Agency
National Institute of Health (NIH)
Institute
National Institute of Environmental Health Sciences (NIEHS)
Type
Postdoctoral Individual National Research Service Award (F32)
Project #
1F32ES005726-01
Application #
2154571
Study Section
Chemical Pathology Study Section (CPA)
Project Start
1996-06-01
Project End
Budget Start
1996-02-01
Budget End
1997-01-31
Support Year
1
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Harvard University
Department
Other Basic Sciences
Type
Schools of Public Health
DUNS #
082359691
City
Boston
State
MA
Country
United States
Zip Code
02115
Ding, H; Demple, B (2000) Direct nitric oxide signal transduction via nitrosylation of iron-sulfur centers in the SoxR transcription activator. Proc Natl Acad Sci U S A 97:5146-50
Demple, B; Hidalgo, E; Ding, H (1999) Transcriptional regulation via redox-sensitive iron-sulphur centres in an oxidative stress response. Biochem Soc Symp 64:119-28
Ding, H; Demple, B (1998) Thiol-mediated disassembly and reassembly of [2Fe-2S] clusters in the redox-regulated transcription factor SoxR. Biochemistry 37:17280-6
Hidalgo, E; Ding, H; Demple, B (1997) Redox signal transduction via iron-sulfur clusters in the SoxR transcription activator. Trends Biochem Sci 22:207-10
Bradley, T M; Hidalgo, E; Leautaud, V et al. (1997) Cysteine-to-alanine replacements in the Escherichia coli SoxR protein and the role of the [2Fe-2S] centers in transcriptional activation. Nucleic Acids Res 25:1469-75
Hidalgo, E; Ding, H; Demple, B (1997) Redox signal transduction: mutations shifting [2Fe-2S] centers of the SoxR sensor-regulator to the oxidized form. Cell 88:121-9
Ding, H; Demple, B (1997) In vivo kinetics of a redox-regulated transcriptional switch. Proc Natl Acad Sci U S A 94:8445-9
Ding, H; Hidalgo, E; Demple, B (1996) The redox state of the [2Fe-2S] clusters in SoxR protein regulates its activity as a transcription factor. J Biol Chem 271:33173-5
Ding, H; Demple, B (1996) Glutathione-mediated destabilization in vitro of [2Fe-2S] centers in the SoxR regulatory protein. Proc Natl Acad Sci U S A 93:9449-53