Catherine Venien Bryan

Summary

Affiliation: University of Oxford
Country: UK

Publications

  1. pmc Structure of human aspartyl aminopeptidase complexed with substrate analogue: insight into catalytic mechanism, substrate specificity and M18 peptidase family
    Apirat Chaikuad
    Structural Genomics Consortium, Old Road Research Campus Building, Oxford OX3 7DQ, UK
    BMC Struct Biol 12:14. 2012
  2. pmc The structure of phosphorylase kinase holoenzyme at 9.9 angstroms resolution and location of the catalytic subunit and the substrate glycogen phosphorylase
    Catherine Venien-Bryan
    Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, South Parks Road, OX1 3QU Oxford, UK
    Structure 17:117-27. 2009
  3. ncbi request reprint Three-dimensional structure of phosphorylase kinase at 22 A resolution and its complex with glycogen phosphorylase b
    Catherine 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
  4. pmc Modeling of an ion channel in its open conformation
    Carmen Domene
    Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QZ, United Kingdom
    Biophys J 89:L01-3. 2005
  5. doi request reprint The HupR receiver domain crystal structure in its nonphospho and inhibitory phospho states
    Karen M Davies
    Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, Oxford, UK
    J Mol Biol 385:51-64. 2009
  6. ncbi request reprint Studies of the ATPase activity of the ABC protein SUR1
    Heidi de Wet
    Henry Wellcome Centre for Gene Function, Department of Physiology, Anatomy and Genetics, University of Oxford, UK
    FEBS J 274:3532-44. 2007
  7. pmc The 3-dimensional structure of a hepatitis C virus p7 ion channel by electron microscopy
    Philipp 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

Collaborators

Detail Information

Publications7

  1. pmc Structure of human aspartyl aminopeptidase complexed with substrate analogue: insight into catalytic mechanism, substrate specificity and M18 peptidase family
    Apirat Chaikuad
    Structural Genomics Consortium, Old Road Research Campus Building, Oxford OX3 7DQ, UK
    BMC Struct Biol 12:14. 2012
    ..Despite previous enzyme and substrate characterization, structural details of DNPEP regarding ligand recognition and catalytic mechanism remain to be delineated...
  2. pmc The structure of phosphorylase kinase holoenzyme at 9.9 angstroms resolution and location of the catalytic subunit and the substrate glycogen phosphorylase
    Catherine 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...
  3. ncbi request reprint Three-dimensional structure of phosphorylase kinase at 22 A resolution and its complex with glycogen phosphorylase b
    Catherine 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...
  4. pmc Modeling of an ion channel in its open conformation
    Carmen 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...
  5. doi request reprint The HupR receiver domain crystal structure in its nonphospho and inhibitory phospho states
    Karen M Davies
    Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, Oxford, UK
    J Mol Biol 385:51-64. 2009
    ....
  6. ncbi request reprint Studies of the ATPase activity of the ABC protein SUR1
    Heidi 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...
  7. pmc The 3-dimensional structure of a hepatitis C virus p7 ion channel by electron microscopy
    Philipp 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...