@article{chen_brglez_boss_1991, title={Inositol phospholipids as plant second messengers}, ISBN={0948601310}, journal={Molecular biology of plant development}, publisher={Cambridge : Published for the Society for Experimental Biology by the Company of Biologists}, author={Chen, Q. Y. and Brglez, I. and Boss, W. F.}, editor={G. I. Jenkins and Schuch, W.Editors}, year={1991}, pages={159} }
 @article{chen_boss_1991, title={NEOMYCIN INHIBITS THE PHOSPHATIDYLINOSITOL MONOPHOSPHATE AND PHOSPHATIDYLINOSITOL BISPHOSPHATE STIMULATION OF PLASMA-MEMBRANE ATPASE ACTIVITY}, volume={96}, ISSN={["0032-0889"]}, DOI={10.1104/pp.96.1.340}, abstractNote={The inositol phospholipids, phosphatidylinositol monophosphate (PIP) and phosphatidylinositol bisphosphate (PIP(2)), have been shown to increase the vanadate-sensitive ATPase activity of plant plasma membranes (AR Memon, Q Chen, WF Boss [1989] Biochem Biophys Res Commun 162: 1295-1301). In this paper, we show the effect of various concentrations of phosphatidyinositol, PIP, and PIP(2) on the plasma membrane vanadate-sensitive ATPase activity. PIP and PIP(2) at concentrations of 10 nanomoles per 30 microgram membrane protein per milliliter of reaction mixture caused a twofold and 1.8-fold increase in the ATPase activity, respectively. The effect of these negatively charged phospholipids on the ATPase activity was inhibited by adding the positively charged aminoglycoside, neomycin. Neomycin did not affect the endogenous plasma membrane ATPase activity in the absence of exogenous lipids.}, number={1}, journal={PLANT PHYSIOLOGY}, author={CHEN, QY and BOSS, WF}, year={1991}, month={May}, pages={340–343} }
 @article{chen_1991, title={Signal transduction in carrot cells: The role of inositol phospholipids}, volume={52}, number={3}, journal={Dissertation Abstracts International. B, Sciences and Engineering}, author={Chen, Q. Y.}, year={1991}, pages={1168} }
 @article{chen_boss_1990, title={SHORT-TERM TREATMENT WITH CELL-WALL DEGRADING ENZYMES INCREASES THE ACTIVITY OF THE INOSITOL PHOSPHOLIPID KINASES AND THE VANADATE-SENSITIVE ATPASE OF CARROT CELLS}, volume={94}, ISSN={["0032-0889"]}, DOI={10.1104/pp.94.4.1820}, abstractNote={Treating carrot (Daucus carota L.) suspension culture cells with a mixture of cell wall degrading enzymes, Driselase, resulted in an increase in the percentage of [(3)H]phosphatidylinositol bisphosphate. Analysis of the lipid kinase activities in the isolated plasma membranes after whole cell treatment indicated that treatment with Driselase (2% weight/volume; the equivalent of 340 units per milliliter of hemicellulase and 400 units per milliliter of cellulase activity) or treatment with hemicellulase (31.7% weight/volume, 20.7 units per milliliter) resulted in an increase in the inositol phospholipid kinase activity. However, treatment with cellulase alone had no effect at 0.5% (weight/volume, 17.2 units per milliliter) or inhibited the kinase activity at 1% (weight/volume, 34.4 units per milliliter). The active stimulus in Driselase was heat sensitive. The plasma membrane vanadate-sensitive ATPase activity also increased when the cells were treated with Driselase. A time course study indicated that both the inositol phospholipid kinases and the plasma membrane vanadate-sensitive ATPase responded to as little as 5 seconds of treatment with 2% Driselase. However, at the lowest concentration of Driselase (0.04%, weight/volume) that resulted in an increase in inositol phospholipid kinase activity, the ATPase activity was not affected. Because inositol phospholipids have been shown to activate the vanadate-sensitive ATPase from plants (AR Memon, Q Chen, WF Boss [1989] Biochem Biophys Res Commun 162: 1295-1301), a stimulus-response pathway involving both the inositol phospholipid kinases and the plasma membrane vanadate-sensitive ATPase activity is discussed.}, number={4}, journal={PLANT PHYSIOLOGY}, author={CHEN, QY and BOSS, WF}, year={1990}, month={Dec}, pages={1820–1829} }