Quantifying protein dynamics and stability in a living organism

As an integral part of modern cell biology, fluorescence microscopy enables quantification of the stability and dynamics of fluorescence-labeled biomolecules inside cultured cells. However, obtaining time-resolved data from individual cells within a live vertebrate organism remains challenging. Here...

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Detalles Bibliográficos
Autores principales: Feng, Ruopei, Gruebele, Martin, Davis, Caitlin M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6414637/
https://www.ncbi.nlm.nih.gov/pubmed/30862837
http://dx.doi.org/10.1038/s41467-019-09088-y
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author Feng, Ruopei
Gruebele, Martin
Davis, Caitlin M.
author_facet Feng, Ruopei
Gruebele, Martin
Davis, Caitlin M.
author_sort Feng, Ruopei
collection PubMed
description As an integral part of modern cell biology, fluorescence microscopy enables quantification of the stability and dynamics of fluorescence-labeled biomolecules inside cultured cells. However, obtaining time-resolved data from individual cells within a live vertebrate organism remains challenging. Here we demonstrate a customized pipeline that integrates meganuclease-mediated mosaic transformation with fluorescence-detected temperature-jump microscopy to probe dynamics and stability of endogenously expressed proteins in different tissues of living multicellular organisms.
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spelling pubmed-64146372019-03-14 Quantifying protein dynamics and stability in a living organism Feng, Ruopei Gruebele, Martin Davis, Caitlin M. Nat Commun Article As an integral part of modern cell biology, fluorescence microscopy enables quantification of the stability and dynamics of fluorescence-labeled biomolecules inside cultured cells. However, obtaining time-resolved data from individual cells within a live vertebrate organism remains challenging. Here we demonstrate a customized pipeline that integrates meganuclease-mediated mosaic transformation with fluorescence-detected temperature-jump microscopy to probe dynamics and stability of endogenously expressed proteins in different tissues of living multicellular organisms. Nature Publishing Group UK 2019-03-12 /pmc/articles/PMC6414637/ /pubmed/30862837 http://dx.doi.org/10.1038/s41467-019-09088-y Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as 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 images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Feng, Ruopei
Gruebele, Martin
Davis, Caitlin M.
Quantifying protein dynamics and stability in a living organism
title Quantifying protein dynamics and stability in a living organism
title_full Quantifying protein dynamics and stability in a living organism
title_fullStr Quantifying protein dynamics and stability in a living organism
title_full_unstemmed Quantifying protein dynamics and stability in a living organism
title_short Quantifying protein dynamics and stability in a living organism
title_sort quantifying protein dynamics and stability in a living organism
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6414637/
https://www.ncbi.nlm.nih.gov/pubmed/30862837
http://dx.doi.org/10.1038/s41467-019-09088-y
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