Peter Gierschik
German Cancer Research Center
12 Papers
236 Citations
Peter Gierschik is an academic researcher from German Cancer Research Center. The author has contributed to research in topics: Phospholipase C & Protein subunit. The author has an hindex of 10, co-authored 12 publications.
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Papers
Activation of phosphatidylinositol lipid-specific phospholipase C-β3 by G-protein βγ subunits
TL;DR: A novel member of the inositol lipid‐specific phospholipase C family, PtdIns‐PLCβ3, is shown to be activated by βγ subunits of the heterotrimeric GTP‐binding protein, transducin, confirming that the effect is due to free βγSubunits.
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Stimulation of phospholipase C-beta 2 by recombinant guanine-nucleotide-binding protein beta gamma dimers produced in a baculovirus/insect cell expression system. Requirement of gamma-subunit isoprenylation for stimulation of phospholipase C.
TL;DR: The results show that γ-subunit isoprenylation and/or additional post-translational processing of the protein are required for βγ subunit stimulation of phospholipase C.
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Farnesylcysteine analogues inhibit chemotactic peptide receptor-mediated G-protein activation in human HL-60 granulocyte membranes
Alexander Scheer,Peter Gierschik +1 more
TL;DR: It is shown that AFC inhibits both basal and fonnyl peptide receptor‐stimulated binding of guanosine 5'‐O‐(3‐thiotriphosphate) (GTP[S]) to and hydrolysis of GTP by membranes of myeloid differentiated HL‐60 granulocytes.
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Mutational analysis of phospholipase C‐β2
TL;DR: To examine the structure-function relationships of a PLCβ isozyme highly sensitive to βγ subunit stimulation, the cDNA of PLC β2 is altered by site-directed mutagenesis and the effects of these structural alterations on the functional properties of the mutant polypeptides are examined.
31
A peptide corresponding to a potential polyphosphoinositide binding site of phospholipase C‐β2 enhances its catalytic activity
TL;DR: A peptide corresponding to a basic consensus amino acid motif present in both actin‐binding proteins and phosphoinositide‐specific phospholipases C was synthesized and its effect on the activity of a recombinantospholipase C‐β2 expressed in baculovirus‐infected insect cells was studied.
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