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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Bibliographic Details
| Main Authors: |
Yasmine White,
Aditi Bagchi,
Jessica Van Ziffle,
Anagha Inguva,
Gideon Bollag,
Chao Zhang,
Heidi Carias,
David Dickens,
Mignon Loh,
Kevin Shannon,
Ari J. Firestone |
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| Format: | Article
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| Language: | English |
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| Published: |
Nature Portfolio
2016-02-01
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| Series: | Nature Communications
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| Online Access: | https://doi.org/10.1038/ncomms10647
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