Browsing SPH Scholarly Articles by Author "Moody, D. Branch"

Now showing items 1-3 of 3

    • Lipidomic discovery of deoxysiderophores reveals a revised mycobactin biosynthesis pathway in Mycobacterium tuberculosis 

      Madigan, Cressida A.; Cheng, Tan-Yun; Layre, Emilie; Young, David C.; McConnell, Matthew J.; Debono, C. Anthony; Murry, Jeffrey P.; Wei, Jun-Rong; Barry, Clifton E. 3rd; Rodriguez, G. Marcela; Matsunaga, Isamu; Rubin, Eric J.; Moody, D. Branch (National Academy of Sciences, 2012)
      To measure molecular changes underlying pathogen adaptation, we generated a searchable dataset of more than 12,000 mass spectrometry events, corresponding to lipids and small molecules that constitute a lipidome for ...

    • Molecular profiling of Mycobacterium tuberculosis identifies tuberculosinyl nucleoside products of the virulence-associated enzyme Rv3378c 

      Layre, Emilie; Lee, Ho Jun; Young, David C.; Martinot, Amanda Jezek; Buter, Jeffrey; Minnaard, Adriaan J.; Annand, John W.; Fortune, Sarah M.; Snider, Barry B.; Matsunaga, Isamu; Rubin, Eric J.; Alber, Tom; Moody, D. Branch (National Academy of Sciences, 2014)
      To identify lipids with roles in tuberculosis disease, we systematically compared the lipid content of virulent Mycobacterium tuberculosis with the attenuated vaccine strain Mycobacterium bovis bacillus Calmette-Guerin. ...

    • Mycobacterial Esx-3 is required for mycobactin-mediated iron acquisition 

      Siegrist, M. Sloan; Unnikrishnan, Meera; McConnell, Matthew J.; Borowsky, Mark; Cheng, Tan-Yun; Siddiqi, Noman; Fortune, Sarah M.; Moody, D. Branch; Rubin, Eric J. (National Academy of Sciences, 2009)
      The Esx secretion pathway is conserved across Gram-positive bacteria. Esx-1, the best-characterized system, is required for virulence of Mycobacterium tuberculosis, although its precise function during infection remains ...