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Versatile synthesis of the signaling peptide glorin

We present a versatile synthesis of the eukaryotic signaling peptide glorin as well as glorinamide, a synthetic analog. The ability of these compounds to activate glorin-induced genes in the social amoeba Polysphondylium pallidum was evaluated by quantitative reverse transcription PCR, whereby both...

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Detalles Bibliográficos
Autores principales: Barnett, Robert, Raszkowski, Daniel, Winckler, Thomas, Stallforth, Pierre
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Beilstein-Institut 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5331329/
https://www.ncbi.nlm.nih.gov/pubmed/28326133
http://dx.doi.org/10.3762/bjoc.13.27
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author Barnett, Robert
Raszkowski, Daniel
Winckler, Thomas
Stallforth, Pierre
author_facet Barnett, Robert
Raszkowski, Daniel
Winckler, Thomas
Stallforth, Pierre
author_sort Barnett, Robert
collection PubMed
description We present a versatile synthesis of the eukaryotic signaling peptide glorin as well as glorinamide, a synthetic analog. The ability of these compounds to activate glorin-induced genes in the social amoeba Polysphondylium pallidum was evaluated by quantitative reverse transcription PCR, whereby both compounds showed bioactivity comparable to a glorin standard. This synthetic route will be useful in conducting detailed structure–activity relationship studies as well as in the design of chemical probes to dissect glorin-mediated signaling pathways.
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spelling pubmed-53313292017-03-21 Versatile synthesis of the signaling peptide glorin Barnett, Robert Raszkowski, Daniel Winckler, Thomas Stallforth, Pierre Beilstein J Org Chem Full Research Paper We present a versatile synthesis of the eukaryotic signaling peptide glorin as well as glorinamide, a synthetic analog. The ability of these compounds to activate glorin-induced genes in the social amoeba Polysphondylium pallidum was evaluated by quantitative reverse transcription PCR, whereby both compounds showed bioactivity comparable to a glorin standard. This synthetic route will be useful in conducting detailed structure–activity relationship studies as well as in the design of chemical probes to dissect glorin-mediated signaling pathways. Beilstein-Institut 2017-02-08 /pmc/articles/PMC5331329/ /pubmed/28326133 http://dx.doi.org/10.3762/bjoc.13.27 Text en Copyright © 2017, Barnett et al. https://creativecommons.org/licenses/by/4.0https://www.beilstein-journals.org/bjoc/termsThis is an Open Access article under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The license is subject to the Beilstein Journal of Organic Chemistry terms and conditions: (https://www.beilstein-journals.org/bjoc/terms)
spellingShingle Full Research Paper
Barnett, Robert
Raszkowski, Daniel
Winckler, Thomas
Stallforth, Pierre
Versatile synthesis of the signaling peptide glorin
title Versatile synthesis of the signaling peptide glorin
title_full Versatile synthesis of the signaling peptide glorin
title_fullStr Versatile synthesis of the signaling peptide glorin
title_full_unstemmed Versatile synthesis of the signaling peptide glorin
title_short Versatile synthesis of the signaling peptide glorin
title_sort versatile synthesis of the signaling peptide glorin
topic Full Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5331329/
https://www.ncbi.nlm.nih.gov/pubmed/28326133
http://dx.doi.org/10.3762/bjoc.13.27
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