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You searched for +publisher:"Georgia Tech" +contributor:("Nick Hud"). Showing records 1 – 2 of 2 total matches.

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Georgia Tech

1. Gokhale, Kavita Chandan. Interactions between endogenous prions, chaperones and polyglutamine proteins in the yeast model.

Degree: PhD, Biology, 2005, Georgia Tech

URL: http://hdl.handle.net/1853/6856 

Poly-Q expanded exon 1 of huntingtin (Q103) fused to GFP is toxic to yeast cells containing endogenous yeast prions, [PIN+] ([RNQ+]) and/or [PSI+], which presumably serve as aggregation nuclei. Propagation of yeast prions is modulated by the chaperones of Hsp100/70/40 complex. While some chaperones were reported to influence poly-Q aggregation in yeast, it was not clear whether they do it directly or via affecting yeast prions. Our data show that while dominant negative Hsp104 mutants antagonize poly-Q aggregation and toxicity by eliminating endogenous yeast prions, some mutant alleles of Hsp104 decreases size and ameliorate toxicity of poly-Q aggregates without affecting prion propagation. Elevated levels of the yeast Hsp40 proteins, Ydj1 and Sis1, exhibit opposite effects on poly-Q aggregation and toxicity without influencing prion propagation. Among the yeast Hsp70s, only overproduction of Ssa4 antagonized poly-Q toxicity. We have also isolated dominant Anti-poly-Q-toxicity (AQT) mutants counteracting poly-Q toxicity only in the absence of the major ubiquitin-conjugating enzyme Ubc4. Prion forming potential of other Q-rich proteins and influence of Q and P-rich regions on prion propagation were also studied. Our data connects poly-Q aggregation and toxicity to the stress defense pathway in yeast. As many stress-defense proteins are conserved between yeast and mammals, our data shed light on possible mechanisms modulating poly-Q aggregation and toxicity in mammalian cells. Advisors/Committee Members: Dr Harish Radhakrishna (Committee Member), Dr Jung Choi (Committee Member), Dr Nick Hud (Committee Member), Dr Roger Wartell (Committee Member), Dr Yury Chernoff (Committee Member).

Subjects/Keywords: Chaperones; Glutamine; Molecular chaperones; Prions; Yeast

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Gokhale, K. C. (2005). Interactions between endogenous prions, chaperones and polyglutamine proteins in the yeast model. (Doctoral Dissertation). Georgia Tech. Retrieved from http://hdl.handle.net/1853/6856

Chicago Manual of Style (16th Edition):

Gokhale, Kavita Chandan. “Interactions between endogenous prions, chaperones and polyglutamine proteins in the yeast model.” 2005. Doctoral Dissertation, Georgia Tech. Accessed January 19, 2021. http://hdl.handle.net/1853/6856.

MLA Handbook (7th Edition):

Gokhale, Kavita Chandan. “Interactions between endogenous prions, chaperones and polyglutamine proteins in the yeast model.” 2005. Web. 19 Jan 2021.

Vancouver:

Gokhale KC. Interactions between endogenous prions, chaperones and polyglutamine proteins in the yeast model. [Internet] [Doctoral dissertation]. Georgia Tech; 2005. [cited 2021 Jan 19]. Available from: http://hdl.handle.net/1853/6856.

Council of Science Editors:

Gokhale KC. Interactions between endogenous prions, chaperones and polyglutamine proteins in the yeast model. [Doctoral Dissertation]. Georgia Tech; 2005. Available from: http://hdl.handle.net/1853/6856

2. Shaffer, Hally A. Engineering the pregnane X receptor and estrogen receptor alpha to bind novel small molecules using negative chemical complementation.

Degree: PhD, Chemistry and Biochemistry, 2011, Georgia Tech

URL: http://hdl.handle.net/1853/39620 

Nuclear receptors are ligand-activated transcription factors that play significant roles in various biological processes within the body, such as cell development, hormone metabolism, reproduction, and cardiac function. As transcription factors, nuclear receptors are involved in many diseases, such as diabetes, cancer, and arthritis, resulting in approximately 10-15% of the pharmaceutical drugs presently on the market being targeted toward nuclear receptors. Structurally, nuclear receptors consist of a DNA-binding domain (DBD), responsible for binding specific sequences of DNA called response elements, fused to a ligand-binding domain (LBD) through a hinge region. The LBD binds a small molecule ligand. Upon ligand binding, the LBD changes to an active conformation leading to the recruitment of coactivator (CoAC) proteins and initiation of transcription. As a result of their involvement in disease, there is an emphasis on engineering nuclear receptors for applications in gene therapy, drug discovery and metabolic engineering. Advisors/Committee Members: Bahareh Azizi (Committee Chair), Donald Doyle (Committee Chair), Andreas Bommarius (Committee Co-Chair), Loren Williams (Committee Co-Chair), Adegboyega Oyelere (Committee Member), Nick Hud (Committee Member), Sheldon May (Committee Member).

Subjects/Keywords: Nuclear receptors; Chemical complementation; Negative chemical complementation; Yeast-two hybrid selection; Pregnane X receptor; Estrogen receptor; Pregnane; Protein engineering; Nuclear receptors (Biochemistry); Transcription factors; Yeast Genetics

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Shaffer, H. A. (2011). Engineering the pregnane X receptor and estrogen receptor alpha to bind novel small molecules using negative chemical complementation. (Doctoral Dissertation). Georgia Tech. Retrieved from http://hdl.handle.net/1853/39620

Chicago Manual of Style (16th Edition):

Shaffer, Hally A. “Engineering the pregnane X receptor and estrogen receptor alpha to bind novel small molecules using negative chemical complementation.” 2011. Doctoral Dissertation, Georgia Tech. Accessed January 19, 2021. http://hdl.handle.net/1853/39620.

MLA Handbook (7th Edition):

Shaffer, Hally A. “Engineering the pregnane X receptor and estrogen receptor alpha to bind novel small molecules using negative chemical complementation.” 2011. Web. 19 Jan 2021.

Vancouver:

Shaffer HA. Engineering the pregnane X receptor and estrogen receptor alpha to bind novel small molecules using negative chemical complementation. [Internet] [Doctoral dissertation]. Georgia Tech; 2011. [cited 2021 Jan 19]. Available from: http://hdl.handle.net/1853/39620.

Council of Science Editors:

Shaffer HA. Engineering the pregnane X receptor and estrogen receptor alpha to bind novel small molecules using negative chemical complementation. [Doctoral Dissertation]. Georgia Tech; 2011. Available from: http://hdl.handle.net/1853/39620

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