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Showing 1 to 7 of 7 for “"Hsp110"”.

  1. Deciphering The Role of Hsp110 Chaperones In Diseases of Protein Misfolding

    … Parkinson’s, and Huntington’s disease. Hsp110 is a member of the Hsp70 class of molecular chaperones and acts as a nucleotide exchange factor (NEF) for Hsp70, the preeminent Hsp70-family protein folding chaperone. Hsp110 promotes rapid cycling of ADP for ATP, allowing Hsp70 to properly …

    uthsc Repository record for Deciphering The Role of Hsp110 Chaperones In Diseases of Protein Misfolding (opens in a new tab)

  2. Mutational analysis of Hsp110 suggests an integral role for the chaperone in yeast prion propagation.

    … in this thesis focuses on the heat shock protein Hsp110. Recent reports have demonstrated how the Hsp110 proteins Sse1 and Sse2 are necessary for promoting the propagation of the yeast prions [PSI+] and [URE3]. A group of Sse1 mutants with impaired ability to propagate [PSI+] were created. These …

    maynooth Repository record for Mutational analysis of Hsp110 suggests an integral role for the chaperone in yeast prion propagation. (opens in a new tab)

  3. Analysis of The Biochemical and Cellular Activities of Substrate Binding By The Molecular Chaperone Hsp110/Sse1

    … protein clients to facilitate folding. The Hsp110 class of chaperones are divergent relatives of Hsp70 that are extremely effective in preventing protein aggregation but lack the hallmark folding activity seen in Hsp70s. Hsp110s serve as Hsp70 nucleotide exchange factors (NEF) that …

    uthsc Repository record for Analysis of The Biochemical and Cellular Activities of Substrate Binding By The Molecular Chaperone Hsp110/Sse1 (opens in a new tab)

  4. Elucidation of the role of the linker motifs of Plasmodium falciparum Hsp70-1 and Hsp70-z

    … is a non-canonical Hsp70 which belongs to the Hsp110 subfamily. Hsp70s exhibit a highly conserved structural architecture characterized by an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD) adjoined by a linker motif. Although canonical Hsp70 linkers …

    venda Repository record for Elucidation of the role of the linker motifs of Plasmodium falciparum Hsp70-1 and Hsp70-z (opens in a new tab)

  5. Functional Analysis of Cytosolic Hsp70 Nucleotide Exchange Factor Networks In Yeast

    … homologous to human counterparts; Sse1/Sse2/HSP110, Fes1/HspBP1, and Snl1/Bag1. In an effort to understand the differential functional contributions of the cytosolic NEFs to protein homeostasis (“proteostasis”), I carried out comparative genetic, biochemical and cell biological analyses. For …

    uthsc Repository record for Functional Analysis of Cytosolic Hsp70 Nucleotide Exchange Factor Networks In Yeast (opens in a new tab)

  6. Untersuchungen zur Regulation des Insl3 Gens

    … bindende transagierende Faktor als Mitglied der hsp110 verwandten Heatshock-Proteinfamilie identifiziert werden. Durch Luciferaseassays sollte die Beteiligung des transagierenden Faktors an der Regulation des Insl3 Gens untersucht werden. Zur Bestimmung der subzellulären Lokalisation des …

    goettingen Repository record for Untersuchungen zur Regulation des Insl3 Gens (opens in a new tab)

  7. Biochemical Characterization of Binding Partners of Two Hsp70 Co-Chaperones In Saccharomyces Cerevisiae

    … non-related cytosolic NEFs are present: Sse1 (Hsp110), Fes1 (HspBP1) and Snl1 (Bag-1). Snl1 is unique among the cytosolic NEFs as it is localized at the ER membrane with its Hsp70 binding (BAG) domain exposed to the cytosol. I discovered that Snl1 distinctly interacts with assembled ribosomes …

    uthsc Repository record for Biochemical Characterization of Binding Partners of Two Hsp70 Co-Chaperones In Saccharomyces Cerevisiae (opens in a new tab)