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Year Number of Results
2004 1
2005 1
2009 2
2011 2
2012 1
2021 0
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Page 1
Contrasting catalytic and allosteric mechanisms for phosphoglycerate dehydrogenases.
Grant GA. Grant GA. Arch Biochem Biophys. 2012 Mar 15;519(2):175-85. doi: 10.1016/j.abb.2011.10.005. Epub 2011 Oct 15. Arch Biochem Biophys. 2012. PMID: 22023909 Free PMC article. Review.
Multiconformational states in phosphoglycerate dehydrogenase.
Bell JK, Grant GA, Banaszak LJ. Bell JK, et al. Biochemistry. 2004 Mar 30;43(12):3450-8. doi: 10.1021/bi035462e. Biochemistry. 2004. PMID: 15035616
Transient kinetic analysis of the interaction of L-serine with Escherichia coli D-3-phosphoglycerate dehydrogenase reveals the mechanism of V-type regulation and the order of effector binding.
Burton RL, Chen S, Xu XL, Grant GA. Burton RL, et al. Biochemistry. 2009 Dec 29;48(51):12242-51. doi: 10.1021/bi901489n. Biochemistry. 2009. PMID: 19924905 Free PMC article.
Transient kinetic analysis of L-serine interaction with Escherichia coli D-3-phosphoglycerate dehydrogenase containing amino acid mutations in the hinge regions.
Grant GA. Grant GA. Biochemistry. 2011 Apr 12;50(14):2900-6. doi: 10.1021/bi200211z. Epub 2011 Mar 22. Biochemistry. 2011. PMID: 21391703 Free PMC article.
Role of the anion-binding site in catalysis and regulation of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase.
Burton RL, Chen S, Xu XL, Grant GA. Burton RL, et al. Biochemistry. 2009 Jun 9;48(22):4808-15. doi: 10.1021/bi900172q. Biochemistry. 2009. PMID: 19388702 Free PMC article.
Identification of amino acid residues contributing to the mechanism of cooperativity in Escherichia coli D-3-phosphoglycerate dehydrogenase.
Grant GA, Hu Z, Xu XL. Grant GA, et al. Biochemistry. 2005 Dec 27;44(51):16844-52. doi: 10.1021/bi051681j. Biochemistry. 2005. PMID: 16363798 Free PMC article.
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