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The FEBS Journal|March 29, 2014
L-Asp is a useful tool in the purification of the ionotropic glutamate receptor A2 ligand-binding domainChristian Krintel, Karla Frydenvang, Anna Ceravalls de Rabassa, et al.
Protein Expression and Purification|January 16, 2010
Over-expression, purification and characterization of an Asc-1 homologue from Gloeobacter violaceusXiaole Wang, Helle Hald, Heidi A Ernst, et al.
Nature Structural Biology|May 10, 2000
Structural basis of cell-cell adhesion by NCAMC Kasper, H Rasmussen, J S Kastrup, et al.
The Journal of Neuroscience : the Official Journal of the Society for Neuroscience|January 30, 2009
Modulation of the dimer interface at ionotropic glutamate-like receptor delta2 by D-serine and extracellular calciumKasper B Hansen, Peter Naur, Natalie L Kurtkaya, et al.
Acta Crystallographica. Section D, Biological Crystallography|September 4, 2013
Structural analysis of the positive AMPA receptor modulators CX516 and Me-CX516 in complex with the GluA2 ligand-binding domainChristian Krintel, Kasper Harpsøe, Linda G Zachariassen, et al.
Acta Crystallographica. Section D, Biological Crystallography|April 20, 2000
Crystallization and molecular-replacement solution of a truncated form of human recombinant tetranectinB B Nielsen, J S Kastrup, H Rasmussen, et al.
Journal of Medicinal Chemistry|January 10, 2003
Competitive antagonism of AMPA receptors by ligands of different classes: crystal structure of ATPO bound to the GluR2 ligand-binding core, in comparison with DNQXAnders Hogner, Jeremy R Greenwood, Tommy Liljefors, et al.
The Journal of Biological Chemistry|September 23, 2006
Structural rearrangements of sucrose phosphorylase from Bifidobacterium adolescentis during sucrose conversionOsman Mirza, Lars K Skov, Desiree Sprogøe, et al.
The Journal of Biological Chemistry|August 17, 2005
A binding site tyrosine shapes desensitization kinetics and agonist potency at GluR2. A mutagenic, kinetic, and crystallographic studyMai Marie Holm, Peter Naur, Bente Vestergaard, et al.
Molecular Cell|December 21, 2005
The SAXS solution structure of RF1 differs from its crystal structure and is similar to its ribosome bound cryo-EM structureBente Vestergaard, Suparna Sanyal, Manfred Roessle, et al.
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