Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Postdoctoral Individual National Research Service Award (F32)
Project #
5F32GM013594-03
Application #
3044792
Study Section
Biological Sciences 2 (BIOL)
Project Start
1992-02-01
Project End
Budget Start
1992-02-01
Budget End
1993-01-31
Support Year
3
Fiscal Year
1992
Total Cost
Indirect Cost
Name
Dana-Farber Cancer Institute
Department
Type
DUNS #
149617367
City
Boston
State
MA
Country
United States
Zip Code
02215
Page, A M; Davis, K; Molineux, C et al. (1998) Mutational analysis of exoribonuclease I from Saccharomyces cerevisiae. Nucleic Acids Res 26:3707-16
Johnson, A W; Kolodner, R D (1995) Synthetic lethality of sep1 (xrn1) ski2 and sep1 (xrn1) ski3 mutants of Saccharomyces cerevisiae is independent of killer virus and suggests a general role for these genes in translation control. Mol Cell Biol 15:2719-27
Heyer, W D; Johnson, A W; Reinhart, U et al. (1995) Regulation and intracellular localization of Saccharomyces cerevisiae strand exchange protein 1 (Sep1/Xrn1/Kem1), a multifunctional exonuclease. Mol Cell Biol 15:2728-36
Johnon, A W; Kolodner, R D (1994) Characterization of the interaction of Saccharomyces cerevisiae strand exchange protein 1 with DNA. J Biol Chem 269:3673-81
Johnson, A W; Kolodner, R D (1994) The activity of the Saccharomyces cerevisiae strand exchange protein 1 intrinsic exonuclease during joint molecule formation. J Biol Chem 269:3664-72
Tishkoff, D X; Johnson, A W; Kolodner, R D (1991) Molecular and genetic analysis of the gene encoding the Saccharomyces cerevisiae strand exchange protein Sep1. Mol Cell Biol 11:2593-608
Heyer, W D; Johnson, A W; Norris, D N et al. (1991) Saccharomyces cerevisiae proteins involved in hybrid DNA formation in vitro. Biochimie 73:269-76
Johnson, A W; Kolodner, R D (1991) Strand exchange protein 1 from Saccharomyces cerevisiae. A novel multifunctional protein that contains DNA strand exchange and exonuclease activities. J Biol Chem 266:14046-54