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The Journal of Biological Chemistry|April 7, 1995
Cooperation of Src homology domains in the regulated binding of phosphatidylinositol 3-kinase. A role for the Src homology 2 domainB Haefner, R Baxter, V J Fincham, et al.
The Biochemical Journal|December 1, 1994
The turkey erythrocyte beta-adrenergic receptor couples to both adenylate cyclase and phospholipase C via distinct G-protein alpha subunitsS R James, C Vaziri, T R Walker, et al.
Biochemical Society Transactions|March 21, 2007
Metabolic switching of PI3K-dependent lipid signalsC P Downes, N R Leslie, I H Batty, et al.
The Biochemical Journal|September 15, 1994
Inositol trisphosphate metabolism in Saccharomyces cerevisiae: identification, purification and properties of inositol 1,4,5-trisphosphate 6-kinaseF Estevez, D Pulford, M J Stark, et al.
Chembiochem : a European Journal of Chemical Biology|February 6, 2002
The 6-OH group of D-inositol 1-phosphate serves as an H-bond donor in the catalytic hydrolysis of the phosphate ester by inositol monophosphataseD J Miller, M W Beaton, J Wilkie, et al.
Nature|June 4, 1984
Correlation between inositol phospholipid hydrolysis and substance P receptors in rat CNSP W Mantyh, R D Pinnock, C P Downes, et al.
Brain Research|December 3, 1984
Neurotensin stimulates inositol phospholipid hydrolysis in rat brain slicesM Goedert, R D Pinnock, C P Downes, et al.
Biochemistry|April 19, 1988
Primary deuterium isotope effects for the 3-methylaspartase-catalyzed deamination of (2S)-aspartic acid, (2S,3S)-3-methylaspartic acid, and (2S,3S)-3-ethylaspartic acidN P Botting, M A Cohen, M Akhtar, et al.
Biochemistry|January 28, 1997
Dependence of the activity of phospholipase C beta on surface pressure and surface composition in phospholipid monolayers and its implications for their regulationS R James, A Paterson, T K Harden, et al.
The Biochemical Journal|June 1, 1988
Phosphoinositide hydrolysis by guanosine 5'-[gamma-thio]triphosphate-activated phospholipase C of turkey erythrocyte membranesT K Harden, P T Hawkins, L Stephens, et al.
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