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J Med Chem 2017

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VadK binding sites are essential for growth on propionate To directly assess the function of the phosphohistidine and ATP-binding domains in propionate metabolism, we constructed an isogenic panel of vadK mutants by complementing vadK with a chromosomally integrated copy of vadK encoding mutations in the His422 catalytic residue

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(1.1) as a single agent for the treatment of patients with recurrent, metastatic non-squamous, NSCLC after prior chemotherapy

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