Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
5R01AI014107-21
Application #
2060047
Study Section
Microbial Physiology and Genetics Subcommittee 2 (MBC)
Project Start
1976-09-30
Project End
2000-03-31
Budget Start
1996-04-01
Budget End
1997-03-31
Support Year
21
Fiscal Year
1996
Total Cost
Indirect Cost
Name
University of Colorado Denver
Department
Microbiology/Immun/Virology
Type
Schools of Medicine
DUNS #
065391526
City
Aurora
State
CO
Country
United States
Zip Code
80045
Jobling, Michael G (2016) The chromosomal nature of LT-II enterotoxins solved: a lambdoid prophage encodes both LT-II and one of two novel pertussis-toxin-like toxin family members in type II enterotoxigenic Escherichia coli. Pathog Dis 74:
Jobling, Michael G; Gotow, Lisa F; Yang, Zhijie et al. (2015) A mutational analysis of residues in cholera toxin A1 necessary for interaction with its substrate, the stimulatory G protein Gs?. Toxins (Basel) 7:919-35
Spinler, Jennifer K; Zajdowicz, Sheryl L W; Haller, Jon C et al. (2009) Development and use of a selectable, broad-host-range reporter transposon for identifying environmentally regulated promoters in bacteria. FEMS Microbiol Lett 291:143-50
Qian, Yilei; Lee, John H; Holmes, Randall K (2002) Identification of a DtxR-regulated operon that is essential for siderophore-dependent iron uptake in Corynebacterium diphtheriae. J Bacteriol 184:4846-56
Feese, M D; Ingason, B P; Goranson-Siekierke, J et al. (2001) Crystal structure of the iron-dependent regulator from Mycobacterium tuberculosis at 2.0-A resolution reveals the Src homology domain 3-like fold and metal binding function of the third domain. J Biol Chem 276:5959-66
Lee, J H; Holmes, R K (2000) Characterization of specific nucleotide substitutions in DtxR-specific operators of Corynebacterium diphtheriae that dramatically affect DtxR binding, operator function, and promoter strength. J Bacteriol 182:432-8
Pohl, E; Holmes, R K; Hol, W G (1999) Crystal structure of a cobalt-activated diphtheria toxin repressor-DNA complex reveals a metal-binding SH3-like domain. J Mol Biol 292:653-67
Goranson-Siekierke, J; Pohl, E; Hol, W G et al. (1999) Anion-coordinating residues at binding site 1 are essential for the biological activity of the diphtheria toxin repressor. Infect Immun 67:1806-11
Pohl, E; Holmes, R K; Hol, W G (1999) Crystal structure of the iron-dependent regulator (IdeR) from Mycobacterium tuberculosis shows both metal binding sites fully occupied. J Mol Biol 285:1145-56
Pohl, E; Qui, X; Must, L M et al. (1997) Comparison of high-resolution structures of the diphtheria toxin repressor in complex with cobalt and zinc at the cation-anion binding site. Protein Sci 6:1114-8

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