E
Edward B. Ziff
Researcher at New York University
Publications - 136
Citations - 18236
Edward B. Ziff is an academic researcher from New York University. The author has contributed to research in topics: AMPA receptor & PDZ domain. The author has an hindex of 60, co-authored 134 publications receiving 17745 citations. Previous affiliations of Edward B. Ziff include Howard Hughes Medical Institute.
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Journal ArticleDOI
Receptor trafficking and the plasticity of excitatory synapses.
Michael F Barry,Edward B. Ziff +1 more
TL;DR: How subunit type dictates the assembly of heteromeric receptors, and how these heteromers interact with the receptor trafficking machinery and synaptic anchorage factors are described and phosphorylation may play an important role in receptor transport and synaptic turnover.
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Adenovirus E1a proteins repress transcription from the SV40 early promoter
Anna Velcich,Edward B. Ziff +1 more
TL;DR: Using a transient expression assay in HeLa cells, it is shown that products from the adenovirus-5 E1a transcription unit repress transcription from the SV40 early promoter, concluding that activation and repression are separate E 1a functions.
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Identification and Verification of Novel Rodent Postsynaptic Density Proteins
Bryen A. Jordan,Brian D. Fernholz,Muriel Boussac,Chong-Feng Xu,Gabriela Grigorean,Edward B. Ziff,Thomas A. Neubert +6 more
TL;DR: The identification of 452 proteins isolated from biochemically purified PSD fractions of rat and mouse brains using nanoflow HPLC coupled to electrospray tandem mass spectrometry suggests new mechanisms by which the PSD helps regulate synaptic strength and transmission.
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Identification and characterization of mRNAs regulated by nerve growth factor in PC12 cells
TL;DR: It is suggested that the NGF-regulated mRNAs may play roles in the establishment of the neuronal phenotype and that the probes described here will be useful to study the mechanism of action of NGF and the development and differentiation of neurons.
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Leucine zippers of fos , jun and GCN4 dictate dimerization specificity and thereby control DNA binding
Tony Kouzarides,Edward B. Ziff +1 more
TL;DR: It is shown that fos, jun and GCN4 have different affinities for the TRE due to differences in the hetero- or homo-dimerization capacity of their leucine zipper domains; the basic motifs of these three proteins have comparable DNA binding potential.