Assay ID | Title | Year | Journal | Article |
AID1352617 | Binding affinity to human serum albumin assessed as fluorescence lifetime decay 1 at HSA:compound ratio of 1:2 after 1 hr by fluorescence spectroscopic analysis (Rvb = 3.917 +/- 0.039 nanoseconds) | 2018 | European journal of medicinal chemistry, Feb-25, Volume: 146 | Unravelling the binding mechanism of benproperine with human serum albumin: A docking, fluorometric, and thermodynamic approach. |
AID1352621 | Binding affinity to human serum albumin assessed as fluorescence lifetime decay 3 at HSA:compound ratio of 1:2 after 1 hr by fluorescence spectroscopic analysis (Rvb = 6.876 +/- 0.177 nanoseconds) | 2018 | European journal of medicinal chemistry, Feb-25, Volume: 146 | Unravelling the binding mechanism of benproperine with human serum albumin: A docking, fluorometric, and thermodynamic approach. |
AID1352622 | Binding affinity to human serum albumin assessed as fluorescence lifetime decay 3 at HSA:compound ratio of 1:10 after 1 hr by fluorescence spectroscopic analysis (Rvb = 6.876 +/- 0.177 nanoseconds) | 2018 | European journal of medicinal chemistry, Feb-25, Volume: 146 | Unravelling the binding mechanism of benproperine with human serum albumin: A docking, fluorometric, and thermodynamic approach. |
AID1352615 | Binding affinity to human serum albumin assessed as Stern-Volmer quenching constant after 1 hr at 25 degC by fluorescence spectroscopic analysis | 2018 | European journal of medicinal chemistry, Feb-25, Volume: 146 | Unravelling the binding mechanism of benproperine with human serum albumin: A docking, fluorometric, and thermodynamic approach. |
AID1352619 | Binding affinity to human serum albumin assessed as fluorescence lifetime decay 2 at HSA:compound ratio of 1:2 after 1 hr by fluorescence spectroscopic analysis (Rvb = 0.584 +/- 0.047 nanoseconds) | 2018 | European journal of medicinal chemistry, Feb-25, Volume: 146 | Unravelling the binding mechanism of benproperine with human serum albumin: A docking, fluorometric, and thermodynamic approach. |
AID1352627 | Induction of conformational changes in human serum albumin assessed as reduction in alpha-helical content at HSA:compound ratio of 1:10 by CD spectral analysis (Rvb = 52.6%) | 2018 | European journal of medicinal chemistry, Feb-25, Volume: 146 | Unravelling the binding mechanism of benproperine with human serum albumin: A docking, fluorometric, and thermodynamic approach. |
AID1352620 | Binding affinity to human serum albumin assessed as fluorescence lifetime decay 2 at HSA:compound ratio of 1:10 after 1 hr by fluorescence spectroscopic analysis (Rvb = 0.584 +/- 0.047 nanoseconds) | 2018 | European journal of medicinal chemistry, Feb-25, Volume: 146 | Unravelling the binding mechanism of benproperine with human serum albumin: A docking, fluorometric, and thermodynamic approach. |
AID1352625 | Binding affinity to human serum albumin by isothermal titration microcalorimetry | 2018 | European journal of medicinal chemistry, Feb-25, Volume: 146 | Unravelling the binding mechanism of benproperine with human serum albumin: A docking, fluorometric, and thermodynamic approach. |
AID1352623 | Binding affinity to human serum albumin assessed as binding constant after 1 hr at 25 degC by fluorescence spectroscopic analysis | 2018 | European journal of medicinal chemistry, Feb-25, Volume: 146 | Unravelling the binding mechanism of benproperine with human serum albumin: A docking, fluorometric, and thermodynamic approach. |
AID1352624 | Binding affinity to human serum albumin assessed as binding constant after 1 hr at 37 degC by fluorescence spectroscopic analysis | 2018 | European journal of medicinal chemistry, Feb-25, Volume: 146 | Unravelling the binding mechanism of benproperine with human serum albumin: A docking, fluorometric, and thermodynamic approach. |
AID1352616 | Binding affinity to human serum albumin assessed as Stern-Volmer quenching constant after 1 hr at 37 degC by fluorescence spectroscopic analysis | 2018 | European journal of medicinal chemistry, Feb-25, Volume: 146 | Unravelling the binding mechanism of benproperine with human serum albumin: A docking, fluorometric, and thermodynamic approach. |
AID1352626 | Induction of conformational changes in human serum albumin assessed as reduction in alpha-helical content at HSA:compound ratio of 1:2 by CD spectral analysis (Rvb = 52.6%) | 2018 | European journal of medicinal chemistry, Feb-25, Volume: 146 | Unravelling the binding mechanism of benproperine with human serum albumin: A docking, fluorometric, and thermodynamic approach. |
AID1352618 | Binding affinity to human serum albumin assessed as fluorescence lifetime decay 1 at HSA:compound ratio of 1:10 after 1 hr by fluorescence spectroscopic analysis (Rvb = 3.917 +/- 0.039 nanoseconds) | 2018 | European journal of medicinal chemistry, Feb-25, Volume: 146 | Unravelling the binding mechanism of benproperine with human serum albumin: A docking, fluorometric, and thermodynamic approach. |
AID1159607 | Screen for inhibitors of RMI FANCM (MM2) intereaction | 2016 | Journal of biomolecular screening, Jul, Volume: 21, Issue:6
| A High-Throughput Screening Strategy to Identify Protein-Protein Interaction Inhibitors That Block the Fanconi Anemia DNA Repair Pathway. |
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023] |