H
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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Journal ArticleDOI
RSC, an Essential, Abundant Chromatin-Remodeling Complex
Bradley R. Cairns,Yahli Lorch,Yang Li,Mincheng Zhang,Lynne Lacomis,Hediye Erdjument-Bromage,Paul Tempst,Jian Du,Brehon C. Laurent,Roger D. Kornberg +9 more
TL;DR: A novel 15-subunit complex with the capacity to remodel the structure of chromatin, termed RSC, has been isolated from S. cerevisiae on the basis of homology to the SWI/SNF complex and is essential for mitotic growth.
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NEDD4-1 Is a Proto-Oncogenic Ubiquitin Ligase for PTEN
Xinjiang Wang,Lloyd C. Trotman,Theresa M. Koppie,Andrea Alimonti,Zhenbang Chen,Zhonghua Gao,Junru Wang,Hediye Erdjument-Bromage,Paul Tempst,Carlos Cordon-Cardo,Pier Paolo Pandolfi,Xuejun Jiang +11 more
TL;DR: It is shown that PTEN level is regulated by ubiquitin-mediated proteasomal degradation, and purified its ubiquitIn ligase as HECT-domain protein NEDD4-1, a potential proto-oncogene that negatively regulates PTEN via ubiquitination, a paradigm analogous to that of Mdm2 and p53.
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The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36.
Robert J. Klose,Kenichi Yamane,Kenichi Yamane,Yangjin Bae,Dianzheng Zhang,Hediye Erdjument-Bromage,Paul Tempst,Jiemin Wong,Yi Zhang,Yi Zhang +9 more
TL;DR: It is demonstrated that JHDM3A (jumonji C (JmjC)-domain-containing histone demethylase 3A) is capable of removing the me3 group from modified H3 lysine 9 (H3K9) and H3Lysine 36 (H2K36), indicating that J HDD3A may function in euchromatin to remove histone methylation marks that are associated with active transcription.
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Erythroid transcription factor NF-E2 is a haematopoietic-specific basic-leucine zipper protein.
Nancy C. Andrews,Hediye Erdjument-Bromage,Mark B. Davidson,Paul Tempst,Stuart H. Orkin,Stuart H. Orkin +5 more
TL;DR: Activity of these regions in vivo requires an erythroid-specific nuclear factor that binds AP-1-like recognition sites and its tissue-specific component has been characterized by complementary DNA cloning as a new basic region–leucine zipper protein which dimerizes with a ubiquitous partner to form native NF-E2.
Journal ArticleDOI
An iron delivery pathway mediated by a lipocalin
Jun Yang,David H. Goetz,Jau Yi Li,Wenge Wang,Kiyoshi Mori,Daria Setlik,Tonggong Du,Hediye Erdjument-Bromage,Paul Tempst,Roland K. Strong,Jonathan Barasch +10 more
TL;DR: It is shown that a member of the lipocalin superfamily (24p3/Ngal) delivers iron to the cytoplasm where it activates or represses iron-responsive genes and identifies an iron delivery pathway active in development and cell physiology.