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Photoconversion in orange and red fluorescent proteins

We report that photoconversion is fairly common among orange and red fluorescent proteins, as a screen of 12 variants yielded 8 that exhibit photoconversion. Specifically, three red fluorescent proteins can be switched into a green state, and two orange variants can be photoconverted to the far red....

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Detalles Bibliográficos
Autores principales: Kremers, Gert-Jan, Hazelwood, Kristin L., Murphy, Christopher S., Davidson, Michael W., Piston, David W.
Formato: Texto
Lenguaje:English
Publicado: 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2675661/
https://www.ncbi.nlm.nih.gov/pubmed/19363494
http://dx.doi.org/10.1038/nmeth.1319
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author Kremers, Gert-Jan
Hazelwood, Kristin L.
Murphy, Christopher S.
Davidson, Michael W.
Piston, David W.
author_facet Kremers, Gert-Jan
Hazelwood, Kristin L.
Murphy, Christopher S.
Davidson, Michael W.
Piston, David W.
author_sort Kremers, Gert-Jan
collection PubMed
description We report that photoconversion is fairly common among orange and red fluorescent proteins, as a screen of 12 variants yielded 8 that exhibit photoconversion. Specifically, three red fluorescent proteins can be switched into a green state, and two orange variants can be photoconverted to the far red. The orange highlighters are ideal for dual-probe highlighter applications, and they exhibit the most red-shifted excitation of all fluorescent protein described to date.
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spelling pubmed-26756612009-11-01 Photoconversion in orange and red fluorescent proteins Kremers, Gert-Jan Hazelwood, Kristin L. Murphy, Christopher S. Davidson, Michael W. Piston, David W. Nat Methods Article We report that photoconversion is fairly common among orange and red fluorescent proteins, as a screen of 12 variants yielded 8 that exhibit photoconversion. Specifically, three red fluorescent proteins can be switched into a green state, and two orange variants can be photoconverted to the far red. The orange highlighters are ideal for dual-probe highlighter applications, and they exhibit the most red-shifted excitation of all fluorescent protein described to date. 2009-04-12 2009-05 /pmc/articles/PMC2675661/ /pubmed/19363494 http://dx.doi.org/10.1038/nmeth.1319 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Kremers, Gert-Jan
Hazelwood, Kristin L.
Murphy, Christopher S.
Davidson, Michael W.
Piston, David W.
Photoconversion in orange and red fluorescent proteins
title Photoconversion in orange and red fluorescent proteins
title_full Photoconversion in orange and red fluorescent proteins
title_fullStr Photoconversion in orange and red fluorescent proteins
title_full_unstemmed Photoconversion in orange and red fluorescent proteins
title_short Photoconversion in orange and red fluorescent proteins
title_sort photoconversion in orange and red fluorescent proteins
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2675661/
https://www.ncbi.nlm.nih.gov/pubmed/19363494
http://dx.doi.org/10.1038/nmeth.1319
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