J. Sheng

Mutagenesis of an amino acid residue in the activator-binding site of cyanobacterial ADP-glucose pyrophosphorylase causes alteration in activator specificity.

J. Preiss, Y. Charng, J. Sheng, 1995, Archives of biochemistry and biophysics.

Site-directed mutagenesis of lysine382, the activator-binding site, of ADP-glucose pyrophosphorylase from Anabaena PCC 7120.

J. Preiss, Y. Charng, J. Sheng, 1996, Biochemistry.

Conformational changes of proteins at an interface induced by a supported planar phosphatidic acid monolayer.

S. Sui, J. Sheng, H. Wu, 1994, Journal of biochemistry.

Crystallization and preliminary X-ray crystallographic analysis of Escherichia coliglutaredoxin 2 in complex with glutathione and of a cysteine-less variant without glutathione.

Jun Ye, B. Rosen, J. Sheng, 2007, Acta crystallographica. Section F, Structural biology and crystallization communications.

Induction of changes in the secondary structure of globular proteins by a hydrophobic surface

Sen-fang Sui, J. Sheng, Hua-Yong Wu, 2004, European Biophysics Journal.

Studies of the Catalytic and Regulatory Sites of the Cyanobacterial and Higher Plant ADP-Glucose Pyrophosphorylase; A Regulatory Enzyme of Starch Synthesis

Ying-Hui Fu, J. Preiss, M. Ballicora, 1995 .

Regulation of Higher Plant Leaf and Reserve Tissue Starch Synthesis

Ying-Hui Fu, J. Preiss, M. Ballicora, 1999 .

Adventitious arsenate reductase activity of the catalytic domain of the human Cdc25B and Cdc25C phosphatases.

A. Ajees, B. Rosen, R. Mukhopadhyay, 2010, Biochemistry.