Other names published for AHA1: YDR214W
AHA1 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Function/Process
- Genetic Interactions
- Mutants/Phenotypes
- Regulation of
- Regulatory Role
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Additional Information
AHA1 - Mutants/Phenotypes (8)
| Reference | Other Genes Addressed |
|---|---|
| Lancaster DL, et al. (2013) Chaperone proteins select and maintain [PIN+] prion conformations in Saccharomyces cerevisiae. J Biol Chem 288(2):1266-76 | |
| Armstrong H, et al. (2012) The Co-Chaperone Hch1 Regulates Hsp90 Function Differently than Its Homologue Aha1 and Confers Sensitivity to Yeast to the Hsp90 Inhibitor NVP-AUY922. PLoS One 7(11):e49322 | |
| Tsutsumi S, et al. (2012) Charged linker sequence modulates eukaryotic heat shock protein 90 (Hsp90) chaperone activity. Proc Natl Acad Sci U S A 109(8):2937-42 | |
| Franzosa EA, et al. (2011) Heterozygous yeast deletion collection screens reveal essential targets of hsp90. PLoS One 6(11):e28211 | |
| Ran F, et al. (2010) Hsp90 cochaperone Aha1 is a negative regulator of the Saccharomyces MAL activator and acts early in the chaperone activation pathway. J Biol Chem 285(18):13850-62 | |
| Meyer P, et al. (2004) Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. EMBO J 23(3):511-9 | |
| Lotz GP, et al. (2003) Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone. J Biol Chem 278(19):17228-35 | |
| Panaretou B, et al. (2002) Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. Mol Cell 10(6):1307-18 |




