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The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2.
- B. Kauppi, B. B. Nielsen, +4 authors H. Eklund
- Chemistry, Medicine
- Journal of molecular biology
- 11 October 1996
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 good… Expand
Crystal structure of tetranectin, a trimeric plasminogen‐binding protein with an α‐helical coiled coil
- B. B. Nielsen, J. Kastrup, +5 authors I. K. Larsen
- Chemistry, Medicine
- FEBS letters
- 28 July 1997
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 triple… Expand
1,8-Naphthyridin-2(1H)-ones. Novel Bicyclic and Tricyclic Analogues of Thymine in Peptide Nucleic Acids (PNAs)
- A. B. Eldrup, B. B. Nielsen, +4 authors P. Nielsen
- Chemistry
- 1 May 2001
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 of… Expand
HUMAN TETRANECTIN, A TRIMERIC PLASMINOGEN BINDING PROTEIN WITH AN ALPHA-HELICAL COILED COIL
- B. B. Nielsen, J. Kastrup, +5 authors I. K. Larsen
- Chemistry
- 3 December 1997
Tyr702 Is an Important Determinant of Agonist Binding and Domain Closure of the Ligand-Binding Core of GluR2
- Anne Frandsen, D. Pickering, +8 authors J. Kastrup
- Biology, Medicine
- Molecular Pharmacology
- 1 March 2005
Ionotropic glutamate receptors mediate most rapid excitatory synaptic transmission in the mammalian central nervous system, and their involvement in neurological diseases has stimulated widespread… Expand
Structure of the C-type lectin carbohydrate recognition domain of human tetranectin.
- J. Kastrup, B. B. Nielsen, +5 authors I. K. Larsen
- Chemistry, Medicine
- Acta crystallographica. Section D, Biological…
- 1 September 1998
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 from… Expand
Crystal structure of a partly self-complementary peptide nucleic acid (PNA) oligomer showing a duplex-triplex network.
- B. Petersson, B. B. Nielsen, +4 authors J. Kastrup
- Medicine, Chemistry
- Journal of the American Chemical Society
- 9 February 2005
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 canonical… Expand
Exploring the GluR2 ligand‐binding core in complex with the bicyclical AMPA analogue (S)‐4‐AHCP
- B. B. Nielsen, D. Pickering, +4 authors J. Kastrup
- Medicine, Chemistry
- The FEBS journal
- 1 April 2005
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)propionic… Expand
Tyr 702 Is an Important Determinant of Agonist Binding and Domain Closure of the Ligand-Binding Core of GluR 2
- Anne Frandsen, D. Pickering, +8 authors J. Kastrup
- 2005
Ionotropic glutamate receptors mediate most rapid excitatory synaptic transmission in the mammalian central nervous system, and their involvement in neurological diseases has stimulated widespread… Expand
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Crystallization and crystallographic investigations of the small subunit of mouse ribonucleotide reductase
- B. B. Nielsen, B. Kauppi, M. Thelander, L. Thelander, I. K. Larsen, H. Eklund
- Biology, Medicine
- FEBS letters
- 16 October 1995
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 are… Expand
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