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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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Tandem bromodomains in the chromatin remodeler RSC recognize acetylated histone H3 Lys14

TL;DR: Rsc4 bears essential tandem bromodomains that rely on H3 Lys14 acetylation to assist RSC complex for gene activation, and displays defects in the activation of genes involved in nicotinic acid biosynthesis, cell wall integrity, and other pathways.
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PARP-1 Determines Specificity in a Retinoid Signaling Pathway via Direct Modulation of Mediator

TL;DR: It is shown that PARP-1 is indispensable to retinoic acid receptor (RAR)-mediated transcription from the RARbeta2 promoter in a highly purified, reconstituted transcription system and that RA-inducible expression of all RAR beta isoforms is abrogated in PARP -1(-/-) cells in vivo.
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Affinity-based proteomics reveal cancer-specific networks coordinated by Hsp90

TL;DR: This work uses PU-H71 affinity capture to design a proteomic approach that, when combined with bioinformatic pathway analysis, identifies dysregulated signaling networks and key oncoproteins in chronic myeloid leukemia and shows that this method can provide global insights into the biology of individual tumors, including primary patient specimens.
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Five Members of a Novel Ca2+-binding Protein (CABP) Subfamily with Similarity to Calmodulin

TL;DR: Five members of a novel Ca2+-binding protein subfamily (CaBP), with 46–58% sequence similarity to calmodulin (CaM), were identified in the vertebrate retina, suggesting that these novel CaBPs are an important component of Ca2-mediated cellular signal transduction in the central nervous system where they may augment or substitute for CaM.
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A new role for Nogo as a regulator of vascular remodeling.

TL;DR: It is shown that Nogo-B is highly expressed in cultured endothelial and smooth muscle cells, as well as in intact blood vessels, and is a regulator of vascular homeostasis and remodeling.