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Paul Tempst

Researcher at Memorial Sloan Kettering Cancer Center

Publications -  312
Citations -  93929

Paul Tempst 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 148, co-authored 309 publications receiving 89225 citations. Previous affiliations of Paul Tempst include Kettering University & Cornell University.

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Role of Histone H3 Lysine 27 Methylation in Polycomb-Group Silencing

TL;DR: The purification and characterization of an EED-EZH2 complex, the human counterpart of the Drosophila ESC-E(Z) complex, is reported, and it is demonstrated that the complex specifically methylates nucleosomal histone H3 at lysine 27 (H3-K27).
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SNAP receptors implicated in vesicle targeting and fusion

TL;DR: The existence of numerous SNARE-related proteins, each apparently specific for a single kind of vesicles or target membrane, indicates that NSF and SNAPs may be universal components of a vesicle fusion apparatus common to both constitutive and regulated fusion (including neurotransmitter release), in which the SNAREs may help to ensure vesICLE-to-target specificity.
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mTOR Interacts with Raptor to Form a Nutrient-Sensitive Complex that Signals to the Cell Growth Machinery

TL;DR: It is reported that mTOR forms a stoichiometric complex with raptor, an evolutionarily conserved protein with at least two roles in the mTOR pathway that through its association with mTOR regulates cell size in response to nutrient levels.
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Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton.

TL;DR: It is found that the rictor-mTOR complex modulates the phosphorylation of Protein Kinase C alpha (PKCalpha) and the actin cytoskeleton, suggesting that this aspect of TOR signaling is conserved between yeast and mammals.
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Cloning of p27Kip1, a cyclin-dependent kinase inhibitor and a potential mediator of extracellular antimitogenic signals

TL;DR: P27 Kip1 as mentioned in this paper is a cyclin-dependent kinase inhibitor implicated in G1 phase arrest by TGFβ and cell-cell contact, and it has been shown to be highly conserved and broadly expressed in human tissues, and its mRNA levels are similar in proliferating and quiescent cells.