Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM022200-19
Application #
2173891
Study Section
Virology Study Section (VR)
Project Start
1977-05-01
Project End
1998-03-31
Budget Start
1996-04-01
Budget End
1998-03-31
Support Year
19
Fiscal Year
1996
Total Cost
Indirect Cost
Name
State University of New York at Buffalo
Department
Biology
Type
Schools of Arts and Sciences
DUNS #
038633251
City
Buffalo
State
NY
Country
United States
Zip Code
14260
Lopinski, J D; Dinman, J D; Bruenn, J A (2000) Kinetics of ribosomal pausing during programmed -1 translational frameshifting. Mol Cell Biol 20:1095-103
Routhier, E; Bruenn, J A (1998) Functions of conserved motifs in the RNA-dependent RNA polymerase of a yeast double-stranded RNA virus. J Virol 72:4427-9
Park, C M; Lopinski, J D; Masuda, J et al. (1996) A second double-stranded RNA virus from yeast. Virology 216:451-4
Yao, W; Bruenn, J A (1995) Interference with replication of two double-stranded RNA viruses by production of N-terminal fragments of capsid polypeptides. Virology 214:215-21
Tu, C; Tzeng, T H; Bruenn, J A (1992) Ribosomal movement impeded at a pseudoknot required for frameshifting. Proc Natl Acad Sci U S A 89:8636-40
Tzeng, T H; Tu, C L; Bruenn, J A (1992) Ribosomal frameshifting requires a pseudoknot in the Saccharomyces cerevisiae double-stranded RNA virus. J Virol 66:999-1006
Huan, B F; Shen, Y Q; Bruenn, J A (1991) In vivo mapping of a sequence required for interference with the yeast killer virus. Proc Natl Acad Sci U S A 88:1271-5
Bruenn, J A (1991) Relationships among the positive strand and double-strand RNA viruses as viewed through their RNA-dependent RNA polymerases. Nucleic Acids Res 19:217-26
Tao, J; Ginsberg, I; Banerjee, N et al. (1990) Ustilago maydis KP6 killer toxin: structure, expression in Saccharomyces cerevisiae, and relationship to other cellular toxins. Mol Cell Biol 10:1373-81
Bruenn, L A; Diamond, M E; Dowhanick, J J (1989) Similarity between the picornavirus VP3 capsid polypeptide and the Saccharomyces cerevisiae virus capsid polypeptide. Nucleic Acids Res 17:7487-93

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