Yingying Lee

Phosphorylation in the catalytic cleft stabilizes and attracts domains of a phosphohexomutase.

S. V. Van Doren, L. Beamer, Jia Xu, 2015, Biophysical journal.

Promotion of Enzyme Flexibility by Dephosphorylation and Coupling to the Catalytic Mechanism of a Phosphohexomutase*

A. Artigues, M. Villar, L. Beamer, 2014, The Journal of Biological Chemistry.

Compromised Catalysis and Potential Folding Defects in in Vitro Studies of Missense Mutants Associated with Hereditary Phosphoglucomutase 1 Deficiency*

L. Beamer, K. Stiers, Yingying Lee, 2014, The Journal of Biological Chemistry.

Phosphorylation-Dependent Effects on the Structural Flexibility of Phosphoglucosamine Mutase from Bacillus anthracis

S. V. Van Doren, L. Beamer, K. Stiers, 2017, ACS omega.

Identification of an essential active‐site residue in the α‐d‐phosphohexomutase enzyme superfamily

C. Furdui, R. Mehra-Chaudhary, L. Beamer, 2013, The FEBS journal.

Solution NMR of a 463-residue phosphohexomutase: domain 4 mobility, substates, and phosphoryl transfer defect.

S. V. Van Doren, Peiwu Qin, R. Mehra-Chaudhary, 2012, Biochemistry.

A Coevolutionary Residue Network at the Site of a Functionally Important Conformational Change in a Phosphohexomutase Enzyme Family

Yingying Lee, C. Furdui, L. Beamer, 2012, PloS one.

deficiency hereditary phosphoglucomutase 1 missense mutants associated with folding defects in in vitro studies of Compromised catalysis and potential

L. Beamer, K. Stiers, Yingying Lee, 2014 .