Skp2-Cks1 Assay for Identication Small Molecule Inhibitors of . . . Skp2-Cks1 Assay for Identication Small Molecule Inhibitors of Establis Preprints are preliminary reports that have not undergone peer review They should not be considered conclusive, used to inform clinical practice, or referenced by the media as validated information
Targeting the Skp2–Cks1 protein–protein interaction: structures, assays . . . Fluorescence-polarization or TR-FRET formats built on these intact assemblies will better capture the conformational states required for p27 ubiquitination, potentially improving assay sensitivity and reducing off-target noise compared to binary Skp2–Cks1 tests
Establishment of high-throughput screening HTRF assay for . . . To evaluate the stability of the Skp2 Skp1-Cks1 HTRF assay for HTS, the following parameters were tested, including the duration of HTRF signal, the concentration of DMSO and the order in which the reactants were added
Establishment of high-throughput screening HTRF assay for . . . In this study, we establish an improved high-throughput screening platform to screen Skp2 inhibitors targeting Skp2-Cks1interaction, which may provide a new therapeutic approach for the clinic
High-Throughput Screening AlphaScreen Assay for Identification of Small . . . Accordingly, perturbation of the Skp2-Cks1 interaction may represent an attractive target for pharmacological intervention Here we describe a high-throughput AlphaScreen assay for discovering small-molecule inhibitors of the Skp2-Cks1 protein-protein interaction in vitro
p27 To determine the factors that control p27 stability, we established a cell-free extract assay that recapitulates the degradation of p27 Phosphorylation of p27 at Thr187 was essential for its degradation