F. Javid-Majd

Overexpression and Mechanistic Analysis of Chromosomally Encoded Aminoglycoside 2′-N-Acetyltransferase (AAC(2′)-Ic) fromMycobacterium tuberculosis *

J. Blanchard, S. Hegde, F. Javid-Majd, 2001, The Journal of Biological Chemistry.

Mechanistic analysis of the argE-encoded N-acetylornithine deacetylase.

J. Blanchard, F. Javid-Majd, 2000, Biochemistry.

The Differentially Conserved Residues of Carbamoyl-Phosphate Synthetase*

F. Raushel, L. S. Mullins, F. Javid-Majd, 2000, The Journal of Biological Chemistry.

The crystal structure of TrpD, a metabolic enzyme essential for lung colonization by Mycobacterium tuberculosis, in complex with its substrate phosphoribosylpyrophosphate.

E. Baker, F. Javid-Majd, Catherine E. Goodfellow, 2006, Journal of molecular biology.

Role of conserved residues within the carboxy phosphate domain of carbamoyl phosphate synthetase.

F. Raushel, L. S. Mullins, F. Javid-Majd, 1996, Biochemistry.

The 1.25 A resolution structure of phosphoribosyl-ATP pyrophosphohydrolase from Mycobacterium tuberculosis.

J. Sacchettini, T. Ioerger, F. Javid-Majd, 2005, Acta crystallographica. Section D, Biological crystallography.

Aminoglycoside 2′-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycoside substrates

J. Blanchard, M. Vetting, S. Hegde, 2002, Nature Structural Biology.

Comparison of the functional differences for the homologous residues within the carboxy phosphate and carbamate domains of carbamoyl phosphate synthetase.

F. Raushel, L. S. Mullins, F. Javid-Majd, 1996, Biochemistry.