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Skip to Search Results- 1Armstrong, Heather K
- 1Horvat, Natalie K
- 1Lancaster, David L
- 1Mercier, Rebecca J
- 1Pare, Justin Mathew
- 1Rashid, Suad
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Analysis of Regulatory Mechanisms on RNA Interference by Molecular Chaperone Hsp90 and Protein Phosphorylation in Yeast
DownloadFall 2016
RNA interference (RNAi) is a conserved mechanism that eukaryotes employ small RNAs to regulate gene expression at transcriptional and post-trnascriptiona levels in a sequence-specific manner. However, current understanding on the regulatory mechanisms of RNAi via its core components is quite...
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Characterization of the motif requirements for the function of Aha1p and its homologue Hch1p
DownloadFall 2013
The Hsp90 chaperone facilitates the maturation of client proteins, which are key players in cancer. Hsp90 inhibitor drugs, such as NVP-AUY922, are promising anti-cancer therapies. Co-chaperones regulate the ATPase-dependent Hsp90 activity and specifically, the co-chaperone Aha1 is the most robust...
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Enzymatic and Biochemical Analysis of the Hsp90 Chaperone: Regulation by Co-chaperones, SUMOylation, and Interdomain Dynamics
DownloadFall 2017
Hsp90 is an essential eukaryotic molecular chaperone that plays a critical role in protein folding. It regulates the stability, maturation, and activation of numerous client proteins, many of which are involved in oncogenesis. It has been well established that Hsp90 is tightly regulated by...
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Hch1p Acts Differently From Its Homologue, Aha1p, in Regulating Sensitivity of Hsp90 to Hsp90 Inhibitors in Yeast
DownloadSpring 2013
Hsp90 is a molecular chaperone that plays a vital role in the regulation of oncoproteins, is targeted by small molecule Hsp90-inhibitors in cancer studies, and is functionally regulated by a cohort of proteins called co-chaperones. We determined that deletion of the co-chaperone Hch1p, but not...
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Hsp90 and its co-chaperones regulate the activity of human Argonaute2 in RNA-mediated silencing pathways
DownloadFall 2011
The potent ability of small, double-stranded RNAs to silence gene expression was initially reported 1998, sparking revolutions in molecular biology and genetics. Since then, intensive research into the mechanism of RNA-mediated silencing has implicated the machinery of this pathway in the...
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Investigation of Hsp90 Regulation by the Aha-type Co-chaperones: Mechanistic Insight into Two Conserved Motifs
DownloadSpring 2019
Hsp90 is a highly conserved and essential molecular chaperone. It regulates the folding, maturation, and activation of client proteins involved in a wide range of cellular processes and pathways, many of which are key players in disease. Hsp90 functions in the context of an ATPase driven...
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Spring 2013
Prions are infectious proteins. In their prion conformation, they catalyze the transformation of non-prion isomers into prions. Another characteristic common to currently identified prions is that they form amyloid aggregates. They occur in several mammals and multiple species of yeast, acting in...
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Fall 2021
Living cells have evolved a complex machinery of molecular chaperones to protect proteins from misfolding/aggregation in the protein-rich intracellular environment. Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone ubiquitously expressed in eubacteria and eukaryotes. The...