Kaare Teilum
Kaare Teilum
Department of Biology, University of Copenhagen
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Cited by
Protein folding: defining a “standard” set of experimental conditions and a preliminary kinetic data set of two‐state proteins
KL Maxwell, D Wildes, A Zarrine‐Afsar, MA De Los Rios, AG Brown, ...
Protein Science 14 (3), 602-616, 2005
Functional aspects of protein flexibility
K Teilum, JG Olsen, BB Kragelund
Cellular and Molecular Life Sciences 66 (14), 2231-2247, 2009
Protein stability, flexibility and function
K Teilum, JG Olsen, BB Kragelund
Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics 1814 (8), 969-976, 2011
Arabidopsis ATP A2 peroxidase. Expression and high-resolution structure of a plant peroxidase with implications for lignification
L Østergaard, K Teilum, O Mirza, O Mattsson, M Petersen, KG Welinder, ...
Plant Molecular Biology 44 (2), 231-243, 2000
Fractional 13C enrichment of isolated carbons using [1-13C]-or [2-13C]-glucose facilitates the accurate measurement of dynamics at backbone Cα and side-chain methyl positions …
P Lundström, K Teilum, T Carstensen, I Bezsonova, S Wiesner, ...
Journal of biomolecular NMR 38 (3), 199-212, 2007
Determination of an ensemble of structures representing the denatured state of the bovine acyl-coenzyme a binding protein
K Lindorff-Larsen, S Kristjansdottir, K Teilum, W Fieber, CM Dobson, ...
Journal of the American Chemical Society 126 (10), 3291-3299, 2004
Structure of soybean seed coat peroxidase: A plant peroxidase with unusual stability and haem‐apoprotein interactions
A Henriksen, O Mirza, C Indiani, K Teilum, G Smulevich, KG Welinder, ...
Protein Science 10 (1), 108-115, 2001
Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP
M Kjaergaard, K Teilum, FM Poulsen
Proceedings of the National Academy of Sciences 107 (28), 12535-12540, 2010
Helical propensity in an intrinsically disordered protein accelerates ligand binding
V Iešmantavičius, J Dogan, P Jemth, K Teilum, M Kjaergaard
Angewandte Chemie International Edition 53 (6), 1548-1551, 2014
Solution structure of human prolactin
K Teilum, JC Hoch, V Goffin, S Kinet, JA Martial, BB Kragelund
Journal of molecular biology 351 (4), 810-823, 2005
Early kinetic intermediate in the folding of acyl-CoA binding protein detected by fluorescence labeling and ultrarapid mixing
K Teilum, K Maki, BB Kragelund, FM Poulsen, H Roder
Proceedings of the National Academy of Sciences 99 (15), 9807-9812, 2002
Remeasuring HEWL pKa values by NMR spectroscopy: Methods, analysis, accuracy, and implications for theoretical pKa calculations
H Webb, BM Tynan‐Connolly, GM Lee, D Farrell, F O'Meara, ...
Proteins: Structure, Function, and Bioinformatics 79 (3), 685-702, 2011
Transient structure formation in unfolded acyl-coenzyme A-binding protein observed by site-directed spin labelling
K Teilum, BB Kragelund, FM Poulsen
Journal of molecular biology 324 (2), 349-357, 2002
Behaviour of intrinsically disordered proteins in protein–protein complexes with an emphasis on fuzziness
JG Olsen, K Teilum, BB Kragelund
Cellular and Molecular Life Sciences 74 (17), 3175-3183, 2017
Protein dielectric constants determined from NMR chemical shift perturbations
P Kukic, D Farrell, LP McIntosh, B García-Moreno E, KS Jensen, Z Toleikis, ...
Journal of the American Chemical Society 135 (45), 16968-16976, 2013
Biosynthetic 13C labeling of aromatic side chains in proteins for NMR relaxation measurements
K Teilum, U Brath, P Lundström, M Akke
Journal of the American Chemical Society 128 (8), 2506-2507, 2006
Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization
K Teilum, MH Smith, E Schulz, LC Christensen, G Solomentsev, ...
Proceedings of the National Academy of Sciences 106 (43), 18273-18278, 2009
The WSXWS motif in cytokine receptors is a molecular switch involved in receptor activation: insight from structures of the prolactin receptor
R Dagil, MJ Knudsen, JG Olsen, C O'Shea, M Franzmann, V Goffin, ...
Structure 20 (2), 270-282, 2012
Rapid formation of a preoligomeric peptide–metal–peptide complex following copper (II) binding to amyloid β peptides
JT Pedersen, K Teilum, NHH Heegaard, J Østergaard, HW Adolph, ...
Angewandte Chemie 123 (11), 2580-2583, 2011
Amyloid-β and α-synuclein decrease the level of metal-catalyzed reactive oxygen species by radical scavenging and redox silencing
JT Pedersen, SW Chen, CB Borg, S Ness, JM Bahl, NHH Heegaard, ...
Journal of the American Chemical Society 138 (12), 3966-3969, 2016
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