Bioorthogonal Chemical Activation of Kinases in Living Systems

[Image: see text] Selective manipulation of protein kinases under living conditions is highly desirable yet extremely challenging, particularly in a gain-of-function fashion. Here we employ our recently developed bioorthogonal cleavage reaction as a general strategy for intracellular activation of i...

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Autores principales: Zhang, Gong, Li, Jie, Xie, Ran, Fan, Xinyuan, Liu, Yanjun, Zheng, Siqi, Ge, Yun, Chen, Peng R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2016
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4882735/
https://www.ncbi.nlm.nih.gov/pubmed/27280167
http://dx.doi.org/10.1021/acscentsci.6b00024
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author Zhang, Gong
Li, Jie
Xie, Ran
Fan, Xinyuan
Liu, Yanjun
Zheng, Siqi
Ge, Yun
Chen, Peng R.
author_facet Zhang, Gong
Li, Jie
Xie, Ran
Fan, Xinyuan
Liu, Yanjun
Zheng, Siqi
Ge, Yun
Chen, Peng R.
author_sort Zhang, Gong
collection PubMed
description [Image: see text] Selective manipulation of protein kinases under living conditions is highly desirable yet extremely challenging, particularly in a gain-of-function fashion. Here we employ our recently developed bioorthogonal cleavage reaction as a general strategy for intracellular activation of individual kinases. Site-specific incorporation of trans-cyclooctene-caged lysine in place of the conserved catalytic lysine, in conjunction with the cleavage partner dimethyl-tetrazine, allowed efficient lysine decaging with the kinase activity chemically rescued in living systems.
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spelling pubmed-48827352016-06-08 Bioorthogonal Chemical Activation of Kinases in Living Systems Zhang, Gong Li, Jie Xie, Ran Fan, Xinyuan Liu, Yanjun Zheng, Siqi Ge, Yun Chen, Peng R. ACS Cent Sci [Image: see text] Selective manipulation of protein kinases under living conditions is highly desirable yet extremely challenging, particularly in a gain-of-function fashion. Here we employ our recently developed bioorthogonal cleavage reaction as a general strategy for intracellular activation of individual kinases. Site-specific incorporation of trans-cyclooctene-caged lysine in place of the conserved catalytic lysine, in conjunction with the cleavage partner dimethyl-tetrazine, allowed efficient lysine decaging with the kinase activity chemically rescued in living systems. American Chemical Society 2016-04-27 2016-05-25 /pmc/articles/PMC4882735/ /pubmed/27280167 http://dx.doi.org/10.1021/acscentsci.6b00024 Text en Copyright © 2016 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
spellingShingle Zhang, Gong
Li, Jie
Xie, Ran
Fan, Xinyuan
Liu, Yanjun
Zheng, Siqi
Ge, Yun
Chen, Peng R.
Bioorthogonal Chemical Activation of Kinases in Living Systems
title Bioorthogonal Chemical Activation of Kinases in Living Systems
title_full Bioorthogonal Chemical Activation of Kinases in Living Systems
title_fullStr Bioorthogonal Chemical Activation of Kinases in Living Systems
title_full_unstemmed Bioorthogonal Chemical Activation of Kinases in Living Systems
title_short Bioorthogonal Chemical Activation of Kinases in Living Systems
title_sort bioorthogonal chemical activation of kinases in living systems
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4882735/
https://www.ncbi.nlm.nih.gov/pubmed/27280167
http://dx.doi.org/10.1021/acscentsci.6b00024
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