• Publications
  • Influence
Structure and interactions of NCAM Ig1-2-3 suggest a novel zipper mechanism for homophilic adhesion.
The neural cell adhesion molecule, NCAM, mediates Ca(2+)-independent cell-cell and cell-substratum adhesion via homophilic (NCAM-NCAM) and heterophilic (NCAM-non-NCAM molecules) binding. NCAM plays aExpand
  • 171
  • 14
  • PDF
Competitive antagonism of AMPA receptors by ligands of different classes: crystal structure of ATPO bound to the GluR2 ligand-binding core, in comparison with DNQX.
Ionotropic glutamate receptors (iGluRs) constitute a family of ligand-gated ion channels that are essential for mediating fast synaptic transmission in the central nervous system. This study presentsExpand
  • 90
  • 8
Structural basis for AMPA receptor activation and ligand selectivity: crystal structures of five agonist complexes with the GluR2 ligand-binding core.
Glutamate is the principal excitatory neurotransmitter within the mammalian CNS, playing an important role in many different functions in the brain such as learning and memory. In this study, aExpand
  • 145
  • 5
Structure of HBP, a multifunctional protein with a serine proteinase fold
The structure of human heparin binding protein reveals that the serine proteinase fold has been used as a scaffold for a multifunctional protein with antibacterial activity, monocyte and t-cellExpand
  • 61
  • 4
Structural basis of cell–cell adhesion by NCAM
The neural cell adhesion molecule NCAM, a member of the immunoglobulin superfamily, mediates cell–cell recognition and adhesion via a homophilic interaction. NCAM plays a key role during developmentExpand
  • 134
  • 2
Structure and function of the N‐linked glycans of HBP/CAP37/azurocidin: Crystal structure determination and biological characterization of nonglycosylated HBP
The three N‐glycosylation sites of human heparin binding protein (HBP) have been mutated to produce a nonglycosylated HBP (ng‐HBP) mutant. ng‐HBP has been crystallized and tested for biologicalExpand
  • 18
  • 2
The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2.
The three-dimensional structure of mouse ribonucleotide reductase R2 has been determined at 2.3 A resolution using molecular replacement and refined to an R-value of 19.1% (Rfree = 25%) with goodExpand
  • 108
  • 1
Characterization of the active site of ribonucleotide reductase of Escherichia coli, bacteriophage T4 and mammalian cells by inhibition studies with hydroxyurea analogues.
Hydroxyurea specifically inhibits the enzyme ribonucleotide reductase by inactivating the essential tyrosine free radical in one of the two non-identical subunits constituting the enzyme. Studies onExpand
  • 73
  • 1
Crystal structure of tetranectin, a trimeric plasminogen‐binding protein with an α‐helical coiled coil
Tetranectin is a plasminogen kringle 4‐binding protein. The crystal structure has been determined at 2.8 Å resolution using molecular replacement. Human tetranectin is a homotrimer forming a tripleExpand
  • 76
  • 1
Atomic resolution structure of human HBP/CAP37/azurocidin.
Crystals of human heparin binding protein (HBP) diffract to 1.1 A when flash-frozen at 120 K. The atomic resolution structure has been refined anisotropically using SHELXL96. The final model of HBPExpand
  • 17
  • 1
  • PDF