L. Keranen

Reversible exposure of the pseudosubstrate domain of protein kinase C by phosphatidylserine and diacylglycerol.

A. Newton, J. Orr, L. Keranen, 1992, The Journal of biological chemistry.

Regulation of the insulin receptor by protein kinase C isoenzymes: preferential interaction with beta isoenzymes and interaction with the catalytic domain of betaII.

J. Olefsky, T. S. Pillay, L. Keranen, 2004, Cellular signalling.

In vivo regulation of protein kinase C by trans-phosphorylation followed by autophosphorylation.

A. Newton, A. Depaoli-Roach, E. Dutil, 1994, The Journal of biological chemistry.

Evidence of two isomers of phosphatidylinositol in plant tissue.

P. Lam, L. Keranen, P. Murthy, 1992, Plant physiology.

Protein kinase C is regulated in vivo by three functionally distinct phosphorylations

A. Newton, E. Dutil, L. Keranen, 1995, Current Biology.

Ca2+ Differentially Regulates Conventional Protein Kinase Cs’ Membrane Interaction and Activation*

A. Newton, L. Keranen, 1997, The Journal of Biological Chemistry.

Phosphatidyl-L-serine is necessary for protein kinase C's high-affinity interaction with diacylglycerol-containing membranes.

A. Newton, L. Keranen, 1994, Biochemistry.

Isozyme-specific inhibition of protein kinase C by RNA aptamers.

A D Ellington, A. Newton, A. Ellington, 1994, The Journal of biological chemistry.