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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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A glutathione S-transferase (GST) isozyme from broccoli with significant sequence homology to the mammalian theta-class of GSTs

TL;DR: The characteristics of the broccoli GST potentially define it as a member of the theta-class, consistent with the view that the theTA-class may have arisen prior to the divergence of animals and plants while the mammalian mu-, pi- and alpha-classes evolved after the two kingdoms were established.
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Schizosaccharomyces pombe carboxyl-terminal domain (CTD) phosphatase Fcp1: distributive mechanism, minimal CTD substrate, and active site mapping.

TL;DR: This work shows that Fcp1 acts distributively during the hydrolysis of substrates containing tandem Ser2-PO4 heptad repeat Y1S2P3T4S5P6S7 and highlights a constellation of 11 amino acids that are conserved in all FCP1 orthologs and likely comprise the active site.
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Photoaffinity labeling and mass spectrometry identify ribosomal protein S3 as a potential target for hybrid polar cytodifferentiation agents.

TL;DR: This work synthesized a photoaffinity labeling reagent structurally based on SAHA, and probed for SAHA-binding proteins in murine erythroleukemia (MEL) cells, identifying a 32-kDa protein (p32) that was specifically labeled by the photoAffinity reagent.
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The laminin receptor modulates granulocyte–macrophage colony-stimulating factor receptor complex formation and modulates its signaling

TL;DR: Findings provide a mechanistic basis for enhancing host defense cell responsiveness to GM-CSF at transendothelial migration sites while suppressing it in circulation.
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The C-terminal domain phosphatase and transcription elongation activities of FCP1 are regulated by phosphorylation

TL;DR: It is demonstrated that FCP1 is a phosphoprotein, and that phosphorylation regulates FCP 1 activities, and it is found that only phosphorylated F CP1 can physically interact with TFIIF.