Selective inhibition of STAT3 signaling using monobodies targeting the coiled-coil and N-terminal domains

STAT3 is an attractive therapeutic target but its homology with other STAT proteins complicates the development of selective inhibitors. Here, the authors develop monobodies with high affinity and selectivity for STAT3 and show that they can interfere with cellular STAT3 activity.

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Autores principales: Grégory La Sala, Camille Michiels, Tim Kükenshöner, Tania Brandstoetter, Barbara Maurer, Akiko Koide, Kelvin Lau, Florence Pojer, Shohei Koide, Veronika Sexl, Laure Dumoutier, Oliver Hantschel
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Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/709f9a713ee849dc860cc5c099ffede8
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spelling oai:doaj.org-article:709f9a713ee849dc860cc5c099ffede82021-12-02T15:10:51ZSelective inhibition of STAT3 signaling using monobodies targeting the coiled-coil and N-terminal domains10.1038/s41467-020-17920-z2041-1723https://doaj.org/article/709f9a713ee849dc860cc5c099ffede82020-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-17920-zhttps://doaj.org/toc/2041-1723STAT3 is an attractive therapeutic target but its homology with other STAT proteins complicates the development of selective inhibitors. Here, the authors develop monobodies with high affinity and selectivity for STAT3 and show that they can interfere with cellular STAT3 activity.Grégory La SalaCamille MichielsTim KükenshönerTania BrandstoetterBarbara MaurerAkiko KoideKelvin LauFlorence PojerShohei KoideVeronika SexlLaure DumoutierOliver HantschelNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-16 (2020)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Grégory La Sala
Camille Michiels
Tim Kükenshöner
Tania Brandstoetter
Barbara Maurer
Akiko Koide
Kelvin Lau
Florence Pojer
Shohei Koide
Veronika Sexl
Laure Dumoutier
Oliver Hantschel
Selective inhibition of STAT3 signaling using monobodies targeting the coiled-coil and N-terminal domains
description STAT3 is an attractive therapeutic target but its homology with other STAT proteins complicates the development of selective inhibitors. Here, the authors develop monobodies with high affinity and selectivity for STAT3 and show that they can interfere with cellular STAT3 activity.
format article
author Grégory La Sala
Camille Michiels
Tim Kükenshöner
Tania Brandstoetter
Barbara Maurer
Akiko Koide
Kelvin Lau
Florence Pojer
Shohei Koide
Veronika Sexl
Laure Dumoutier
Oliver Hantschel
author_facet Grégory La Sala
Camille Michiels
Tim Kükenshöner
Tania Brandstoetter
Barbara Maurer
Akiko Koide
Kelvin Lau
Florence Pojer
Shohei Koide
Veronika Sexl
Laure Dumoutier
Oliver Hantschel
author_sort Grégory La Sala
title Selective inhibition of STAT3 signaling using monobodies targeting the coiled-coil and N-terminal domains
title_short Selective inhibition of STAT3 signaling using monobodies targeting the coiled-coil and N-terminal domains
title_full Selective inhibition of STAT3 signaling using monobodies targeting the coiled-coil and N-terminal domains
title_fullStr Selective inhibition of STAT3 signaling using monobodies targeting the coiled-coil and N-terminal domains
title_full_unstemmed Selective inhibition of STAT3 signaling using monobodies targeting the coiled-coil and N-terminal domains
title_sort selective inhibition of stat3 signaling using monobodies targeting the coiled-coil and n-terminal domains
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/709f9a713ee849dc860cc5c099ffede8
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