• Publications
  • Influence
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
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
1,8-Naphthyridin-2(1H)-ones. Novel Bicyclic and Tricyclic Analogues of Thymine in Peptide Nucleic Acids (PNAs)
The synthesis of two novel PNA nucleobases derived from 1,8-naphthyridin-2(1H)-one (bT) and benzo[b]-1,8-naphthyridin-2(1H)-one (tT) are reported, together with their incorporation into oligomers ofExpand
  • 38
  • 1
Tyr702 Is an Important Determinant of Agonist Binding and Domain Closure of the Ligand-Binding Core of GluR2
Ionotropic glutamate receptors mediate most rapid excitatory synaptic transmission in the mammalian central nervous system, and their involvement in neurological diseases has stimulated widespreadExpand
  • 42
Structure of the C-type lectin carbohydrate recognition domain of human tetranectin.
Tetranectin (TN) is a C-type lectin involved in fibrinolysis, being the only endogenous ligand known to bind specifically to the kringle 4 domain of plasminogen. TN was originally isolated fromExpand
  • 29
  • PDF
Crystal structure of a partly self-complementary peptide nucleic acid (PNA) oligomer showing a duplex-triplex network.
The X-ray structure of a partly self-complementary peptide nucleic acid (PNA) decamer (H-GTAGATCACT-l-Lys-NH(2)) to 2.60 A resolution is reported. The structure is mainly controlled by the canonicalExpand
  • 47
  • PDF
Exploring the GluR2 ligand‐binding core in complex with the bicyclical AMPA analogue (S)‐4‐AHCP
The X‐ray structure of the ionotropic GluR2 ligand‐binding core (GluR2‐S1S2J) in complex with the bicyclical AMPA analogue (S)‐2‐amino‐3‐(3‐hydroxy‐7,8‐dihydro‐6H‐cyclohepta[d]‐4‐isoxazolyl)propionicExpand
  • 20
Tyr 702 Is an Important Determinant of Agonist Binding and Domain Closure of the Ligand-Binding Core of GluR 2
Ionotropic glutamate receptors mediate most rapid excitatory synaptic transmission in the mammalian central nervous system, and their involvement in neurological diseases has stimulated widespreadExpand
  • 6
  • PDF
Crystallization and crystallographic investigations of the small subunit of mouse ribonucleotide reductase
The R2 protein component of mouse ribonucleotide reductase has been obtained from overproducing Escherichia coli bacteria. It has been crystallized using NaCl as precipitant. The crystals areExpand
  • 11
...
1
2
...