Selected publications from Beactica scientists:
Mechanistic and kinetic characterization of hepatitis C virus NS3 protein interactions with NS4A and protease inhibitors, Geitmann M, Dahl G & Danielson UH, J Mol Recognit, 2010, (In press).
Biotinylated lipid bilayer disks as model membranes for biosensor analyses, Lundquist A, Hansen SB, Nordström H, Danielson UH & Edwards K, Analytical Biochemistry, 2010 (In press).
Development of surface plasmon resonance biosensor assays for primary and secondary screening of acetylcholine binding protein ligands, Retra K, Geitmann M, Kool J, Smit G, de Esch IJP, Danielson UH & Irth H, Analytical Biochemistry, 2010 (In press).
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.
