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Oncogenic mutations in RAS provide a compelling yet intractable therapeutic target. Using co-immunoprecipitation mass spectrometry, we uncovered an interaction between RAS and Argonaute 2 (AGO2). Endogenously, RAS and AGO2 co-sediment and co-localize in the endoplasmic reticulum. The AGO2 N-terminal domain directly binds the Switch II region of KRAS,(More)
  • A Gruber, Ahagon, +25 authors D J Gapped
  • 2003
DNA reads generated by large-scale sequencing projects have to be processed before further analyses in order to perform vector/primer masking, low-quality trimming and contaminant removal. This sequential processing involves several steps and the use of different computer programs, each one following its own calling convention and input/output formats. As a(More)
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(More)
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