Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
2R01GM040094-08
Application #
2180173
Study Section
Genetics Study Section (GEN)
Project Start
1988-04-01
Project End
1997-12-31
Budget Start
1996-01-22
Budget End
1996-12-31
Support Year
8
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Columbia University (N.Y.)
Department
Microbiology/Immun/Virology
Type
Schools of Medicine
DUNS #
167204994
City
New York
State
NY
Country
United States
Zip Code
10032
Moretti, P; Shore, D (2001) Multiple interactions in Sir protein recruitment by Rap1p at silencers and telomeres in yeast. Mol Cell Biol 21:8082-94
Vannier, D; Damay, P; Shore, D (2001) A role for Sds3p, a component of the Rpd3p/Sin3p deacetylase complex, in maintaining cellular integrity in Saccharomyces cerevisiae. Mol Genet Genomics 265:560-8
Marcand, S; Wotton, D; Gilson, E et al. (1997) Rap1p and telomere length regulation in yeast. Ciba Found Symp 211:76-93; discussion 93-103
Marcand, S; Gilson, E; Shore, D (1997) A protein-counting mechanism for telomere length regulation in yeast. Science 275:986-90
Shore, D (1997) Telomere length regulation: getting the measure of chromosome ends. Biol Chem 378:591-7
Wotton, D; Shore, D (1997) A novel Rap1p-interacting factor, Rif2p, cooperates with Rif1p to regulate telomere length in Saccharomyces cerevisiae. Genes Dev 11:748-60
Shore, D (1997) Telomerase and telomere-binding proteins: controlling the endgame. Trends Biochem Sci 22:233-5
Marcand, S; Buck, S W; Moretti, P et al. (1996) Silencing of genes at nontelomeric sites in yeast is controlled by sequestration of silencing factors at telomeres by Rap 1 protein. Genes Dev 10:1297-309
Chi, M H; Shore, D (1996) SUM1-1, a dominant suppressor of SIR mutations in Saccharomyces cerevisiae, increases transcriptional silencing at telomeres and HM mating-type loci and decreases chromosome stability. Mol Cell Biol 16:4281-94
Wotton, D; Freeman, K; Shore, D (1996) Multimerization of Hsp42p, a novel heat shock protein of Saccharomyces cerevisiae, is dependent on a conserved carboxyl-terminal sequence. J Biol Chem 271:2717-23

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