scholarly journals Use of BODIPY-Labeled ATP Analogues in the Development and Validation of a Fluorescence Polarization-Based Assay for Screening of Kinase Inhibitors

ACS Omega ◽  
2020 ◽  
Vol 5 (16) ◽  
pp. 9064-9070
Author(s):  
Bernardo Pereira Moreira ◽  
Tom Armstrong ◽  
Izabella Cristina Andrade Batista ◽  
Naiara Clemente Tavares ◽  
Camilla Valente Pires ◽  
...  
Keyword(s):  
Fluorescence Polarization ◽  
Kinase Inhibitors ◽  
Atp Analogues ◽  
Development And Validation

Development and Validation of a Fluorescence Polarization-Based Competitive Peptide-Binding Assay for HLA-A*0201A New Tool for Epitope Discovery

Biochemistry ◽  
2005 ◽  
Vol 44 (37) ◽  
pp. 12491-12507 ◽  
Author(s):  
Rico Buchli ◽  
Rodney S. VanGundy ◽  
Heather D. Hickman-Miller ◽  
Christopher F. Giberson ◽  
Wilfried Bardet ◽  
...  
Keyword(s):  
Fluorescence Polarization ◽  
Binding Assay ◽  
Peptide Binding ◽  
Epitope Discovery ◽  
Peptide Binding Assay ◽  
Development And Validation

An improved zinc cocktail-mediated fluorescence polarization-based kinase assay for high-throughput screening of kinase inhibitors

2008 ◽  
Vol 380 (1) ◽  
pp. 143-145 ◽  
Author(s):  
Puneet Chopra ◽  
Kamna Nanda ◽  
Mou Chatterjee ◽  
Malini Bajpai ◽  
Sunanda G. Dastidar ◽  
...  
Keyword(s):  
High Throughput ◽  
Fluorescence Polarization ◽  
High Throughput Screening ◽  
Kinase Inhibitors ◽  
Kinase Assay

scholarly journals Use of Red-Shifted Dyes in a Fluorescence Polarization AKT Kinase Assay for Detection of Biological Activity in Natural Product Extracts

2004 ◽  
Vol 9 (1) ◽  
pp. 52-61 ◽  
Author(s):  
Tammy C. Turek-Etienne ◽  
Ming Lei ◽  
Joseph S. Terracciano ◽  
Erik F. Langsdorf ◽  
Robert W. Bryant ◽  
...  
Keyword(s):  
Natural Product ◽  
Fluorescence Polarization ◽  
Kinase Inhibitors ◽  
Chemotherapeutic Agents ◽  
Kinase Assay ◽  
Akt Kinase ◽  
Control Set ◽  
High Concentrations ◽  
Important Therapeutic Target ◽  
Assay Interference

Kinases are an important therapeutic target for drug discovery, and many cancer chemotherapeutic agents have been derived from natural product sources. Natural product samples, however, have the likelihood of assay interference, particularly at elevated test concentrations. The authors developed a competitive fluorescence polarization (FP) assay using red-shifted fluorophores for the AKT kinase and demonstrated utility for testing concentrated natural product extracts. A set of 7 actinomycetes cultures containing indolocarbazoles, known nonselective kinase inhibitors, and a control set of 22 nonproducing indolocarbazole cultures were evaluated. Using red-shifted dyes (Cy3B™ or Cy5™), the authors identified active samples with minimal interference up to the extract concentrations that are 3 times nonextracted culture levels. In contrast, a significant number of interferences were observed using either a fluorescein competitive FP assay or a [33P]ATP Flashplate assay. This work demonstrates that one can screen natural product extracts at high concentrations successfully using FP technology with red-shifted dyes. ( Journal of Biomolecular Screening 2004:52-61)

scholarly journals Identification of selective inhibitors of RET and comparison with current clinical candidates through development and validation of a robust screening cascade

