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 20 of 418 for “"chaperone"”.
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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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The Role of Sacsin as a Molecular Chaperone
… proteins require the assistance of molecular chaperones. While substantial gains in our knowledge of the function of general chaperones have been made in the last two decades, the role of molecular chaperones in brain-specific processes is not clearly defined. In this study, we examined the …
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Mechanisms Behind the Chaperone Activity of Nucleic Acids
… others have shown nucleic acids can be powerful chaperones. Previous work has shown both RNA and DNA can prevent protein aggregation and RNA can pass off protein clients to the heat shock protein (Hsp) system. Here we explore the underlying physical properties and kinetics of how nucleic acids …
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Effects and dynamics of the UNC-45B molecular chaperone
… and assembly. Instead, the molecular chaperones work in a precise network to allow a nascent polypeptide to be protected from aggregation and folded to the precisely native product. The assembly of this myosin into a thick filament can proceed largely from the self-directed …
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Deciphering the role of Hsp31 as a multitasking chaperone
… Previously, we have shown that Hsp31 possesses chaperone properties with protective effects against α-syn toxicity in yeast. Recently, it is shown that Hsp31 has a methylglyoxalase activity that converts the toxic metabolite methylglyoxal into lactate. Here, we confirmed that Hsp31 is a robust …
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Investigations into the roles of bacterial TorD family chaperone proteins
… process, involving the binding of cytoplasmic chaperone proteins to the substrate signal peptide to prevent premature translocation before maturation is complete. A large group of these proteins form the TorD family of chaperone proteins, of which two examples are DmsD and TorD. DmsD is known …
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Towards Understanding Helicase and Chaperone Activities in the RNA Degradosome
… been previously shown to associate with the RNA chaperone Hfq to form a small RNA guided machinery that targets defined transcripts. This thesis attempts to investigate several characteristics of the degradosome, including the importance of RhlB, the structure of a portion of the RNase E …
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Studies of the UNC-45A Molecular Chaperone Expression in Human Cancer
… elegans UNC-45 acts as a molecular chaperone for myosin. Vertebrate genomes encode two UNC-45 genes: the UNC-45A(a) (general cell isoform) is expressed in many organs, whereas the UNC-45B(b) (striated muscle isoform) is exclusively expressed in striated muscle tissues. Our project …
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Studies of the UNC-45A Molecular Chaperone Expression in Human Cancer
… elegans UNC-45 acts as a molecular chaperone for myosin. Vertebrate genomes encode two UNC-45 genes: the UNC-45A(a) (general cell isoform) is expressed in many organs, whereas the UNC-45B(b) (striated muscle isoform) is exclusively expressed in striated muscle tissues. Our project …
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Investigating The Role Of Chaperone-Mediated Autophagy In Glioma Stem Cells
… of glioma stem cells, the activity of chaperone-mediated autophagy (CMA), a form of autophagy that selectively targets cytoplasmic proteins for lysosomal degradation, is significantly upregulated. Moreover, increasing of CMA activity through either forced expression of LAMP2A or the CMA …
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Mechanism and consequences of Mu transpososome remodeling by the ClpX chaperone
E. coli ClpX is a member of the Clp/Hsp100 family of ATPases that remodel multi-component complexes and facilitate ATP-dependent protein degradation. Protein remodelers alter the biological activity of their substrates, typically by changing the quaternary structure of their target proteins. ClpX …
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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 GGMP …
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Regulation of the histone H3K36 methyltransferase Set2 by the histone chaperone Spt6
… that Set2 activity in vivo requires the histone chaperone Spt6. Genetic studies in yeast suggested that Spt6 regulation occurs via controlling a Set2 autoinhibitory domain (AID) and recent structural studies of active Set2 demonstrated a direct physical interaction between Set2 and Spt6. These …
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The Role of BiP Co-chaperone SIL1 in Marinesco-Sjögren Syndrome Pathogenesis
… for the endoplasmicreticulum- resident Hsp70 chaperone, BiP. To date, there are 46 MSS-associated mutations that have been reported in SIL1, which occur throughout this gene and are predicted to result in a loss of SIL1’s function. The large majority of these mutations cause deletions of large …
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Characterization Of Arsd: An Arsenic Chaperone For The Arsab As(iii)-Translocating Atpase
… by a variety of proteins called metal ion chaperones, scaffolds or intracellular carriers. ArsD was recently shown to be a chaperone for transfer of cytosolic As(III) to the 583-residue ArsA ATPase, the catalytic subunit of the efflux pump. ArsD is a 120-residue protein with three conserved …
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The UNC-45 molecular chaperone: Its interactions with myosin and its thermosensing properties
… for others additional assistance of molecular chaperones is needed. The molecular chaperones are proteins which through interactions with the client proteins, prevent the formation of aggregates and promote the folding process without being present in their final structure. One of the most …
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Roles of the Histone Chaperone FACT in Drosophila Gene Regulation and Chromatin Architecture
The highly conserved histone chaperone FACT (Facilitates Chromatin Transcription) is thought to contribute to the disassembly and reassembly of nucleosomes in the wake of RNA polymerase II passage through chromatin. In yeast, mutation of FACT subunits leads to decreased nucleosome occupancy at the …
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Investigating the role of R2TP-like co-chaperone complexes during axonemal dynein assembly
… tightly regulated by multiple proteins including chaperones, dynein axonemal assembly factors (DNAAFs), microtubule inner proteins (MIPs), the outer arm docking complex (ODA-DC) and the nexin-dynein regulatory complex (N-DRC). Chaperones work with co-chaperones to regulate their many functions …
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Investigating the self-assembly and molecular chaperone ability of casein proteins and polyproline
… aggregates or to facilitate their molecular chaperone activity whereby they stabilize partly unfolded proteins. This thesis (i) examines the sequence and structures of caseins underlying their chaperone ability and fibril-forming propensity; and (ii) explores whether the fibril-forming …
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