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@ARTICLE{Wingen:829997,
author = {Wingen, Marcus and Jaeger, Karl-Erich and Gensch, Thomas
and Drepper, Thomas},
title = {{N}ovel {T}hermostable {F}lavin-binding {F}luorescent
{P}roteins from {T}hermophilic {O}rganisms},
journal = {Photochemistry and photobiology},
volume = {93},
number = {3},
issn = {0031-8655},
address = {Malden, Mass.},
publisher = {Wiley-Blackwell},
reportid = {FZJ-2017-03599},
pages = {849 - 856},
year = {2017},
abstract = {Flavin-binding fluorescent proteins (FbFPs) are small,
oxygen-independent in vivo reporters, derived from Light
Oxygen Voltage (LOV) domains of photoreceptors. Here, we
investigated the thermostability of existing, as well as
novel FbFPs, whose genes were identified in genome sequences
of various thermophilic bacteria as well as metagenomic
libraries from hot springs in the Yellowstone National Park.
Detailed in vitro analyses revealed that two of those
fluorescent reporter proteins were highly thermostable,
exhibiting melting temperatures above 75°C.},
cin = {ICS-4 / IMET},
ddc = {570},
cid = {I:(DE-Juel1)ICS-4-20110106 / I:(DE-Juel1)IMET-20090612},
pnm = {552 - Engineering Cell Function (POF3-552) / 581 -
Biotechnology (POF3-581)},
pid = {G:(DE-HGF)POF3-552 / G:(DE-HGF)POF3-581},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000401262000023},
pubmed = {pmid:28500719},
doi = {10.1111/php.12740},
url = {https://juser.fz-juelich.de/record/829997},
}