Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Method to Extend Research in Time (MERIT) Award (R37)
Project #
5R37AI022835-11
Application #
2062002
Study Section
Special Emphasis Panel (NSS)
Project Start
1985-05-01
Project End
1997-04-30
Budget Start
1995-05-01
Budget End
1997-04-30
Support Year
11
Fiscal Year
1995
Total Cost
Indirect Cost
Name
Michigan State University
Department
Biochemistry
Type
Schools of Earth Sciences/Natur
DUNS #
193247145
City
East Lansing
State
MI
Country
United States
Zip Code
48824
Meyer, C R; Yirsa, J; Gott, B et al. (1998) A kinetic study of site-directed mutants of Escherichia coli ADP-glucose pyrophosphorylase: the role of residue 295 in allosteric regulation. Arch Biochem Biophys 352:247-54
Meyer, C R; Bork, J A; Nadler, S et al. (1998) Site-directed mutagenesis of a regulatory site of Escherichia coli ADP-glucose pyrophosphorylase: the role of residue 336 in allosteric behavior. Arch Biochem Biophys 353:152-9
Zaidi, T S; Preston, M J; Pier, G B (1997) Inhibition of bacterial adherence to host tissue does not markedly affect disease in the murine model of Pseudomonas aeruginosa corneal infection. Infect Immun 65:1370-6
Guan, H; Li, P; Imparl-Radosevich, J et al. (1997) Comparing the properties of Escherichia coli branching enzyme and maize branching enzyme. Arch Biochem Biophys 342:92-8
Preiss, J (1996) ADPglucose pyrophosphorylase: basic science and applications in biotechnology. Biotechnol Annu Rev 2:259-79
Alonso, M D; Lomako, J; Lomako, W M et al. (1994) Properties of carbohydrate-free recombinant glycogenin expressed in an Escherichia coli mutant lacking UDP-glucose pyrophosphorylase activity. FEBS Lett 352:222-6
Iglesias, A A; Charng, Y Y; Ball, S et al. (1994) Characterization of the kinetic, regulatory, and structural properties of ADP-glucose pyrophosphorylase from Chlamydomonas reinhardtii. Plant Physiol 104:1287-94
Meyer, C R; Ghosh, P; Nadler, S et al. (1993) Cloning, expression, and sequence of an allosteric mutant ADPglucose pyrophosphorylase from Escherichia coli B. Arch Biochem Biophys 302:64-71
Iglesias, A A; Kakefuda, G; Preiss, J (1992) Involvement of arginine residues in the allosteric activation and inhibition of Synechocystis PCC 6803 ADPglucose pyrophosphorylase. J Protein Chem 11:119-28
Charng, Y Y; Kakefuda, G; Iglesias, A A et al. (1992) Molecular cloning and expression of the gene encoding ADP-glucose pyrophosphorylase from the cyanobacterium Anabaena sp. strain PCC 7120. Plant Mol Biol 20:37-47

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