Year |
Citation |
Score |
2003 |
Goulding CW, Perry LJ, Anderson D, Sawaya MR, Cascio D, Apostol MI, Chan S, Parseghian A, Wang SS, Wu Y, Cassano V, Gill HS, Eisenberg D. Structural genomics of Mycobacterium tuberculosis: a preliminary report of progress at UCLA. Biophysical Chemistry. 105: 361-70. PMID 14499904 DOI: 10.1016/S0301-4622(03)00101-7 |
0.686 |
|
2003 |
Terwilliger TC, Park MS, Waldo GS, Berendzen J, Hung LW, Kim CY, Smith CV, Sacchettini JC, Bellinzoni M, Bossi R, De Rossi E, Mattevi A, Milano A, Riccardi G, Rizzi M, ... ... Gill HS, et al. The TB structural genomics consortium: a resource for Mycobacterium tuberculosis biology. Tuberculosis (Edinburgh, Scotland). 83: 223-49. PMID 12906835 DOI: 10.1016/S1472-9792(03)00051-9 |
0.677 |
|
2002 |
Goulding CW, Apostol M, Anderson DH, Gill HS, Smith CV, Kuo MR, Yang JK, Waldo GS, Suh SW, Chauhan R, Kale A, Bachhawat N, Mande SC, Johnston JM, Lott JS, et al. The TB structural genomics consortium: providing a structural foundation for drug discovery. Current Drug Targets. Infectious Disorders. 2: 121-41. PMID 12462144 DOI: 10.2174/1568005023342551 |
0.666 |
|
2002 |
Gill HS, Pfluegl GM, Eisenberg D. Multicopy crystallographic refinement of a relaxed glutamine synthetase from Mycobacterium tuberculosis highlights flexible loops in the enzymatic mechanism and its regulation. Biochemistry. 41: 9863-72. PMID 12146952 DOI: 10.1021/Bi020254S |
0.412 |
|
2001 |
Gill HS, Eisenberg D. The crystal structure of phosphinothricin in the active site of glutamine synthetase illuminates the mechanism of enzymatic inhibition. Biochemistry. 40: 1903-12. PMID 11329256 DOI: 10.1021/Bi002438H |
0.451 |
|
2000 |
Eisenberg D, Gill HS, Pfluegl GM, Rotstein SH. Structure-function relationships of glutamine synthetases. Biochimica Et Biophysica Acta. 1477: 122-45. PMID 10708854 DOI: 10.1016/S0167-4838(99)00270-8 |
0.486 |
|
1999 |
Gill HS, Pfluegl GM, Eisenberg D. Preliminary crystallographic studies on glutamine synthetase from Mycobacterium tuberculosis. Acta Crystallographica. Section D, Biological Crystallography. 55: 865-8. PMID 10089318 DOI: 10.1107/S0907444998017685 |
0.528 |
|
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