KRAS insertion mutations are oncogenic and exhibit distinct functional properties

Amino acid substitutions in K-Ras that constitutively activate the protein are common in cancer. Here, the authors describe mutations in the K-RasSwitch 2 domain and show that the mutant proteins accumulate in the active conformation, exhibit defective binding to PI3 kinase, and are hypersensitive t...

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Autores principales:	Yasmine White, Aditi Bagchi, Jessica Van Ziffle, Anagha Inguva, Gideon Bollag, Chao Zhang, Heidi Carias, David Dickens, Mignon Loh, Kevin Shannon, Ari J. Firestone
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/c8ee34111da64f238c6f182195674d48
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spelling	oai:doaj.org-article:c8ee34111da64f238c6f182195674d482021-12-02T16:49:58ZKRAS insertion mutations are oncogenic and exhibit distinct functional properties10.1038/ncomms106472041-1723https://doaj.org/article/c8ee34111da64f238c6f182195674d482016-02-01T00:00:00Zhttps://doi.org/10.1038/ncomms10647https://doaj.org/toc/2041-1723Amino acid substitutions in K-Ras that constitutively activate the protein are common in cancer. Here, the authors describe mutations in the K-RasSwitch 2 domain and show that the mutant proteins accumulate in the active conformation, exhibit defective binding to PI3 kinase, and are hypersensitive to MEK inhibitors.Yasmine WhiteAditi BagchiJessica Van ZiffleAnagha InguvaGideon BollagChao ZhangHeidi CariasDavid DickensMignon LohKevin ShannonAri J. FirestoneNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-8 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Yasmine White Aditi Bagchi Jessica Van Ziffle Anagha Inguva Gideon Bollag Chao Zhang Heidi Carias David Dickens Mignon Loh Kevin Shannon Ari J. Firestone KRAS insertion mutations are oncogenic and exhibit distinct functional properties
description	Amino acid substitutions in K-Ras that constitutively activate the protein are common in cancer. Here, the authors describe mutations in the K-RasSwitch 2 domain and show that the mutant proteins accumulate in the active conformation, exhibit defective binding to PI3 kinase, and are hypersensitive to MEK inhibitors.
format	article
author	Yasmine White Aditi Bagchi Jessica Van Ziffle Anagha Inguva Gideon Bollag Chao Zhang Heidi Carias David Dickens Mignon Loh Kevin Shannon Ari J. Firestone
author_facet	Yasmine White Aditi Bagchi Jessica Van Ziffle Anagha Inguva Gideon Bollag Chao Zhang Heidi Carias David Dickens Mignon Loh Kevin Shannon Ari J. Firestone
author_sort	Yasmine White
title	KRAS insertion mutations are oncogenic and exhibit distinct functional properties
title_short	KRAS insertion mutations are oncogenic and exhibit distinct functional properties
title_full	KRAS insertion mutations are oncogenic and exhibit distinct functional properties
title_fullStr	KRAS insertion mutations are oncogenic and exhibit distinct functional properties
title_full_unstemmed	KRAS insertion mutations are oncogenic and exhibit distinct functional properties
title_sort	kras insertion mutations are oncogenic and exhibit distinct functional properties
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/c8ee34111da64f238c6f182195674d48
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KRAS insertion mutations are oncogenic and exhibit distinct functional properties

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