J
Jeffrey R. Neumann
Researcher at Massachusetts Institute of Technology
Publications - 7
Citations - 901
Jeffrey R. Neumann is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Cellular differentiation & Cytidine deaminase. The author has an hindex of 7, co-authored 7 publications receiving 875 citations.
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Journal ArticleDOI
n -Butyrate causes histone modification in HeLa and Friend erythroleukaemia cells
TL;DR: Rapid, dramatic, and reversible increases in histone acetylation in the presence of n-butyrate are described.
Journal ArticleDOI
Hemin does not cause commitment of murine erythroleukemia (MEL) cells to terminal differentiation
James F. Gusella,Susan C. Weil,Asterios S. Tsiftsoglou,Vladimir Volloch,Jeffrey R. Neumann,Cheryl Keys,David E. Housman +6 more
TL;DR: Observations suggest that hemin differs from DMSO and thioguanine in that it exerts specific effects on globin expression in MEL cells without triggering commitment to the terminal differentiation program.
Journal ArticleDOI
Nuclear protein synthesis and phosphorylation in Friend erythroleukemia cells stimulated with DMSO.
TL;DR: Patterns of nuclear protein synthesis and phosphorylation have been investigated in Friend erythroleukemia cells and another protein, of molecular weight 65 000, appears to be induced in low amounts.
Journal ArticleDOI
Dissociation of hemoglobin accumulation and commitment during murine erythroleukemia cell differentiation by treatment with imidazole
James F. Gusella,Asterios S. Tsiftsoglou,Vladimir Volloch,Susan C. Weil,Jeffrey R. Neumann,David E. Housman +5 more
TL;DR: Observations suggest that imidazole effectively dissociates two aspects of the erythroid differentiation program of MEL cells: globin gene expression and commitment to loss of proliferative capacity.
Journal ArticleDOI
Nucleosome-associated proteins and phosphoproteins of differentiating Friend erythroleukemia cells
TL;DR: The rate of phosphorylation of histone H1 associated with mononucleosomes was 3 to 4-fold greater in cells induced with DMSO and most of the other phosphorylated non-histones were modified at the same rate in control and induced cells.