Bisubstrate Adenylation Inhibitors of Biotin Protein Ligase from Mycobacterium tuberculosis
- 1 November 2011
- journal article
- Published by Elsevier in Chemistry & Biology
- Vol. 18 (11) , 1432-1441
Abstract
No abstract availableKeywords
This publication has 49 references indexed in Scilit:
- PHENIX: a comprehensive Python-based system for macromolecular structure solutionActa Crystallographica Section D Structural Biology, 2010
- Intrinsic Nucleofugality Scale within the Framework of Density Functional Reactivity TheoryThe Journal of Physical Chemistry A, 2008
- Crystal Structures of Biotin Protein Ligase from Pyrococcus horikoshii OT3 and its Complexes: Structural Basis of Biotin ActivationJournal of Molecular Biology, 2005
- Use of Binding Enthalpy To Drive an Allosteric TransitionBiochemistry, 2005
- The Biotin Repressor: Modulation of Allostery by Corepressor AnalogsJournal of Molecular Biology, 2004
- Expression in Escherichia coli of N- and C-terminally Deleted Human Holocarboxylase SynthetaseJournal of Biological Chemistry, 2001
- The ATP binding cassette (ABC) transport systems ofMycobacterium tuberculosisFEMS Microbiology Reviews, 2000
- The salicylate-derived mycobactin siderophores of Mycobacterium tuberculosis are essential for growth in macrophagesProceedings of the National Academy of Sciences, 2000
- The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificityTrends in Biochemical Sciences, 1999
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D Structural Biology, 1994