Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
5R01AI016692-16
Application #
2060398
Study Section
Bacteriology and Mycology Subcommittee 2 (BM)
Project Start
1980-05-01
Project End
2000-04-30
Budget Start
1996-05-01
Budget End
1997-04-30
Support Year
16
Fiscal Year
1996
Total Cost
Indirect Cost

  Institution

Name
University of Texas Sw Medical Center Dallas
Department
Microbiology/Immun/Virology
Type
Schools of Medicine
DUNS #
City
Dallas
State
TX
Country
United States
Zip Code
75390

  Publications

Scheuermann, Thomas H; Brautigam, Chad A (2015) High-precision, automated integration of multiple isothermal titration calorimetric thermograms: new features of NITPIC. Methods 76:87-98
Sheffield, Jeanne S; Wendel Jr, George D; McIntire, Donald D et al. (2009) The effect of progesterone levels and pregnancy on HIV-1 coreceptor expression. Reprod Sci 16:20-31
Tomson, Farol L; Conley, Patrick G; Norgard, Michael V et al. (2007) Assessment of cell-surface exposure and vaccinogenic potentials of Treponema pallidum candidate outer membrane proteins. Microbes Infect 9:1267-75
Sheffield, Jeanne S; Wendel Jr, George D; McIntire, Donald D et al. (2007) Effect of genital ulcer disease on HIV-1 coreceptor expression in the female genital tract. J Infect Dis 196:1509-16
Deka, Ranjit K; Goldberg, Martin S; Hagman, Kayla E et al. (2004) The Tp38 (TpMglB-2) lipoprotein binds glucose in a manner consistent with receptor function in Treponema pallidum. J Bacteriol 186:2303-8
Deka, Ranjit K; Machius, Mischa; Norgard, Michael V et al. (2002) Crystal structure of the 47-kDa lipoprotein of Treponema pallidum reveals a novel penicillin-binding protein. J Biol Chem 277:41857-64
Lee, Yong-Hwan; Dorwart, Michael R; Hazlett, Karsten R O et al. (2002) The crystal structure of Zn(II)-free Treponema pallidum TroA, a periplasmic metal-binding protein, reveals a closed conformation. J Bacteriol 184:2300-4
Bouis, D A; Popova, T G; Takashima, A et al. (2001) Dendritic cells phagocytose and are activated by Treponema pallidum. Infect Immun 69:518-28
Sellati, T J; Wilkinson, D A; Sheffield, J S et al. (2000) Virulent Treponema pallidum, lipoprotein, and synthetic lipopeptides induce CCR5 on human monocytes and enhance their susceptibility to infection by human immunodeficiency virus type 1. J Infect Dis 181:283-93
Deka, R K; Lee, Y H; Hagman, K E et al. (1999) Physicochemical evidence that Treponema pallidum TroA is a zinc-containing metalloprotein that lacks porin-like structure. J Bacteriol 181:4420-3

Showing the most recent 10 out of 53 publications