Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM049244-03
Application #
2186815
Study Section
Molecular and Cellular Biophysics Study Section (BBCA)
Project Start
1994-08-01
Project End
1997-07-31
Budget Start
1996-08-01
Budget End
1997-07-31
Support Year
3
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Oregon Health and Science University
Department
Biochemistry
Type
Schools of Medicine
DUNS #
009584210
City
Portland
State
OR
Country
United States
Zip Code
97239
Allen, Gregory S; Steinhauer, Katrin; Hillen, Wolfgang et al. (2003) Crystal structure of HPr kinase/phosphatase from Mycoplasma pneumoniae. J Mol Biol 326:1203-17
Steinhauer, Katrin; Allen, Gregory S; Hillen, Wolfgang et al. (2002) Crystallization, preliminary X-ray analysis and biophysical characterization of HPr kinase/phosphatase of Mycoplasma pneumoniae. Acta Crystallogr D Biol Crystallogr 58:515-8
Huffman, Joy L; Lu, Fu; Zalkin, Howard et al. (2002) Role of residue 147 in the gene regulatory function of the Escherichia coli purine repressor. Biochemistry 41:511-20
Schumacher, Maria A; Pearson, Robert F; Moller, Thorleif et al. (2002) Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like protein. EMBO J 21:3546-56
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Zheleznova, E E; Markham, P N; Neyfakh, A A et al. (1999) Structural basis of multidrug recognition by BmrR, a transcription activator of a multidrug transporter. Cell 96:353-62
Glasfeld, A; Koehler, A N; Schumacher, M A et al. (1999) The role of lysine 55 in determining the specificity of the purine repressor for its operators through minor groove interactions. J Mol Biol 291:347-61
Lu, F; Schumacher, M A; Arvidson, D N et al. (1998) Structure-based redesign of corepressor specificity of the Escherichia coli purine repressor by substitution of residue 190. Biochemistry 37:971-82
Lu, F; Brennan, R G; Zalkin, H (1998) Escherichia coli purine repressor: key residues for the allosteric transition between active and inactive conformations and for interdomain signaling. Biochemistry 37:15680-90

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