Flemming Poulsen, Ph.D.

Affiliations: 
University of Copenhagen, København, Denmark 
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Publications

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Erlendsson S, Rathje M, Heidarsson PO, et al. (2014) Protein interacting with C-kinase 1 (PICK1) binding promiscuity relies on unconventional PSD-95/discs-large/ZO-1 homology (PDZ) binding modes for nonclass II PDZ ligands. The Journal of Biological Chemistry. 289: 25327-40
Ozenne V, Noel JK, Heidarsson PO, et al. (2014) Exploring the minimally frustrated energy landscape of unfolded ACBP. Journal of Molecular Biology. 426: 722-34
Iešmantavi?ius V, Jensen MR, Ozenne V, et al. (2013) Modulation of the intrinsic helix propensity of an intrinsically disordered protein reveals long-range helix-helix interactions. Journal of the American Chemical Society. 135: 10155-63
Kenchappa CS, Heidarsson PO, Kragelund BB, et al. (2013) Solution properties of the archaeal CRISPR DNA repeat-binding homeodomain protein Cbp2. Nucleic Acids Research. 41: 3424-35
Poulsen JW, Madsen CT, Young C, et al. (2013) Using guanidine-hydrochloride for fast and efficient protein digestion and single-step affinity-purification mass spectrometry. Journal of Proteome Research. 12: 1020-30
Heidarsson PO, Valpapuram I, Camilloni C, et al. (2012) A highly compliant protein native state with a spontaneous-like mechanical unfolding pathway. Journal of the American Chemical Society. 134: 17068-75
Bojesen KB, Clausen O, Rohde K, et al. (2012) Nectin-1 binds and signals through the fibroblast growth factor receptor. The Journal of Biological Chemistry. 287: 37420-33
Kjaergaard M, Poulsen FM, Kragelund BB. (2012) Analyzing temperature-induced transitions in disordered proteins by NMR spectroscopy and secondary chemical shift analyses. Methods in Molecular Biology (Clifton, N.J.). 896: 249-56
Kjaergaard M, Poulsen FM, Kragelund BB. (2012) Temperature-induced transitions in disordered proteins probed by NMR spectroscopy. Methods in Molecular Biology (Clifton, N.J.). 896: 233-47
Kjaergaard M, Poulsen FM, Teilum K. (2012) Is a malleable protein necessarily highly dynamic? The hydrophobic core of the nuclear coactivator binding domain is well ordered. Biophysical Journal. 102: 1627-35
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