Abstract

The central goals of this proposal concern the relationship between protein structure and protein function. The powerful techniques of recombinant DNA technology will be applied by four investigators to study distinct groups of biologically important macromolecules. Most of these molecules are involved in cell-cell communication and in most instances, DNA probes are available to allow a more global approach to a full appreciation of the synthesis, expression and activity of a particular protein. The Program Project mechanism is requested as the technologies required to carry out each individual project require not only the intense intellectual interaction presently taking place, but, in addition, the pooling of resources and equipment. All the studies largely involve protocols in the mouse and rat, although the results of these projects will have clear applications to man.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Program Projects (P01)
Project #
5P01GM031689-09
Application #
3096167
Study Section
Special Emphasis Panel (SSS (C))
Project Start
1984-04-01
Project End
1994-03-31
Budget Start
1992-04-01
Budget End
1993-03-31
Support Year
9
Fiscal Year
1992
Total Cost
Indirect Cost

  Institution

Name
University of Texas Sw Medical Center Dallas
Department
Type
Schools of Medicine
DUNS #
City
Dallas
State
TX
Country
United States
Zip Code
75390

  Publications

Sinclair, A M; Lee, J A; Goldstein, A et al. (2001) Lymphoid apoptosis and myeloid hyperplasia in CCAAT displacement protein mutant mice. Blood 98:3658-67
Potter, K N; Li, Y; Mageed, R A et al. (1999) Molecular characterization of the VH1-specific variable region determinants recognized by anti-idiotypic monoclonal antibodies G6 and G8. Scand J Immunol 50:14-20
Kroon, E; MacDonald, R J; Hammer, R E (1997) The transcriptional regulatory strategy of the rat tissue kallikrein gene family. Genes Funct 1:309-19
Potter, K N; Li, Y; Pascual, V et al. (1997) Staphylococcal protein A binding to VH3 encoded immunoglobulins. Int Rev Immunol 14:291-308
Potter, K N; Li, Y C; Abraham, G N et al. (1996) The MoAb-V kappa IIIb cross-reactive idiotope on A27a (Humkv325) encoded kappa chains maps to framework region 3. off. Scand J Immunol 44:305-13
MacDonald, R J; Southard-Smith, E M; Kroon, E (1996) Disparate tissue-specific expression of members of the tissue kallikrein multigene family of the rat. J Biol Chem 271:13684-90
Potter, K N; Li, Y; Capra, J D (1996) Staphylococcal protein A simultaneously interacts with framework region 1, complementarity-determining region 2, and framework region 3 on human VH3-encoded Igs. J Immunol 157:2982-8
Li, Y; Spellerberg, M B; Stevenson, F K et al. (1996) The I binding specificity of human VH 4-34 (VH 4-21) encoded antibodies is determined by both VH framework region 1 and complementarity determining region 3. J Mol Biol 256:577-89
Herrscher, R F; Kaplan, M H; Lelsz, D L et al. (1995) The immunoglobulin heavy-chain matrix-associating regions are bound by Bright: a B cell-specific trans-activator that describes a new DNA-binding protein family. Genes Dev 9:3067-82
Widhopf 2nd, G F; Pascual, V; Baer, R et al. (1995) Characterization and genomic mapping of a novel leader peptide associated with the human VH4-21 (VH4-34) gene segment. Ann N Y Acad Sci 764:62-71

Showing the most recent 10 out of 96 publications