Selected publications from Beactica scientists:
Fragment library screening and lead characterization using SPR biosensors. Danielson UH, Current Topics in Medicinal Chemistry, 2009, 9, 1725-35.
Small kinase assay panels can provide a measure of selectivity. Brandt P, Jensen AJ, Nilsson J., Bioorg Med Chem Lett, 2009 19(20):5861-3.
Integrating surface plasmon resonance biosensor-based interaction kinetic analyses into the lead discovery and optimization process. Danielson UH, Future Medicinal Chemistry, 2009, 1(8), 1399-414.
Screening for NNRTIs with Slow Dissociation and High Affinity for a Panel of HIV-1 RT Variants. Elinder M, Nordström H, Geitmann M, Hämäläinen M, Vrang L, Öberg B & Danielson UH, J Biomol Screen, 2009, 14:395-403.
Structural and functional analysis of hepatitis C virus strain JFH1 polymerase. Simister P, Schmitt M, Geitmann M, Wicht O, Danielson UH, Klein R, Bressanelli S, & Lohmann V, J Virol 2009, 83(22):11926-39
Characterization of Ca2+ and phosphocholine interactions with C-reactive protein using a surface plasmon resonance biosensor. Christopeit T, Gossas T & Danielson UH, Analytical Biochemistry, 2009, 391(1), 39-44.
Identification of MMP-12 inhibitors by using biosensor-based screening of a fragment library. Nordström H, Gossas T, Hämäläinen M, Källblad P, Nyström S, Wallberg H & Danielson UH, J Med Chem, 2008, 51:3449-59.
Additional level of information about complex interaction between non-nucleoside inhibitor and HIV-1 reverse transcriptase using biosensor-based thermodynamic analysis. Geitmann M & Danielson UH, Bioorg Med Chem, 2007, 15:7344-54.
Interaction kinetic characterization of HIV-1 reverse transcriptase non-nucleoside inhibitor resistance. Geitmann M, Unge T & Danielson UH, J Med Chem, 2006, 49:2375-87.
Biosensor-based kinetic characterization of the interaction between HIV-1 reverse transcriptase and non-nucleoside inhibitors. Geitmann M, Unge T & Danielson UH, J Med Chem, 2006, 49:2367-74.
Biosensor-based screening and characterization of HIV-1 inhibitor interactions with Sap1, Sap2 and Sap3 from Candida albicans. Backman D, Monod M & Danielson UH, J Biomol Screen, 2006, 11:165-75.
Structure-activity relationships for the selectivity of hepatitis C virus NS3 protease inhibitors. Poliakov A, Johansson A, Åkerblom E, Oscarsson K, Samuelsson B, Hallberg A & Danielson UH, Biochim Biophys Acta, 2004, 1672:51-9.
Receptor flexibility in the in silico screening of reagents in the S1′ pocket of human collagenase. Källblad P, Todorov NP, Willems HMG, Alberts IL , J Med Chem, 2004, 47:2761–7.
Assessment of multiple binding modes in ligand-protein docking. Källblad P, Mancera RL, Todorov NP, J Med Chem, 2004, 47:3334–7.
Improved structure-activity relationship analysis of HIV-1 protease inhibitors using interaction kinetic data. Shuman CF, Vrang L & Danielson UH, J Med Chem, 2004, 47:5953-61.
Kinetic and thermodynamic characterization of HIV-1 protease inhibitors. Shuman CF, Hämäläinen M & Danielson UH, J Mol Recognit, 2004, 17:106-19.
Elucidation of HIV-1 protease resistance by characterization of interaction kinetics between inhibitors and enzyme variants. Shuman CF, Markgren P-O, Hämäläinen M & Danielson UH, Antiviral Research, 2003, 58:235-42.
Relationships between structure and interaction kinetics for HIV-1 protease inhibitors. Markgren P-O, Schaal W, Hämäläinen M, Karlén A, Hallberg A, Samuelsson B & Danielson UH, J Med Chem, 2002, 45:5430-39.
