (2007) 0.75