Search Results - "Kastrup, J. S."

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  1. 1

    The structure of the mite allergen Blo t 1 explains the limited antibody cross‐reactivity to Der p 1 by Meno, K. H., Kastrup, J. S., Kuo, I.‐C., Chua, K. Y., Gajhede, M.

    Published in Allergy (Copenhagen) (01-04-2017)
    “…The Blomia tropicalis (Blo t) mite species is considered a storage mite in temperate climate zones and an important source of indoor allergens causing allergic…”
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  2. 2

    Structural Basis for AMPA Receptor Activation and Ligand Selectivity: Crystal Structures of Five Agonist Complexes with the GluR2 Ligand-binding Core by Hogner, A., Kastrup, J.S., Jin, R., Liljefors, T., Mayer, M.L., Egebjerg, J., Larsen, I.K., Gouaux, E.

    Published in Journal of molecular biology (06-09-2002)
    “…Glutamate is the principal excitatory neurotransmitter within the mammalian CNS, playing an important role in many different functions in the brain such as…”
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  3. 3

    GluR2 ligand-binding core complexes: importance of the isoxazolol moiety and 5-substituent for the binding mode of AMPA-type agonists by Kasper, C, Lunn, M.-L, Liljefors, T, Gouaux, E, Egebjerg, J, Kastrup, J.S

    Published in FEBS letters (06-11-2002)
    “…X-ray structures of the GluR2 ligand-binding core in complex with ( S)-Des-Me-AMPA and in the presence and absence of zinc ions have been determined. (…”
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  4. 4

    The Influence of a Chiral Amino Acid on the Helical Handedness of PNA in Solution and in Crystals by Rasmussen, H., Liljefors, T., Petersson, B., Nielsen, P. E., Kastrup, J. S.

    “…The X-ray structure of a self-complementary PNA hexamer (H-CGTACG-L-Lys-NH 2 ) has been determined to 2.35 Å resolution. The introduction of an L-lysine moiety…”
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    Structure and function of the N-linked glycans of HBP/CAP37/azurocidin: Crystal structure determination and biological characterization of nonglycosylated HBP by IVERSEN, L.F., KASTRUP, J.S., BJØRN, S.E., WIBERG, F.C., LARSEN, I.K., FLODGAARD, H.J., RASMUSSEN, P.B.

    Published in Protein science (01-10-1999)
    “…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…”
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  7. 7

    Structure of the C-Type Lectin Carbohydrate Recognition Domain of Human Tetranectin by Kastrup, Jette Sandholm, Nielsen, Bettina Bryde, Rasmussen, Hanne, Holtet, Thor Las, Graversen, Jonas Heilskov, Etzerodt, Michael, Thøgersen, Hans Christian, Larsen, Ingrid Kjøller

    “…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…”
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  8. 8

    The SAXS Solution Structure of RF1 Differs from Its Crystal Structure and Is Similar to Its Ribosome Bound Cryo-EM Structure by Vestergaard, Bente, Sanyal, Suparna, Roessle, Manfred, Mora, Liliana, Buckingham, Richard H., Kastrup, Jette S., Gajhede, Michael, Svergun, Dmitri I., Ehrenberg, Måns

    Published in Molecular cell (22-12-2005)
    “…Bacterial class I release factors (RFs) are seen by cryo-electron microscopy (cryo-EM) to span the distance between the ribosomal decoding and peptidyl…”
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    X-ray Structure of the 154-Amino-Acid Form of Recombinant Human Basic Fibroblast Growth Factor. Comparison with the Truncated 146-Amino-Acid Form by Kastrup, J. S., Eriksson, E. S., Dalbøge, H., Flodgaard, H.

