Flemming Poulsen, Ph.D.

University of Copenhagen, København, Denmark 
"Flemming Poulsen"
BETA: Related publications


You can help our author matching system! If you notice any publications incorrectly attributed to this author, please sign in and mark matches as correct or incorrect.

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
See more...