Catherine Venien Bryan
Affiliation: University of Oxford
- The structure of phosphorylase kinase holoenzyme at 9.9 angstroms resolution and location of the catalytic subunit and the substrate glycogen phosphorylaseCatherine Venien-Bryan
Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, South Parks Road, OX1 3QU Oxford, UK
Structure 17:117-27. 2009..The PhK preparation contained a number of smaller particles whose structure at 9.8 angstroms resolution was consistent with a proteolysed activated form of PhK that had lost the alpha subunits and possibly the gamma subunits...
- Three-dimensional structure of phosphorylase kinase at 22 A resolution and its complex with glycogen phosphorylase bCatherine Venien-Bryan
Laboratory of Molecular Biophysics, Oxford Centre for Molecular Sciences, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom
Structure 10:33-41. 2002..The PhK/GPb model provides an explanation for the formation of hybrid GPab intermediates in the PhK-catalyzed phosphorylation of GPb...
- Modeling of an ion channel in its open conformationCarmen Domene
Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QZ, United Kingdom
Biophys J 89:L01-3. 2005..Overall, these simulations suggest that the open conformer is stable, providing a plausible all-atom model that will enable the study of potential gating mechanisms in more detail...
- The HupR receiver domain crystal structure in its nonphospho and inhibitory phospho statesKaren M Davies
Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, Oxford, UK
J Mol Biol 385:51-64. 2009....
- Studies of the ATPase activity of the ABC protein SUR1Heidi de Wet
Henry Wellcome Centre for Gene Function, Department of Physiology, Anatomy and Genetics, University of Oxford, UK
FEBS J 274:3532-44. 2007..These data demonstrate that the ATPase activity of sulfonylurea receptor 1 differs from that of the isolated nucleotide-binding domains, suggesting that the transmembrane domains may influence the activity of the protein...
- The 3-dimensional structure of a hepatitis C virus p7 ion channel by electron microscopyPhilipp Luik
Department of Biochemistry and Oxford Glycobiology Institute, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom
Proc Natl Acad Sci U S A 106:12712-6. 2009..This broadest part of the channel presents a comparatively large surface area providing potential interaction sites for cellular and virally encoded ER resident proteins...