ADP-ribosylation of rho p21 inhibits lysophosphatidic acid-induced protein tyrosine phosphorylation and phosphatidylinositol 3-kinase activation in cultured Swiss 3T3 cells.
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Summary
It is suggested that rho p21 works as a link between the LPA receptor signal and the subsequent tyrosine phosphorylation and PI 3-kinase activation in these cells.
- Type
- article
- Published
- 1993-11-25
- Cited by
- 190
- References
- 0
- Access
- Open access
- OpenAlex
- https://openalex.org/W1481203098
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:25624015
Keywords
Tyrosine phosphorylation, Lysophosphatidic acid, Phosphorylation, Exoenzyme, Cell biology
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Cited by
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- Activatory properties of lysophosphatidic acid (LPA) on human THP-1 monocytes
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- Signal transduction in cell-matrix interactions.
- Differentielle Rekrutierung der Isoformen des kleinen G-Proteins Rho bei der Invasion von Shigellen in Epithelzellen
- Preparation of native and recombinant Clostridium botulinum C3 ADP-ribosyltransferase and identification of Rho proteins by ADP-ribosylation.
- Inhibition of lymphocyte-mediated cytotoxicity by Clostridium botulinum C3 transferase.
- Lymphocyte aggregation assay and inhibition by Clostridium botulinum C3 ADP-ribosyltransferase.
- Cellular consequences of thrombin-receptor activation.
- Die Invasion von Epithelzellen durch E. coli Shigella
- The therapeutic potential of Rho GTPase intervention
- The small GTP-binding protein, rho p21, is involved in bone resorption by regulating cytoskeletal organization in osteoclasts.
- Rho as a mediator of G protein-coupled receptor signaling.
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