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FKBP12-Rapamycin-associated Protein (FRAP) Autophosphorylates at Serine 2481 under Translationally Repressive Conditions*
The FKBP12-rapamycin associated protein (FRAP, also RAFT, mTOR) belongs to a family of phosphatidylinositol kinase-related kinases. These kinases mediate cellular responses to stresses such as DNAExpand
Control of p70 S6 kinase by kinase activity of FRAP in vivo
WHEN complexed with the intracellular protein FKBP12, rapamy-cin is a potent immunosuppressant1,2 and an inhibitor of a mitogen-stimulated signalling pathway that leads to activation of p70 S6Expand
Small molecule inhibitors of the RNA-dependent protein kinase.
The RNA-dependent protein kinase (PKR) is an interferon-induced serine/threonine protein kinase that phosphorylates the alpha subunit of the eukaryotic initiation factor 2 in response to viralExpand
Structures of human ADAR2 bound to dsRNA reveal base-flipping mechanism and basis for site selectivity
Adenosine deaminases acting on RNA (ADARs) are editing enzymes that convert adenosine to inosine in duplex RNA, a modification reaction with wide-ranging consequences in RNA function. UnderstandingExpand
Control of p70 S6 kinase by kinase activity of FRAP in vivo
the middle panel of Fig. 4d of this Letter did not print up properly. The complete figure is shown here.
Identifying epimetabolites by integrating metabolome databases with mass spectrometry cheminformatics
Novel metabolites distinct from canonical pathways can be identified through the integration of three cheminformatics tools: BinVestigate, which queries the BinBase gas chromatography–massExpand
DNA editing in DNA/RNA hybrids by adenosine deaminases that act on RNA
Abstract Adenosine deaminases that act on RNA (ADARs) carry out adenosine (A) to inosine (I) editing reactions with a known requirement for duplex RNA. Here, we show that ADARs also react withExpand
RNA editing changes the lesion specificity for the DNA repair enzyme NEIL1
Editing of the pre-mRNA for the DNA repair enzyme NEIL1 causes a lysine to arginine change in the lesion recognition loop of the protein. The two forms of NEIL1 are shown here to have distinctExpand
Phosphorylation of the RNA-dependent protein kinase regulates its RNA-binding activity.
The RNA-dependent protein kinase (PKR) is an interferon-induced, RNA-activated enzyme that phosphorylates the alpha-subunit of eukaryotic initiation factor 2 (eIF2alpha), inhibiting the function ofExpand
Controlling activation of the RNA-dependent protein kinase by siRNAs using site-specific chemical modification
The RNA-dependent protein kinase (PKR) is activated by binding to double-stranded RNA (dsRNA). Activation of PKR by short-interfering RNAs (siRNAs) and stimulation of the innate immune response hasExpand
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