F1000Research ◽  
2016 ◽  
Vol 5 ◽  
pp. 1005 ◽  
Author(s):  
Amanda J. Watson ◽  
Gemma V. Hopkins ◽  
Samantha Hitchin ◽  
Habiba Begum ◽  
Stuart Jones ◽  
...  
Keyword(s):  
Tyrosine Kinases ◽  
Kinase Inhibitors ◽  
Vascular Endothelial ◽  
Pharmacological Activities ◽  
Medullary Thyroid ◽  
Development And Validation ◽  
Endothelial Growth Factor ◽  
Medullary Thyroid Carcinomas ◽  
Dose Limiting Toxicity ◽  
Screening Cascade

RET (REarranged during Transfection) is a receptor tyrosine kinase, which plays pivotal roles in regulating cell survival, differentiation, proliferation, migration and chemotaxis. Activation of RET is a mechanism of oncogenesis in medullary thyroid carcinomas where both germline and sporadic activating somatic mutations are prevalent. At present, there are no known specific RET inhibitors in clinical development, although many potent inhibitors of RET have been opportunistically identified through selectivity profiling of compounds initially designed to target other tyrosine kinases. Vandetanib and cabozantinib, both multi-kinase inhibitors with RET activity, are approved for use in medullary thyroid carcinoma, but additional pharmacological activities, most notably inhibition of vascular endothelial growth factor - VEGFR2 (KDR), lead to dose-limiting toxicity. The recent identification of RET fusions present in ~1% of lung adenocarcinoma patients has renewed interest in the identification and development of more selective RET inhibitors lacking the toxicities associated with the current treatments. In an earlier publication [Newton et al, 2016; 1] we reported the discovery of a series of 2-substituted phenol quinazolines as potent and selective RET kinase inhibitors. Here we describe the development of the robust screening cascade which allowed the identification and advancement of this chemical series.  Furthermore we have profiled a panel of RET-active clinical compounds both to validate the cascade and to confirm that none display a RET-selective target profile.

scholarly journals High quality, small molecule-activity datasets for kinase research

F1000Research ◽  
2016 ◽  
Vol 5 ◽  
pp. 1366 ◽  
Author(s):  
Rajan Sharma ◽  
Stephan C. Schürer ◽  
Steven M. Muskal
Keyword(s):  
Kinase Inhibitors ◽  
Therapeutic Potential ◽  
Activity Data ◽  
Chemical Structures ◽  
Methods Development ◽  
Structure Activity ◽  
Regulate Cell Growth ◽  
Data Points ◽  
Kinase Structure ◽  
Development And Validation

Kinases regulate cell growth, movement, and death. Deregulated kinase activity is a frequent cause of disease. The therapeutic potential of kinase inhibitors has led to large amounts of published structure activity relationship (SAR) data. Bioactivity databases such as the Kinase Knowledgebase (KKB), WOMBAT, GOSTAR, and ChEMBL provide researchers with quantitative data characterizing the activity of compounds across many biological assays. The KKB, for example, contains over 1.8M kinase structure-activity data points reported in peer-reviewed journals and patents. In the spirit of fostering methods development and validation worldwide, we have extracted and have made available from the KKB 258K structure activity data points and 76K associated unique chemical structures across eight kinase targets. These data are freely available for download within this data note.

Design and characterization of bivalent Smac-based peptides as antagonists of XIAP and development and validation of a fluorescence polarization assay for XIAP containing both BIR2 and BIR3 domains

2008 ◽  
Vol 374 (1) ◽  
pp. 87-98 ◽  
Author(s):  
Zaneta Nikolovska-Coleska ◽  
Jennifer L. Meagher ◽  
Sheng Jiang ◽  
Steven A. Kawamoto ◽  
Wei Gao ◽  
...  
Keyword(s):  
Fluorescence Polarization ◽  
Fluorescence Polarization Assay ◽  
Development And Validation

Development and Validation of a Simultaneous Quantification Method of 14 Tyrosine Kinase Inhibitors in Human Plasma Using LC-MS/MS

2017 ◽  
Vol 39 (1) ◽  
pp. 43-54 ◽  
Author(s):  
Huu H. Huynh ◽  
Claire Pressiat ◽  
Hélène Sauvageon ◽  
Isabelle Madelaine ◽  
Patricia Maslanka ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Human Plasma ◽  
Tyrosine Kinase Inhibitors ◽  
Kinase Inhibitors ◽  
Quantification Method ◽  
Simultaneous Quantification ◽  
Development And Validation
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