Global ETD Search
Search theses and dissertations gathered from participating repositories worldwide. Every result links back to the library that holds it. No account is needed.
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Showing 1 to 17 of 17 for “"Co-Chaperones"”.
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Regulation of mammalian IRE1α: Co-chaperones and their importance
… nucleus by promoting oligomerisation of IRE1, a conserved transmembrane ER stress receptor. Despite significant research, the mechanism of coupling ER stress to IRE1 oligomerisation and activation has remained contested. There are two proposed mechanisms by which IRE1 may sense accumulating …
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Biochemical Characterization of Binding Partners of Two Hsp70 Co-Chaperones In Saccharomyces Cerevisiae
… cardiovascular disease and cystic fibrosis. To combat proteotoxic stress, cells deploy an array of molecular chaperones that assist in the repair or removal of misfolded proteins.</p> <p>Hsp70, an evolutionarily conserved molecular chaperone, promotes protein folding and helps maintain them in a …
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Functional significance of Hsp70 post-translational modification in prion propagation and cellular function
… (proteinaceous infectious particles) was first coined by Stanley Prusiner while naming the causative agent responsible for a group of invariably fatal neurodegenerative diseases collectively termed transmissible spongiform encephalopathies (TSE). A breakthrough in prion research came with the …
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Investigating the role of R2TP-like co-chaperone complexes during axonemal dynein assembly
… by structures called axonemal dynein motor complexes. These are large, multi-subunit structures, and so it is crucial that they are assembled correctly. In humans, if the motility of these is defective, it can lead to a disorder called Primary Ciliary Dyskinesia, or PCD. This is a …
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The Role of Sacsin as a Molecular Chaperone
… appears to be related to protein misfolding, comprising a large public health burden. For example, the two most common neurodegenerative diseases, Alzheimer’s and Parkinson’s diseases, possess protein misfolding as a core component of their pathology. In order to properly fold, many proteins …
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Physico-Chemical Characterisation of Disease-Related Protein-Protein Interactions in Solution
… protein-protein interactions require volumes and concentrations significantly higher than those relevant under physiological conditions. Microfluidic diffusional sizing offers an alternative method for investigating protein-protein interactions and protein assembly under physiological conditions …
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Assessing the role of Hsp70 in prion propagation in Saccharomyces cerevisiae
… responsible for many neurodegenerative diseases, collectively termed as transmissible spongioform encephalopathies, including; BSE, vBSE, scrapie and CJD. Prions are also present in fungi. There have been a number of prion proteins discovered in the yeast Saccharomyces cerevisiae. Probably the …
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Leveraging Protein Homeostasis as a Disease-modifying Strategy
… functional states, more work is needed to uncover the complex proteostasis mechanisms that are particularly vulnerable to collapse in disease. To address this problem, bioinformatics approaches were deployed to investigate the links between proteostasis and disease. By coupling bioinformatic …
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An Investigation of TorsinA Interaction Partners
… binding. We found that while TorsinA N-glycosylation is required for Calnexin binding, terminal mono-glucosylation is not. This finding deviates from Calnexin’s interactions with its canonical substrates, as Calnexin’s lectin domain specifically recognizes mono-glucosylated N-glycans. …
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Relationships Between Expression of Heat Shock Protein Genes and Photosynthetic Behavior During Drought Stress in Plants
… expressed in response to environmental stresses. Compared to other kingdoms, plant HSP families are larger, presumably the result of adaptation to a wide range of stresses. Following on an analysis of drought stress characteristics in loblolly pine (Watkinson et al., 2003), expression patterns of …
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Inhibitory effects of Green synthesized Senna alexandrina silver nanoparticles (SAAgNPs) on Escherichia coli DnaK
Plant extracts have garnered considerable interest in the environmentally friendly and economically viable production of silver nanoparticles (AgNPs) through their application in green synthesis. However, Plant-derived nanoparticles may potentially have unique physicochemical characteristics. This …
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The Role of Phosducin-like Protein and the Cytosolic Chaperonin CCT in G beta gamma dimer Assembly
… the three-dimensional structure of PhLP:CCT complex has been solved by cryoelectron microscopy. PhLP was found to bind only one of the chaperonin rings with both N- and C-terminal domains. It spans the central folding cavity of CCT and interacts with two opposite sides of the top apical …
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Hsp90 as a molecular target
Heat shock protein 90 (Hsp90), a highly conserved molecular chaperone, has been proposed to play a vital role in tumorigenesis. Hsp90 has two isoforms, of which Hsp90α is the major isoform of the Hsp90 complex and has an inducible expression profile. The molecular chaperone Hsp90α has been …
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Deciphering Functional Significance of Substrate-Binding Domain of Ssa1 on Heat-Shock Response and Prion Propagation
The Hsp70 (70kDa heat shock protein) is highly conserved in all species and has been implicated in a variety of important cellular functions such as heat shock response, prion propagation, protein folding and refolding, translocation across membranes and assembly of macromolecular complexes. A …
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Assembly and biochemical properties of a human chaperone/co-chaperone protein complex
… protein family (eg. Hsp70) function as molecular chaperones by binding to exposed hydrophobic patches on nascent polypeptides forming non-covalent interactions, thereby preventing their aggregation and facilitating their proper folding. The folding reaction comprises of cyclic binding and release …
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Investigation of the role of the GGMP motif of Plasmodium falciparum Hsp70-1 on the chaperone function of the protein and its interaction with a co-chaperone, PfHop
… of PfHsp70-1 with its functional regulators (co-chaperones). P. falciparum Hsp70/Hsp90 organizing protein (PfHop) constitutes one of the functional regulators of PfHsp70-1. PfHop allows PfHsp70-1 and its chaperone partner, PfHsp90 to form a functional partnership. Given the proximity of the …
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The regulation of yeast homotypic vacuole fusion by phosphatidic acid and diacylglycerol
Eukaryotic membrane fusion is a highly conserved process that is necessary to maintain cellular homeostasis. Ultimately, two membrane compartments are brought to each other, direct contact is established, and the bilayers and lumenal contents mix. In Saccharomyces cerevisiae, homotypic vacuole …