Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
7R01GM036960-02
Application #
3291708
Study Section
Allergy and Immunology Study Section (ALY)
Project Start
1987-12-01
Project End
1990-03-31
Budget Start
1987-12-01
Budget End
1988-03-31
Support Year
2
Fiscal Year
1987
Total Cost
Indirect Cost
Name
Medical Biology Institute
Department
Type
DUNS #
City
La Jolla
State
CA
Country
United States
Zip Code
92037
Ogata, R T; Low, P J (1997) Complement-inhibiting peptides identified by proximity to indels in the C3/4/5 protein family. J Immunol 158:3852-60
Ogata, R T; Low, P J (1995) Complement component C5: engineering of a mutant that is specifically cleaved by the C4-specific C1s protease. J Immunol 155:2642-51
Ogata, R T; Low, P J; Kawakami, M (1995) Substrate specificities of the protease of mouse serum Ra-reactive factor. J Immunol 154:2351-7
Ogata, R T; Low, P J; Bradt, B M et al. (1994) Substrate specificities of murine C1s. J Immunol 152:5890-5
Ogata, R T; Mathias, P; Bradt, B M et al. (1993) Murine C4b-binding protein. Mapping of the ligand binding site and the N-terminus of the pre-protein. J Immunol 150:2273-80
Mathias, P; Shreffler, D C; Cooper, N R et al. (1990) Conversion of the C4d.2 serologic allotype of murine complement component C4 to the C4d.1 allotype by site-specific mutagenesis. J Immunol 144:607-9
Ogata, R T; Cooper, N R; Bradt, B M et al. (1989) Murine complement component C4 and sex-limited protein: identification of amino acid residues essential for C4 function. Proc Natl Acad Sci U S A 86:5575-9
Picchi, M A; Bradt, B M; Cooper, N R et al. (1989) Transfected cDNA directs expression of hemolytically active murine C4 in cultured mouse and monkey cells. Complement Inflamm 6:442-52