Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM031708-14
Application #
2176276
Study Section
Bacteriology and Mycology Subcommittee 2 (BM)
Project Start
1982-09-01
Project End
1998-03-31
Budget Start
1996-04-01
Budget End
1997-03-31
Support Year
14
Fiscal Year
1996
Total Cost
Indirect Cost

  Institution

Name
University of Washington
Department
Pharmacology
Type
Schools of Medicine
DUNS #
135646524
City
Seattle
State
WA
Country
United States
Zip Code
98195

  Publications

Oldenburg, D J; Storm, D R (1993) Identification of a domain in Bordetella pertussis adenylyl cyclase important for subunit interactions and cell invasion activity. Microb Pathog 15:153-7
Oldenburg, D J; Gross, M K; Smith, A L et al. (1993) Virulence of a Bordetella pertussis strain expressing a mutant adenylyl cyclase with decreased calmodulin affinity. Microb Pathog 14:489-93
Oldenburg, D J; Gross, M K; Wong, C S et al. (1992) High-affinity calmodulin binding is required for the rapid entry of Bordetella pertussis adenylyl cyclase into neuroblastoma cells. Biochemistry 31:8884-91
Gross, M K; Au, D C; Smith, A L et al. (1992) Targeted mutations that ablate either the adenylate cyclase or hemolysin function of the bifunctional cyaA toxin of Bordetella pertussis abolish virulence. Proc Natl Acad Sci U S A 89:4898-902
Donovan, M G; Storm, D R (1990) Evidence that the adenylate cyclase secreted from Bordetella pertussis does not enter animal cells by receptor-mediated endocytosis. J Cell Physiol 145:444-9
Masure, H R; Au, D C; Gross, M K et al. (1990) Secretion of the Bordetella pertussis adenylate cyclase from Escherichia coli containing the hemolysin operon. Biochemistry 29:140-5
Xia, Z G; Storm, D R (1990) A-type ATP binding consensus sequences are critical for the catalytic activity of the calmodulin-sensitive adenylyl cyclase from Bacillus anthracis. J Biol Chem 265:6517-20
Donovan, M G; Masure, H R; Storm, D R (1989) Isolation of a protein fraction from Bordetella pertussis that facilitates entry of the calmodulin-sensitive adenylate cyclase into animal cells. Biochemistry 28:8124-9
Au, D C; Masure, H R; Storm, D R (1989) Site-directed mutagenesis of lysine 58 in a putative ATP-binding domain of the calmodulin-sensitive adenylate cyclase from Bordetella pertussis abolishes catalytic activity. Biochemistry 28:2772-6
Masure, H R; Storm, D R (1989) Characterization of the bacterial cell associated calmodulin-sensitive adenylate cyclase from Bordetella pertussis. Biochemistry 28:438-42

Showing the most recent 10 out of 15 publications