Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
3R01GM046888-01A1S1
Application #
3306384
Study Section
Genetics Study Section (GEN)
Project Start
1992-09-30
Project End
1996-08-31
Budget Start
1992-09-30
Budget End
1993-08-31
Support Year
1
Fiscal Year
1993
Total Cost
Indirect Cost
Name
Stanford University
Department
Type
Schools of Medicine
DUNS #
800771545
City
Stanford
State
CA
Country
United States
Zip Code
94305
Amberg, D C; Zahner, J E; Mulholland, J W et al. (1997) Aip3p/Bud6p, a yeast actin-interacting protein that is involved in morphogenesis and the selection of bipolar budding sites. Mol Biol Cell 8:729-53
Doyle, T; Botstein, D (1996) Movement of yeast cortical actin cytoskeleton visualized in vivo. Proc Natl Acad Sci U S A 93:3886-91
Miller, C J; Doyle, T C; Bobkova, E et al. (1996) Mutational analysis of the role of hydrophobic residues in the 338-348 helix on actin in actomyosin interactions. Biochemistry 35:3670-6
Amberg, D C; Basart, E; Botstein, D (1995) Defining protein interactions with yeast actin in vivo. Nat Struct Biol 2:28-35
Amberg, D C; Botstein, D; Beasley, E M (1995) Precise gene disruption in Saccharomyces cerevisiae by double fusion polymerase chain reaction. Yeast 11:1275-80
Mulholland, J; Preuss, D; Moon, A et al. (1994) Ultrastructure of the yeast actin cytoskeleton and its association with the plasma membrane. J Cell Biol 125:381-91
Clark, C D; Palzkill, T; Botstein, D (1994) Systematic mutagenesis of the yeast mating pheromone receptor third intracellular loop. J Biol Chem 269:8831-41
Ohya, Y; Botstein, D (1994) Diverse essential functions revealed by complementing yeast calmodulin mutants. Science 263:963-6
Ohya, Y; Botstein, D (1994) Structure-based systematic isolation of conditional-lethal mutations in the single yeast calmodulin gene. Genetics 138:1041-54