Unknown

Dataset Information

0

Quantifying protein dynamics and stability in a living organism.


ABSTRACT: 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.

SUBMITTER: Feng R 

PROVIDER: S-EPMC6414637 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

Quantifying protein dynamics and stability in a living organism.

Feng Ruopei R   Gruebele Martin M   Davis Caitlin M CM  

Nature communications 20190312 1


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  ...[more]

Similar Datasets

| S-EPMC4970330 | biostudies-literature
| S-EPMC6045628 | biostudies-literature
| S-EPMC7295171 | biostudies-literature
| S-EPMC2042177 | biostudies-literature
| S-EPMC6016732 | biostudies-literature
| S-EPMC3123922 | biostudies-literature
| S-EPMC6594219 | biostudies-literature
| S-EPMC4128145 | biostudies-literature
| S-EPMC5161448 | biostudies-literature
| S-EPMC5612114 | biostudies-literature