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Cell-free expression of functional receptor tyrosine kinases

Receptor tyrosine kinases (RTKs) play critical roles in physiological and pathological processes, and are important anticancer drug targets. In vitro mechanistic and drug discovery studies of full-length RTKs require protein that is both fully functional and free from contaminating proteins. Here we...

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Autores principales: He, Wei, Scharadin, Tiffany M., Saldana, Matthew, Gellner, Candice, Hoang-Phou, Steven, Takanishi, Christina, Hura, Gregory L., Tainer, John A, Carraway III, Kermit L., Henderson, Paul T., Coleman, Matthew A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4929682/
https://www.ncbi.nlm.nih.gov/pubmed/26274523
http://dx.doi.org/10.1038/srep12896
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author He, Wei
Scharadin, Tiffany M.
Saldana, Matthew
Gellner, Candice
Hoang-Phou, Steven
Takanishi, Christina
Hura, Gregory L.
Tainer, John A
Carraway III, Kermit L.
Henderson, Paul T.
Coleman, Matthew A.
author_facet He, Wei
Scharadin, Tiffany M.
Saldana, Matthew
Gellner, Candice
Hoang-Phou, Steven
Takanishi, Christina
Hura, Gregory L.
Tainer, John A
Carraway III, Kermit L.
Henderson, Paul T.
Coleman, Matthew A.
author_sort He, Wei
collection PubMed
description Receptor tyrosine kinases (RTKs) play critical roles in physiological and pathological processes, and are important anticancer drug targets. In vitro mechanistic and drug discovery studies of full-length RTKs require protein that is both fully functional and free from contaminating proteins. Here we describe a rapid cell-free and detergent-free co-translation method for producing full-length and functional ERBB2 and EGFR receptor tyrosine kinases supported by water-soluble apolipoprotein A-I based nanolipoprotein particles.
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spelling pubmed-49296822016-07-06 Cell-free expression of functional receptor tyrosine kinases He, Wei Scharadin, Tiffany M. Saldana, Matthew Gellner, Candice Hoang-Phou, Steven Takanishi, Christina Hura, Gregory L. Tainer, John A Carraway III, Kermit L. Henderson, Paul T. Coleman, Matthew A. Sci Rep Article Receptor tyrosine kinases (RTKs) play critical roles in physiological and pathological processes, and are important anticancer drug targets. In vitro mechanistic and drug discovery studies of full-length RTKs require protein that is both fully functional and free from contaminating proteins. Here we describe a rapid cell-free and detergent-free co-translation method for producing full-length and functional ERBB2 and EGFR receptor tyrosine kinases supported by water-soluble apolipoprotein A-I based nanolipoprotein particles. Nature Publishing Group 2015-08-14 /pmc/articles/PMC4929682/ /pubmed/26274523 http://dx.doi.org/10.1038/srep12896 Text en Copyright © 2015, Macmillan Publishers Limited http://creativecommons.org/licenses/by-nc-nd/4.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/4.0/
spellingShingle Article
He, Wei
Scharadin, Tiffany M.
Saldana, Matthew
Gellner, Candice
Hoang-Phou, Steven
Takanishi, Christina
Hura, Gregory L.
Tainer, John A
Carraway III, Kermit L.
Henderson, Paul T.
Coleman, Matthew A.
Cell-free expression of functional receptor tyrosine kinases
title Cell-free expression of functional receptor tyrosine kinases
title_full Cell-free expression of functional receptor tyrosine kinases
title_fullStr Cell-free expression of functional receptor tyrosine kinases
title_full_unstemmed Cell-free expression of functional receptor tyrosine kinases
title_short Cell-free expression of functional receptor tyrosine kinases
title_sort cell-free expression of functional receptor tyrosine kinases
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4929682/
https://www.ncbi.nlm.nih.gov/pubmed/26274523
http://dx.doi.org/10.1038/srep12896
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