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Diana Mandelker

Researcher at Johns Hopkins University

Publications -  17
Citations -  4192

Diana Mandelker is an academic researcher from Johns Hopkins University. The author has contributed to research in topics: Medicine & Internal medicine. The author has an hindex of 8, co-authored 10 publications receiving 4095 citations. Previous affiliations of Diana Mandelker include Johns Hopkins University School of Medicine & Howard Hughes Medical Institute.

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Consensus coding sequences of human breast and colorectal cancers

TL;DR: In this paper, the authors analyzed 13,023 genes in 11 breast and 11 colorectal cancers and found that individual tumors accumulate an average of 90 mutant genes but only a subset of these contribute to the neoplastic process.
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The Structure of a Human p110α/p85α Complex Elucidates the Effects of Oncogenic PI3Kα Mutations

TL;DR: The structure of PI3Kα shows that many of the mutations occur at residues lying at the interfaces between p110 α and p85α or between the kinase domain of p110α and other domains within the catalytic subunit, which suggests specific mechanisms for the effect of oncogenic mutations.
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A frequent kinase domain mutation that changes the interaction between PI3Kα and the membrane

TL;DR: Structural and biochemical data suggest a previously undescribed mechanism for mutational activation of a kinase that involves perturbation of its interaction with the cellular membrane, which is differentially regulated by lipid membrane composition.
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PGP9.5 promoter methylation is an independent prognostic factor for esophageal squamous cell carcinoma.

TL;DR: Results suggest that PGP9.5 promoter methylation could be a clinically applicable marker for ESCC progression, as well as an independent prognostic factor for ES CC survival.
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Structural comparisons of class I phosphoinositide 3-kinases

TL;DR: The recently determined structure of PI3Kα reveals features that distinguish this enzyme from related lipid kinases, and identified structural features that could potentially be exploited for the design of isoform-specific inhibitors.