ArticleNature communications2016
KRAS insertion mutations are oncogenic and exhibit distinct functional properties.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 17 citations in OpenAlex.
- Harnessing liquid biopsy to unveil RAS-MEK pathway somatic pathogenic variants in extracranial arterio-venous malformations.Communications medicine · 2025Article
- Excited-state observation of active K-Ras reveals differential structural dynamics of wild-type versus oncogenic G12D and G12C mutants.Nature structural & molecular biology · 2023Article
- A saturation-mutagenesis analysis of the interplay between stability and activation in Ras.eLife · 2022Article
- Rational antibody design for undruggable targets using kinetically controlled biomolecular probes.Science advances · 2021Article
- Article
- KRAS and BRAF mutations in Iranian colorectal cancer patients: A systematic review and meta-analysis.Caspian journal of internal medicine · 2020Review
- Functional characterisation of a novel class of in-frame insertion variants of KRAS and HRAS.Scientific reports · 2019Article
- Analysis of acquired mutations in transgenes arising in Ba/F3 transformation assays: findings and recommendations.Oncotarget · 2017Article
- Article
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
Abstract
Oncogenic KRAS mutations introduce discrete amino acid substitutions that reduce intrinsic Ras GTPase activity and confer resistance to GTPase-activating proteins (GAPs). Here we discover a partial duplication of the switch 2 domain of K-Ras encoding a tandem repeat of amino acids G60_A66dup in a child with an atypical myeloproliferative neoplasm. K-Ras proteins containing this tandem duplication or a similar five amino acid E62_A66dup mutation identified in lung and colon cancers transform the growth of primary myeloid progenitors and of Ba/F3 cells. Recombinant K-Ras(G60_A66dup) and K-Ras(E62_A66dup) proteins display reduced intrinsic GTP hydrolysis rates, accumulate in the GTP-bound conformation and are resistant to GAP-mediated GTP hydrolysis. Remarkably, K-Ras proteins with switch 2 insertions are impaired for PI3 kinase binding and Akt activation, and are hypersensitive to MEK inhibition. These studies illuminate a new class of oncogenic KRAS mutations and reveal unexpected plasticity in oncogenic Ras proteins that has diagnostic and therapeutic implications.
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Registered trials
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