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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2017
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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. |
format | Online Article Text |
id | pubmed-5485739 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT kangkyungtae tetrazineligationforchemicalproteomics AT parkjongmin tetrazineligationforchemicalproteomics AT kimeunha tetrazineligationforchemicalproteomics |