    “…The crystal structure of the 154‐amino‐acid form of human basic fibroblast growth factor (hbFGF154), probably representing the intact form of hbFGF as deduced…”
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    Crystal Structure of Sucrose Phosphorylase from Bifidobacterium adolescentis by Sprogøe, Desiree, van den Broek, Lambertus A. M, Mirza, Osman, Kastrup, Jette S, Voragen, Alphons G. J, Gajhede, Michael, Skov, Lars K

    Published in Biochemistry (Easton) (10-02-2004)
    “…Around 80 enzymes are implicated in the generic starch and sucrose pathways. One of these enzymes is sucrose phosphorylase, which reversibly catalyzes the…”
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  13. 13

    Characterization of the allosteric binding pocket of human liver fructose‐1,6‐bisphosphatase by protein crystallography and inhibitor activity studies by Iversen, L. F., Brzozowski, M., Hastrup, S., Hubbard, R., Kastrup, J. S., Larsen, I. K., Nærum, L., Nørskov‐Lauridsen, L., Rasmussen, P. B., Thim, L., Wiberg, F. C., Lundgren, K.

    Published in Protein science (01-05-1997)
    “…The structures of three complexes of human fructose‐1,6‐bisphosphatase (FB) with the allosteric inhibitor AMP and two AMP analogues have been determined and…”
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  14. 14

    Structural Characterization of the Stringent Response Related Exopolyphosphatase/Guanosine Pentaphosphate Phosphohydrolase Protein Family by Kristensen, Ole, Laurberg, Martin, Liljas, Anders, Kastrup, Jette Sandholm, Gajhede, Michael

    Published in Biochemistry (Easton) (20-07-2004)
    “…Exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (PPX/GPPA) enzymes play central roles in the bacterial stringent response induced by starvation…”
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  15. 15

    Structural basis of cell-cell adhesion by NCAM by Larsen, Ingrid K, Kasper, Christina, Rasmussen, Hanne, Kastrup, Jette S, Ikemizu, Shinji, Jones, E. Yvonne, Berezin, Vladimir, Bock, Elisabeth

    Published in Nature structural biology (01-05-2000)
    “…The neural cell adhesion molecule NCAM, a member of the immunoglobulin superfamily, mediates cell-cell recognition and adhesion via a homophilic interaction…”
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    Structure of HBP, a multifunctional protein with a serine proteinase fold by Iversen, Lars Fogh, Kastrup, Jette Sandholm, Bjørn, Søren Erik, Rasmussen, Poul Baad, Wiberg, Finn Christoph, Flodgaard, Hans Jacob, Larsen, Ingrid Kjøller

    Published in Nature structural biology (01-04-1997)
    “…The structure of human heparin binding protein reveals that the serine proteinase fold has been used as a scaffold for a multifunctional protein with…”
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  18. 18

    Crystal structure of a peptide nucleic acid (PNA) duplex at 1.7 Å resolution by Rasmussen, Hanne, Kastrup, Jette Sandholm, Nielsen, Jens Nederby, Nielsen, Jesper M, Nielsen, Peter E

    Published in Nature structural biology (01-02-1997)
    “…The crystal structure of a PNA duplex reveals both a right- and a left-handed helix in the unit cell. The helices are wide (28A), large pitched (18bp) with the…”
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  19. 19

    Crystal structure of tetranectin, a trimeric plasminogen-binding protein with an α-helical coiled coil by Nielsen, Bettina Bryde, Kastrup, Jette Sandholm, Rasmussen, Hanne, Holtet, Thor Las, Graversen, Jonas Heilskov, Etzerodt, Michael, Thøgersen, Hans Christian, Larsen, Ingrid Kjøller

    Published in FEBS letters (28-07-1997)
    “…Tetranectin is a plasminogen kringle 4-binding protein. The crystal structure has been determined at 2.8 Å resolution using molecular replacement. Human…”
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  20. 20

    Crystal structure of a peptide nucleic acid (PNA) duplex at 1.7 angstrom resolution by Rasmussen, H, Kastrup, J S, Nielsen, J N, Nielsen, J M, Nielsen, P E

    Published in Nature structural biology (01-02-1997)
    “…The crystal structure of a PNA duplex reveals both a right- and a left-handed helix in the unit cell. The helices are wide (28 angstrom), large pitched (18 bp)…”
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