Recent Publications: Gerald M. Carlson

Andreeva, I.E., Rice, N.A. and Carlson, G.M. (2002)  The regulatory a subunit of phosphorylase kinase may directly participate in the binding of glycogen phosphorylase. Biochemistry (Moscow) 67, 1197-1202

Rice, N.A., Nadeau, O.W., Yang, Q. and Carlson, G.M. (2002)  The calmodulin-binding domain of the catalytic g subunit of phosphorylase kinase interacts with its inhibitory a subunit: evidence for a Ca2+-sensitive network of quaternary interactions. J. Biol. Chem. 277, 14681-14687

Vénien-Bryan, C., Lowe, E.D., Boisset, N., Traxler, K.W., Johnson, L.N. and Carlson, G.M. (2002) Three-dimensional structure of phosphorylase kinase at 22 Ĺ resolution and its complex with glycogen phosphorylase b. Structure 10, 33-41.

Nadeau, O.W., Carlson, G.M. and Gogol, E.P. (2002) A Ca2+-dependent global conformational change in the 3-D structure of phosphorylase kinase obtained from electron microscopy. Structure 10, 23-32.

Traxler, K.W., Norcum, M.T., Hainfeld, J.F. and Carlson, G.M. (2001) Direct visualization of the calmodulin subunit of phosphorylase kinase via subunit exchange and electron microscopy. J. Struct. Biol. 135, 231-238.

Ayers, N.A., Wilkinson, D.A., Fitzgerald, T.J. and Carlson, G.M. (1999) Self-association of the alpha subunit of phosphorylase kinase as determined by two-hybrid screening. J. Biol. Chem. 274, 35583-35590.

Xu, Y.-X. and Carlson, G.M. (1999) Structural features contributing to complex formation between glycogen phosphorylase and phosphorylase kinase. Biochemistry 38, 9562-9569.

Nadeau, O.W., Traxler, K.W., Fee, L.R., Baldwin, B.A. and Carlson, G.M. (1999) Activators of phosphorylase kinase alter the cross-linking of its catalytic subunit to the C-terminal one-sixth of its regulatory a subunit. Biochemistry 38, 2551-2559.

Wilkinson, D.A., Fitzgerald, T.J., Marion, T.N. and Carlson, G.M. (1999) Mg2+ induces conformational changes in the g subunit of phosphorylase kinase, whether by itself or as part of the holoenzyme complex. J. Prot. Chem. 18, 157-164.


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