| Year |
Citation |
Score |
| 2003 |
Hu Y, Chen L, Ha S, Gross B, Falcone B, Walker D, Mokhtarzadeh M, Walker S. Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases. Proceedings of the National Academy of Sciences of the United States of America. 100: 845-9. PMID 12538870 DOI: 10.1073/Pnas.0235749100 |
0.623 |
|
| 2002 |
Chen L, Men H, Ha S, Ye XY, Brunner L, Hu Y, Walker S. Intrinsic lipid preferences and kinetic mechanism of Escherichia coli MurG. Biochemistry. 41: 6824-33. PMID 12022887 DOI: 10.1021/Bi0256678 |
0.629 |
|
| 2001 |
Ha S, Gross B, Walker S. E. Coli MurG: a paradigm for a superfamily of glycosyltransferases. Current Drug Targets. Infectious Disorders. 1: 201-13. PMID 12455415 DOI: 10.2174/1568005014606116 |
0.545 |
|
| 2000 |
Ha S, Walker D, Shi Y, Walker S. The 1.9 A crystal structure of Escherichia coli MurG, a membrane-associated glycosyltransferase involved in peptidoglycan biosynthesis. Protein Science : a Publication of the Protein Society. 9: 1045-52. PMID 10892798 DOI: 10.1110/Ps.9.6.1045 |
0.551 |
|
| 1999 |
Ha S, Chang E, Lo MC, Men H, Park P, Ge M, Walker S. The kinetic characterization of Escherichia coli MurG using synthetic substrate analogues Journal of the American Chemical Society. 121: X. DOI: 10.1021/Ja991556T |
0.658 |
|
| 1999 |
Ha S, Chang E, Lo MC, Men H, Park P, Ge M, Walker S. The kinetic characterization of Escherichia coli MurG using synthetic substrate analogues Journal of the American Chemical Society. 121: X. |
0.675 |
|
| 1998 |
Lo MC, Ha S, Pelczer I, Pal S, Walker S. The solution structure of the DNA-binding domain of Skn-1. Proceedings of the National Academy of Sciences of the United States of America. 95: 8455-60. PMID 9671699 DOI: 10.1073/Pnas.95.15.8455 |
0.577 |
|
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