P
Phillip A. Sharp
Researcher at Massachusetts Institute of Technology
Publications - 618
Citations - 125567
Phillip A. Sharp is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: RNA & Gene. The author has an hindex of 172, co-authored 614 publications receiving 117126 citations. Previous affiliations of Phillip A. Sharp include McGovern Institute for Brain Research & Medical Research Council.
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Mammalian suppressor genes
TL;DR: A method of suppressing a nonsense codon in a gene in a mammalian cell by preparing an oligonucleotide primer having a mismatched anticodon region corresponding to the nonsense codons was proposed in this paper.
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Erratum: siRNA-directed inhibition of HIV-1 infection (Nature Medicine (2002) 8 (681-686))
Carl D. Novina,Michael F. Murray,Derek M. Dykxhoorn,Paul J. Beresford,Jonathan W. Riess,Sang-Kyung Lee,Ronald G. Collman,Judy Lieberman,Premlata Shankar,Phillip A. Sharp +9 more
TL;DR: The reported antisense strand of the CD19 siRNA used as a negative control in Figure 3 (p. 683) did not have the appropriate sequence, and was therefore not relevant as an unrelated siRNA control.
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Mouse lymphoid cell line selected to have high immunoglobulin promoter activity
Dean Tantin,Phillip A. Sharp +1 more
TL;DR: The murine lymphoid cell line 2017 was engineered to express the green fluorescent protein under the control of an immunoglobulin heavy chain promoter and selected for high activity using multiple rounds of fluorescence-activated cell sorting, demonstrating higher activities in the selected cell lines relative to the parental line and to the non-cell-type-specific histone H2B promoter.
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Monocarboxylate transporter expression is associated with the absorption of benzoic acid in human intestinal epithelial cells
TL;DR: It is established that benzoic acid uptake is pH-dependent (resulting in intracellular acidification) and is enhanced in cells expressing higher levels of MCT1 protein, suggesting that these small organic acids may all be substrates for the same transport pathway.
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Binding of proflavine and ethidium bromide to two forms of T2 bacteriophage with different sedimentation coefficients
TL;DR: Equilibrium and kinetic studies of binding of proflavine and ethidium bromide to T2 phage indicate that most of the intraphage DNA is accessible to Proflavine.