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Hediye Erdjument-Bromage

Researcher at Memorial Sloan Kettering Cancer Center

Publications -  251
Citations -  80981

Hediye Erdjument-Bromage is an academic researcher from Memorial Sloan Kettering Cancer Center. The author has contributed to research in topics: Histone code & Histone methyltransferase. The author has an hindex of 128, co-authored 240 publications receiving 76640 citations. Previous affiliations of Hediye Erdjument-Bromage include Kettering University.

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DNMT3L connects unmethylated lysine 4 of histone H3 to de novo methylation of DNA.

TL;DR: DNMT3L recognizes histone H3 tails that are unmethylated at lysine 4 and induces de novo DNA methylation by recruitment or activation of DNMT3A2, and substitution of key residues in the binding site eliminated the H3 tail–DN MT3L interaction.
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Protein S-nitrosylation: a physiological signal for neuronal nitric oxide.

TL;DR: Protein S-nitrosylation is established as a physiological signalling mechanism for neuronally generated NO in mice harbouring a genomic deletion of neuronal NO synthase (nNOS).
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Phosphorylation and Functional Inactivation of TSC2 by Erk: Implications for Tuberous Sclerosis and Cancer Pathogenesis

TL;DR: The findings position the Ras/MAPK pathway upstream of the TSC complex and suggest that Erk may modulate mTOR signaling and contribute to disease progression through phosphorylation and inactivation of TSC2.
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TLR signalling augments macrophage bactericidal activity through mitochondrial ROS

TL;DR: It is demonstrated that engagement of a subset of Toll-like receptors results in the recruitment of mitochondria to macrophage phagosomes and augments mROS production, revealing a novel pathway linking innate immune signalling to mitochondria, implicate mR OS as an important component of antibacterial responses and further establish mitochondria as hubs for innate immune signaling.
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Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation

TL;DR: A novel polypeptide highly related to the metastasis-associated protein 1, MTA2, and the methyl-CpG-binding domain-containing protein, MBD3, were found to be subunits of the NuRD complex, which may provide a means of gene silencing by DNA methylation.