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A Cell-Based Protein-Protein Interaction Method Using a Permuted Luciferase Reporter

We have developed a novel cell-based protein-protein interaction assay method. The method relies on conversion of an inactive permuted luciferase containing a Tobacco Etch Virus protease (TEV) cleavage sequence fused onto protein (A) to an active luciferase upon interaction and cleavage by another p...

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Detalles Bibliográficos
Autores principales: Eishingdrelo, Haifeng, Cai, Jidong, Weissensee, Paul, Sharma, Praveen, Tocci, Michael J, Wright, Paul S
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Bentham Open 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3242404/
https://www.ncbi.nlm.nih.gov/pubmed/22207892
http://dx.doi.org/10.2174/1875397301105010122
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author Eishingdrelo, Haifeng
Cai, Jidong
Weissensee, Paul
Sharma, Praveen
Tocci, Michael J
Wright, Paul S
author_facet Eishingdrelo, Haifeng
Cai, Jidong
Weissensee, Paul
Sharma, Praveen
Tocci, Michael J
Wright, Paul S
author_sort Eishingdrelo, Haifeng
collection PubMed
description We have developed a novel cell-based protein-protein interaction assay method. The method relies on conversion of an inactive permuted luciferase containing a Tobacco Etch Virus protease (TEV) cleavage sequence fused onto protein (A) to an active luciferase upon interaction and cleavage by another protein (B) fused with the TEV protease. We demonstrate assay applicability for ligand-induced protein-protein interactions including G-protein coupled receptors, receptor tyrosine kinases and nuclear hormone receptors.
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spelling pubmed-32424042011-12-29 A Cell-Based Protein-Protein Interaction Method Using a Permuted Luciferase Reporter Eishingdrelo, Haifeng Cai, Jidong Weissensee, Paul Sharma, Praveen Tocci, Michael J Wright, Paul S Curr Chem Genomics Article We have developed a novel cell-based protein-protein interaction assay method. The method relies on conversion of an inactive permuted luciferase containing a Tobacco Etch Virus protease (TEV) cleavage sequence fused onto protein (A) to an active luciferase upon interaction and cleavage by another protein (B) fused with the TEV protease. We demonstrate assay applicability for ligand-induced protein-protein interactions including G-protein coupled receptors, receptor tyrosine kinases and nuclear hormone receptors. Bentham Open 2011-11-30 /pmc/articles/PMC3242404/ /pubmed/22207892 http://dx.doi.org/10.2174/1875397301105010122 Text en © Eishingdrelo et al.; Licensee Bentham Open. http://creativecommons.org/licenses/by-nc/3.0/ This is an open access article licensed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited.
spellingShingle Article
Eishingdrelo, Haifeng
Cai, Jidong
Weissensee, Paul
Sharma, Praveen
Tocci, Michael J
Wright, Paul S
A Cell-Based Protein-Protein Interaction Method Using a Permuted Luciferase Reporter
title A Cell-Based Protein-Protein Interaction Method Using a Permuted Luciferase Reporter
title_full A Cell-Based Protein-Protein Interaction Method Using a Permuted Luciferase Reporter
title_fullStr A Cell-Based Protein-Protein Interaction Method Using a Permuted Luciferase Reporter
title_full_unstemmed A Cell-Based Protein-Protein Interaction Method Using a Permuted Luciferase Reporter
title_short A Cell-Based Protein-Protein Interaction Method Using a Permuted Luciferase Reporter
title_sort cell-based protein-protein interaction method using a permuted luciferase reporter
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3242404/
https://www.ncbi.nlm.nih.gov/pubmed/22207892
http://dx.doi.org/10.2174/1875397301105010122
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