Richard Gaber
Affiliations: | Northwestern University, Evanston, IL |
Area:
Microbiology BiologyGoogle:
"Richard Gaber"Children
Sign in to add trainee| Marc Vidal | grad student | 1988-1992 | Northwestern (Neurotree) |
| Richard B. Kurtz | grad student | 2001 | Northwestern |
| Marija Tesic | grad student | 2003 | Northwestern |
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Publications
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| Tesic M, Gaber RF. (2007) HSP90 Co-chaperones in saccharomyces cerevisiae Yeast as a Tool in Cancer Research. 141-177 |
| Tesic M, Marsh JA, Cullinan SB, et al. (2003) Functional interactions between Hsp90 and the co-chaperones Cns1 and Cpr7 in Saccharomyces cerevisiae. The Journal of Biological Chemistry. 278: 32692-701 |
| Riggs DL, Roberts PJ, Chirillo SC, et al. (2003) The Hsp90-binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo. The Embo Journal. 22: 1158-67 |
| Marsh JA, Kalton HM, Gaber RF. (1998) Cns1 is an essential protein associated with the hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Delta cells. Molecular and Cellular Biology. 18: 7353-9 |
| Duina AA, Kalton HM, Gaber RF. (1998) Requirement for Hsp90 and a CyP-40-type cyclophilin in negative regulation of the heat shock response. The Journal of Biological Chemistry. 273: 18974-8 |
| Duina AA, Marsh JA, Kurtz RB, et al. (1998) The peptidyl-prolyl isomerase domain of the CyP-40 cyclophilin homolog Cpr7 is not required to support growth or glucocorticoid receptor activity in Saccharomyces cerevisiae. The Journal of Biological Chemistry. 273: 10819-22 |
| Wright MB, Howell EA, Gaber RF. (1996) Amino acid substitutions in membrane-spanning domains of Hol1, a member of the major facilitator superfamily of transporters, confer nonselective cation uptake in Saccharomyces cerevisiae. Journal of Bacteriology. 178: 7197-205 |
| Duina AA, Chang HC, Marsh JA, et al. (1996) A cyclophilin function in Hsp90-dependent signal transduction. Science (New York, N.Y.). 274: 1713-5 |
| Duina AA, Marsh JA, Gaber RF. (1996) Identification of two CyP-40-like cyclophilins in Saccharomyces cerevisiae, one of which is required for normal growth. Yeast (Chichester, England). 12: 943-52 |