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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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MicroRNA functions in stress responses.
TL;DR: This work has shown that miRNAs play key roles in fundamental cellular processes, including how cells respond to changes in environment or stresses, and dysregulation of these processes contributes to chronic diseases, including cancers.
Journal ArticleDOI
The RNAi revolution
Carl D. Novina,Phillip A. Sharp +1 more
TL;DR: The term RNAi — short for RNA interference — crops up again and again in biology research these days because of its power as a laboratory tool, and in part because it is a widespread natural phenomenon.
Genome editing with Cas9 in adult mice corrects a disease mutation and phenotype
Hao Yin,Wen Xue,Sidi Chen,Roman L. Bogorad,Eric Benedetti,Markus Grompe,Victor Koteliansky,Phillip A. Sharp,Tyler Jacks,Daniel G. Anderson +9 more
TL;DR: This study indicates that CRISPR-Cas9–mediated genome editing is possible in adult animals and has potential for correction of human genetic diseases.
Journal ArticleDOI
Regulation of Synaptic Structure and Function by FMRP-Associated MicroRNAs miR-125b and miR-132
Dieter Edbauer,Joel R. Neilson,Kelly A. Foster,Chi-Fong Wang,Daniel P. Seeburg,Matthew N. Batterton,Tomoko Tada,Bridget M. Dolan,Phillip A. Sharp,Morgan Sheng +9 more
TL;DR: In this article, the NMDA receptor subunit NR2A was identified as a target of miR-125b and showed that NR 2A mRNA is specifically associated with FMRP in brain.
Journal ArticleDOI
The POU domain: a large conserved region in the mammalian pit-1, oct-1, oct-2, and Caenorhabditis elegans unc-86 gene products
Winship Herr,Richard A. Sturm,Roger G. Clerc,Lynn M. Corcoran,David Baltimore,Phillip A. Sharp,Holly A. Ingraham,Michael G. Rosenfeld,Michael Finney,Gary Ruvkun +9 more
TL;DR: The POU domain is a novel bipartite DNA-binding structure in which the POU homoeo and POU-specific regions form two subdomains that are both required for DNA binding but are held together by a flexible linker.