Shirli Homburg

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We present the first evidence for a fast activation of the nuclear protein poly(ADP-ribose) polymerase (PARP) by signals evoked in the cell membrane, constituting a novel mode of signaling to the cell nucleus. PARP, an abundant, highly conserved, chromatin-bound protein found only in eukaryotes, exclusively catalyzes polyADP-ribosylation of DNA-binding(More)
GTP-binding protein(s) recognized by antibodies against the alpha-subunits of Gi- and Go-proteins were detected in crude nuclei isolated from rat brain stem and cortex. Immunohistochemical staining indicated that in the cortex these proteins are perinuclear, or are embedded in the nuclear membrane. Evidence is presented for an endogenous ADP-ribosylation of(More)
We have recently reported that human soluble epoxide hydrolase (sEH) is a bifunctional enzyme with a novel phosphatase enzymatic activity. Based on a structural relationship with other members of the haloacid dehalogenase superfamily, the sEH N-terminal phosphatase domain revealed four conserved sequence motifs, including the proposed catalytic nucleophile(More)
We present the first evidence for a fast activation of the nuclear protein poly(ADP-ribose) poly-merase (PARP) by signals evoked in the cell membrane , constituting a novel mode of signaling to the cell nucleus. PARP, an abundant, highly conserved, chroma-tin-bound protein found only in eukaryotes, exclusively catalyzes polyADP-ribosylation of DNA-binding(More)
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