Spencer A. Dean

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The function of arginine 65, a conserved residue located at the periphery of the active site cleft in yeast 3-phosphoglycerate kinase (PGK), has been investigated by site-directed mutagenesis. Mutant enzymes with glutamine, serine and alanine at position 65 all have very similar kinetic properties. The maximum velocities, determined in the absence of(More)
A cluster of conserved histidines and arginines (His-62, His-167, Arg-21, Arg-38, and Arg-168) in 3-phosphoglycerate kinase (PGK) has been implicated as possibly involved in the binding of 3-phosphoglycerate (3-PG) and/or stabilization of the negatively charged transition state. The role of these residues in the catalytic function of yeast PGK and in the(More)
We recently reported a novel form of BMP2, designated nBMP2, which is translated from an alternative downstream start codon and is localized to the nucleus rather than secreted from the cell. To examine the function of nBMP2 in the nucleus, we engineered a gene-targeted mutant mouse model (nBmp2NLS(tm)) in which nBMP2 cannot be translocated to the nucleus.(More)
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