A Photoactivatable GFP for Selective Photolabeling of Proteins and Cells. Patterson, G. H. & Lippincott-Schwartz, J. Science, 297(5588):1873--1877, September, 2002. Paper doi abstract bibtex We report a photoactivatable variant of theAequorea victoria green fluorescent protein (GFP) that, after intense irradiation with 413-nanometer light, increases fluorescence 100 times when excited by 488-nanometer light and remains stable for days under aerobic conditions. These characteristics offer a new tool for exploring intracellular protein dynamics by tracking photoactivated molecules that are the only visible GFPs in the cell. Here, we use the photoactivatable GFP both as a free protein to measure protein diffusion across the nuclear envelope and as a chimera with a lysosomal membrane protein to demonstrate rapid interlysosomal membrane exchange.
@article{patterson_photoactivatable_2002,
title = {A {Photoactivatable} {GFP} for {Selective} {Photolabeling} of {Proteins} and {Cells}},
volume = {297},
issn = {0036-8075, 1095-9203},
url = {http://www.sciencemag.org/content/297/5588/1873},
doi = {10.1126/science.1074952},
abstract = {We report a photoactivatable variant of theAequorea victoria green fluorescent protein (GFP) that, after intense irradiation with 413-nanometer light, increases fluorescence 100 times when excited by 488-nanometer light and remains stable for days under aerobic conditions. These characteristics offer a new tool for exploring intracellular protein dynamics by tracking photoactivated molecules that are the only visible GFPs in the cell. Here, we use the photoactivatable GFP both as a free protein to measure protein diffusion across the nuclear envelope and as a chimera with a lysosomal membrane protein to demonstrate rapid interlysosomal membrane exchange.},
language = {en},
number = {5588},
urldate = {2014-05-19TZ},
journal = {Science},
author = {Patterson, George H. and Lippincott-Schwartz, Jennifer},
month = sep,
year = {2002},
pmid = {12228718},
pages = {1873--1877}
}
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