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Tetrazine ligation for chemical proteomics

Determining small molecule—target protein interaction is essential for the chemical proteomics. One of the most important keys to explore biological system in chemical proteomics field is finding first-class molecular tools. Chemical probes can provide great spatiotemporal control to elucidate biolo...

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Detalles Bibliográficos
Autores principales: Kang, Kyungtae, Park, Jongmin, Kim, Eunha
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5485739/
https://www.ncbi.nlm.nih.gov/pubmed/28674480
http://dx.doi.org/10.1186/s12953-017-0121-5
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author Kang, Kyungtae
Park, Jongmin
Kim, Eunha
author_facet Kang, Kyungtae
Park, Jongmin
Kim, Eunha
author_sort Kang, Kyungtae
collection PubMed
description Determining small molecule—target protein interaction is essential for the chemical proteomics. One of the most important keys to explore biological system in chemical proteomics field is finding first-class molecular tools. Chemical probes can provide great spatiotemporal control to elucidate biological functions of proteins as well as for interrogating biological pathways. The invention of bioorthogonal chemistry has revolutionized the field of chemical biology by providing superior chemical tools and has been widely used for investigating the dynamics and function of biomolecules in live condition. Among 20 different bioorthogonal reactions, tetrazine ligation has been spotlighted as the most advanced bioorthogonal chemistry because of their extremely faster kinetics and higher specificity than others. Therefore, tetrazine ligation has a tremendous potential to enhance the proteomic research. This review highlights the current status of tetrazine ligation reaction as a molecular tool for the chemical proteomics.
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spelling pubmed-54857392017-07-03 Tetrazine ligation for chemical proteomics Kang, Kyungtae Park, Jongmin Kim, Eunha Proteome Sci Review Determining small molecule—target protein interaction is essential for the chemical proteomics. One of the most important keys to explore biological system in chemical proteomics field is finding first-class molecular tools. Chemical probes can provide great spatiotemporal control to elucidate biological functions of proteins as well as for interrogating biological pathways. The invention of bioorthogonal chemistry has revolutionized the field of chemical biology by providing superior chemical tools and has been widely used for investigating the dynamics and function of biomolecules in live condition. Among 20 different bioorthogonal reactions, tetrazine ligation has been spotlighted as the most advanced bioorthogonal chemistry because of their extremely faster kinetics and higher specificity than others. Therefore, tetrazine ligation has a tremendous potential to enhance the proteomic research. This review highlights the current status of tetrazine ligation reaction as a molecular tool for the chemical proteomics. BioMed Central 2017-06-26 /pmc/articles/PMC5485739/ /pubmed/28674480 http://dx.doi.org/10.1186/s12953-017-0121-5 Text en © The Author(s). 2017 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Review
Kang, Kyungtae
Park, Jongmin
Kim, Eunha
Tetrazine ligation for chemical proteomics
title Tetrazine ligation for chemical proteomics
title_full Tetrazine ligation for chemical proteomics
title_fullStr Tetrazine ligation for chemical proteomics
title_full_unstemmed Tetrazine ligation for chemical proteomics
title_short Tetrazine ligation for chemical proteomics
title_sort tetrazine ligation for chemical proteomics
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5485739/
https://www.ncbi.nlm.nih.gov/pubmed/28674480
http://dx.doi.org/10.1186/s12953-017-0121-5
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